|
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, ... |
95-775 |
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: 1245.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGaevDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKK---ESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQN 414
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 415 CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKgIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 495 LEQEEYAREGIQWVFIDFGLDLQACIELIEKP-LGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFekpKPPKGKQG 573
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNF---KKPKPKKS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 574 EAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYttqeeaaakAKEGGGGGKKKGKSGSFMT 653
Cdd:cd01377 474 EAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSS-DPLVASLFKDY---------EESGGGGGKKKKKGGSFRT 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 654 VSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILA 733
Cdd:cd01377 544 VSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILA 623
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 734 AKEAKSDDDKKKCAEAIMSKlvnDGSLSEEMFRIGLTKVFFK 775
Cdd:cd01377 624 PNAIPKGFDDGKAACEKILK---ALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-775 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1105.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 83 TEDMSNLSFLNDASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNML 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 163 QDHENQSMLITGESGAGKTENTKKVICYFAAVGASQQEGgaevdpnkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRF 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG--------NVGRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 243 GKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQ-AELIIDGI 321
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNP-KDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 322 DDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPR 401
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 402 VKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVN 481
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 482 EKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHP 560
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 561 NFEKPKPpkgkQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeAAAKAKEGGG 640
Cdd:pfam00063 470 HFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSS-DPLLAELFPDYETA--ESAAANESGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 641 GGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRT 720
Cdd:pfam00063 543 STPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRI 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 721 LHPDFVQRYAILAAKEAKS-DDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:pfam00063 623 TFQEFVQRYRILAPKTWPKwKGDAKKGCEAILQSL----NLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-787 |
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: 1011.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 76 NPPKFEKTEDMSNLSFLNDASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 156 EAYRNMLQDHENQSMLITGESGAGKTENTKKVICYFAAVGASqqeggaevdpNKKKVTLEDQIVQTNPVLEAFGNAKTVR 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS----------NTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 236 NNNSSRFGKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSdFRPELKKELLLDLPIKDYWFVAQA- 314
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLA-GASEELKKELGLKSPEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 315 ELIIDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQA-EPDGTDEAEKASNMYGIGCEEF 393
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 394 LKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFE 473
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKD-GSTYFIGVLDIYGFEIFEVNSFE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 474 QLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLV 552
Cdd:smart00242 389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 553 dQHLGKHPNFEKPKppkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeaa 632
Cdd:smart00242 468 -QHHKKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSK-NPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 633 akakegggggkkKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRIC 712
Cdd:smart00242 538 ------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 713 RKGFPNRTLHPDFVQRYAILAAKEAKS-DDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFKAGVLAHLEDIRD 787
Cdd:smart00242 606 RAGFPYRLPFDEFLQRYRVLLPDTWPPwGGDAKKACEALLQSL----GLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-775 |
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: 963.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGAEvdpnKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA----KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQN 414
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 415 CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQ-KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 495 LEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQGE 574
Cdd:cd14909 396 LEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 575 AHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeaaaKAKEGGGGGKKKGKSGSFMTV 654
Cdd:cd14909 476 AHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQ-NKLLIEIFADHAGQ-----SGGGEQAKGGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 655 SMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAA 734
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 17509401 735 KEAKSDDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14909 630 AGIQGEEDPKKAAEIILESI----ALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-775 |
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: 885.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGA--SQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNK 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 253 HGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDE 332
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 333 AFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKG 412
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 413 QNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKgIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHM 492
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTK-LPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 493 FVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQ 572
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 573 GEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTqeeAAAKAKEGGGGGKKKGKSGSFM 652
Cdd:cd14927 480 YEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQ-NKLLATLYENYVG---SDSTEDPKSGVKEKRKKAASFQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 653 TVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAIL 732
Cdd:cd14927 556 TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 17509401 733 AAKEAKSDD--DKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14927 636 NPSAIPDDKfvDSRKATEKLLGSL----DIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-775 |
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: 847.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASqqeggaeVDPNKK-----KVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF 250
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT-------GDLAKKkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 251 NKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLT 330
Cdd:cd14913 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 331 DEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVS 410
Cdd:cd14913 235 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 411 KGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKgIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNH 490
Cdd:cd14913 315 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTK-LPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 491 HMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKG 570
Cdd:cd14913 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 KqGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsAMKQSKGNDLLVEIWQDYTTqeeaaaKAKEGGGGGKKKGKSGS 650
Cdd:cd14913 474 R-AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVV-GLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKKKGSS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 651 FMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 730
Cdd:cd14913 546 FQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17509401 731 ILAAK---EAKSDDDKKKCaeaimSKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14913 626 VLNASaipEGQFIDSKKAC-----EKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-775 |
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: 835.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASqqeGGAEVDpnkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT---GKQSSD---GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14934 155 KLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQN 414
Cdd:cd14934 235 DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 415 CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKgIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14934 315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTK-MQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 495 LEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQGE 574
Cdd:cd14934 394 LEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 575 AHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSkgNDLLVEIWQDyttqeeaaakAKEGGGGGKKKGKSGSFMTV 654
Cdd:cd14934 474 AHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKS--SLGLLALLFK----------EEEAPAGSKKQKRGSSFMTV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 655 SMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAA 734
Cdd:cd14934 542 SNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNP 621
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 735 KE-AKSDDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14934 622 NViPQGFVDNKKASELLLGSI----DLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-775 |
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: 808.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASqqeggaeVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM-------IESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANP-SDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQN 414
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 415 CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKgIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAK-LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 495 LEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKgKQGE 574
Cdd:cd14929 392 LEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDK-KKFE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 575 AHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTqeeaaaKAKEGGGGGKKKGKSGSFMTV 654
Cdd:cd14929 471 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSS-NRLLASLFENYIS------TDSAIQFGEKKRKKGASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 655 SMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAA 734
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17509401 735 KE-AKSD-DDKKKCAEAIMSKLVNDGSlseeMFRIGLTKVFFK 775
Cdd:cd14929 624 RTfPKSKfVSSRKAAEELLGSLEIDHT----QYRFGITKVFFK 662
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-775 |
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: 802.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGK-RKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKgRSADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGASQQEggaevDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSS-----KSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYS----DFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQL 329
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAglsdGAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 330 TDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREE--QAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTE 407
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 408 WVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRD-YFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQ 486
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 487 FFNHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKP 565
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH-GSHPRFFSK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 566 KppkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgndllveiwqdyttqeeaaakakegggggkkk 645
Cdd:cd00124 474 K----RKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS-------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 646 gksgsfmtvsmLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDF 725
Cdd:cd00124 518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17509401 726 VQRYAILAAKEAKSDDDKKKCAEAIMSKLvndGSLSEEMFRIGLTKVFFK 775
Cdd:cd00124 587 LKRYRILAPGATEKASDSKKAAVLALLLL---LKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-775 |
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: 791.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKG--TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNC 415
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 416 EQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 496 EQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQgEA 575
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKP-EA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 576 HFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsAMKQSKGNDLLVEIWQDYTtqeeaaAKAKEGGGGGKKKGKSGSFMTVS 655
Cdd:cd14917 478 HFSLIHYAGTVDYNIIGWLQKNKDPLNETVV-GLYQKSSLKLLSNLFANYA------GADAPIEKGKGKAKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 656 MLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAIL--A 733
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpA 630
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 734 AKEAKSDDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14917 631 AIPEGQFIDSRKGAEKLLSSL----DIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-775 |
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: 782.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAEVdPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKEN-PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNC 415
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 416 EQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 496 EQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQgEA 575
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQ-EA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 576 HFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsAMKQSKGNDLLVEIWQDYTTqeeaaAKAKEGGGGGKKKGKSGSFMTVS 655
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVV-GLYQKSSLKLMATLFSTYAS-----ADTGDSGKGKGGKKKGSSFQTVS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 656 MLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAK 735
Cdd:cd14916 553 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 736 EAKSDD--DKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14916 633 AIPEGQfiDSRKGAEKLLGSL----DIDHNQYKFGHTKVFFK 670
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
24-1114 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 779.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 24 SKPYDSKKNVWIPDPEEGYLAGEITATkGDQVTIVTARGNEVTLKKElvqEMNPPKFEKTEDMSNLSFLNDASVLHNLRS 103
Cdd:COG5022 13 WIPDEEKGWIWAEIIKEAFNKGKVTEE-GKKEDGESVSVKKKVLGND---RIKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 104 RYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGESGAGKTEN 183
Cdd:COG5022 89 RYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 184 TKKVICYFAAVGASQQEGgaevdpnkkKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGRLASCDIEH 263
Cdd:COG5022 169 AKRIMQYLASVTSSSTVE---------ISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 264 YLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAEL-IIDGIDDVEEFQLTDEAFDILNFSAV 342
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNP-KDYIYLSQGGCdKIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 343 EKQDCYRLMSAHMHMGNMKFKQRpREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAV 422
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFKED-RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 423 GAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAR 502
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSA-AASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 503 EGIQWVFIDFgLDLQACIELIEK--PLGIISMLDEECIVPKATDLTLASKLVDQ-HLGKHPNFEKPkppkgKQGEAHFAM 579
Cdd:COG5022 477 EGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKS-----RFRDNKFVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 580 RHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYttqeeaaakakegggggKKKGKSGSFMTVSMLYR 659
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKAST-NEFVSTLFDDE-----------------ENIESKGRFPTLGSRFK 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 660 ESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEAKS 739
Cdd:COG5022 613 ESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWT 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 740 DDDKKKCAEAIMSKLV-NDGSLSEEMFRIGLTKVFFKAGVLAHLEDIRDEKLATILTGFQSQIRWHLGLKDRKRRMEQRA 818
Cdd:COG5022 693 GEYTWKEDTKNAVKSIlEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIK 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 819 GLLIVQRNVRSWCTLRTWEWFKLYGKVKPMLKAGKEAEELEKINDKVKALEDSLakeeklrkELEESSAKLVEEKTSLft 898
Cdd:COG5022 773 KIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI--------KREKKLRETEEVEFSL-- 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 899 NLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLAdnEDRTADVQRAKKKIEAEVEalkKQIQDLEMSLRKAESEKQ 978
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELA--ERQLQELKIDVKSISSLKL---VNLELESEIIELKKSLSS 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 979 skdhqirSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEdlQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLD 1058
Cdd:COG5022 918 -------DLIENLEFKTELIARLKKLLNNIDLEEGPSIE--YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGN 988
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1059 KQKRKVEGELKIAQENIDESGRQRHDLE--NNLKKKESELHSVSSRLEDEQALVSKLQ 1114
Cdd:COG5022 989 KANSELKNFKKELAELSKQYGALQESTKqlKELPVEVAELQSASKIISSESTELSILK 1046
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-775 |
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: 771.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVgASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATI-AVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNC 415
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 416 EQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 496 EQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKqGEA 575
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGK-AEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 576 HFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsAMKQSKGNDLLVEIWQDYTTqeeaAAKAKEGGGGGKKKGKSGSFMTVS 655
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVV-GLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 656 MLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAK 735
Cdd:cd14923 554 AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAS 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 736 EAKSDD--DKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14923 634 AIPEGQfiDSKNASEKLLNSI----DVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-775 |
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: 765.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 97 VLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 177 GAGKTENTKKVICYFAAVGASQQEGGAEvdPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGRL 256
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 257 ASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFDI 336
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 337 LNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCE 416
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 417 QVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLE 496
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 497 QEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKqGEAH 576
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 577 FAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsAMKQSKGNDLLVEIWQDYTTqeeaaaKAKEGGGGGKKKGKSGSFMTVSM 656
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVV-GLYQKSAMKTLASLFSTYAS------AEADSGAKKGAKKKGSSFQTVSA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 657 LYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKE 736
Cdd:cd14918 552 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASA 631
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 17509401 737 AKSDD--DKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14918 632 IPEGQfiDSKKASEKLLASI----DIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-775 |
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: 765.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNC 415
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 416 EQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 496 EQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKqGEA 575
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGK-AEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 576 HFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGNDLLveiwQDYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVS 655
Cdd:cd14912 480 HFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLA----YLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 656 MLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAK 735
Cdd:cd14912 556 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 736 EAKSDD--DKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14912 636 AIPEGQfiDSKKASEKLLASI----DIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-775 |
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: 761.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNC 415
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 416 EQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 496 EQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQgEA 575
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKV-EA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 576 HFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsAMKQSKGNDLLVEIWQDYTTqeeaaAKAKEGGGGGKKKGKSGSFMTVS 655
Cdd:cd14910 480 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVV-GLYQKSSMKTLALLFSGAAA-----AEAEEGGGKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 656 MLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAK 735
Cdd:cd14910 554 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 736 EAKSDD--DKKKCAEaimsKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14910 634 AIPEGQfiDSKKASE----KLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-775 |
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: 761.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNC 415
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 416 EQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 496 EQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKqGEA 575
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-AEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 576 HFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGNDLLveiwqdYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVS 655
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLA------FLFSGGQTAEAEGGGGKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 656 MLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAK 735
Cdd:cd14915 554 ALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17509401 736 EAKSDD--DKKKCAEaimsKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14915 634 AIPEGQfiDSKKASE----KLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-775 |
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: 743.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGA-----EVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGavphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 250 FNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAELIIDGIDDVEEFQL 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV-KSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 330 TDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEW 408
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 409 VSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 488
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 489 NHHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKPKpp 568
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTD-- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 569 kgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDytTQEEAAAKAKEGGGGGKKKGKS 648
Cdd:cd14911 476 --FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ-DPFVVNIWKD--AEIVGMAQQALTDTQFGARTRK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 649 GSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 728
Cdd:cd14911 551 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17509401 729 YAILAAKE-AKSDDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14911 631 YELLTPNViPKGFMDGKKACEKMIQAL----ELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-775 |
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: 718.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE----LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14920 157 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-AGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQ 413
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 414 NCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMF 493
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 494 VLEQEEYAREGIQWVFIDFGLDLQACIELIEKPL---GIISMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPKPPKg 570
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLK- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 kqGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQ--DYTTQEEAAAKAKEGGGGGKKKGKS 648
Cdd:cd14920 473 --DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS-DRFVAELWKdvDRIVGLDQVTGMTETAFGSAYKTKK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 649 GSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 728
Cdd:cd14920 550 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17509401 729 YAILAAKE-AKSDDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14920 630 YEILTPNAiPKGFMDGKQACERMIRAL----ELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-775 |
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: 670.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAM-LIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEggaevdpnkkKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG----------ETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAE-LIIDGIDDVEEFQLTDEA 333
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAA-ASLPELKELHLGSAEDFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRpREEQAEPDGTDEA-EKASNMYGIGCEEFLKALTKPRVKVGTEWVSKG 412
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKAT-RNDSASISPDDEHlQIACELLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 413 QNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDY-FIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHH 491
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 492 MFVLEQEEYAREGIQWVFIDFgLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGK-HPNFEKPKPPKG 570
Cdd:cd01380 390 VFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 KqgeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGNdllveiwqdyttqeeaaakakegggggkkkgksgs 650
Cdd:cd01380 469 A-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR----------------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 651 FMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 730
Cdd:cd01380 509 KKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYR 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 17509401 731 ILAAKEAKSDDDKKKCAEAIMSKLVNDgslsEEMFRIGLTKVFFK 775
Cdd:cd01380 589 VLLPSKEWLRDDKKKTCENILENLILD----PDKYQFGKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-775 |
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: 662.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKdYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSK-YRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQ 413
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 414 NCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMF 493
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 494 VLEQEEYAREGIQWVFIDFGLDLQACIELIEKPL---GIISMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPKPPKg 570
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLK- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 kqGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYT-TQEEAAAKAKEGGGGGKKKGKSG 649
Cdd:cd14932 477 --DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQST-DKFVSELWKDVDrIVGLDKVAGMGESLHGAFKTRKG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 650 SFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 729
Cdd:cd14932 554 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17509401 730 AILAAKEAKSD--DDKKKCaeAIMSKLVndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14932 634 EILTPNAIPKGfmDGKQAC--VLMVKAL---ELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-775 |
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: 639.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQeggaevdpNKKKVT----LEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF 250
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHK--------GKKDTSitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 251 NKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLpIKDYWFVAQAELIIDGIDDVEEFQLT 330
Cdd:cd14921 153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEG-FNNYTFLSNGFVPIPAAQDDEMFQET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 331 DEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEWV 409
Cdd:cd14921 232 LEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 410 SKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 489
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 490 HHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPL---GIISMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPK 566
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 567 PPKGKqgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDY--TTQEEAAAKAKEGGGGGKK 644
Cdd:cd14921 470 QLKDK---TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASS-DKFVADLWKDVdrIVGLDQMAKMTESSLPSAS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 645 KGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPD 724
Cdd:cd14921 546 KTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 725 FVQRYAILAAKE-AKSDDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14921 626 FRQRYEILAANAiPKGFMDGKQACILMIKAL----ELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-775 |
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: 627.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEggaevdpNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKS-------KKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14919 154 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQ 413
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 414 NCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMF 493
Cdd:cd14919 312 TKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 494 VLEQEEYAREGIQWVFIDFGLDLQACIELIEKPL---GIISMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPKPPKG 570
Cdd:cd14919 392 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 KqgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDY--TTQEEAAAKAKEGGGGGKKKGKS 648
Cdd:cd14919 471 K---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS-DKFVSELWKDVdrIIGLDQVAGMSETALPGAFKTRK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 649 GSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 728
Cdd:cd14919 547 GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 17509401 729 YAILAAKEAKSDDDKKKCAEAIMSKLVndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14919 627 YEILTPNSIPKGFMDGKQACVLMIKAL---ELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-775 |
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: 624.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLpIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLEN-YNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQ 413
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNT-AAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 414 NCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMF 493
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 494 VLEQEEYAREGIQWVFIDFGLDLQACIELIEKPL---GIISMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPKPPKg 570
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPKKLK- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 kqGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAKAKEGGGGGKKKGKSGS 650
Cdd:cd15896 477 --DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQST-DKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 651 FMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 730
Cdd:cd15896 554 FRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 17509401 731 ILAAKEAKSD--DDKKKCAEAIMSKlvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd15896 634 ILTPNAIPKGfmDGKQACVLMIKSL-----ELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-775 |
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: 618.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAELIIDGiDDVEEFQLTDEAF 334
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTdEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQ 413
Cdd:cd14930 235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 414 NCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMF 493
Cdd:cd14930 314 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 494 VLEQEEYAREGIQWVFIDFGLDLQACIELIEKPL---GIISMLDEECIVPKATDLTLASKlVDQHLGKHPNFEKpkpPKG 570
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEK-VAQEQGGHPKFQR---PRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 KQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAKAKEGGGGGKKKGKSGS 650
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQST-DRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 651 FMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 730
Cdd:cd14930 549 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 17509401 731 ILAAKEAKSD--DDKKKCaeaimSKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14930 629 ILTPNAIPKGfmDGKQAC-----EKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-775 |
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: 604.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEggaevdpnkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHSW-------------VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSD-FRPELKKELLLDLPIKDYWFVAQAELI-IDGIDDVEEFQLTDEA 333
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQSGCIrIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE-PDGTDEAEKASNMYGIGCEEFLKALTKPRVKVgtewvsKG 412
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINV------RG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 413 QNCE---QVNWAV---GAMAKGLYSRVFNWLVKKCNLTLDqKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQ 486
Cdd:cd14883 303 NVTEiplKVQEARdnrDAMAKALYSRTFAWLVNHINSCTN-PGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 487 FFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIEK-PLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKP 565
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 566 KPPKGKQgeaHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWqDYTTQEEAAAKAKEGGGGGKKK 645
Cdd:cd14883 460 DRRRWKT---EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSK-NKFVKELF-TYPDLLALTGLSISLGGDTTSR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 646 GKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDF 725
Cdd:cd14883 535 GTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17509401 726 VQRYAILAAKEAKSDDDKKKCAEAIMSKLVNdgsLSEEMFRIGLTKVFFK 775
Cdd:cd14883 615 VDRYLCLDPRARSADHKETCGAVRALMGLGG---LPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-775 |
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: 600.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFmgKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGAsqqeGGAEVdpnkkkvtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG----GSSGI---------ENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAE-LIIDGIDDVEEFQLTDEAF 334
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSA-SEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQN 414
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 415 CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 495 LEQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVdQHLGKHPNFekpkppKGKQG 573
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLK-QHLKSNSCF------KGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 574 EAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGnDLLveiwqdyttQEEAAAKAKEGGGGGKKKGKSGS-FM 652
Cdd:cd01383 458 GA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSC-QLP---------QLFASKMLDASRKALPLTKASGSdSQ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 653 --TVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 730
Cdd:cd01383 527 kqSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYG 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 17509401 731 ILAAKEAKSDDDKKKCAEAIMSKLVndgsLSEEMFRIGLTKVFFK 775
Cdd:cd01383 607 FLLPEDVSASQDPLSTSVAILQQFN----ILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-775 |
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: 598.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGAsqqeggaevdpnkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG-------------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAELII-DGIDDVEEFQLTDEA 333
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDA-SDYYYLTQGNCLTcEGRDDAAEFADIRSA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPRE--EQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSK 411
Cdd:cd01381 227 MKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 412 GQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL---DQKGIDRdYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 488
Cdd:cd01381 307 PLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSR-TSIGVLDIFGFENFEVNSFEQLCINFANENLQQFF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 489 NHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELI-EKPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKPKp 567
Cdd:cd01381 386 VRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPK- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 568 pkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYttqeeaaakakegggGGKKKGK 647
Cdd:cd01381 463 ---SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSK-NKFLKQLFNED---------------ISMGSET 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 648 SGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQ 727
Cdd:cd01381 524 RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVE 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17509401 728 RYAIL--AAKEAKSDDDKKKCAEAIMSKLvndgsLSEEMFRIGLTKVFFK 775
Cdd:cd01381 604 RYRVLvpGIPPAHKTDCRAATRKICCAVL-----GGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-775 |
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: 572.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGASQQEGGAEVdpnkkkvtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSV---------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIySDFRPELKKELLLDLPIKDYWFVAQAELI-IDGIDDVEEFQLTDE 332
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQL-CAGAPPEDREKYKLKDPKQFHYLNQSKCFeLDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 333 AFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDgTDEAEK----ASNMYGIGCEEFLKALTKPRVKVGTEW 408
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPK-DEKSEFhlkaAAELLMCDEKALEDALCKRVIVTPDGI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 409 VSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQkGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 488
Cdd:cd01384 310 ITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQ-DPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 489 NHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVDQhLGKHPNFEKPKP 567
Cdd:cd01384 389 NQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 568 PKGKqgeahFAMRHYAGTVRYNCLNWLEKNKdplnDTVVS---AMKQSKGNDLLVEIWqdyttqeeaaakakeGGGGGKK 644
Cdd:cd01384 467 SRTD-----FTIDHYAGDVTYQTDLFLDKNK----DYVVAehqALLNASKCPFVAGLF---------------PPLPREG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 645 KGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPD 724
Cdd:cd01384 523 TSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEE 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 17509401 725 FVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGslseemFRIGLTKVFFK 775
Cdd:cd01384 603 FLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKG------YQIGKTKVFLR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-775 |
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: 568.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAEVDpnkkkvtleDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERVK---------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFD 335
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ILNFSAVEKQDCYRLMSAHMHMGNMKFKQrprEEQAEPDGTDEA--EKASNMYGIGCEEFLKALTKPRVKVGTEW---VS 410
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAISDTSvlDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 411 KGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNH 490
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 491 hmFVL--EQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECI-VPKATDLTLASKLvDQHLGKHPNFEKPK 566
Cdd:cd01378 390 --LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 567 PPKGkQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAKAkegggggkkkg 646
Cdd:cd01378 466 GHFE-LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSS-NPFLRSLFPEGVDLDSKKRPP----------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 647 ksgsfmTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFV 726
Cdd:cd01378 533 ------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFL 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 17509401 727 QRYAILA-----AKEAKSDDDkkkcAEAImsklVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd01378 607 ERYKLLSpktwpAWDGTWQGG----VESI----LKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-753 |
2.02e-164 |
|
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: 518.18 E-value: 2.02e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEggaevdpnkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPikdYWFVAQAELI-IDGIDDVEEFQLTDEA 333
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA---YGYLSLSGCIeVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKqrprEEQAEPDGT-------DEAEKASNMYGIGCEEFLKALTKPRVKVgt 406
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFA----SGGGKSLVSgstvanrDVLKEVATLLGVDAATLEEALTSRLMEI-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 407 ewvsKGQN-------CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINF 479
Cdd:cd14872 299 ----KGCDptripltPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 480 VNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELIEK-PLGIISMLDEECIVPKATDLTLASKLvDQHLGK 558
Cdd:cd14872 375 TNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 559 HPNFEkpkPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLND---TVVSAMKQSKGNDLLVEIWQDYTTqeeaaaka 635
Cdd:cd14872 453 KSTFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKdlyVLLSSSKNKLIAVLFPPSEGDQKT-------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 636 kegggggkkkgksgSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKG 715
Cdd:cd14872 522 --------------SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTG 587
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 17509401 716 FPNRTLHPDFVQRYAILAAKEAKSD--DDKKKCAEAIMSK 753
Cdd:cd14872 588 YPFRYSHERFLKRYRFLVKTIAKRVgpDDRQRCDLLLKSL 627
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-775 |
4.37e-162 |
|
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: 512.18 E-value: 4.37e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGASQQEggaevdpnkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG------------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPElkkellldlpikdywfVAQAELIIDGIDDVEEFQLTDEA 333
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPED----------------LREKLLKDPLLDDVGDFIRMDKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREE----QAEPDGTDEAEKASNMYGIGCEEFLKALTKpRVKVGTEWV 409
Cdd:cd01382 213 MKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 410 SKGQ------NCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKgiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEK 483
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE--TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 484 LQQFFNHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKlVDQHLGKHPNF 562
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSA-VHQKHKNHFRL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 563 EKPKPPKGKqgeAH--------FAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTqeeaaak 634
Cdd:cd01382 448 SIPRKSKLK---IHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESK-DKFIRSLFESSTN------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 635 akeGGGGGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRK 714
Cdd:cd01382 517 ---NNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509401 715 GFPNRTLHPDFVQRYA-ILAAKEAKSddDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd01382 594 GFPSRTSFHDLYNMYKkYLPPKLARL--DPRLFCKALFKAL----GLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-773 |
2.51e-161 |
|
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: 510.10 E-value: 2.51e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFM--GKRK----TEMPPHLFAVSDEAYRNMLQDHE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYehGERRaageRKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 167 --NQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 244
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERE----NVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 245 FIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPeLKKELLLDLPIKDYWFVAQAELII--DGID 322
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASS-DELHALGLTHVEEYKYLNSSQCYDrrDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 323 DVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREeqaepDGTDEAEKASNM------YGIGCEEFLKA 396
Cdd:cd14901 236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGE-----GGTFSMSSLANVraacdlLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 397 LTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKG-IDRDYFIGVLDIAGFEIFDFNSFEQL 475
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEsTGASRFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 476 WINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVDQ 554
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 555 hLGKHPNFEKPKPpkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEiwqdyttqeeaaak 634
Cdd:cd14901 470 -LAKHASFSVSKL---QQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSS-NAFLSS-------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 635 akegggggkkkgksgsfmTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRK 714
Cdd:cd14901 531 ------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 715 GFPNRTLHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGSLSEEM--FRIGLTKVF 773
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLppFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-775 |
4.19e-159 |
|
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: 504.31 E-value: 4.19e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDH----ENQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 170 MLITGESGAGKTENTKKVICYFAAVGASQQEGGAEV-----DPNKKKVT-LEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEgeaasEAIEQTLGsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 244 KFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIkDYWFVAQAELIIDGIDD 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPV-EYFYLRGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 324 VEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEA-EKASNMYGIGCEEFLKALTKPRV 402
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 403 KVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNE 482
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPD-DKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 483 KLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-----KPlGIISMLDeECIVPKAT--DLTLASKLVDQH 555
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 556 ------------LGKHPNFEKPKPPKGKQgeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGNdlLVEIwq 623
Cdd:cd14890 476 grksgsggtrrgSSQHPHFVHPKFDADKQ----FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRS--IREV-- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 624 dyttqeeaaakakegggggkkkgksgsfmTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCN 703
Cdd:cd14890 548 -----------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYS 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509401 704 GVLEGIRICRKGFPNRTLHPDFVQRYAILaakeaKSDDDKKKCAEAIMSKLVNdgsLSEEMFRIGLTKVFFK 775
Cdd:cd14890 599 GMMEAIQIRQQGFALREEHDSFFYDFQVL-----LPTAENIEQLVAVLSKMLG---LGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-775 |
7.70e-157 |
|
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: 498.13 E-value: 7.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEM---PPHLFAVSDEAYRNMLQD----HEN 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVgkgqGTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 168 QSMLITGESGAGKTENTKKVICYFAAvgASQQEGGAEVDPNKKKV--TLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKF 245
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAT--ASKLAKGASTSKGAANAheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 246 IRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAELI-IDGIDDV 324
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAG-LDANENAALELTPAESFLFLNQGNCVeVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 325 EEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQR--PREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKpRV 402
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVT-QT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 403 KVGTewvsKGQ------NCEQVNWAVGAMAKGLYSRVFNWLVKKCN------LTLDQKGIDRDY---FIGVLDIAGFEIF 467
Cdd:cd14892 317 TSTA----RGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkqqTSGVTGGAASPTfspFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 468 DFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIEK-PLGIISMLDEECIVP-KATDL 545
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 546 TLASKLVDQHLGKHPNFEKPKppkgKQGEaHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGndllveiwqdy 625
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPR----FECD-EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 626 ttqeeaaakakegggggkkkgksgsfmtvsmlYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGV 705
Cdd:cd14892 536 --------------------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 706 LEGIRICRKGFPNRTLHPDFVQRYAILA---AKEAKSDDDKKKCAEAIMSKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14892 584 LEVVRIRREGFPIRRQFEEFYEKFWPLArnkAGVAASPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-775 |
2.51e-156 |
|
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: 496.91 E-value: 2.51e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEmPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISK-SPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGASQQeggaevdpnKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNK- 252
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDI---------KKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 253 --------HGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELI------- 317
Cdd:cd14888 151 kskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPIsidmssf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 318 ----------------IDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFK-QRPREEQA--EPDGTDE 378
Cdd:cd14888 231 ephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAvvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 379 AEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGV 458
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 459 LDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELI-EKPLGIISMLDEEC 537
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 538 IVPKATDLTLASKLVDQHLGkHPNFekpKPPKGKQgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDL 617
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKG-HKRF---DVVKTDP--NSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK-NPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 618 LVEIWQDYTTQEEAAAKAKEGggggkkkgksgsFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVL 697
Cdd:cd14888 543 ISNLFSAYLRRGTDGNTKKKK------------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVN 610
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 698 NQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEaksdddkkkcaeaimsklvndGSLSEEMFRIGLTKVFFK 775
Cdd:cd14888 611 EQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGE---------------------GKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-775 |
3.65e-156 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 497.28 E-value: 3.65e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVgaSQQEGGAEVdpnkkkvtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL--SQKGYGSGV---------EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAE-LIIDGIDDVEEFQLTDEA 333
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNQSDcYTLEGEDEKYEFERLKQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRP--REEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSK 411
Cdd:cd01385 229 MEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLIL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 412 GQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL---DQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 488
Cdd:cd01385 309 PYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 489 NHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKPkp 567
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH-KDNKYYEKP-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 568 pkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEI-------------------------- 621
Cdd:cd01385 465 ---QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSS-SAFVRELigidpvavfrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 622 ----WQDYTTQEEAAAKAKEGGGGGKKKGKSGSfMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVL 697
Cdd:cd01385 541 agrrRAQRTAGHSLTLHDRTTKSLLHLHKKKKP-PSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 698 NQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEAKSD-DDKKKCAEAImsklvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSkEDIKDFLEKL--------NLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-775 |
4.37e-156 |
|
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: 495.85 E-value: 4.37e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVgaSQQEGGAEVDPNKKKVtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVI--SQQSLELSLKEKTSCV--EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAELIID-GIDDVEEFQLTDE 332
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTP-ENYHYLNQSGCVEDkTISDQESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 333 AFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQrprEEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKG 412
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 413 QNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLdqKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHM 492
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 493 FVLEQEEYAREGIQWVFIDFgLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKPkppkgKQ 572
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKP-----RV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 573 GEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAKAKEGGGGGKkkgksgsfm 652
Cdd:cd14873 464 AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESR-FDFIYDLFEHVSSRNNQDTLKCGSKHRRP--------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 653 TVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAIL 732
Cdd:cd14873 534 TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVL 613
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17509401 733 AAKEAKSDDDKKKCAeAIMSKLvnDGSLSEemFRIGLTKVFFK 775
Cdd:cd14873 614 MRNLALPEDVRGKCT-SLLQLY--DASNSE--WQLGKTKVFLR 651
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-775 |
9.93e-155 |
|
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: 492.37 E-value: 9.93e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGasqqeGGAEVDPNKKkvtledqIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----GGLNDSTIKK-------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDlpiKDYWFVAQAELI-IDGIDDVEEFQLTDE 332
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA---NECAYTGANKTIkIEGMSDRKHFARTKE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 333 AFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAE--PDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVS 410
Cdd:cd14903 226 ALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 411 KGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYfIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNH 490
Cdd:cd14903 306 VPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANH-IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 491 HMFVLEQEEYAREGIQWVFIDFgLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKg 570
Cdd:cd14903 385 DVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 kqgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWqDYTTQEEAAAKAKEGGGGGKKKGKSGS 650
Cdd:cd14903 463 ----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSS-KPFLRMLF-KEKVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 651 FMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 730
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 17509401 731 I-LAAKEAKSDDDKKKCaEAIMSKLVNDgslSEEMFRIGLTKVFFK 775
Cdd:cd14903 617 LfLPEGRNTDVPVAERC-EALMKKLKLE---SPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-775 |
8.40e-154 |
|
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: 488.71 E-value: 8.40e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASqqeggaevdPNKkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA---------NNR---TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKD-YWFVAQAELIIDGIDD---VEEFQLTD 331
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPpRYLQNDGLTVQDIVNNsgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 332 EAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQ----AEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTE 407
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 408 WVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL--DQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQ 485
Cdd:cd01379 310 TIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 486 QFFNHHMFVLEQEEYAREGIQWVFIDFG-----LDLqacieLIEKPLGIISMLDEECIVPKATDLTLASKLvdQHLGKHP 560
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 561 NFEKPkppkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVeiwqdyttqeeaaakakeggg 640
Cdd:cd01379 463 YYWRP-----KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSE-NPLVR--------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 641 ggkkkgksgsfMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRT 720
Cdd:cd01379 516 -----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 721 LHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGslseemFRIGLTKVFFK 775
Cdd:cd01379 585 LFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDN------WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-775 |
4.53e-152 |
|
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: 485.03 E-value: 4.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVgasQQEGGAEVdpnkkkvtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFnKHG 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV---NQRRNNLV---------TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd01387 148 VIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPRE---EQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSK 411
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 412 GQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNlTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHH 491
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 492 MFVLEQEEYAREGIQWVFIDFgLDLQACIELI-EKPLGIISMLDEECIVPKATDLTLASKLVDQHlGKHPNFEKPkppkg 570
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKP----- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 KQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeaaakakegGGGGKKKGKSGS 650
Cdd:cd01387 460 RMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSR-TRVVAHLFSSHRAQ----------TDKAPPRLGKGR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 651 FMTvsMLYR---------ESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTL 721
Cdd:cd01387 529 FVT--MKPRtptvaarfqDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLP 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 722 HPDFVQRY-AILAAKEAKSDDDKKKCaeAIMSKLvnDGSLSEEMFRIGLTKVFFK 775
Cdd:cd01387 607 FQVFIDRYrCLVALKLPRPAPGDMCV--SLLSRL--CTVTPKDMYRLGATKVFLR 657
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1932 |
4.27e-141 |
|
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: 468.50 E-value: 4.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 853 KEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELN 932
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 933 DQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEIN 1012
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1013 RKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKK 1092
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1093 ESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEV 1172
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1173 NKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKL 1252
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1253 NNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEA 1332
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1333 RERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEgLLKADELEDAKRRQAQKINELQEA 1412
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED-AGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1413 LDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFK 1492
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1493 AKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQV 1572
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1573 EVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNL 1652
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1653 KRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSL 1732
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1733 TSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAA 1812
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1813 ALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVE 1892
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 17509401 1893 EAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSK 1932
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-775 |
1.59e-140 |
|
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: 452.22 E-value: 1.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKR-KTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGASQQEggaevdpnkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS------------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPikDYWFVAQAELIIDGI-DDVEEF----Q 328
Cdd:cd14897 149 GQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDP--DCHRILRDDNRNRPVfNDSEELeyyrQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 329 LTDEAFDIL---NFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVG 405
Cdd:cd14897 227 MFHDLTNIMkliGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 406 TEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL----DQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVN 481
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 482 EKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELI-EKPLGIISMLDEECIVPKATDLTLASKLVDqHLGKHP 560
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 561 NFekpKPPKGkqGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYttqeeaaakakeggg 640
Cdd:cd14897 465 RY---VASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSN-NEFISDLFTSY--------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 641 ggkkkgksgsfmtvsmlYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRT 720
Cdd:cd14897 524 -----------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRI 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 721 LHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGslseemFRIGLTKVFFK 775
Cdd:cd14897 587 KYEDFVKRYKEICDFSNKVRSDDLGKCQKILKTAGIKG------YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-738 |
1.02e-138 |
|
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: 446.68 E-value: 1.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP------------IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNM-- 161
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmakylLSFEARSSSTRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 162 --LQDHENQSMLITGESGAGKTENTKKVICYFAAVGASQQEggAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNS 239
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLA--ASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 240 SRFGKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLldlpikdywfvaqaeliid 319
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDM------------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 320 giddveeFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEA-------EKASNMYGIGCEE 392
Cdd:cd14900 221 -------YRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 393 FLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDY----FIGVLDIAGFEIFD 468
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHgglhFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 469 FNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELI-EKPLGIISMLDEECIVPKATDLTL 547
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 548 ASKLVdQHLGKHPNFEKPKPPKGKqgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsamkqskgnDLLVEIWQdytt 627
Cdd:cd14900 453 ASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV---------DLFVYGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 628 qeeaaakakegggggkkkgksgsfmtvsmlYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLE 707
Cdd:cd14900 516 ------------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660 670
....*....|....*....|....*....|.
gi 17509401 708 GIRICRKGFPNRTLHPDFVQRYAILAAKEAK 738
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-732 |
1.71e-133 |
|
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: 433.69 E-value: 1.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRK--------TEMPPHLFAVSDEAYRNMLQDH 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIqngeyfdiKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 166 ENQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDP-------NKKKVTLEDQIVQTNPVLEAFGNAKTVRNNN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLtssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 239 SSRFGKFIRIHFNKH-GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKD--YWFVAQAE 315
Cdd:cd14907 161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGdrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 316 LI-IDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQR--PREEQAEPDGTDEAEKASNMYGIGCEE 392
Cdd:cd14907 241 CYeVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 393 FLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYF-------IGVLDIAGFE 465
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQLfqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 466 IFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVF--IDFgLDLQACIELIEK-PLGIISMLDEECIVPKA 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 543 TDLTLASKLVDQhlgkHPNFEKPKPPKGKQGEAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIW 622
Cdd:cd14907 480 TDEKLLNKIKKQ----HKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSK-NRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 623 QDYTTQeeaaakakEGGGGGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTC 702
Cdd:cd14907 554 SGEDGS--------QQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|
gi 17509401 703 NGVLEGIRICRKGFPNRTLHPDFVQRYAIL 732
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-775 |
3.70e-129 |
|
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: 420.60 E-value: 3.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNL--RSRYAAMLIYTYSGLFCVVINPYKRLPiytDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHE---NQS 169
Cdd:cd14891 1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 170 MLITGESGAGKTENTKKVICYF---AAVGASQQEGGAEVDPNKKK---VTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLttrAVGGKKASGQDIEQSSKKRKlsvTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 244 KFIRIHF-NKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGID 322
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 323 DVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREE----QAEPDGTDEAEKASNMYGIGCEEFLKALT 398
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 399 KPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDqKGIDRDYFIGVLDIAGFEIFD-FNSFEQLWI 477
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG-HDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 478 NFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELI-EKPLGIISMLDEECIVPKATDLTLASKLVDQHl 556
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 557 GKHPNFEKPKPpkgKQGEAHFAMRHYAGTVRYNCLNWLEKNkdplNDTVVSAMkqskgndllveiwqdyttqeeaaakak 636
Cdd:cd14891 475 KRHPCFPRPHP---KDMREMFIVKHYAGTVSYTIGSFIDKN----NDIIPEDF--------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 637 egggggkkkgksGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGF 716
Cdd:cd14891 521 ------------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGL 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 717 PNRTLHPDFVQRYAILAAKEAKS--DDDKKKCAEAIMSKLvndgSLSEEMFRIGLTKVFFK 775
Cdd:cd14891 589 PTRVTYAELVDVYKPVLPPSVTRlfAENDRTLTQAILWAF----RVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-775 |
1.07e-127 |
|
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: 418.59 E-value: 1.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQ-------DHENQ 168
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLRRrlhepgaSKKNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 169 SMLITGESGAGKTENTKKVICYFAAvgaSQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 248
Cdd:cd14895 82 TILVSGESGAGKTETTKFIMNYLAE---SSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 249 HFNKHG-----RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYS--DFRPELKKELLLDLPiKDYWFVAQAELII--D 319
Cdd:cd14895 159 FFEGHEldtslRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAgaADDMKLELQLELLSA-QEFQYISGGQCYQrnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 320 GIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGT------------------DEAEK 381
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvqQHLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 382 ASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQK----------GID 451
Cdd:cd14895 318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRqfalnpnkaaNKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 452 RDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGLDlQACIELIE-KPLGII 530
Cdd:cd14895 398 TTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 531 SMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPKPpkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMK 610
Cdd:cd14895 477 SLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASRT---DQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 611 QSKgNDLLVEIWQDYttQEEAAAKAKEGGGGGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGM 690
Cdd:cd14895 553 KTS-DAHLRELFEFF--KASESAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQ 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 691 IDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEAKSDDDkkkcAEAIMSKLVNDGSlseemfRIGLT 770
Cdd:cd14895 630 FDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDAT----ASALIETLKVDHA------ELGKT 699
|
....*
gi 17509401 771 KVFFK 775
Cdd:cd14895 700 RVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-775 |
1.45e-124 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 407.63 E-value: 1.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQeggaevdpnkkkvtlEDQIVQTN---PVLEAFGNAKTVRNNNSSRFGKFIRIHFn 251
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQT---------------EDRLRQPEdvlPILESFGHAKTILNANASRFGQVLRLHL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 252 KHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAELI-IDGIDDVEEFQLT 330
Cdd:cd14896 145 QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGP-ETYYYLNQGGACrLQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 331 DEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPRE--EQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEW 408
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 409 VSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKG-IDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 487
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGeAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 488 FNHHMFVLEQEEYAREGIQWVFIDfGLDLQACIELI-EKPLGIISMLDEECIVPKATDLTLASKlVDQHLGKHPNFEKPK 566
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQK-CHYHHGDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 567 PPKgkqgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAKAKegggggkkkg 646
Cdd:cd14896 462 LPL-----PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQ-LQLVGSLFQEAEPQYGLGQGKP---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 647 ksgsfmTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFV 726
Cdd:cd14896 526 ------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFL 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17509401 727 QRYAILAAKEAKSDDDKKKCAeAIMSKLVNDgslSEEMFRIGLTKVFFK 775
Cdd:cd14896 600 ARFGALGSERQEALSDRERCG-AILSQVLGA---ESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-775 |
1.68e-124 |
|
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: 408.91 E-value: 1.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYT---------DSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGkeilesyrqEGLLRSQGIESPQALGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 165 HENQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKkVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 244
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGK-LSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 245 FIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQI--------YSDFRPELKKELLLDLPiKDYWFVAQAEL 316
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLlrggdeeeHEKYEFHDGITGGLQLP-NEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 317 I-IDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAE---KASNMYGIGCEE 392
Cdd:cd14908 239 PdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 393 FLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLdqkGIDRDYFI----GVLDIAGFEIFD 468
Cdd:cd14908 319 LLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSI---NWENDKDIrssvGVLDIFGFECFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 469 FNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVP-KATDLT 546
Cdd:cd14908 396 HNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 547 LASKLVDQHLGK----HPNFEKPKPPKGKQGEAHFAMRHYAGTVRYNC-LNWLEKNKDPLNDTvvsamkqskgndllvei 621
Cdd:cd14908 475 YASRLYETYLPEknqtHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLT----------------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 622 wqdyttqeeaaakakegggggkkkgkSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLT 701
Cdd:cd14908 538 --------------------------ADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLR 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 702 CNGVLEGIRICRKGFPNRTLHPDFVQRYAIL---AAKEAKS-----DDDKKKCAEAI---------MSKLVNDGSLSEEM 764
Cdd:cd14908 592 YGGVLEAVRVARSGYPVRLPHKDFFKRYRMLlplIPEVVLSwsmerLDPQKLCVKKMckdlvkgvlSPAMVSMKNIPEDT 671
|
730
....*....|.
gi 17509401 765 FRIGLTKVFFK 775
Cdd:cd14908 672 MQLGKSKVFMR 682
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-775 |
2.41e-124 |
|
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: 407.76 E-value: 2.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 97 VLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNML----QDHENQSMLI 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 173 TGESGAGKTENTKKVICYFAAV--GASQqeggaevdpnkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF 250
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELcrGNSQ---------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 251 nKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAeliiDGIDDVEEFQLT 330
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKREVQYWKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 331 -DE---AFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREE-QAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVG 405
Cdd:cd14889 223 yDEvcnAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 406 TEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL---DQKGIDRDYfIGVLDIAGFEIFDFNSFEQLWINFVNE 482
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLapkDDSSVELRE-IGILDIFGFENFAVNRFEQACINLANE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 483 KLQQFFNHHMFVLEQEEYAREGIQWVFIDFgLDLQACIEL-IEKPLGIISMLDEECIVPKATDLTLASKLvDQHLGKHPN 561
Cdd:cd14889 382 QLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 562 FEKP--KPPKgkqgeahFAMRHYAGTVRYNCLNWLEKNKdplnDTVVSAMKQSKGNDLLVEIWQDYTTQEEAAAKAKEGG 639
Cdd:cd14889 460 YGKSrsKSPK-------FTVNHYAGKVTYNASGFLEKNR----DTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 640 GGGKKKGKSGSF---MTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGF 716
Cdd:cd14889 529 KLPQAGSDNFNStrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGF 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 717 PNRTLHPDFVQRYAILAAKEAKSdDDKKKCAEAIMSKLVNDgslseemFRIGLTKVFFK 775
Cdd:cd14889 609 SWRPSFAEFAERYKILLCEPALP-GTKQSCLRILKATKLVG-------WKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-775 |
1.40e-120 |
|
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: 396.62 E-value: 1.40e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGasqqeGGaevdpnKKKVTLeDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA-----GG------RKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFrPELKKELLLDLPIKDYWFVAQ--AELIIDGIDDVEEFQLTD 331
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGL-SSEERKEFGLDPNCQYQYLGDslAQMQIPGLDDAKLFASTQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 332 EAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGtDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSK 411
Cdd:cd14904 228 KSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 412 GQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLdqkGIDRDYF---IGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 488
Cdd:cd14904 307 PLAPVEAEENRDALAKAIYSKLFDWMVVKINAAI---STDDDRIkgqIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 489 NHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQH--LGKHPNFEKPK 566
Cdd:cd14904 384 TTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 567 PPKgkqgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDyttqeeaaAKAKEGGGGGKKKG 646
Cdd:cd14904 463 VKR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSS-LDLLTELFGS--------SEAPSETKEGKSGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 647 KSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFV 726
Cdd:cd14904 529 GTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17509401 727 QRYAILAAKEAKSDDDKKKCAeAIMSKLvndGSLSEEMFRIGLTKVFFK 775
Cdd:cd14904 609 TRYAIMFPPSMHSKDVRRTCS-VFMTAI---GRKSPLEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
85-828 |
1.05e-119 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 399.79 E-value: 1.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 85 DMSNLSFLNDASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRK-TEMPPHLFAVSDEAYRNMLQ 163
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDsDKLPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 164 DHENQSMLITGESGAGKTENTKKVICYFAAvGASQQEGGaevdpnkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGNMDL----------KIQNAIMAANPVLEAFGNAKTIRNNNSSRFG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 244 KFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPeLKKELLLDLPIKDYWFVAQAELIIDGIDD 323
Cdd:PTZ00014 249 RFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGAND-EMKEKYKLKSLEEYKYINPKCLDVPGIDD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 324 VEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKqrPREEQAEPDG---TDEAE----KASNMYGIGCEEFLKA 396
Cdd:PTZ00014 328 VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDAaaiSDESLevfnEACELLFLDYESLKKE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 397 LTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLW 476
Cdd:PTZ00014 406 LTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPG-GFKVFIGMLDIFGFEVFKNNSLEQLF 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 477 INFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQhL 556
Cdd:PTZ00014 485 INITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-L 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 557 GKHPNFEKPKppkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAakak 636
Cdd:PTZ00014 564 KNNPKYKPAK----VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASP-NPLVRDLFEGVEVEKGKL---- 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 637 egggggkkkgksGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGF 716
Cdd:PTZ00014 635 ------------AKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGF 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 717 PNRTLHPDFVQRYAI--LAAKEAKSDDDKKKCaeaimSKLVNDGSLSEEMFRIGLTKVFFKAGVLAHLEDIRDEKLATil 794
Cdd:PTZ00014 703 SYRRTFAEFLSQFKYldLAVSNDSSLDPKEKA-----EKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAA-- 775
|
730 740 750
....*....|....*....|....*....|....*...
gi 17509401 795 tgFQSQIR----WHLGLKDRKRRMEQRAGLLIVQRNVR 828
Cdd:PTZ00014 776 --WEPLVSvleaLILKIKKKRKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-755 |
1.42e-118 |
|
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: 393.10 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMF--------MGKRKTEMPPHLFAVSDEAYRNMLQDH 165
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 166 E-NQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDpnkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 244
Cdd:cd14902 81 RrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGS---DAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 245 FIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYS----DFRPELKKELLLDLPIKDYWFVAQAELIIDG 320
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEgadkTLLDLLGLQKGGKYELLNSYGPSFARKRAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 321 IDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEA---EKASNMYGIGCEEFLKAL 397
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 398 TKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLD------QKGIDRDYF--IGVLDIAGFEIFDF 469
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavSISDEDEELatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 470 NSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVPKATDLTLA 548
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 549 SKLVDQHLgkhpnfekpkppkgkqGEAHFAMRHYAGTVRYNCLNWLEKNKD--PLNdtvVSAMKQSKGNDLLVEIWQDYT 626
Cdd:cd14902 477 TKFYRYHG----------------GLGQFVVHHFAGRVCYNVEQFVEKNTDalPAD---ASDILSSSSNEVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 627 TQEEAAAKAKEGGGGGKKKGKSgsfmTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVL 706
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRAP----SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17509401 707 EGIRICRKGFPNRTLHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLV 755
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFSGFKCFLSTRDRAAKMNNHDLAQALV 662
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-775 |
1.85e-114 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 378.95 E-value: 1.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRK-TEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDlTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAVGASQQEGgaevdpnkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKH 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDL-----------RIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEA 333
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKG-ADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKqrPREEQAEPD-----GTDEA--EKASNMYGIGCEEFLKALTKPRVKVGT 406
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKIT--GKTEQGVDDaaaisNESLEvfKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 407 EWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQ 486
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPG-GFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 487 FFNHHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQhLGKHpnfEKPK 566
Cdd:cd14876 386 NFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSN---GKFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 567 PPKGKQgEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeaaakakegggggkkKG 646
Cdd:cd14876 462 PAKVDS-NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQAST-NPVVKALFEGVVVE----------------KG 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 647 KSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFV 726
Cdd:cd14876 524 KIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFL 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 17509401 727 QRYAI--LAAKEAKSDDDKKKCaeaimSKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14876 604 YQFKFldLGIANDKSLDPKVAA-----LKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-773 |
3.92e-113 |
|
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: 375.34 E-value: 3.92e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGK-RKTEMPPHLFAVSDEAYRNM--LQDHENQSM 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVksLIEPVNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 171 LITGESGAGKTENTKKVICYFAAVGASQqeggAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF 250
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP----TSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 251 NKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfrPELKKELLLDLPIK-DYWFVAQAEliidgiDDVEE--F 327
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKG--ASADERLQWHLPEGaAFSWLPNPE------RNLEEdcF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 328 QLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQA---EPDGTDEAEKASNMYGIGCEEFLKALTKPRVKV 404
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 405 GTEWVSKGQNCEQV--NWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNE 482
Cdd:cd14880 309 GKQQQVFKKPCSRAecDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 483 KLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPN 561
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 562 FEKPKPPKgkqgEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSkgndllveiwQDYTTQEEAAAKAKEGGGG 641
Cdd:cd14880 468 LGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQS----------QDPLLQKLFPANPEEKTQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 642 GKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTL 721
Cdd:cd14880 534 EPSGQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVS 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 722 HPDFVQRYAILAAKEAKSDDDKKKCAEAimsklvndGSLSEEMFrIGLTKVF 773
Cdd:cd14880 614 HQNFVERYKLLRRLRPHTSSGPHSPYPA--------KGLSEPVH-CGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-775 |
4.00e-104 |
|
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: 349.19 E-value: 4.00e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKR-----KTEMPPHLFAVSDEAYRNMLQDHENQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADtsrgfPSDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 169 SMLITGESGAGKTENTKKVICYFAaVGASQqeggaevdpNKKKVtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFA-YGHST---------SSTDV--QSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 249 HFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLpIKDYWFVAQAELI-IDGIDDVEEF 327
Cdd:cd14886 149 LVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKS-LESYNFLNASKCYdAPGIDDQKEF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 328 QLTDEAFDILnFSAVEKQDCYRLMSAHMHMGNMKFKQRPR---EEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKV 404
Cdd:cd14886 228 APVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 405 GTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYfIGVLDIAGFEIFDFNSFEQLWINFVNEKL 484
Cdd:cd14886 307 NNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW-IGILDIYGFEFFERNTYEQLLINYANERL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 485 QQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIEKP-LGIISMLDEECIVPkatdlTLASKLVDQHLGKHPNFE 563
Cdd:cd14886 386 QQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQ-----TGSSEKFTSSCKSKIKNN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 564 KPKPPKGKQgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAkakegggggk 643
Cdd:cd14886 460 SFIPGKGSQ--CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGST-NPIVNKAFSDIPNEDGNMK---------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 644 kkgksGSFmtVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHP 723
Cdd:cd14886 527 -----GKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 724 DFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGSLSEEmFRIGLTKVFFK 775
Cdd:cd14886 600 EFFHRNKILISHNSSSQNAGEDLVEAVKSILENLGIPCSD-YRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-773 |
1.10e-100 |
|
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: 341.19 E-value: 1.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRK-TEMPPHLFAVSDEAYRNMLQDHENQSMLI 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 173 TGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVtlEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF-N 251
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSI--EKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 252 KHGRLASCDIEHYLLEKSRVI-RQAPGERCYHIFYQ-IYSDFRPELKKELLLDLPIKDYWFVAQAELI------------ 317
Cdd:cd14906 159 SDGKIDGASIETYLLEKSRIShRPDNINLSYHIFYYlVYGASKDERSKWGLNNDPSKYRYLDARDDVIssfksqssnkns 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 318 --IDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQ---RPREEQAEPDGTDEAEKASNMYGIGCEE 392
Cdd:cd14906 239 nhNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdsdFSKYAYQKDKVTASLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 393 FLKALTKPRVKVGTEW--VSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRD----------YFIGVLD 460
Cdd:cd14906 319 FKQALLNRNLKAGGRGsvYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDlaggsnkknnLFIGVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 461 IAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELIE-KPLGIISMLDEECIV 539
Cdd:cd14906 399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 540 PKATDLTLASKLVDQHlgkhpnFEKPKPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLV 619
Cdd:cd14906 478 PKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASS-NFLKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 620 EIWQDYTTqeeaaakakegGGGGKKKGKSGSfMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQ 699
Cdd:cd14906 551 SLFQQQIT-----------STTNTTKKQTQS-NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQ 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 700 LTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEAKSDDDKKKCA-----EAIMSKLVNDGSL-------------- 760
Cdd:cd14906 619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLAsqlilQNIQSKLKTMGISnnkkknnsnsnsnt 698
|
730
....*....|....*
gi 17509401 761 --SEEMFRIGLTKVF 773
Cdd:cd14906 699 tnDKPLFQIGKTKIF 713
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-729 |
2.61e-100 |
|
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: 340.53 E-value: 2.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCAR--------MFMGKRKTEMP--PHLFAVSDEAYRNMLQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRgyaydhnsQFGDRVTSTDPrePHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 164 DHENQSMLITGESGAGKTENTKKVICYFAAVGA-----SQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 239 SSRFGKFIRIHFNKHGR-LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPI----KDYWFVAQ 313
Cdd:cd14899 161 SSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKQVLALsggpQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 314 A--ELIIDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRP--REEQAEPDGT----------DEA 379
Cdd:cd14899 241 SlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEArvmssttgafDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 380 EKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGI--------- 450
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 451 -----DRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE- 524
Cdd:cd14899 401 vddeeDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 525 KPLGIISMLDEECIVPKATDLTLASK--LVDQHLGKHPNFekpKPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLN 602
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKyyLEFEKKNSHPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 603 DTVVSAMKQSKgNDLLVEIWQDYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVSM--LYRESLNNLMTMLNKTHPHFIRCI 680
Cdd:cd14899 557 ESAAQLLAGSS-NPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVgtQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17509401 681 IPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 729
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-775 |
8.45e-98 |
|
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: 331.39 E-value: 8.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAM-LIYTYSGLFCVVINPYKRLPIYTD-SCARMFMGKRKTEMPPHLFAVSDEAYRNM-LQDHENQSML 171
Cdd:cd14875 1 ATLLHCIKERFEKLhQQYSLMGEMVLSVNPFRLMPFNSEeERKKYLALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 172 ITGESGAGKTENTKKVICYFAAVG------ASQQEGGAEVDPNKKkvtledqivQTNPVLEAFGNAKTVRNNNSSRFGKF 245
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSymhssnTSQRSIADKIDENLK---------WSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 246 IRIHFNK-HGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDY-------WFVAQAeli 317
Cdd:cd14875 152 IKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 318 IDG--IDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFkqrpreeqaEPDGTDEAEKAS-NMYGIGCEEFL 394
Cdd:cd14875 229 VDGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF---------ESDQNDKAQIADeTPFLTACRLLQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 395 KALTKPR----VKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKG-IDRDYFIGVLDIAGFEIFDF 469
Cdd:cd14875 300 LDPAKLRecflVKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdCSGCKYIGLLDIFGFENFTR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 470 NSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGlDLQACIELIE-KPLGIISMLDEECIVPKATDLTLA 548
Cdd:cd14875 380 NSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFT 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 549 SKLVDQHLGKHPNFEKPKPPKGKQgeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgndllVEIWQDYTTQ 628
Cdd:cd14875 459 TNLWDQWANKSPYFVLPKSTIPNQ----FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNST-----DEFIRTLLST 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 629 EEAAAKAKEgggggkkkgksgsfmTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEG 708
Cdd:cd14875 530 EKGLARRKQ---------------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQT 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 709 IRICRKGFPNRTLHPDFVqRYAILAAKEAKSDDDKKKCAEAIMSKLVNDG----SLSEEMFRIGLTKVFFK 775
Cdd:cd14875 595 IALKRQGYPVRRPIEQFC-RYFYLIMPRSTASLFKQEKYSEAAKDFLAYYqrlyGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-775 |
7.25e-87 |
|
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: 299.04 E-value: 7.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFM---GKRKTEMPPHLFAVSDEAYRNMLQDHENQSML 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 172 ITGESGAGKTENTKKVICYFAAVGASqqeggaevdpnkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF- 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFc 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 251 NKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYqIYSDFRPELKKELLLDLPIKDYWFVAQAELiidgiDDV------ 324
Cdd:cd14878 149 ERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFY-LLMDGLSAEEKYGLHLNNLCAHRYLNQTMR-----EDVstaers 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 325 ---EEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPR 401
Cdd:cd14878 223 lnrEKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 402 VKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL---DQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWIN 478
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 479 FVNEKLQQFFNHHMFVLEQEEYAREGI----------QWVFIDFgldlqacieLIEKPLGIISMLDEECIVPKATDLTLA 548
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGVtmetayspgnQTGVLDF---------FFQKPSGFLSLLDEESQMIWSVEPNLP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 549 SKLVDQHLGKHPN--FEKPK------PPKGkQGEAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVE 620
Cdd:cd14878 454 KKLQSLLESSNTNavYSPMKdgngnvALKD-QGTA-FTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSE-NVVINH 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 621 IWQdyttqeeaaakakegggggkkkgksGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQL 700
Cdd:cd14878 531 LFQ-------------------------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQL 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 701 TCNGVLEGIRICRKGFPNRTLHPDFVQRYAILA---AKEAKSDDDKKKCAEAIMS-KLvndgslseEMFRIGLTKVFFK 775
Cdd:cd14878 586 QYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtlLGEKKKQSAEERCRLVLQQcKL--------QGWQMGVRKVFLK 656
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-775 |
8.46e-87 |
|
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: 300.00 E-value: 8.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQqeggaevdpnKKKVTLEdQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSV----------GGVLSVE-KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIY----SDFRPELKKELLLDLPIKDYWFVAQAEliiDGIDDVEEFQLT 330
Cdd:cd01386 150 QLASASIQTLLLERSRVARRPEGESNFNVFYYLLagadAALRTELHLNQLAESNSFGIVPLQKPE---DKQKAAAAFSKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 331 DEAFDILNFSAVEKQDCYRLMSAHMHMGN---MKFKQRPREEQAEPDGtdeAEKASNMYGIGCEEFLKALTKPRVKVGTE 407
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARPEW---AQRAAYLLGCTLEELSSAIFKHHLSGGPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 408 WVSKGQNCEQVNW------------AVGAMAKGLYSRVFNWLVKKCN--LTLDQKGIDRdyfIGVLDIAGFEIFDFN--- 470
Cdd:cd01386 304 QSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINrsLSSSHHSTSS---ITIVDTPGFQNPAHSgsq 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 471 ---SFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQwvfIDFGLD---LQACIELIEKPL---------------GI 529
Cdd:cd01386 381 rgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQAPqqalvrsdlrdedrrGL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 530 ISMLDEECIVPKATDLTLASKLVdQHLGKHPNFEKPKPPKGKQGEAHFAMRHYAGT--VRYNCLNWLEKNK-DPLNDTVV 606
Cdd:cd01386 458 LWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNAT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 607 SAMKQSKgndllveiwqdyttqeeaaakakeggGGGKKKGKSGSFMTVSMlyreSLNNLMTMLNKTHPHFIRCIIPNEKK 686
Cdd:cd01386 537 QLLQESQ--------------------------KETAAVKRKSPCLQIKF----QVDALIDTLRRTGLHFVHCLLPQHNA 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 687 QSG------------MIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAakeaksDDDKKKCAEAimSKL 754
Cdd:cd01386 587 GKDerstsspaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLA------PPLTKKLGLN--SEV 658
|
730 740 750
....*....|....*....|....*....|.
gi 17509401 755 VNDGSLSEEM----------FRIGLTKVFFK 775
Cdd:cd01386 659 ADERKAVEELleeldlekssYRIGLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-775 |
1.40e-85 |
|
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: 294.62 E-value: 1.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLpiytDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAvgasqqegGAEVDpNKKKVTLEDqivqTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14937 77 ESGSGKTEASKLVIKYYLS--------GVKED-NEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPiKDYWFVAQAELIIDGIDDVEEFQLTDEAF 334
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSE-NEYKYIVNKNVVIPEIDDAKDFGNLMISF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 335 DILNFSAVeKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDE-----AEKASNMYGIGCEEFLKALTKPRVKVGTEWV 409
Cdd:cd14937 223 DKMNMHDM-KDDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKnnlelVNEISNLLGINYENLKDCLVFTEKTIANQKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 410 SKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGiDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 489
Cdd:cd14937 302 EIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 490 HHMFVLEQEEYAREGIQWVFIDFGLDlQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQhLGKHPNFEKPKppk 569
Cdd:cd14937 381 YIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNK-FSKHEKYASTK--- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 570 gKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQEEAaakakegggggkkkgksG 649
Cdd:cd14937 456 -KDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSN-NKLVRSLYEDVEVSESL-----------------G 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 650 SFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRIcRKGFPNRTLHPDFVQRY 729
Cdd:cd14937 517 RKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17509401 730 AIL--AAKEAKSDDDKKKcaeaiMSKLVNDgSLSEEMFRIGLTKVFFK 775
Cdd:cd14937 596 EYLdySTSKDSSLTDKEK-----VSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-732 |
6.07e-83 |
|
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: 285.25 E-value: 6.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLpiyTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQdHENQSMLITGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETI---YGAGAMKAYLKNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFaavgasqqeggaeVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNkhGR 255
Cdd:cd14898 78 SGSGKTENAKLVIKYL-------------VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRpelkkELLLDLPIKDYWFVAQAELIIDgidDVEEFQLTDEAFD 335
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR-----LNIKNDFIDTSSTAGNKESIVQ---LSEKYKMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 336 ---ILNFSAVEkqDCyrlMSAHMHMGNMKFKQRPREEQAEPDGTDEAekaSNMYGIGCEEFLKALTKPRVKVGTEWVSKG 412
Cdd:cd14898 215 slgIANFKSIE--DC---LLGILYLGSIQFVNDGILKLQRNESFTEF---CKLHNIQEEDFEESLVKFSIQVKGETIEVF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 413 QNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGidrDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHM 492
Cdd:cd14898 287 NTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSG---ERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 493 FVLEQEEYAREGIQWVFIDFgLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKhpnfekpkpPKGKQ 572
Cdd:cd14898 364 FRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGF---------INTKA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 573 GEAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVsamkqskGNDLLVEiwqdyttqeeaaakakegggggkkkgkSGSFM 652
Cdd:cd14898 434 RDK-IKVSHYAGDVEYDLRDFLDKNREKGQLLIF-------KNLLIND---------------------------EGSKE 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 653 TVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAIL 732
Cdd:cd14898 479 DLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-784 |
8.86e-79 |
|
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: 275.20 E-value: 8.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 92 LNDASVLHNLRSRYAAMLIYTY---SGLfcVVINPYKRLPI--------YTDSCARMFMGKRKTEMPpHLFAVSDEAYRN 160
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLPP-HAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 161 MLQDHENQSMLITGESGAGKTENTKKVICYFAAVGAsqqeggaevdPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSS 240
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSS----------HSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNAS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 241 RFGKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIkDYWFVAQAELI--- 317
Cdd:cd14879 148 RFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPS-DYALLASYGCHplp 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 318 -IDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRP--REEQAEPDGTDEAEKASNMYGIGCEEFL 394
Cdd:cd14879 227 lGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 395 KALTKPRVKVGTEWVSKGQNceqvnwAVGAM------AKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFD 468
Cdd:cd14879 307 TSLTYKTKLVRKELCTVFLD------PEGAAaqrdelARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 469 ---FNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFgLDLQACIELI-EKPLGIISMLDEEC-IVPKAT 543
Cdd:cd14879 381 stgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 544 DLTLASKLVdQHLGKHPNFEKPKPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQskgndllveiwq 623
Cdd:cd14879 460 DEQMLEALR-KRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRG------------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 624 dyTTQEeaaakakegggggkkkgksgsfmtvsmlyRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCN 703
Cdd:cd14879 527 --ATQL-----------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSL 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 704 GVLEGIRICRKGFPNRTLHPDFVQRYAilaakeaksDDDKKKCAEAIMSKLVNDGSLSEEMFRIGLTKVFFKAGVLAHLE 783
Cdd:cd14879 576 GLPELAARLRVEYVVSLEHAEFCERYK---------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFLSYAAWRMLE 646
|
.
gi 17509401 784 D 784
Cdd:cd14879 647 D 647
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-775 |
4.74e-76 |
|
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: 269.21 E-value: 4.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAML--------IYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHE 166
Cdd:cd14887 1 PNLLENLYQRYNKAYinkenrncIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 167 NQSMLITGESGAGKTENTKKVICYFAAVgaSQQEGGAEVDpnkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV--SDRRHGADSQ------GLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 247 RIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfrpELKKELLLDLPIKDYWFVAQAELIIdgiddvee 326
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNA---AVAAATQKSSAGEGDPESTDLRRIT-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 327 fqltdEAFDILNFSAVEKQDCYRLMSAHMHMGNMKF--KQRPREEQAEPD-----GTDE-AEKASNMYGIGC-------- 390
Cdd:cd14887 222 -----AAMKTVGIGGGEQADIFKLLAAILHLGNVEFttDQEPETSKKRKLtsvsvGCEEtAADRSHSSEVKClssglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 391 EEFLKALTKPRVKVGTEWVSKGQN-------------------CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQ--KG 449
Cdd:cd14887 297 EASRKHLKTVARLLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRsaKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 450 IDRDY-----------FIGVLDIAGFEIF---DFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGiqwVFID---- 511
Cdd:cd14887 377 SESDSdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEG---VFQNqdcs 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 512 -FGLDLQACIELIEKPLGIISML------DEECIVPKATDLTLASKLVDQHLGKHPNFE--------------------- 563
Cdd:cd14887 454 aFPFSFPLASTLTSSPSSTSPFSptpsfrSSSAFATSPSLPSSLSSLSSSLSSSPPVWEgrdnsdlfyeklnkniinsak 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 564 -KPKPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVvsamkqskgnDLLVEIWQDYTTQEEAAAKAKEGGGGG 642
Cdd:cd14887 534 yKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDEL----------ERLFLACSTYTRLVGSKKNSGVRAISS 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 643 KKKGKSGSFmtvsmlyRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLH 722
Cdd:cd14887 604 RRSTLSAQF-------ASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPY 676
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 17509401 723 PDFVQRYA-ILAAKEAKSDDDKKKCAEAIMSKLVNDGSlseemFRIGLTKVFFK 775
Cdd:cd14887 677 VELWRRYEtKLPMALREALTPKMFCKIVLMFLEINSNS-----YTFGKTKIFFR 725
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-742 |
4.08e-73 |
|
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: 259.45 E-value: 4.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKTE-------MPPHLFAVSDEAYRNMLQDHE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 167 NQSMLITGESGAGKTENTKKVICYFAAVGASQQeggaevdpnkkKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 246
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQ-----------MTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 247 RIHFNK---------HGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAE-- 315
Cdd:cd14884 150 LLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEsh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 316 ----------LIIDGIDDVEEFQLTDEA-FDIL-------NFSAVEKQDCYRLMSAHMHMGNMKFKQrpreeqaepdgtd 377
Cdd:cd14884 230 qkrsvkgtlrLGSDSLDPSEEEKAKDEKnFVALlhglhyiKYDERQINEFFDIIAGILHLGNRAYKA------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 378 eaekASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTL----DQKGIDRD 453
Cdd:cd14884 297 ----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckEKDESDNE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 454 Y-------FIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQW--VFIDFGLDLQACIELIE 524
Cdd:cd14884 373 DiysineaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 525 KPLGIISMLDEECivPKATDLTLASKLVD-----QHLGKH------PNFEKPKPPKGKQGEAHFAMRHYAGTVRYNCLNW 593
Cdd:cd14884 453 RRLDDITKLKNQG--QKKTDDHFFRYLLNnerqqQLEGKVsygfvlNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 594 LEKNKDPLNDTVVSAMKQSKGNDLlveiwqdyttqeeaaakakeggGGGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTH 673
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFL----------------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509401 674 PHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKE---AKSDDD 742
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQIAKElekCNSNTD 660
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
94-751 |
5.21e-68 |
|
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: 243.10 E-value: 5.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 94 DAsVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPiytdsCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLIT 173
Cdd:cd14881 1 DA-VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG-----NPLTLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVI-CYFAAVGasqqeGGAEVDPNKkkvtledQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNK 252
Cdd:cd14881 75 GTSGSGKTYASMLLLrQLFDVAG-----GGPETDAFK-------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 253 hGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELkkellldlpikdywfvaQAELIIDG--IDDVEEFQLT 330
Cdd:cd14881 143 -GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEE-----------------RVKLHLDGysPANLRYLSHG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 331 D----EAFDILNFSA---------VEKQDCYRLMSAHMHMGNMKFKQrPREEQAEPDGTDEAEKASNMYGIGCEEFLKAL 397
Cdd:cd14881 205 DtrqnEAEDAARFQAwkaclgilgIPFLDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 398 TKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNL------TLDQKGIDRdyFIGVLDIAGFEIFDFNS 471
Cdd:cd14881 284 TTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTHATDG--FIGILDMFGFEDPKPSQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 472 FEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQW-VFIDFgLDLQACIELIEK-PLGIISMLDEECiVPKATDLTLAS 549
Cdd:cd14881 362 LEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVEC-SPRGTAESYVA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 550 KLVDQHLGkHPNFEKPKPPKGKQgeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAM-KQSKGNDLLVEIwQDYTTQ 628
Cdd:cd14881 440 KIKVQHRQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFyKQNCNFGFATHT-QDFHTR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 629 eeaaakakegggggkkkgksgsfmtvsmlyresLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEG 708
Cdd:cd14881 514 ---------------------------------LDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLET 560
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 17509401 709 IRICRKGFPNRTLHPDFVQRYAILAA-KEAKSDDDKKKCAEAIM 751
Cdd:cd14881 561 VNLMAGGYPHRMRFKAFNARYRLLAPfRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-775 |
1.28e-65 |
|
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: 235.92 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 95 ASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFmgkrktemppHLFAVSDEAYRNMLQDHENQSMLI-T 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 174 GESGAGKTENTKKVICYFAAvgasqqeggaevDPNKKKVTLEDQIVQTnpVLEAFGNAKTVRNNNSSRFGKFIRIHFnKH 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS------------QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLY-KR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 254 GRLASCDIEHYL-LEKSRVIRQAPGERCYHIFYQIYSDFrpelKKELLLDLPIKD---YWFVAQAELIIDGIDDVEEFQL 329
Cdd:cd14874 136 NVLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGL----NDEMKAKFGIKGlqkFFYINQGNSTENIQSDVNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 330 TDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQR--PREEQ--AEPDGTDEAEKASNMYGIGCEEFLKALTkPRVKVG 405
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKrnPNVEQdvVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 406 TEWvskgqnceQVNWAVG---AMAKGLYSRVFNWLVKKCNLTLdqKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNE 482
Cdd:cd14874 291 TTI--------DLNAALDnrdSFAMLIYEELFKWVLNRIGLHL--KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 483 KLQQFFNHHMFVLEQEEYAREGIQwvfIDF----GLDLQACIELI-EKPLGIISMLDEECIVPKATDLTLASKLVDQHLG 557
Cdd:cd14874 361 RIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 558 KhPNFEKPKppkgKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeaaakake 637
Cdd:cd14874 438 R-SSYGKAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSK-NPIIGLLFESYSSN--------- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 638 gggggkkkgKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFP 717
Cdd:cd14874 503 ---------TSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYP 573
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 718 NRTLHPDFVQRY-AILAAKEAKSDDDKkkcaEAIMSKLVNDGSLSEEMFRIGLTKVFFK 775
Cdd:cd14874 574 VKISKTTFARQYrCLLPGDIAMCQNEK----EIIQDILQGQGVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-774 |
5.88e-59 |
|
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: 218.69 E-value: 5.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 98 LHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRK----------TEMPPHLFAVSDEAYRNMLQDHEN 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 168 QSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 248 IHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFR--PELKKELLLDLPIKDYWFVAQAELIIDGID-DV 324
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 325 EEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDG--TDEAEKASNMYGIGCEEFLKAL---TK 399
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALKDPAQILLAAKlleVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 400 PRV------------KVGTEWVS--KGQNCEQVNWAVGAMAKGLYSRVFNWLVK--------------KCNLTLDQKGID 451
Cdd:cd14893 324 PVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVEtlngilggifdryeKSNIVINSQGVH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 452 rdyfigVLDIAGFEIFD--FNSFEQLWINFVNEKLQQFFNHHMFV-----LEQEEYAREGIQWV--FIDFGLDLQACIEL 522
Cdd:cd14893 404 ------VLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENRLTVnsNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 523 IE-KPLGIISMLDEECIVPKATDLTLASKL--VDQHLG--KHPNF------EKPKPPkgKQGEAHFAMRHYAGTVRYNCL 591
Cdd:cd14893 478 FEdKPFGIFDLLTENCKVRLPNDEDFVNKLfsGNEAVGglSRPNMgadttnEYLAPS--KDWRLLFIVQHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 592 NWLEKNKDPLNDTVVSAMKQSKgNDLL------------VEIWQDYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVSMLYR 659
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSK-NAVLhavgaaqmaaasSEKAAKQTEERGSTSSKFRKSASSARESKNITDSAATDVYN 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 660 ESlNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYailaakeaKS 739
Cdd:cd14893 635 QA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY--------KN 705
|
730 740 750
....*....|....*....|....*....|....*
gi 17509401 740 DDDKKKCAEAIMSKLVNDGSLSEEMFRIGLTKVFF 774
Cdd:cd14893 706 VCGHRGTLESLLRSLSAIGVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-775 |
7.36e-57 |
|
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: 211.10 E-value: 7.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLP-IYTDSCARMFMGKRKteMPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG--LPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFAAVGASQQEggaevdpnkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHG 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 255 RLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFrPELKKELLLDLPIKDYWFVAQAELI-IDGIDDVEEFQLTDEA 333
Cdd:cd14905 148 EIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGI-TDEEKAAYQLGDINSYHYLNQGGSIsVESIDDNRVFDRLKMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 334 FDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRpreeqaepDGTDEAEKASNMygigcEEFLKALTKPRVKVGTEWVSkgQ 413
Cdd:cd14905 227 FVFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--------NGKTEVKDRTLI-----ESLSHNITFDSTKLENILIS--D 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 414 NCEQVNWAV---GAMAKGLYSRVFNWLVKKCNLTLdqKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNH 490
Cdd:cd14905 292 RSMPVNEAVenrDSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 491 HMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKplgIISMLDEECIVPKATDLTLASKLvDQHLGKHPNFEKpKPPKg 570
Cdd:cd14905 370 TVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 571 kqgeahFAMRHYAGTVRYNCLNWLEKNKDPL--------NDTVVSAMKQSKG----NDLLVEIWQDYTTQEEAAAKAKEG 638
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEIlqrtnvlhKNSITKYLFSRDGvfniNATVAELNQMFDAKNTAKKSPLSI 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 639 GGGGKK----------------------------KGKSGSFMTVSMLYRESLNNlmtmlNKTHPHFIRCIIPNEKKQSGM 690
Cdd:cd14905 518 VKVLLScgsnnpnnvnnpnnnsgggggggnsgggSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPNSKKTHLT 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 691 IDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILaakeAKSDDDKKKCAEAIMSKLVNDGSLSEEMFRIGLT 770
Cdd:cd14905 593 FDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFF----FQNQRNFQNLFEKLKENDINIDSILPPPIQVGNT 668
|
....*
gi 17509401 771 KVFFK 775
Cdd:cd14905 669 KIFLR 673
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
9.08e-57 |
|
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: 194.49 E-value: 9.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 117 FCVVINPYKRLPIYTDS-CARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGESGAGKTENTKKVICYFAAVG 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 196 ASQQEGGAE---VDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 248
Cdd:cd01363 81 FNGINKGETegwVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-775 |
2.88e-50 |
|
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: 190.34 E-value: 2.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 176 SGAGKTENTKKVICYFAAVGASQQEGGAevdpnkkkvtledQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGR 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG-------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 256 LASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKkellldlpIKDYWFVAQAEL----IIDGI---------D 322
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--------LKEYNLKAGRNYrylrIPPEVppsklkyrrD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 323 D----VEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQrpREEQAEPDGTDEAEKASNMYGIGCEEFLKALT 398
Cdd:cd14882 221 DpegnVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 399 KPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCN--LTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLW 476
Cdd:cd14882 299 NYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINmkMSFPRAVFGDKYSISIHDMFGFECFHRNRLEQLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 477 INFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEecivpKATDLTLASKLVDQHL 556
Cdd:cd14882 379 VNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 557 GKHPNFEKPkppkgkQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKgNDLLVEIWQDYTTQeeaaakak 636
Cdd:cd14882 454 EKHSQFVKK------HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSL-DESVKLMFTNSQVR-------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 637 egggggKKKGKSGSFMTVSMlyrESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGF 716
Cdd:cd14882 519 ------NMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 717 PNRTLHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGslseemFRIGLTKVFFK 775
Cdd:cd14882 590 SYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLLLIRLKMEG------WAIGKTKVFLK 642
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-752 |
2.88e-44 |
|
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: 173.48 E-value: 2.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 96 SVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTE-MPPHLFAVSDEAYRNMLQDHENQSMLITG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 175 ESGAGKTENTKKVICYFA-----------AVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 244 KFIRIHFNKHgRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDfRPELKKELLLDLPIKDYWFVAQAELIIDGIDD 323
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIING-SSDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 324 VEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPRE-----------------------EQAEPDGTDEAE 380
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKksllmgknqcgqninyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 381 K----ASNMYGIGCEEFLKALTKPRVkVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKK--CNLTLDQKGIDRDY 454
Cdd:cd14938 320 KnlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKinEKCTQLQNININTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 455 FIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGLD-LQACIELIEKPLGIISML 533
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 534 DEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQgeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSk 613
Cdd:cd14938 479 LENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 614 GNDLLVEIWQDYT-------TQEEAAAKAKEGGGGGKKKGKSGSFMTVSMLyRESLNNLMTMLNKTHPHFIRCIIPNEKK 686
Cdd:cd14938 556 ENEYMRQFCMFYNydnsgniVEEKRRYSIQSALKLFKRRYDTKNQMAVSLL-RNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 687 QS-GMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAIlaakeaKSDDDKKKCAEAIMS 752
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI------KNEDLKEKVEALIKS 695
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
889-1760 |
2.04e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 141.73 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 889 LVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQrakkkieAEVEALKKQIQDLEM 968
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 969 SLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLE 1048
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1049 REKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHsvSSRLEDEQALVSKLQRQIKDGQSRISELE 1128
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1129 EELENERQSRSKADRAKSDLQRELEELGEKLDeqggataaqveVNKKREAELAKLRRDLeEANMNHENQLGGlrkkHTDA 1208
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLD-----------SLERLQENLEGFSEGV-KALLKNQSGLSG----ILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1209 VAELTdqldqlnkakaKVEKDKAQAVrdAEDLAAQLDQETSGKLNNEKLAKQFELQltelqskadeqsrqlqdftSLKGR 1288
Cdd:TIGR02168 525 LSELI-----------SVDEGYEAAI--EAALGGRLQAVVVENLNAAKKAIAFLKQ-------------------NELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1289 LHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEeaRRTADEEAR--------------ERQTVAAQAKNYQHEAeQLQE 1354
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGY-RIVT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1355 SLEEEIEGKNEILRQLSKANADIQQWKARFEgegllkadELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDL 1434
Cdd:TIGR02168 650 LDGDLVRPGGVITGGSAKTNSSILERRREIE--------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1435 DDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSL 1514
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1515 SQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKrIQEKEEEFEN 1594
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1595 TRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVREL-QLQVEEEQRNG 1673
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALE 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1674 ADTREQFFNAEKRATLLQSEKEELLVANEAAErarkqAEYEAADARDQanEANAQVSSLTSAKRKLEGEIQAIHadlDET 1753
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAI-----EEYEELKERYD--FLTAQKEDLTEAKETLEEAIEEID---REA 1030
|
....*..
gi 17509401 1754 LNEYKAA 1760
Cdd:TIGR02168 1031 RERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1009-1865 |
1.83e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 128.64 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1009 EEINRKLmEDLQSEEDKGNHQNKVKAKLEQT-LDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLEN 1087
Cdd:TIGR02168 196 NELERQL-KSLERQAEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1088 NLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQggatA 1167
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL----K 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1168 AQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKhtdaVAELTDQLDQLNKakakvekDKAQAVRDAEDLAAQLDQE 1247
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNN-------EIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1248 TSgklnneklakqfelQLTELQSKADEQSRQlqdftslkgRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRT 1327
Cdd:TIGR02168 420 QQ--------------EIEELLKKLEEAELK---------ELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1328 ADEEARERQTVAAQAKNYQheaeQLQESLEEEIEGKNEILRQLSKANADIQQWKARFE-GEGLLKADELEDAKRRQAQKI 1406
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvDEGYEAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1407 NELQEALDAANS-KNASLEKTKSRLVGDLDDAQVDVERAN---------GVASALEKKQKGFDKIIDEWRKKTDdLAAEL 1476
Cdd:TIGR02168 553 ENLNAAKKAIAFlKQNELGRVTFLPLDSIKGTEIQGNDREilkniegflGVAKDLVKFDPKLRKALSYLLGGVL-VVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1477 DGAQRDLRNTST---------DLFKAKNAQEELAEVVEGLRRENKslsQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKE 1547
Cdd:TIGR02168 632 DNALELAKKLRPgyrivtldgDLVRPGGVITGGSAKTNSSILERR---REIEELEEKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1548 ELQhaldeaeaaleaeeskvlraqvevsQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKL 1627
Cdd:TIGR02168 709 ELE-------------------------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1628 EGDINELEialdhankanaDAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERA 1707
Cdd:TIGR02168 764 EELEERLE-----------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1708 RKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQH 1787
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1788 VDRLRKGLEQQLKEIQVRLDEAEAAalkggkkvIAKLEQRVRELES-ELDGEQRRFQDANKNLGRADRRVRELQFQVDE 1865
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVR--------IDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
849-1415 |
1.57e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 849 LKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQL 928
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 929 SELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQ 1008
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1009 EEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENN 1088
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1089 LKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRIsELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAA 1168
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1169 QVEVnkkrEAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELtDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQET 1248
Cdd:COG1196 537 EAAL----EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF-LPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1249 SGKLNNEKLAKQFELQLTELQSKADEQSRQLQD---FTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEAR 1325
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1326 RTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQlskaNADIQQWKARFEGEGLLKADELEDAKRRQAQK 1405
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE----ELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
570
....*....|.
gi 17509401 1406 -INELQEALDA 1415
Cdd:COG1196 768 eLERLEREIEA 778
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-713 |
2.17e-23 |
|
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: 108.29 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 218 IVQTNPVLEAFGNAKTVRNNNSSRFGKF--IRIHFNKHG---RLASCDIEHYLLEKSRVIRQA------PGERCYHIFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 287 IYSDFRPElkkellldlpikDYWFVAQAELIIDGID--------------------------DVEEFQLTDEAFDILNFS 340
Cdd:cd14894 329 MVAGVNAF------------PFMRLLAKELHLDGIDcsaltylgrsdhklagfvskedtwkkDVERWQQVIDGLDELNVS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 341 AVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGT---DEAEKASNMYGIGCEEFLKALTKPR---VKVGTEWVSKGQN 414
Cdd:cd14894 397 PDEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 415 CEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRD----------------YFIGVLDIAGFEIFDFNSFEQLWIN 478
Cdd:cd14894 477 KGQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSALSTDgnkhqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCIN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 479 FVNEKLqqffnhhmfvleqeeYAREGiQWVFIDF-------GLDLQACIELI-EKPLGIISMLDEECIVPKATDLTLA-- 548
Cdd:cd14894 557 YLSEKL---------------YAREE-QVIAVAYssrphltARDSEKDVLFIyEHPLGVFASLEELTILHQSENMNAQqe 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 549 ---SKLVDQHLGKHPNFEKPKPPKG-KQGEAH---------FAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGN 615
Cdd:cd14894 621 ekrNKLFVRNIYDRNSSRLPEPPRVlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSS 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 616 DLLVEIwqDYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVSMlYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAAL 695
Cdd:cd14894 701 HFCRML--NESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDL 777
|
570
....*....|....*...
gi 17509401 696 VLNQLTCNGVLEGIRICR 713
Cdd:cd14894 778 VEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1298-1929 |
3.08e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1298 RQLEDAESQVNQLTRLKSQLTSQLEEARRTAdEEARERQTVAAQAKNYQHEAEQLQ-ESLEEEIEGKNEILRQLSKANAD 1376
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERQA-EKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1377 IQQWKARFEGEgllkADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQK 1456
Cdd:COG1196 258 LEAELAELEAE----LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1457 GFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQ 1536
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1537 KIIRRLEIEKEELQhaldeaeaaleAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKG 1616
Cdd:COG1196 414 ERLERLEEELEELE-----------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1617 KAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTReqffnaekratllqsekEE 1696
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-----------------LA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1697 LLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAE 1776
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1777 ELRQEQEHSqhVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAK---LEQRVRELESELDGEQRRFQDANKNLGRAD 1853
Cdd:COG1196 626 TLVAARLEA--ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELlaaLLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1854 RRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKM 1929
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
906-1549 |
6.62e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 906 QLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIR 985
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 986 SLQDEMQQQDEAIAKLNKEKKHQEEinrklmedlqseedkgnhqnkVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVE 1065
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEE---------------------ELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1066 GELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAK 1145
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1146 SDLQRELEELGEKLDEQGGATA---AQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKA 1222
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAAlleAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1223 KAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDftSLKGRLHSENGDLVRQLED 1302
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA--ALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1303 AESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKA 1382
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1383 RFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERAngvasALEKKQKGFDkiI 1462
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-----ALEELPEPPD--L 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1463 DEWRKKTDDLAAELD--GAQrDLRntstdlfkaknAQEELAEVVEGLRrenkSLSQEIKDLTdqlgeggRSVHEMQKIIR 1540
Cdd:COG1196 763 EELERELERLEREIEalGPV-NLL-----------AIEEYEELEERYD----FLSEQREDLE-------EARETLEEAIE 819
|
....*....
gi 17509401 1541 RLEIEKEEL 1549
Cdd:COG1196 820 EIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1057-1778 |
9.86e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1057 LDKQKRKVEGELKIAQENIDESGRQRHDLENNLKkkeselhsvssrledeqalvsKLQRQikdgqsriseleeelenerq 1136
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLEDILGELERQLE---------------------PLERQ-------------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1137 sRSKADRAKsDLQRELEELgekldeQGGATAAQVEvnkKREAELAKLRRDLEEANMNHENQLGGLRKKHTdAVAELTDQL 1216
Cdd:COG1196 209 -AEKAERYR-ELKEELKEL------EAELLLLKLR---ELEAELEELEAELEELEAELEELEAELAELEA-ELEELRLEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1217 DQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQdftslkgRLHSENGDL 1296
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE-------ELEEELEEA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1297 VRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANAD 1376
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1377 IQqwkarfegEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQK 1456
Cdd:COG1196 430 LA--------ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1457 GFDKIIDEWRKKtdDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEV--VEGLRRENKSLSQEIKDLTDQLgeGGRSVHE 1534
Cdd:COG1196 502 DYEGFLEGVKAA--LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAK--AGRATFL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1535 MQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEA 1614
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1615 KGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEK 1694
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1695 EELLVANEAAERARKQAEYEAADARDQANEAnaqvssLTSAKRKLEG-------------EIQAIHADLDETLNEYKAAE 1761
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERE------LERLEREIEAlgpvnllaieeyeELEERYDFLSEQREDLEEAR 811
|
730
....*....|....*..
gi 17509401 1762 ERSKKAIADATRLAEEL 1778
Cdd:COG1196 812 ETLEEAIEEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1288-1935 |
4.45e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.29 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1288 RLHSENGDLVRqLEDAESQVN-QLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEI 1366
Cdd:TIGR02168 180 KLERTRENLDR-LEDILNELErQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1367 LRQLSKANADIqqwkarfegegllkaDELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANG 1446
Cdd:TIGR02168 259 TAELQELEEKL---------------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1447 VASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLG 1526
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1527 EGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIR--------SEIEKRIQEKEEEFENTRKN 1598
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElerleealEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1599 HAR------ALESMQASLETEAKGKAELLRIKKKLEGDIN--------------ELEIAL------------DHANKA-N 1645
Cdd:TIGR02168 484 LAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaAIEAALggrlqavvvenlNAAKKAiA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1646 ADAQKNLKRyqeqVRELQLQVEEEQRNGADTREQFFNAEKRATLLQS-----EKEELLVAN------------EAAERAR 1708
Cdd:TIGR02168 564 FLKQNELGR----VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvkfdPKLRKALSYllggvlvvddldNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1709 KQAEYEAADARD------------QANEANAQVSSLTSAKRKLEGEIQAIHADLDET---LNEYKAAEERSKKAIADATR 1773
Cdd:TIGR02168 640 KLRPGYRIVTLDgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELekaLAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1774 LAEELRQE------------------QEHSQHVDRLRKGLEQQLKEIQVRLDEAEaAALKGGKKVIAKLEQRVRE----- 1830
Cdd:TIGR02168 720 ELEELSRQisalrkdlarleaeveqlEERIAQLSKELTELEAEIEELEERLEEAE-EELAEAEAEIEELEAQIEQlkeel 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1831 --LESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQL 1908
Cdd:TIGR02168 799 kaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
730 740
....*....|....*....|....*..
gi 17509401 1909 THQLEDAEERADQAENSLSKMRSKSRA 1935
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRE 905
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
900-1830 |
5.70e-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: 100.91 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 900 LESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEdRTADVQraKKKIEAEVEALKKQIQDLEMSLRKAESEKQS 979
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALL--KEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 980 KDHQIRSLQDEMQQQDEAIAKLNKEKkhqEEINRKLMeDLQSEEdkgnhQNKVKAKLEqtldDLEDSLEREKRARADLDK 1059
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLL---EELNKKIK-DLGEEE-----QLRVKEKIG----ELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1060 QKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDgqsriseleeeleneRQSRS 1139
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---------------VDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1140 KADRAK-SDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEAnmnhENQLGGLRKKHTDAVAELTDQLDQ 1218
Cdd:TIGR02169 381 AETRDElKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1219 LNKAKAKVEKDKAQAVRDAEDLAAQldqetsgklnnEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVr 1298
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRV-----------EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH- 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1299 qledaeSQVNQLTRLKSQLTSQLEEAR-RTADEEARERQTVAAQAKNY--QHEAEQLQESLEEEIEGKNEILRQLSKANA 1375
Cdd:TIGR02169 525 ------GTVAQLGSVGERYATAIEVAAgNRLNNVVVEDDAVAKEAIELlkRRKAGRATFLPLNKMRDERRDLSILSEDGV 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1376 -----DIQQWKARFE-------GEGLLkADELEDAKR-----RQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQ 1438
Cdd:TIGR02169 599 igfavDLVEFDPKYEpafkyvfGDTLV-VEDIEAARRlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1439 VDVERANGVASALEKKQKGFDKIidewRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEI 1518
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRI----ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1519 KDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKvlraqvEVSQIRSEIEKRIQEKEeefentrkn 1598
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS------KLEEEVSRIEARLREIE--------- 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1599 haRALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELqlqveeeqrngadtre 1678
Cdd:TIGR02169 819 --QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL---------------- 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1679 qffnaEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYK 1758
Cdd:TIGR02169 881 -----ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1759 AAEERSKKAIADATRLAEELRQEQEHSQHVDRLrkgleQQLKEIQVRLdEAEAAALkggKKVIAKLEQRVRE 1830
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-----DELKEKRAKL-EEERKAI---LERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1174-1851 |
8.31e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 8.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1174 KKREAE--LAKLRRDLEEANmnhenqlgglrkkhtDAVAELTDQLDQLNKAKAKVEK-----------DKAQAVRDAEDL 1240
Cdd:COG1196 173 RKEEAErkLEATEENLERLE---------------DILGELERQLEPLERQAEKAERyrelkeelkelEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1241 AAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQ 1320
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1321 LEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEgEGLLKADELEDAKR 1400
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1401 RQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQ 1480
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1481 RDLRNtstdlfkaknAQEELAEvveglRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAAL 1560
Cdd:COG1196 477 AALAE----------LLEELAE-----AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1561 EAEESKVLRAQVEVSQIRSEIEKRIQEKEEE------FENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINEL 1634
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1635 EIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYE 1714
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1715 AADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEqehsqhVDRLRKG 1794
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE------LERLERE 775
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1795 LE----------QQLKEIQVRLDE--AEAAALKggkKVIAKLEQRVRELESEldgEQRRFQDA----NKNLGR 1851
Cdd:COG1196 776 IEalgpvnllaiEEYEELEERYDFlsEQREDLE---EARETLEEAIEEIDRE---TRERFLETfdavNENFQE 842
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
889-1616 |
2.68e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.60 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 889 LVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLAD--------NEDRTADVQRAKKKIEAEVEALK 960
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlGEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 961 KQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEK-KHQEEIN--RKLMEDLQS---EEDKGNHQNKVK- 1033
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdKLTEEYAelKEELEDLRAeleEVDKEFAETRDEl 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1034 AKLEQTLDDLEDSLEREKRARADLDKQKRKVEGE-------LKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDE 1106
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEEladlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1107 QALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGE-------------KLDEQ---------GG 1164
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgtvaqlgSVGERyataievaaGN 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1165 ATAAQV---EVNKKREAELAKLRR-------DLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAqAV 1234
Cdd:TIGR02169 548 RLNNVVvedDAVAKEAIELLKRRKagratflPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTL-VV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1235 RDAEDLAAQLDQ-----------ETSGKLNNEKLAKQFelqlteLQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDA 1303
Cdd:TIGR02169 627 EDIEAARRLMGKyrmvtlegelfEKSGAMTGGSRAPRG------GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1304 ESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKAr 1383
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE- 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1384 fegegllkadELEDAKRRQA-QKINELQEALDaansknaSLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKII 1462
Cdd:TIGR02169 780 ----------ALNDLEARLShSRIPEIQAELS-------KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1463 DEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRL 1542
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1543 EIEKEELQHALDEAEAALEAEESKVLRAQVE--VSQIRSEIEKRIQEKE-------EEFENTRKNHaRALESMQASLETE 1613
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSLedVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRL-DELKEKRAKLEEE 1001
|
...
gi 17509401 1614 AKG 1616
Cdd:TIGR02169 1002 RKA 1004
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1223-1921 |
8.29e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.52 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1223 KAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLED 1302
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1303 AESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQlskanADIQQWKA 1382
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM-----AHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1383 RFEGEGLLKADELedakrRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQkgfdkii 1462
Cdd:PTZ00121 1271 AIKAEEARKADEL-----KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA------- 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1463 dEWRKKTDDLAAELDGAQRDlrntstdlfKAKNAQEElAEVVEGLRRENKSLSQEIKdltdQLGEGGRSVHEMQKIIRRL 1542
Cdd:PTZ00121 1339 -EEAKKAAEAAKAEAEAAAD---------EAEAAEEK-AEAAEKKKEEAKKKADAAK----KKAEEKKKADEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1543 EIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLR 1622
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1623 IKKKLEGDINELEIALDHANKANADAQK--NLKRYQEQVRELQLQVEEEQRNGADTREQffnAEKRatllqsEKEELLVA 1700
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKA---EEKK------KADELKKA 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1701 NEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADldetlnEYKAAEERSKKAiADATRLAEELRQ 1780
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE------EKKMKAEEAKKA-EEAKIKAEELKK 1627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1781 EQEHSQHVDRLRKGLEQQLKEI-QVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVREL 1859
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1860 QFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEE----AEELANLNLQKyKQLTHQLEDAEERADQ 1921
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEdkkkAEEAKKDEEEK-KKIAHLKKEEEKKAEE 1772
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
996-1862 |
8.85e-19 |
|
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: 93.64 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 996 EAIAKLNKEKKHQ-EEINRKLMEDLQSEEDKG--------NHQNKVKaKLEQTLDDLEDSLEREKRARADLDKQKRKVEG 1066
Cdd:pfam15921 74 EHIERVLEEYSHQvKDLQRRLNESNELHEKQKfylrqsviDLQTKLQ-EMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1067 ELKIA----QENIDESGRQRHDLENNLKKKESELHSVSSRLED-EQALVSKLQRQikDGQSRISEleeeleneRQSRSKA 1141
Cdd:pfam15921 153 ELEAAkclkEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEH--DSMSTMHF--------RSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1142 DRAKSDLQRELEEL-GEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLN 1220
Cdd:pfam15921 223 SKILRELDTEISYLkGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1221 KAKAKVEKDKAQAVRDAEDLAAQLDQETSgKLNN---------EKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHS 1291
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRS-ELREakrmyedkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1292 ENGDLVRQLEDAESQVNQLTRLKSQLTSQ---LEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILR 1368
Cdd:pfam15921 382 LLADLHKREKELSLEKEQNKRLWDRDTGNsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1369 QLSKANADIQQWKARFEG---EGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQvdveran 1445
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKvveELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ------- 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1446 gvasalekkqkgfdkiidewrkktddlaaELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRrenkslsQEIKDLTDQL 1525
Cdd:pfam15921 535 -----------------------------HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILR-------QQIENMTQLV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1526 GEGGRSVHEMQkiIRRLEIEKE------ELQHALDEAEAALEAEE--------------------SKVLRAQVEVSQIRS 1579
Cdd:pfam15921 579 GQHGRTAGAMQ--VEKAQLEKEindrrlELQEFKILKDKKDAKIRelearvsdlelekvklvnagSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1580 EIEKRIQEKE-------EEFENTRKNHARALESMQAsleTEAKGKAELLRIKKKLEGDINEL---EIALDHANKANADAQ 1649
Cdd:pfam15921 657 QLLNEVKTSRnelnslsEDYEVLKRNFRNKSEEMET---TTNKLKMQLKSAQSELEQTRNTLksmEGSDGHAMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1650 KNLKRYQEQVRELQ--LQVEEEQRNGADTREQFFNAEKRA-----TLLQSEKEELLVANEAAERARKQAEYEAADARDQA 1722
Cdd:pfam15921 734 KQITAKRGQIDALQskIQFLEEAMTNANKEKHFLKEEKNKlsqelSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1723 NEANAQVSSLTSAKRKLEGEiqAIHADLDETLN--EYKAAEERSKKAI-------ADATRLAEELRQEQ-------EHSQ 1786
Cdd:pfam15921 814 DKASLQFAECQDIIQRQEQE--SVRLKLQHTLDvkELQGPGYTSNSSMkprllqpASFTRTHSNVPSSQstasflsHHSR 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1787 HVDRLR----KGLEQQLKEIQVRLDEAEAAAL-----KGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVR 1857
Cdd:pfam15921 892 KTNALKedptRDLKQLLQELRSVINEEPTVQLskaedKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSS 971
|
....*
gi 17509401 1858 ELQFQ 1862
Cdd:pfam15921 972 ETCSR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
899-1255 |
1.70e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.81 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 899 NLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQ 978
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 979 SKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVK-------AKLEQTLDDLEDSLEREK 1051
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1052 RARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEEL 1131
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1132 ENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNK-KREAELAKLRRDLEEA----------NMNHENQLGG 1200
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRLenkikelgpvNLAAIEEYEE 997
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1201 LRKKHTdavaELTDQLDQLNKAKAKVEkdkaQAVRDAEDLAAQLDQETSGKLNNE 1255
Cdd:TIGR02168 998 LKERYD----FLTAQKEDLTEAKETLE----EAIEEIDREARERFKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1190 |
2.18e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.43 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 856 EELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQL 935
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 936 ADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEeinrKL 1015
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE----RR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1016 MEDLQSEEDKGNHQnkvKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESE 1095
Cdd:TIGR02168 840 LEDLEEQIEELSED---IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1096 LHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSR-SKADRAKSDLQRELEELGEKLDEQGG---ATAAQVE 1171
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPvnlAAIEEYE 996
|
330
....*....|....*....
gi 17509401 1172 VNKKREAELAKLRRDLEEA 1190
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEA 1015
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1003-1876 |
4.12e-18 |
|
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: 91.57 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1003 KEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKR-ARADLDKQKRKVEGELKIAQENIDESGRQ 1081
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLkEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1082 RHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDE 1161
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1162 QGGATAAQVEVNKKREAELAKLRRDLEEanmnHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKdkaqAVRDAEDLA 1241
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREA----EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS----AAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1242 AQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGD-LVRQLEDAESQVNQLTRLKSQLTSQ 1320
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEeLEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1321 LEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKR 1400
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1401 RQAQKINELQEALDAANSKNASLE-KTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGA 1479
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRlLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1480 QRDLRNTSTDLFKAKNAQEELAEVVEglRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAA 1559
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSE--VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1560 LEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRknharaLESMQASLETEAKGKAELLRIKKklegdiNELEIALD 1639
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE------EKSRLKKEEKEEEKSELSLKEKE------LAEEREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1640 HANKANADAQKNLKRYQEQVRELQLQVEEEqrngaDTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADAR 1719
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEE-----AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1720 DQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQL 1799
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1800 KE-IQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNlgRADRRVRELQFQVDEDKKNFERLQDL 1876
Cdd:pfam02463 939 ELlLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE--RYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
996-1803 |
4.15e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.74 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 996 EAIAKLNKEKKHQEEINRKlmeDLQSEEDKGNHQNKVKAK--------LEQTLDDLEDSLEREKRARADLDKQKRKVEGE 1067
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEK---DIIDEDIDGNHEGKAEAKahvgqdegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1068 LKIAQENIDESGRQrhdlENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSD 1147
Cdd:PTZ00121 1104 KKTETGKAEEARKA----EEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1148 LQRELEELGEKLDEQGGATAAQVEVNKKREAElaklrRDLEEANMNHEnqlgglrKKHTDAVAELTDQLDQLNKAKAKVE 1227
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEE-----RKAEEARKAED-------AKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1228 KDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQdftslkgrlhsengdlVRQLEDAESQV 1307
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE----------------KKKADEAKKKA 1311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1308 NQlTRLKSQLTSQLEEARRTADEEAR--ERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKArfe 1385
Cdd:PTZ00121 1312 EE-AKKADEAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA--- 1387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1386 gEGLLKADELEDAKRRQAQKINELQEAldAANSKNASLEKTKSRLVGDLDDAQVDVE----------RANGVASALEKKQ 1455
Cdd:PTZ00121 1388 -EEKKKADEAKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKAEeakkadeakkKAEEAKKAEEAKK 1464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1456 KGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDltdqlGEGGRSVHEM 1535
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEA 1539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1536 QKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAK 1615
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1616 GKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKE 1695
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1696 EllvaNEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKlegeiqaihadldetlneykaAEERSKKaiadatrlA 1775
Cdd:PTZ00121 1700 E----AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---------------------AEEDKKK--------A 1746
|
810 820
....*....|....*....|....*...
gi 17509401 1776 EELRQEQEHSQHVDRLRKGLEQQLKEIQ 1803
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1530 |
2.43e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 853 KEAEELEKINDKVKALEDSLAKE-EKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSEL 931
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEElRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 932 NDQLADN--EDRTADVQRAKKKIEAEVEALKKQIQDLEmSLRKAE----SEKQSKDHQIRSLQDEMQQQDEAIAKLNKEK 1005
Cdd:PTZ00121 1250 NNEEIRKfeEARMAHFARRQAAIKAEEARKADELKKAE-EKKKADeakkAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1006 KHQEEINRKLMEDLQSEEDKgnhqnkvKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQEnidesgRQRHDl 1085
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAA-------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE------KKKAD- 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1086 enNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGA 1165
Cdd:PTZ00121 1395 --EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1166 TAAQVEVNKKREAElaKLRRDLEEANMNHENqlggLRKKhtdavAELTDQLDQLNKAKakvEKDKAQAVRDAEDL-AAQL 1244
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--EAKKKAEEAKKKADE----AKKA-----AEAKKKADEAKKAE---EAKKADEAKKAEEAkKADE 1538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1245 DQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEA 1324
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1325 RRTADE---EARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQW-KARFEGEGLLKADELEDAKR 1400
Cdd:PTZ00121 1619 KIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEA 1698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1401 RQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERangvasalEKKQKGFDKIIDEWRKKTDDLAAELDGAQ 1480
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE--------DKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17509401 1481 RDLRNTSTDLFKaknaqEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGR 1530
Cdd:PTZ00121 1771 EEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
946-1781 |
2.81e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 946 QRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDK 1025
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1026 GNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLED 1105
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1106 EQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDL---QRELEELGEKLDEQGGATAAQVEVNKKREAELAK 1182
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELlakKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1183 LRRDLEEANMNHENQLGGLRKKHTDAV--AELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQ 1260
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIelKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1261 FELQLTELQSKA-------------DEQSRQLQDFTSLKGRLH----SENGDLVRQLEDAESQVNQLTRLKSQLTSQLEE 1323
Cdd:pfam02463 493 QKLEERSQKESKarsglkvllalikDGVGGRIISAHGRLGDLGvaveNYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1324 ARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDakrrQA 1403
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES----GL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1404 QKINELQEALDAANSKNASLEKTKSRLVG--DLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQR 1481
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEiqELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1482 DLRNTSTDLFKaKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEElqhaldEAEAALE 1561
Cdd:pfam02463 729 EAQDKINEELK-LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE------KLKAQEE 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1562 AEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEialDHA 1641
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK---EEE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1642 NKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVaNEAAERARKQAEYEAADARDQ 1721
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE-PEELLLEEADEKEKEENNKEE 957
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1722 ANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQE 1781
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
826-1485 |
1.93e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.35 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 826 NVRSWCTLRTWEWFKLYGKVKPMLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEE--KTSLFTNLEST 903
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 904 KT--QLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTAD-----VQRAKKKIEAEVEALKKQIQDLEMSLRKAE-- 974
Cdd:PTZ00121 1290 KKadEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaa 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 975 ----SEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAkleqtlDDLEDSLERE 1050
Cdd:PTZ00121 1370 ekkkEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA------DEAKKKAEEA 1443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1051 KRARADLDK--QKRKVEGELKIAQE--NIDESGRQRHDLE--NNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRI 1124
Cdd:PTZ00121 1444 KKADEAKKKaeEAKKAEEAKKKAEEakKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1125 SELEEELENERqsrsKADRA-KSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRK 1203
Cdd:PTZ00121 1524 ADEAKKAEEAK----KADEAkKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1204 KHTDAVAELTDQLdqlnkAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFT 1283
Cdd:PTZ00121 1600 LYEEEKKMKAEEA-----KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1284 SLKGRLHSENGDlVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADE---EARERQTVAAQAKNYQHEAEQLQESLEEEI 1360
Cdd:PTZ00121 1675 KKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1361 EGKNEI---LRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQK--INELQEALDAANSKNASLEKTKSRLVGDLD 1435
Cdd:PTZ00121 1754 EEKKKIahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKdiFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17509401 1436 DAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRN 1485
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1177-1938 |
3.86e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.12 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1177 EAELAKLRRDLEEAnmnhenqlgGLRKKHTDAV-AELTDQLDQLNKAKAKVEKDKaqavrdaeDLAAQLdQETSGKLNNE 1255
Cdd:TIGR02169 169 DRKKEKALEELEEV---------EENIERLDLIiDEKRQQLERLRREREKAERYQ--------ALLKEK-REYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1256 KLaKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLT-----RLKSQL---TSQLEEARRT 1327
Cdd:TIGR02169 231 EK-EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlRVKEKIgelEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1328 ADEEARERQTVAAQAKNYQHEaeqlqesleeeiegKNEILRQLSKANADIQQWKARFEGEGllkaDELEDAKRRQAQKIN 1407
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAE--------------IDKLLAEIEELEREIEEERKRRDKLT----EEYAELKEELEDLRA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1408 ELQEaldaansknasLEKTKSRLVGDLDDAQVDVERANgvaSALEKKQKGFDKIIDEWRKktddlaaeLDGAQRDLRNts 1487
Cdd:TIGR02169 372 ELEE-----------VDKEFAETRDELKDYREKLEKLK---REINELKRELDRLQEELQR--------LSEELADLNA-- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1488 tDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKV 1567
Cdd:TIGR02169 428 -AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1568 L--RAQVEV-----SQIRSEIEKRIQEKEEefentrknHARALES-----MQA-SLETEAKGKA--ELLRIKK------- 1625
Cdd:TIGR02169 507 RggRAVEEVlkasiQGVHGTVAQLGSVGER--------YATAIEVaagnrLNNvVVEDDAVAKEaiELLKRRKagratfl 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1626 ----------------------------------------------------------------KLEGDINELEIALDHA 1641
Cdd:TIGR02169 579 plnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvTLEGELFEKSGAMTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1642 NKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQ 1721
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1722 ANEANAQVSSLTSAKRKLEGEIQAIHADLD---ETLNEYKAAEERSKKAIADatrlaEELRQEQEHSQHVDRLRKGLEQQ 1798
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEeleEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEAR 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1799 LKEIQVRLdEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLID 1878
Cdd:TIGR02169 814 LREIEQKL-NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1879 KLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRASAS 1938
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
888-1429 |
6.97e-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: 84.01 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 888 KLVEEKTSLFTNL-ESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTA----DVQRAKKKIEAEVEALKKQ 962
Cdd:pfam15921 271 QLISEHEVEITGLtEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSqlrsELREAKRMYEDKIEELEKQ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 963 IQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKL----------MEDLQSEEDKGNHQ--- 1029
Cdd:pfam15921 351 LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitIDHLRRELDDRNMEvqr 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1030 ---------NKVKAKLEQTLDDLE---DSLEREKRARADLDKQK---RKVEGELKIAQENIDESGRQRHDLENNLKKKES 1094
Cdd:pfam15921 431 leallkamkSECQGQMERQMAAIQgknESLEKVSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1095 ELHSVSSRLEDEQALVS-KLQ--RQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELgEKLDEQGGATAAQVE 1171
Cdd:pfam15921 511 AIEATNAEITKLRSRVDlKLQelQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1172 VNKKR-EAELAKLRRDLEEANMnhenqlggLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQetsg 1250
Cdd:pfam15921 590 VEKAQlEKEINDRRLELQEFKI--------LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ---- 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1251 KLNNEKLAKqfelqlTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTA-- 1328
Cdd:pfam15921 658 LLNEVKTSR------NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmg 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1329 ---DEEARERQTVAAQAK-NYQHEAEQLQESLEEEI-EGKNEILRQLSKANADiqqwKARFEGEgllkADELEDAKRRQA 1403
Cdd:pfam15921 732 mqkQITAKRGQIDALQSKiQFLEEAMTNANKEKHFLkEEKNKLSQELSTVATE----KNKMAGE----LEVLRSQERRLK 803
|
570 580
....*....|....*....|....*.
gi 17509401 1404 QKINELQEALDAANSKNASLEKTKSR 1429
Cdd:pfam15921 804 EKVANMEVALDKASLQFAECQDIIQR 829
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1653-1953 |
7.00e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1653 KRYQEQVRELQLQVEEEQRNGADTREQffNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSL 1732
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELE--ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1733 TSAKRKLEGEIQAihadldetlneykaAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAA 1812
Cdd:COG1196 294 LAELARLEQDIAR--------------LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1813 alkggkkvIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVE 1892
Cdd:COG1196 360 --------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1893 EAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRASASVAPGLQSSASAAVIR 1953
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
892-1486 |
1.45e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.04 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 892 EKTSLFTNLESTKTQ---LSDAEERLAKLEaQQKDASKQLSELNDQLADNEDRTADVQRAKKKieAEVEALKKQIQDLEM 968
Cdd:COG4913 219 EEPDTFEAADALVEHfddLERAHEALEDAR-EQIELLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 969 SLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLnkekkhqeeinrklmedlqsEEDKGNHQNKVKAKLEQTLDDLEDSLE 1048
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDEL--------------------EAQIRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1049 REKRARADLDKQKRKVEGElkiAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELE 1128
Cdd:COG4913 356 ERERRRARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1129 eelenerqsrskadRAKSDLQRELEELGEKLDEQGGATAAQVEVnkkrEAELAKLRRDLEEANMNHENQLGGLR------ 1202
Cdd:COG4913 433 --------------RRKSNIPARLLALRDALAEALGLDEAELPF----VGELIEVRPEEERWRGAIERVLGGFAltllvp 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1203 KKHTDAVAELTDQLD-----QLNKAKAKVEKDKAQAVrDAEDLAAQLDQETS---GKLNNEkLAKQF---------ELQL 1265
Cdd:COG4913 495 PEHYAAALRWVNRLHlrgrlVYERVRTGLPDPERPRL-DPDSLAGKLDFKPHpfrAWLEAE-LGRRFdyvcvdspeELRR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1266 T------ELQSKADEQSRQLQDftslKGRLHSEN---GDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRtADEEARERQ 1336
Cdd:COG4913 573 HpraitrAGQVKGNGTRHEKDD----RRRIRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1337 TVAAQAKNYQhEAEQLQESLEEEIEGKNEILRQLSKANADIQqwkarfegegllkadELEDAKRRQAQKINELQEALDAA 1416
Cdd:COG4913 648 EALQRLAEYS-WDEIDVASAEREIAELEAELERLDASSDDLA---------------ALEEQLEELEAELEELEEELDEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1417 NSKNASLEKTKSRLVGDLDDAQVDVERANGVAS-----------ALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRN 1485
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelralleerfAAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
.
gi 17509401 1486 T 1486
Cdd:COG4913 792 A 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1142-1874 |
1.67e-15 |
|
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: 82.81 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1142 DRAKSDLQRELEELGEKLDEqggATAAQVEVNKKREA------------ELAKLRRDLEEANMNHENQLGGLRKKHTDA- 1208
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIER---LDLIIDEKRQQLERlrrerekaeryqALLKEKREYEGYELLKEKEALERQKEAIERq 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1209 VAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLN--NEKLAKqFELQLTELQSKADEQSRQLQDFTSLK 1286
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvKEKIGE-LEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1287 GRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEI 1366
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1367 LRQLSKanadIQQWKARFEGEGLLKADELEDAKrrqaQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANG 1446
Cdd:TIGR02169 405 KRELDR----LQEELQRLSEELADLNAAIAGIE----AKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1447 VASALEKKQKGFDKIIDEWRKKTDDLAAELDG--AQRDLRN--------TSTDLFKAKNAQEELAEVVEGLRR-----EN 1511
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGgrAVEEVLKasiqgvhgTVAQLGSVGERYATAIEVAAGNRLnnvvvED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1512 KSLSQE-IKDLTDQlgEGGRS----VHEMQKIIRRLEIEKEE----LQHALDEAEAALEAEESKVLRAQVEVSQI----R 1578
Cdd:TIGR02169 557 DAVAKEaIELLKRR--KAGRAtflpLNKMRDERRDLSILSEDgvigFAVDLVEFDPKYEPAFKYVFGDTLVVEDIeaarR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1579 SEIEKRIQEKEEE-FENTR-----KNHARALESMQASLETEAkgkAELLRIKKKLEGDINELEIALDHANKANADAQKNL 1652
Cdd:TIGR02169 635 LMGKYRMVTLEGElFEKSGamtggSRAPRGGILFSRSEPAEL---QRLRERLEGLKRELSSLQSELRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1653 KRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELL-----VANEAAERARKQAEYEAADARDQANEANA 1727
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKselkeLEARIEELEEDLHKLEEALNDLEARLSHS 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1728 QVSSLTSAKRKLEgeiqAIHADLDETLNEYKAAEERskkaiadatrLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLD 1807
Cdd:TIGR02169 792 RIPEIQAELSKLE----EEVSRIEARLREIEQKLNR----------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 1808 EAEAAaLKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQ 1874
Cdd:TIGR02169 858 NLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
949-1541 |
9.51e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 949 KKKIEAEVEALKKQIQDLEMSLRKAESEKQskdhQIRSLQDEMQQQDEAiaklnKEKKHQEEINRKLMEDLQSEEDKgnh 1028
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDARE----QIELLEPIRELAERY-----AAARERLAELEYLRAALRLWFAQ--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1029 qnKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHD-LENNLKKKESELHSVSSRLEDEQ 1107
Cdd:COG4913 288 --RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1108 ALVSKL-----------QRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLdeqggataAQVEVNKKR 1176
Cdd:COG4913 366 ALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI--------ASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1177 -EAELAKLRRDLEEA---------------NMNHENQ---------LGGLR------KKHTDAVAELTDQLD-----QLN 1220
Cdd:COG4913 438 iPARLLALRDALAEAlgldeaelpfvgeliEVRPEEErwrgaiervLGGFAltllvpPEHYAAALRWVNRLHlrgrlVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1221 KAKAKVEKDKAQAVrDAEDLAAQLDQETS---GKLNNEkLAKQF---------ELQLT------ELQSKADEQSRQLQDf 1282
Cdd:COG4913 518 RVRTGLPDPERPRL-DPDSLAGKLDFKPHpfrAWLEAE-LGRRFdyvcvdspeELRRHpraitrAGQVKGNGTRHEKDD- 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1283 tslKGRLHSEN---GDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRtadeearERQTVAAQAknyqheaeqlqesleee 1359
Cdd:COG4913 595 ---RRRIRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEA-------ELDALQERR----------------- 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1360 iegknEILRQLSKANADIQQWKArfegegllkadeledAKRRQAQKINELqEALDAANSKNASLEKTKSRLVGDLDDAQV 1439
Cdd:COG4913 648 -----EALQRLAEYSWDEIDVAS---------------AEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1440 DVERANGVASALEKKqkgfdkiIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRenkSLSQEIK 1519
Cdd:COG4913 707 ELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE---NLEERID 776
|
650 660
....*....|....*....|..
gi 17509401 1520 DLTDQLgegGRSVHEMQKIIRR 1541
Cdd:COG4913 777 ALRARL---NRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
972-1688 |
4.64e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.75 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 972 KAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKkhqeeinrklmedLQSEEDKGNHQNKVKaKLEQTLDDLEDSLEREK 1051
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNL-------------NKDEEKINNSNNKIK-ILEQQIKDLNDKLKKNK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1052 RARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEEL 1131
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1132 ENERQSRSKADRAKSDLQRELEELGEKLdeqggataAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAE 1211
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1212 LTDQLDQLNKAKAKVEKDKaqavrdaedlaAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDftSLKGRLHS 1291
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIK-----------KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1292 ENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQaknyqheaeqlqesleeeIEGKNEILRQLS 1371
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE------------------LEEKQNEIEKLK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1372 KANADIQQWKARFEgeglLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASAL 1451
Cdd:TIGR04523 377 KENQSYKQEIKNLE----SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1452 EKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLfKAKNAQeelaevVEGLRRENKSLSQEIKDLTDQlgeggrs 1531
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL-KSKEKE------LKKLNEEKKELEEKVKDLTKK------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1532 VHEMQKIIRRLEIEKEELQhaldeaeAALEAEESKVLRAQVEVSqiRSEIEKRIQEKEEEFENTrKNHARALESMQASLE 1611
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKE-------SKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEEL-KQTQKSLKKKQEEKQ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1612 TEAKGK-AELLRIKKKLEGD---INELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRA 1687
Cdd:TIGR04523 589 ELIDQKeKEKKDLIKEIEEKekkISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKI 668
|
.
gi 17509401 1688 T 1688
Cdd:TIGR04523 669 K 669
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
856-1525 |
6.58e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.37 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 856 EELEKINDKVKALEDSlakeeklrkeleessaklveektslftnlestktqLSDAEERLAKLEAQQKDASKQLSELNDQL 935
Cdd:TIGR04523 47 NELKNKEKELKNLDKN-----------------------------------LNKDEEKINNSNNKIKILEQQIKDLNDKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 936 ADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQ-------IRSLQDEMQQQDEAIAKLNKEKKHQ 1008
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNidkflteIKKKEKELEKLNNKYNDLKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1009 EEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVegelKIAQENIDESGRQRHDLENN 1088
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN----NQLKDNIEKKQQEINEKTTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1089 LKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAK-SDLQRELEELGEKLDEQGGATA 1167
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1168 AQVEVNKKREAELAKLRRDLEEANMNHENQlgglrkkhtdaVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQE 1247
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESE-----------NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1248 TSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRT 1327
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1328 ADEEARERQTVAAQAKNYQHEaeqlqesleeeIEGKNEILRQLSKANADIQQWKARFegegLLKADELEDAKRRQAQKIN 1407
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKE-----------LKKLNEEKKELEEKVKDLTKKISSL----KEKIEKLESEKKEKESKIS 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1408 ELQEALDAANSknaslEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTS 1487
Cdd:TIGR04523 542 DLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
650 660 670
....*....|....*....|....*....|....*...
gi 17509401 1488 TDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQL 1525
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
28-72 |
1.01e-13 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 67.07 E-value: 1.01e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 17509401 28 DSKKNVWIPDPEEGYLAGEITATKGDQVTIVTARGNEVTLKKELV 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
853-1232 |
1.25e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.65 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 853 KEAEELEKINDKVKALEDSLAKeeklrkeleessakLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELN 932
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSS--------------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 933 DQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRK-----AESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKH 1007
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKleealNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1008 QEEINRKLMEDLQSEEDKGNHqnkvkakLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLEN 1087
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQE-------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1088 NLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISEleeelenerqsrskadraKSDLQRELEELGEKLDEQGGATA 1167
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA------------------LEEELSEIEDPKGEDEEIPEEEL 951
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1168 AQVEVNKKREAELAKLrRDLEEANMnhenqlgglrkKHTDAVAELTDQLDQLNKAKAKVEKDKAQ 1232
Cdd:TIGR02169 952 SLEDVQAELQRVEEEI-RALEPVNM-----------LAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
853-1672 |
1.30e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.93 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 853 KEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELN 932
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 933 DQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSlrKAESEKQSKDHQIRSLQDEmQQQDEAIAKLNKEKKHQEEI- 1011
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE--IEELEKELKELEIKREAEE-EEEEELEKLQEKLEQLEEELl 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1012 --NRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNL 1089
Cdd:pfam02463 377 akKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1090 KKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQ 1169
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1170 VEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAK--VEKDKAQAVRDAEDLAAQLDQE 1247
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiAVLEIDPILNLAQLDKATLEAD 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1248 TSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAesQVNQLTRLKSQLTSQLEearrt 1327
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT--KELLEIQELQEKAESEL----- 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1328 adEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKIN 1407
Cdd:pfam02463 690 --AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1408 ELQEaldaaNSKNASLEKTKSRLvgdlddaqvdvERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTS 1487
Cdd:pfam02463 768 ELSL-----KEKELAEEREKTEK-----------LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1488 TDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKV 1567
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1568 LRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQAS--LETEAKGKAELLRIKKKLEGDINELEIALDHANKAN 1645
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENnkEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
810 820
....*....|....*....|....*..
gi 17509401 1646 ADAQKNLKRYQEQVRELQLQVEEEQRN 1672
Cdd:pfam02463 992 KDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1302-1935 |
3.72e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1302 DAESQVNQLTRLKSQLtsqlEEARRTADEEARERQTVAaQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWK 1381
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSY----KDFDFDAKEDNRADEATE-EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1382 ARfEGEGLLKADELEDAKR----RQAQKINELQEALDAANSKNASlektKSRLVGDLDDAQvDVERANGVASALEKKQKG 1457
Cdd:PTZ00121 1136 AE-DARKAEEARKAEDAKRveiaRKAEDARKAEEARKAEDAKKAE----AARKAEEVRKAE-ELRKAEDARKAEAARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1458 FDKIIDEWRKKTDDLAAEldgAQRDLRNTSTDLFKAKNAQEElAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQK 1537
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAE---AVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1538 iirrleiekEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGK 1617
Cdd:PTZ00121 1286 ---------AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1618 AELLRIKKKLEGDINELEIAldhanKANADAQKNLKRYQEQVRELQLQVEEEQRNgADTREQFFNAEKRATLLQSEKEEL 1697
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEA-----KKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEK 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1698 LVANEAAERARKQAEyeAADARDQANEANAQVSSLTSAKRKLEGEiqaihaDLDETLNEYKAAEERSKKAiADATRLAEE 1777
Cdd:PTZ00121 1431 KKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEAKKAD------EAKKKAEEAKKADEAKKKA-EEAKKKADE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1778 LRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVR 1857
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1858 ELQFQVDEDKKNFERLQDLIDKLQQK----------LKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEE-RADQAENSL 1926
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMkaeeakkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKI 1661
|
....*....
gi 17509401 1927 SKMRSKSRA 1935
Cdd:PTZ00121 1662 KAAEEAKKA 1670
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
895-1416 |
4.65e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 895 SLFTNLESTKTQLSDAEER---LAKLEAQQKDASKQLSELNDQlaDNEDRTADVQRAKKKI---EAEVEALKKQIQDLEM 968
Cdd:COG4913 232 EHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLellEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 969 SLRKAESEKQSKDHQIRSLQDEMQQQD--------EAIAKLNKEKKHQEEINRKLMEDLQ--------SEEDKGNHQNKV 1032
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAalglplpaSAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1033 KA---KLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQE---NID-ESGRQRHDLENNLKKKESE---------- 1095
Cdd:COG4913 390 AAlleALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPaRLLALRDALAEALGLDEAElpfvgeliev 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1096 --------------LHSVSSRL--EDEQ-ALVSKLQRQIKDGQsRISELEEELENERQSRSKADR-------------AK 1145
Cdd:COG4913 470 rpeeerwrgaiervLGGFALTLlvPPEHyAAALRWVNRLHLRG-RLVYERVRTGLPDPERPRLDPdslagkldfkphpFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1146 SDLQREL------------EEL-------------------GEKLDEQ--------GGATAAQVEVnkkREAELAKLRRD 1186
Cdd:COG4913 549 AWLEAELgrrfdyvcvdspEELrrhpraitragqvkgngtrHEKDDRRrirsryvlGFDNRAKLAA---LEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1187 LEEAnmnhENQLGGLRkkhtDAVAELTDQLDQLNKAKAKV--EKDKAQAVRDAEDLAAQLDQ--ETSGKLnneklaKQFE 1262
Cdd:COG4913 626 LAEA----EERLEALE----AELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELERldASSDDL------AALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1263 LQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQ-LTSQLEEARRTADEEARERQTVAAQ 1341
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1342 AKNYQHEAEQLQESLEEEIEGKNEILRQLS----------KANADIQQWKARFEGEGLLKA-DELEDAKRRQA-QKINEL 1409
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAFNREWPaetadldadlESLPEYLALLDRLEEDGLPEYeERFKELLNENSiEFVADL 851
|
....*..
gi 17509401 1410 QEALDAA 1416
Cdd:COG4913 852 LSKLRRA 858
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
934-1550 |
9.87e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 934 QLADNEDRTADVQRAKKKIEAEVEALKKQIQ---DLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEE 1010
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1011 InRKLMEDLQSEEDKgnhQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIdesgrqrhDLENNLK 1090
Cdd:PRK03918 236 L-KEEIEELEKELES---LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI--------KLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1091 KKESELHSVSSRLEDEQALVSKLQRQIKDGqsriseleeelenerqsrskadrakSDLQRELEELGEKLDEQggataaqv 1170
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKEL-------------------------EEKEERLEELKKKLKEL-------- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1171 evnKKREAELAKLRRDLEEAnMNHENQLGGLRKKHTD-AVAELTDQLDQLNKAKAKVEKDkaqaVRDAEDLAAQLDQETS 1249
Cdd:PRK03918 351 ---EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1250 GKLNNEKLAKQFELQLTELQSKADEQSRQlqdftSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTAD 1329
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1330 EEarerqTVAAQAKNYQHEaeqLQESLEEEIEGKNEILRQLSKANADIqqwkarfEGEGLLKADELEdakrrqaqKINEL 1409
Cdd:PRK03918 498 LK-----ELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKL-------KGEIKSLKKELE--------KLEEL 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1410 QEALDAANSKNASLEKTKSRLVGDLDDAQV-DVERANGVASALEK------KQKGFDKIIDEWRKKTDDLAAELDGAQRD 1482
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEE 634
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1483 LRNTSTDLFKAKNAQEEL-----AEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQ 1550
Cdd:PRK03918 635 LAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1207-1797 |
1.18e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1207 DAVAELTDQLDQLNKAKAKVEKDKAQ------AVRDAEDLAAQLDQETSGKLNNEKLAKQF-ELQLTELQSKADEQSRQL 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQiellepIRELAERYAAARERLAELEYLRAALRLWFaQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1280 QDFTSLKGRLHSENGDLVRQLEDAESQVNQL-TRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQEslee 1358
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1359 eiegknEILRQLSKANADIQQWKARfegegllkADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRL-------- 1430
Cdd:COG4913 381 ------EFAALRAEAAALLEALEEE--------LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllalr 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1431 ----------------VGDL-----DDAQ-----------------VDVERANGVASALEKKQKG----FDKIIDEWRKK 1468
Cdd:COG4913 447 dalaealgldeaelpfVGELievrpEEERwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRgrlvYERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1469 T------DDLAAELDGAQRDLRNTstdlfkaknAQEELAEV--------VEGLRRENKSLSQE--IKdltdqlGEGGRSV 1532
Cdd:COG4913 527 ErprldpDSLAGKLDFKPHPFRAW---------LEAELGRRfdyvcvdsPEELRRHPRAITRAgqVK------GNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1533 HEMQKIIRR--------------LEIEKEELQhaldeAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKN 1598
Cdd:COG4913 592 KDDRRRIRSryvlgfdnraklaaLEAELAELE-----EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1599 HAR--ALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADT 1676
Cdd:COG4913 667 EREiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1677 REQFFnAEKRATLLQSEKEELLVAN-----EAAERARKQAEYEAADARDQANEA-NAQVSSLTSAKRKLEgEIQAIHADL 1750
Cdd:COG4913 747 LRALL-EERFAAALGDAVERELRENleeriDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLP-EYLALLDRL 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1751 DET-LNEYKA--AEERSKKAIADATRLAEELRQEQEH-SQHVDRLRKGLEQ 1797
Cdd:COG4913 825 EEDgLPEYEErfKELLNENSIEFVADLLSKLRRAIREiKERIDPLNDSLKR 875
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
896-1146 |
1.68e-12 |
|
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: 71.33 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 896 LFTNLESTKTQLSDAEERLAKLEaqqkdasKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAES 975
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 976 EKQSKDHQIRSLQDEMQQQDEAIAKLNKeKKHQEEINRKLMEDLQSEEdkGNHQNKVKAKLEQTLDDLEDSLEREKRARA 1055
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLR-ALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1056 DLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENER 1135
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|.
gi 17509401 1136 QSRSKADRAKS 1146
Cdd:COG4942 241 ERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
887-1333 |
2.92e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 887 AKLVEEKTSLFT----NLESTKTQLSDAEERLAKLEAQQKdaskQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQ 962
Cdd:COG4717 49 ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 963 IQ--DLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQseedkgnhqnKVKAKLEQTL 1040
Cdd:COG4717 125 LQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE----------QLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1041 DDLEDSLEREKRARADLDKQKRKVEGELKIAQENID--ESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIK 1118
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1119 DG------------QSRISELEEELENERQSRSKADRAKSDL-QRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRR 1185
Cdd:COG4717 275 IAgvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELeEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1186 DLEEAN------MNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKdkaqavrdAEDLAAQLDQetsgkLNNEKLAK 1259
Cdd:COG4717 355 EAEELEeelqleELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--------LEELEEQLEE-----LLGELEEL 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1260 QFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQvNQLTRLKSQLTSQLEEARRTADEEAR 1333
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAA 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
899-1476 |
2.92e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 899 NLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEM---SLRKAES 975
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 976 EKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLmEDLQSEEDK-------GNHQNKVKAKLEQTLDDLEDSLE 1048
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1049 REKRARADLDKQKRKVEGELKIAQENIDESGR--QRHDLENNLKKKESELHSVSSRLEDEQalVSKLQRQIKdgqsrise 1126
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEEAKAKKEELERLKKRLTGLT--PEKLEKELE-------- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1127 leeelenerqsrsKADRAKSDLQRELEELGEK---LDEQGGATAAQVEVNKKREAELAKLRRDLEEanmnhENQLGGLRK 1203
Cdd:PRK03918 395 -------------ELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTE-----EHRKELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1204 KHTD------AVAELTDQLDQLNKAKAKVEK--DKAQAVRDAEDLAAQLD--QETSGKLNNEKLAKQFElQLTELQSKAD 1273
Cdd:PRK03918 457 YTAElkriekELKEIEEKERKLRKELRELEKvlKKESELIKLKELAEQLKelEEKLKKYNLEELEKKAE-EYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1274 EQSRQLQdftSLKGRLHSENgDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARER-------QTVAAQAKNYQ 1346
Cdd:PRK03918 536 KLKGEIK---SLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1347 HEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGeglLKADELEDAKRRQAQKINELQEALDAANSKNASLEKT 1426
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE---LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 17509401 1427 KSRLVGDLDDAQVDVERANGVASALEKKQKGFDKiIDEWRKKTDDLAAEL 1476
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1298-1810 |
6.51e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1298 RQLEDAESQVNQLTRLKsqltsQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESleeeiegkneilRQLSKANADI 1377
Cdd:COG4913 242 EALEDAREQIELLEPIR-----ELAERYAAARERLAELEYLRAALRLWFAQRRLELLE------------AELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1378 QQWKARfegegllkADELEDAKRRQAQKINELQEALDAANSKN-ASLEKTKSRLVGDLDDAQVDVERANGVASALEKK-- 1454
Cdd:COG4913 305 ARLEAE--------LERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPlp 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1455 --QKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEG-GRS 1531
Cdd:COG4913 377 asAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1532 VHEMQ-----------------------------------------KIIRRLEIEK----EELQHALDEAEAALEAEESK 1566
Cdd:COG4913 457 EAELPfvgelievrpeeerwrgaiervlggfaltllvppehyaaalRWVNRLHLRGrlvyERVRTGLPDPERPRLDPDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1567 VLRAQVEVSQIRSEIEKRIQ--------EKEEEFentrKNHARALES---MQASLETEAKGKAELLR---------IKKK 1626
Cdd:COG4913 537 AGKLDFKPHPFRAWLEAELGrrfdyvcvDSPEEL----RRHPRAITRagqVKGNGTRHEKDDRRRIRsryvlgfdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1627 --LEGDINELEIALDHANKANADAQKNLKRYQEQVRELQlQVEEEQRNGADTREqffnAEKRATLLQSEKEELLVAN--- 1701
Cdd:COG4913 613 aaLEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS----AEREIAELEAELERLDASSddl 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1702 EAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLdetlneykaaEERSKKAIADATRLAEELRQE 1781
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL----------EAAEDLARLELRALLEERFAA 757
|
570 580
....*....|....*....|....*....
gi 17509401 1782 QEHSQHVDRLRKGLEQQLKEIQVRLDEAE 1810
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAE 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1625-1945 |
7.19e-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: 70.86 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1625 KKLEGDINELEIALDHAnKANADAQKNLKRYQEQVRELQLQVeeeqrngADTREQFFNAEKRATLLQSEKEELLVANEAA 1704
Cdd:TIGR02168 189 DRLEDILNELERQLKSL-ERQAEKAERYKELKAELRELELAL-------LVLRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1705 ERARKQAEYEAADAR-----DQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELR 1779
Cdd:TIGR02168 261 ELQELEEKLEELRLEvseleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1780 QeqehsqhvdrlrkgLEQQLKEIQVRLDEAEAAaLKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVREL 1859
Cdd:TIGR02168 341 E--------------LEEKLEELKEELESLEAE-LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1860 QFQVDEDKKNFERLQDLI-----DKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSR 1934
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330
....*....|.
gi 17509401 1935 ASASVAPGLQS 1945
Cdd:TIGR02168 486 QLQARLDSLER 496
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1085-1917 |
1.17e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.39 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1085 LENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGG 1164
Cdd:pfam02463 147 IAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1165 ATAAQVEVNKKREAELAKLRRDLEEanmnHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQL 1244
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQE----EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1245 DQETSGKL-------NNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQL 1317
Cdd:pfam02463 303 LKLERRKVddeeklkESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1318 TSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANaDIQQWKARFEGEGLLKADELED 1397
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI-ELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1398 AKRRQAQKInELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELD 1477
Cdd:pfam02463 462 KDELELKKS-EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1478 GAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDqlgEGGRSVHEMQKIIRRLEIEKEELQHALDEAE 1557
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK---LKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1558 AALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIA 1637
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1638 LDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAAD 1717
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1718 ARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKaiadatrlAEELRQEQEHSQHVDRLRKGLEQ 1797
Cdd:pfam02463 778 EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ--------EEKIKEEELEELALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1798 QLKEIQVRLDEAEAAALKG-GKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDL 1876
Cdd:pfam02463 850 KLAEEELERLEEEITKEELlQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 17509401 1877 IDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEE 1917
Cdd:pfam02463 930 LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1330 |
1.87e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 843 GKVKPMLKAGKEAEE-----LEKINDKVKALEDSLAK----------EEKLRKELEESSAKLVEEKTSLFTNLESTKTQL 907
Cdd:PRK03918 168 GEVIKEIKRRIERLEkfikrTENIEELIKEKEKELEEvlreineissELPELREELEKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 908 SDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEaEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSL 987
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 988 QDEMQQQDEAIAKLNKEKKHQEEINRKLME------DLQSEEDKGNHQNKVKAKLE-QTLDDLEDSLEREKRARADLDKQ 1060
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1061 KRKVEG-----------------ELKIAQENIDESGRQ--RHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKD-- 1119
Cdd:PRK03918 407 ISKITArigelkkeikelkkaieELKKAKGKCPVCGREltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREle 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1120 ----GQSRISELEEELENERQSRSK-----ADRAKSDlQRELEELGEKLDEQGG---ATAAQVEVNKKREAELAKLRRDL 1187
Cdd:PRK03918 487 kvlkKESELIKLKELAEQLKELEEKlkkynLEELEKK-AEEYEKLKEKLIKLKGeikSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1188 EEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAK------VEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQF 1261
Cdd:PRK03918 566 DELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1262 ELQLTELQSKADEQsrQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADE 1330
Cdd:PRK03918 646 RKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
892-1434 |
1.97e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 892 EKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRtadvqrakkkiEAEVEALKKQIQDLEMSLR 971
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-----------REELETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 972 KAESEKQSKDHQIRSLQDEMQQQDEAIAKLnKEKKHQEEINRKLMEDLQSEedkgnhqnkvkakLEQTLDDLEDSLEREK 1051
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDL-LAEAGLDDADAEAVEARREE-------------LEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1052 RARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEEL 1131
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1132 ENERQSRSKADRAKSDLQRELEELGEKLDE--------------QGGATAAQVEVNKKREAELAKLRRDLEEAnmnhENQ 1197
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEaealleagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDL----EEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1198 LGGLRKKHTDAV--AELTDQLDQLNKAKAKVEK---DKAQAVRDAEDLAAQLDQEtSGKLNNEklAKQFELQLTELQSKA 1272
Cdd:PRK02224 491 VEEVEERLERAEdlVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRER-AAELEAE--AEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1273 DEQSRQLQDF----TSLKGRLHSEN--GDLVRQLEDAESQVNQLTRLKSQLTSQLEEAR-RTADEEARERQTVAAQAKNY 1345
Cdd:PRK02224 568 EEAREEVAELnsklAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDERReRLAEKRERKRELEAEFDEAR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1346 QHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEgllkADELEDAKRRQAQkINELQEALDAANSKNASLEK 1425
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE----LEELEELRERREA-LENRVEALEALYDEAEELES 722
|
....*....
gi 17509401 1426 TKSRLVGDL 1434
Cdd:PRK02224 723 MYGDLRAEL 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1292-1935 |
2.00e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1292 ENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEearerqtvaAQAKNYQHEaeqlqesleeeieGKNEILRQLS 1371
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE---------ADEVLEEHE-------------ERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1372 KANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNAS----------LEKTKSRLVGDLDDAQVDV 1441
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADaeavearreeLEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1442 ERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRntstdlfKAKNAQEELAEVVEglrrenkSLSQEIKDL 1521
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIE-------ELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1522 TDQLGEggrsvhemqkiirrLEIEKEELQHALDEaeaaleaeeskvLRAQV-EVSQIRSEIEKRIQEKEEEFENTR---- 1596
Cdd:PRK02224 404 PVDLGN--------------AEDFLEELREERDE------------LREREaELEATLRTARERVEEAEALLEAGKcpec 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1597 ------KNHARALEsmqaslETEAKgKAELLRIKKKLEGDINELEIALDHANKAnADAQKNLKRYQEQvRELQLQVEEEQ 1670
Cdd:PRK02224 458 gqpvegSPHVETIE------EDRER-VEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEER-REDLEELIAER 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1671 RNGADTREQffnaekRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEgeiqAIHADL 1750
Cdd:PRK02224 529 RETIEEKRE------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1751 DEtlneykaaeerskkaIADATRLAEELRQEQEHSQHVDRLRKgleQQLKEiqvrldeaeaaalkggkkviakLEQRVRE 1830
Cdd:PRK02224 599 AA---------------IADAEDEIERLREKREALAELNDERR---ERLAE----------------------KRERKRE 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1831 LESELDGEqrRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANlnlqkykqlTH 1910
Cdd:PRK02224 639 LEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN---------RV 707
|
650 660
....*....|....*....|....*.
gi 17509401 1911 Q-LEDAEERADQAENSLSKMRSKSRA 1935
Cdd:PRK02224 708 EaLEALYDEAEELESMYGDLRAELRQ 733
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1055 |
2.35e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.87 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 850 KAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLS 929
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 930 ELNDQLAD------------------NEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEM 991
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 992 QQQDEAIAKLNKEKKHQEeinrKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARA 1055
Cdd:COG4942 181 AELEEERAALEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1393-1932 |
3.50e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1393 DELEDAKRRQA--QKINELQEALDAANSKNASLEKTKSRLvgDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTD 1470
Cdd:COG4913 242 EALEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1471 DLAAELDGAQRDLRNtstdlfkaknaqeelaevvEGLRREnKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEK---- 1546
Cdd:COG4913 320 ALREELDELEAQIRG-------------------NGGDRL-EQLEREIERLERELEERERRRARLEALLAALGLPLpasa 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1547 ---EELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEF---ENTRKNHARALESMQASLETEAKGKAEL 1620
Cdd:COG4913 380 eefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIaslERRKSNIPARLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1621 LRIkkklegdINEL-EIALDHANKANAdaqknLKRYQEQVReLQLQVEEEQRNGAdtrEQFFNAEKRATLLQSEKEELLV 1699
Cdd:COG4913 460 LPF-------VGELiEVRPEEERWRGA-----IERVLGGFA-LTLLVPPEHYAAA---LRWVNRLHLRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1700 ANEAAERARKQA-----EYEAADARDQANE-------------------------ANAQVSSLT---------------- 1733
Cdd:COG4913 524 PDPERPRLDPDSlagklDFKPHPFRAWLEAelgrrfdyvcvdspeelrrhpraitRAGQVKGNGtrhekddrrrirsryv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1734 ---SAKRKLEgEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRkGLEQQLKEIQVRLDEAE 1810
Cdd:COG4913 604 lgfDNRAKLA-ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1811 AaalkgGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQ 1890
Cdd:COG4913 682 A-----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 17509401 1891 VEEAEELANlnlQKYKQLTHQLEDAEERADQAENSLSKMRSK 1932
Cdd:COG4913 757 AALGDAVER---ELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
895-1519 |
3.92e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 68.71 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 895 SLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSE----LNDQLADNEDRT--------ADVQRAKKKIEAeVEALKKQ 962
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETLIASRQEERQETSAELNQllrtLDDQWKEKRDELngelsaadAAVAKDRSELEA-LEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 963 IQDLEMSLRKAESEkqskdhQIRSLQDEMQQQdeaiaklNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVK-AKLEQTLD 1041
Cdd:pfam12128 334 FLDADIETAAADQE------QLPSWQSELENL-------EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1042 DLEDSLEREKRA-RADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQR-QIKD 1119
Cdd:pfam12128 401 KIREARDRQLAVaEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERaREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1120 GQSR--ISELEEELENERQSRSKADRAKSD-------LQRELEELGEKLDEQGGA-------TAAQVEVNKKREAELAKL 1183
Cdd:pfam12128 481 EAANaeVERLQSELRQARKRRDQASEALRQasrrleeRQSALDELELQLFPQAGTllhflrkEAPDWEQSIGKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1184 RR-----DLEEANMNHENQLGGLRkKHTDA--VAELTDQLDQLNKAKAKVEKdkaqAVRDAEDLAAQLDQE---TSGKLn 1253
Cdd:pfam12128 561 HRtdldpEVWDGSVGGELNLYGVK-LDLKRidVPEWAASEEELRERLDKAEE----ALQSAREKQAAAEEQlvqANGEL- 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1254 nEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLhseNGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEAR 1333
Cdd:pfam12128 635 -EKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1334 ERQTvaaQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANAD-IQQWKAR------FEGEGLLK-ADELEDAKRRQAQK 1405
Cdd:pfam12128 711 EART---EKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRdlaslgVDPDVIAKlKREIRTLERKIERI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1406 INELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLR- 1484
Cdd:pfam12128 788 AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRc 867
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17509401 1485 -----NTSTDLFKAKNAQEELAEV---VEGLRRENKSLSQEIK 1519
Cdd:pfam12128 868 emsklATLKEDANSEQAQGSIGERlaqLEDLKLKRDYLSESVK 910
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1462-1930 |
6.97e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1462 IDEWRKKTDDLAAELDGAQRDLRntstDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRR 1541
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1542 L-EIEKEELQHALDEAEAALEAEESKVLRAQVE-VSQIRSEIEKRIQEKE------EEFENTRKNHARALESMQASLET- 1612
Cdd:PRK03918 285 LkELKEKAEEYIKLSEFYEEYLDELREIEKRLSrLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELy 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1613 -EAKGK-AELLRIKKKLEG-DINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATL 1689
Cdd:PRK03918 365 eEAKAKkEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1690 LQSEKEELLVANEAAERARKQAEYEAADARDQANEAN--------AQVSSLTSAK------RKLEGEIQAIHA-DLDETL 1754
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKElrelekvlKKESELIKLKelaeqlKELEEKLKKYNLeELEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1755 NEYKAAEERSKKAIADATRLAEELRQEQEhsqhVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELES- 1833
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPf 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1834 -----ELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKtqkkqVEEAEELANLNLQK---Y 1905
Cdd:PRK03918 601 yneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-----EEEYEELREEYLELsreL 675
|
490 500
....*....|....*....|....*
gi 17509401 1906 KQLTHQLEDAEERADQAENSLSKMR 1930
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLK 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
949-1332 |
2.07e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 949 KKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEM---QQQDEAIAK----LNKEKKHQEEINRKLMEDLQS 1021
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdaSRKIGEIEKeieqLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1022 EEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLdkqkrkvegELKIAQENIDESGRQRHDLENNLKKKESELHSVSS 1101
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1102 RLEDEQALVSKLQRQIKDGQSRISEleeelenerqsrskADRAKSDLQRELEELGEKLDEqggaTAAQVEVNKKREAELA 1181
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRID--------------LKEQIKSIEKEIENLNGKKEE----LEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1182 KLRRDLEEANMNHENQLGGLRKKhtdavaeltdqldqLNKAKAKVEKDKAQAVRDAEDLAAQLDQETS--GKLNNEKLAK 1259
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERK--------------IEELEAQIEKKRKRLSELKAKLEALEEELSEieDPKGEDEEIP 947
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1260 QFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQL---TSQLEEARRTADEEA 1332
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIlerIEEYEKKKREVFMEA 1023
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1029-1289 |
2.65e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1029 QNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELhsvsSRLEDEQA 1108
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1109 lvsKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLE 1188
Cdd:COG4942 94 ---ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1189 EAnmnhenqlgglRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQEtsgklnnEKLAKQFELQLTEL 1268
Cdd:COG4942 171 AE-----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEALIARL 232
|
250 260
....*....|....*....|...
gi 17509401 1269 QSKADEQSRQL--QDFTSLKGRL 1289
Cdd:COG4942 233 EAEAAAAAERTpaAGFAALKGKL 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
924-1151 |
3.30e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 924 ASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNK 1003
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1004 EKKHQEEINRKLMEDLQSeEDKGNHQNKVKAkLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRH 1083
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGS-ESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1084 DLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRE 1151
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
887-1341 |
3.83e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 887 AKLVEEKTSLFTNLESTKTQLSDAEERLAKLE--------------AQQKDASKQLSELNDQLADNEDRTADVQRAKKKI 952
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEeerddllaeaglddADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 953 EAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKkhqeEINRKLMEDlqSEEDKGNhqnkV 1032
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI----EELRERFGD--APVDLGN----A 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1033 KAKLEQTLDDLEDSLEREKRARADLDK-QKRKVEGELKIAQ----------------ENIDESGRQRHDLENNLKKKESE 1095
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTaRERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1096 LHSVSSRLEDEQALV------SKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKldeqggATAAQ 1169
Cdd:PRK02224 491 VEEVEERLERAEDLVeaedriERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA------AAEAE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1170 VEVNKKREaELAKLRRDLEEANmnheNQLGGLRKKHT--DAVAELTDQLDQLN---KAKAKVE---KDKAQAVRD-AEDL 1240
Cdd:PRK02224 565 EEAEEARE-EVAELNSKLAELK----ERIESLERIRTllAAIADAEDEIERLRekrEALAELNderRERLAEKRErKREL 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1241 AAQLDQETSGKLNNEKlaKQFELQLTELQSKADEQSRQlqdftslKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLtsq 1320
Cdd:PRK02224 640 EAEFDEARIEEAREDK--ERAEEYLEQVEEKLDELREE-------RDDLQAEIGAVENELEELEELRERREALENRV--- 707
|
490 500
....*....|....*....|.
gi 17509401 1321 leEARRTADEEARERQTVAAQ 1341
Cdd:PRK02224 708 --EALEALYDEAEELESMYGD 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
890-1312 |
4.11e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 890 VEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELndqlaDNEDRTADVQRAKKKIEAEVEALKKQIQDLEMS 969
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 970 LRKAESEKQskdhQIRSLQDEMQQQDEAIAKLnkekkhQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLER 1049
Cdd:COG4717 148 LEELEERLE----ELRELEEELEELEAELAEL------QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1050 EKRARADLDKQKRKVEGELKIAQEN---------------------------------------------IDESGRQRHD 1084
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEerlkearlllliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1085 LENNLKKKESELHSVSSRLEDE--QALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRE--LEELGEKLD 1160
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1161 EQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAV-AELTDQLDQLNKAKAKVEKDKAQAVRDAED 1239
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 1240 LAAQLDQ-ETSGKLnnEKLAKQFELQLTELQSKADEQSRQ---LQDFTSLKGRLHSENGDLVrqLEDAESQVNQLTR 1312
Cdd:COG4717 458 LEAELEQlEEDGEL--AELLQELEELKAELRELAEEWAALklaLELLEEAREEYREERLPPV--LERASEYFSRLTD 530
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
888-1550 |
7.73e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.22 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 888 KLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLAdNEDRTADVQRAKKKIEAEVEALKKQIQDLE 967
Cdd:TIGR00618 198 LLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 968 MSLRKAESEKQSKDHQIRSLQD-----EMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDD 1042
Cdd:TIGR00618 277 AVLEETQERINRARKAAPLAAHikavtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1043 LEDSLEREKRARADLDKQKRKVEgELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQR---QIKD 1119
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHakkQQEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1120 GQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREA---ELAKLRRDLEEA--NMNH 1194
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLArllELQEEPCPLCGSciHPNP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1195 ENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVE-------------KDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQF 1261
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltserkqraslKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1262 ELQLTELQSKADEQSRQLQDFTSLKGrlhsengdlvrQLEDAESQVNQLTRLKSQLTSQLEEAR-RTADEEARERQTVAA 1340
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLRKL-----------QPEQDLQDVRLHLQQCSQELALKLTALhALQLTLTQERVREHA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1341 QAKNYQHEAEQLQEsleeeiegkneiLRQLSKANADIQQWKARFEG--EGLLKADELEDAKRRQAQKINELQEALDAANS 1418
Cdd:TIGR00618 665 LSIRVLPKELLASR------------QLALQKMQSEKEQLTYWKEMlaQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1419 KNASLEKTKSRLVGDLDDAQVDVERangvASALEKKQKGFDKIIDEWR-KKTDDLAAELDGAQRdLRNTSTDLFKAKNAQ 1497
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLK----ARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNR-LREEDTHLLKTLEAE 807
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1498 --EELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQ 1550
Cdd:TIGR00618 808 igQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
922-1867 |
1.12e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.91 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 922 KDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKaesekqskdhqIRSLQDEMQQQDEAIAKL 1001
Cdd:TIGR00606 213 KQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK-----------IMKLDNEIKALKSRKKQM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1002 NKEKKHQEEINRKLME--DLQSEEDKGNHQNKVKAKlEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDEsg 1079
Cdd:TIGR00606 282 EKDNSELELKMEKVFQgtDEQLNDLYHNHQRTVREK-ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADR-- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1080 RQRHDLENNLKKKESELHSVSSRLE---DEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADraksdlQRELEELG 1156
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFErgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLK------QEQADEIR 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1157 EKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLG---GLRKKHTD-AVAELTDQLDQLNKAKAKVEKDKAQ 1232
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEldqELRKAERElSKAEKNSLTETLKKEVKSLQNEKAD 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1233 AVRDAEDLA---AQLDQETSGKLNNEKLAKQfelQLTELQSKADEQSRQLQDFTSLKGRLHSENgDLVRQLEDAESQVNQ 1309
Cdd:TIGR00606 513 LDRKLRKLDqemEQLNHHTTTRTQMEMLTKD---KMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1310 LTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQ---------HEAEQLQESLEEEIEGKNEILRQLSKANADIQQW 1380
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1381 KARFEGEG---LLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVEranGVASALEKKQKg 1457
Cdd:TIGR00606 669 ITQLTDENqscCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP---GRQSIIDLKEK- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1458 fdkiidewrkktddlaaELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTdqlgeggrsvhemqk 1537
Cdd:TIGR00606 745 -----------------EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT--------------- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1538 IIRRLEIEKEELQHALDEAEAALEAeeskvlraqVEVSQIRSEIEKRIQEKEEEfentrknharaLESMQASLETEAKGK 1617
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQG---------SDLDRTVQQVNQEKQEKQHE-----------LDTVVSKIELNRKLI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1618 AELLRIKKKLEGDINELEIALDHANKANADAQKnlkrYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEEL 1697
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ----FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1698 LvanEAAERARKQAEYEAADARDQANEANAQVSSLTSA--------KRKLEGEIQAIHADLDETLNEYKAAEE--RSKKA 1767
Cdd:TIGR00606 929 I---SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddyLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQ 1005
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1768 IADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKviaKLEQRVRELESELDGEQRRFQDANK 1847
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQ---KLEENIDLIKRNHVLALGRQKGYEK 1082
|
970 980
....*....|....*....|
gi 17509401 1848 NLGRADRRVRELQFQVDEDK 1867
Cdd:TIGR00606 1083 EIKHFKKELREPQFRDAEEK 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1035-1630 |
1.36e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1035 KLEQTLDDLEDSLEREKRARADLDKQKRKVE---------GELKIAQENIDESGRQRHDLEnnLKKKESELHSVSSRLED 1105
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllepirelaERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1106 EQALVSKLQRQIKDGQSRISELEEELENERQSRSKAD-RAKSDLQRELEELGEKLDEQggataaqvevnKKREAELAKLR 1184
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEER-----------ERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1185 RDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNN--------EK 1256
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllalrDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1257 LAKQFELQLTEL-------QSKADEQSRQlqdfTSLKGRLHSENGDLV---RQLEDAESQVNQlTRLKSQLTSQ-LEEAR 1325
Cdd:COG4913 449 LAEALGLDEAELpfvgeliEVRPEEERWR----GAIERVLGGFALTLLvppEHYAAALRWVNR-LHLRGRLVYErVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1326 RTADEEARERQTVAAQ----AKNYQHEAEQLQESLEEEIEGKN-EILRQLSKA---NADIQQWKARFEgegllKADEleD 1397
Cdd:COG4913 524 PDPERPRLDPDSLAGKldfkPHPFRAWLEAELGRRFDYVCVDSpEELRRHPRAitrAGQVKGNGTRHE-----KDDR--R 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1398 AKRRQ-------AQKINELQEALDAansknasLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIID--EWRKK 1468
Cdd:COG4913 597 RIRSRyvlgfdnRAKLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1469 TDDLAAELdgaqRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEE 1548
Cdd:COG4913 670 IAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1549 LQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLE 1628
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
..
gi 17509401 1629 GD 1630
Cdd:COG4913 826 ED 827
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1566-1933 |
1.99e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.05 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1566 KVLRAQVEVSQIRSEIEKrIQEKEEEFenTRKnhARALESMQASLETEAKGKA-------ELLRIKKKLE---GDINELE 1635
Cdd:PRK04863 287 EALELRRELYTSRRQLAA-EQYRLVEM--ARE--LAELNEAESDLEQDYQAASdhlnlvqTALRQQEKIEryqADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1636 IALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSekeellvANEAAERARKQ---AE 1712
Cdd:PRK04863 362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQ-------AVQALERAKQLcglPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1713 YEAADARDQANEANAQVSSLTSAKRKLEgeiqaihadldETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLR 1792
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEELLSLE-----------QKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1793 KGLEQQlkeiqvrldeAEAAALKGgkkviakLEQRVRELESELDGEQrrfqdanknlgRADRRVRELQFQVDEDKKNFER 1872
Cdd:PRK04863 504 RLREQR----------HLAEQLQQ-------LRMRLSELEQRLRQQQ-----------RAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1873 LQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERAD---QAENSLSKMRSKS 1933
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlAAQDALARLREQS 619
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
886-1229 |
2.39e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 886 SAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQD 965
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 966 LEMSLRKAEsekqskdhqirSLQDE-------MQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEedkgnhQNKVKAKLEQ 1038
Cdd:PRK02224 438 ARERVEEAE-----------ALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------VEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1039 --TLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQ 1116
Cdd:PRK02224 501 aeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1117 IKDGQSRIseleeeLENERQSRSKADRAksDLQRELEELGEKLDEQGgataaqvEVNKKREAELAKLR---RDLEEAnmN 1193
Cdd:PRK02224 581 LAELKERI------ESLERIRTLLAAIA--DAEDEIERLREKREALA-------ELNDERRERLAEKRerkRELEAE--F 643
|
330 340 350
....*....|....*....|....*....|....*....
gi 17509401 1194 HENQLGGLRKKHTDAV---AELTDQLDQLNKAKAKVEKD 1229
Cdd:PRK02224 644 DEARIEEAREDKERAEeylEQVEEKLDELREERDDLQAE 682
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1046-1918 |
3.05e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.37 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1046 SLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESElHSVSSRLEDEQALVSKLQRQIKDGQSRIS 1125
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1126 ELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQ--------------------------GGATAAQVEVNKKREAE 1179
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlndlyhnhqrtvrekerelvdcqrelEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1180 LAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAK 1259
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1260 QfelQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLT------SQLEEARRTADEEAR 1333
Cdd:TIGR00606 426 E---QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRkaerelSKAEKNSLTETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1334 ERQTVAAQA---KNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKA--------DELEDAKRRQ 1402
Cdd:TIGR00606 503 VKSLQNEKAdldRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkKQLEDWLHSK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1403 AQKINELQEALDAANSKNASLEKTKSRLVGDLDdaqvdverangvaSALEKKQKGFDKIIDEWrkKTDDLAAELDGAQRD 1482
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELE-------------SKEEQLSSYEDKLFDVC--GSQDEESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1483 LRNTSTDLFKAKNAQEELAEVVEGLRRENKS--------------LSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEE 1548
Cdd:TIGR00606 648 IEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqteaeLQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1549 LqhaldeaEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHaRALESMQASLETEAKGKAELLRIKK-KL 1627
Cdd:TIGR00606 728 M-------LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE-TLLGTIMPEEESAKVCLTDVTIMERfQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1628 EGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERA 1707
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1708 RKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQH 1787
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1788 V-DRLRKGLEQQLKEIQVRLDEAeAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRR--VREL----- 1859
Cdd:TIGR00606 960 IeNKIQDGKDDYLKQKETELNTV-NAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKREneLKEVeeelk 1038
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1860 -------QFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEElaNLNLQKYKQLTHQLEDAEER 1918
Cdd:TIGR00606 1039 qhlkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK--EIKHFKKELREPQFRDAEEK 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
902-1217 |
4.83e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 902 STKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTA-------------DVQRAKKKIEA-------------E 955
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswdeiDVASAEREIAEleaelerldassdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 956 VEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEM----QQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNK 1031
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELeqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1032 VKAKLEQTLDDLEDSLEREK----RARADLDKQKRKVEGELKIAQENIDESGRQRHDLENN-LKKKESELHSVSSRLEDE 1106
Cdd:COG4913 767 LRENLEERIDALRARLNRAEeeleRAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERFKELLNENSIE 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1107 Q--ALVSKLQRQIKDGQSRIseleeelenerqsrskadrakSDLQRELEELgekldEQGGATAAQVEVNKKREAELAKLR 1184
Cdd:COG4913 847 FvaDLLSKLRRAIREIKERI---------------------DPLNDSLKRI-----PFGPGRYLRLEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|...
gi 17509401 1185 RDLEEANMNHENQLGGLRKKHTDAVAELTDQLD 1217
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARFAALKRLIERLR 933
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1932 |
4.99e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1694 KEELLVANEAAERARKQAEY--EAADARDQANEANAQVSSLTSAKRKLEgEIQAIHADLDEtlNEYKAAEERSKKAIADA 1771
Cdd:COG4913 214 REYMLEEPDTFEAADALVEHfdDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAE--LEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1772 TRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALK-GGkkviakleQRVRELESELDGEQRRFQDANKNLG 1850
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGG--------DRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1851 RADRRVRELQFQVDEDKKNFERLQDLIDklqqklktqkKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMR 1930
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAA----------ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
..
gi 17509401 1931 SK 1932
Cdd:COG4913 433 RR 434
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
950-1230 |
5.50e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 61.18 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 950 KKIEAEVEALKKQIQDLEMSLRKAESekqskdhQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQ 1029
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQ-------QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1030 nkvKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENidesgrqrhdlennlkkkeSELHSVSSRLEDEQAL 1109
Cdd:PHA02562 243 ---LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG-------------------GVCPTCTQQISEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1110 VSKLQRQIKDGQSRISELEEELENERQSRSKADraksDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDlee 1189
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE--- 373
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17509401 1190 anmnhenqlgglRKKHTDAVAELTDQLDQLNKAKAKVEKDK 1230
Cdd:PHA02562 374 ------------FVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
905-1077 |
8.27e-09 |
|
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: 58.40 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 905 TQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKqskdhQI 984
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 985 RSLQDEMQQQDEAIAKLnkekkhqEEINRKLMEDLQSEEDKgnhQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKV 1064
Cdd:COG1579 92 EALQKEIESLKRRISDL-------EDEILELMERIEELEEE---LAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 17509401 1065 EGELKIAQENIDE 1077
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1426 |
9.47e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 856 EELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLES-------TKTQLSDAEERLAKL----------- 917
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaeTRDELKDYREKLEKLkreinelkrel 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 918 -----EAQQKDAskQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQ 992
Cdd:TIGR02169 409 drlqeELQRLSE--ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 993 QQDEAIAKLNKEKK--HQEEINRKLMEDLQSEEDKGNHQ----------------------------------------- 1029
Cdd:TIGR02169 487 KLQRELAEAEAQARasEERVRGGRAVEEVLKASIQGVHGtvaqlgsvgeryataievaagnrlnnvvveddavakeaiel 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1030 --------------NKVKAK--------LEQTLDDLEDSLEREKR--------------------ARADLDK-------- 1059
Cdd:TIGR02169 567 lkrrkagratflplNKMRDErrdlsilsEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvedieaARRLMGKyrmvtleg 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1060 ---------------------QKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIK 1118
Cdd:TIGR02169 647 elfeksgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1119 DGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEqggataaqvevnkkREAELAKLRRDLE--EANMNHE- 1195
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE--------------LEEDLHKLEEALNdlEARLSHSr 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1196 -NQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADE 1274
Cdd:TIGR02169 793 iPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1275 QSRQLQDftslkgrLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTAdeearERQTVAAQAKNYQHEAEQLQE 1354
Cdd:TIGR02169 873 LEAALRD-------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL-----SELKAKLEALEEELSEIEDPK 940
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1355 SLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQaqkiNELQEALDAANSKNASLEKT 1426
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL----DELKEKRAKLEEERKAILER 1008
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
898-1082 |
9.66e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 898 TNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRK-AESE 976
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 977 KQSKD------------------HQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQ 1038
Cdd:COG3883 96 YRSGGsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17509401 1039 TLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQR 1082
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
852-1065 |
1.28e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 852 GKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSEL 931
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 932 NDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQqqdEAIAKLNKEKKHQEEI 1011
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQL 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1012 NRKLmedlqsEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVE 1065
Cdd:TIGR02168 928 ELRL------EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
859-1337 |
1.38e-08 |
|
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: 60.45 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 859 EKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERL--AKLEAQQKDAS-KQLSELNDQL 935
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELkfVIKELQQLEGSsDRILELDQEL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 936 --ADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSL-QDEMQQQDEAIA------------- 999
Cdd:TIGR00606 481 rkAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtQMEMLTKDKMDKdeqirkiksrhsd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1000 --------------------KLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTL-------------DDLEDS 1046
Cdd:TIGR00606 561 eltsllgyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLssyedklfdvcgsQDEESD 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1047 LEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHD---LENNLKKKESELHSVSSRLEDEQALVSKLQRQIKdgqsr 1123
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE----- 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1124 iSELEEELENERQSRSKADRAKSDLQRELEELGEKLDEqggataaqvevNKKREAELAKLRRDLEEanmnHENQLGGLRK 1203
Cdd:TIGR00606 716 -SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK-----------LQKVNRDIQRLKNDIEE----QETLLGTIMP 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1204 KHTDAVAELTDQ--LDQLNKAKAKVEKDKAQAVRDAEDLAAQLdqeTSGKLNNEKLAKQFEL-----QLTELQSKADEQS 1276
Cdd:TIGR00606 780 EEESAKVCLTDVtiMERFQMELKDVERKIAQQAAKLQGSDLDR---TVQQVNQEKQEKQHELdtvvsKIELNRKLIQDQQ 856
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1277 RQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQT 1337
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1387-1949 |
2.16e-08 |
|
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: 59.75 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1387 EGLLKADELEDAKRRQAQKINELQEALdaaNSKNASLEKTKSRLVGDLDDAQVDVERangvasaLEKKQKGFDKIIDEWR 1466
Cdd:pfam15921 121 EMQMERDAMADIRRRESQSQEDLRNQL---QNTVHELEAAKCLKEDMLEDSNTQIEQ-------LRKMMLSHEGVLQEIR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1467 KKTDDLAAELDGAQRDLRNTSTDLFKakNAQEELAEVVEGLRRENKSLSQEIKDLTDQLgEGGRSvHEMQKIIRRLEIEK 1546
Cdd:pfam15921 191 SILVDFEEASGKKIYEHDSMSTMHFR--SLGSAISKILRELDTEISYLKGRIFPVEDQL-EALKS-ESQNKIELLLQQHQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1547 EELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKrIQEKEEEFENTRKNHARALESMQASLeteakgKAELLRIKKK 1626
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI-IQEQARNQNSMYMRQLSDLESTVSQL------RSELREAKRM 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1627 LEGDINELEIALDHANKANADAQKNLKRYQEQV----------------RELQLQVEEEQRN---GADTREQFFNAEKRA 1687
Cdd:pfam15921 340 YEDKIEELEKQLVLANSELTEARTERDQFSQESgnlddqlqklladlhkREKELSLEKEQNKrlwDRDTGNSITIDHLRR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1688 TLLQSEKE-ELLVANEAAERARKQAEYEAADARDQA-NEANAQVSSLTSakrKLEGEIQAIHADLDEtLNEYKAAEERSK 1765
Cdd:pfam15921 420 ELDDRNMEvQRLEALLKAMKSECQGQMERQMAAIQGkNESLEKVSSLTA---QLESTKEMLRKVVEE-LTAKKMTLESSE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1766 KAIADAT-RLAEELRQEQEHSQHVDRLRKGLEQQLKEIQ--------VRLDEAEAAALK----GGKKVIAKLEQRVR--- 1829
Cdd:pfam15921 496 RTVSDLTaSLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegdhLRNVQTECEALKlqmaEKDKVIEILRQQIEnmt 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1830 ------------------ELESELDGEQRRFQDANKNLGRADRRVRELQFQVDE---DKKNF-----ERLQDLIDKLQQK 1883
Cdd:pfam15921 576 qlvgqhgrtagamqvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLvnagsERLRAVKDIKQER 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1884 LKTQKKQVEEAEELANLNlQKYK------------------QLTHQLEDAEERADQAENSLSKMRSKSRASASVAPGLQS 1945
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLS-EDYEvlkrnfrnkseemetttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK 734
|
....
gi 17509401 1946 SASA 1949
Cdd:pfam15921 735 QITA 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1594-1816 |
2.60e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1594 NTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNG 1673
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1674 ADTREQFFNAEKRATLL-QSEKEELLVANEAAERARKQAEY----------EAADARDQANEANAQVSSLTSAKRKLEGE 1742
Cdd:COG4942 100 EAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1743 IQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKG 1816
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1488-1933 |
3.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1488 TDLFKAKNAQEELAEVVEGLRRENKSLSQEIK---DLTDQLGEGGRSVHEMQKIIRRLEIEKEELqhaldeaeaalEAEE 1564
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPEL-----------REEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1565 SKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHA--RALESMQASLETEAKGKAELLRIKKKLEGDINE---LEIALD 1639
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkiRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1640 HANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREqffnAEKRATLLQSEKEELLVANEAAERAR-KQAEYEAADA 1718
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKaKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1719 RDQAN---EANAQVSSLTSAKRKLEGEIQAIH---ADLDETLNEYKAAEERSKKAIADATRLAEELRQEqehsqHVDRLR 1792
Cdd:PRK03918 380 RLTGLtpeKLEKELEELEKAKEEIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE-----HRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1793 KGLEQQLKEIQVRLDEAEAAalkggkkvIAKLEQRVRELESELDGEQR--RFQDANKNLGRADRRVRELQFQ-VDEDKKN 1869
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEK--------ERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEeLEKKAEE 526
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1870 FERLQDLIDKLQQKLKTQKKQVEEAEELANlnlqKYKQLTHQLEDAEERADQAENSLSKMRSKS 1933
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEELAELLKELEELGFES 586
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1628-1950 |
3.57e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1628 EGDINELEIALDHANKANADAQKN-LKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEA--- 1703
Cdd:PTZ00121 1044 EKDIIDEDIDGNHEGKAEAKAHVGqDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAkkk 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1704 AERARKQAEYEAADARDQANEA-NAQVSSLTSAKRKLEgeiQAIHADLDETLNEYKAAEERSKkaiADATRLAEELRQEQ 1782
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAEEArKAEDAKRVEIARKAE---DARKAEEARKAEDAKKAEAARK---AEEVRKAEELRKAE 1197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1783 EHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDAnknlgRADRRVRELQFQ 1862
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA-----RMAHFARRQAAI 1272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1863 VDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYK--QLTHQLEDAEERADQAENSLSKMRSKSRASASVA 1940
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
330
....*....|
gi 17509401 1941 PGLQSSASAA 1950
Cdd:PTZ00121 1353 EAAADEAEAA 1362
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
959-1858 |
4.86e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.43 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 959 LKKQIQDLEMSLRK------AESEKQSKDHQIRSLQDEMQQQDEAiaklnKEKKHQEEINRKLMEDLQSEEDKGNHQNKV 1032
Cdd:COG3096 227 VRKAFQDMEAALREnrmtleAIRVTQSDRDLFKHLITEATNYVAA-----DYMRHANERRELSERALELRRELFGARRQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1033 ---KAKLEQTLDDLEDSLEREKRARADLDKQK---RKVEGELKiAQENIDesgRQRHDLEnnlkkkeselhSVSSRLEDE 1106
Cdd:COG3096 302 aeeQYRLVEMARELEELSARESDLEQDYQAASdhlNLVQTALR-QQEKIE---RYQEDLE-----------ELTERLEEQ 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1107 QALVSKLQRQIKDGQSRiseleeelenERQSRSKADRAKS---DLQRELEELgekldeQGGATAAQVEVNKKREAE---- 1179
Cdd:COG3096 367 EEVVEEAAEQLAEAEAR----------LEAAEEEVDSLKSqlaDYQQALDVQ------QTRAIQYQQAVQALEKARalcg 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1180 ------------LAKLRRDLEEANmnheNQLGGLRKKHTDAVAELTdQLDQ----LNKAKAKVEKDKA-----QAVRDAE 1238
Cdd:COG3096 431 lpdltpenaedyLAAFRAKEQQAT----EEVLELEQKLSVADAARR-QFEKayelVCKIAGEVERSQAwqtarELLRRYR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1239 DLAAQLDQETsgklnneklakQFELQLTELQSKADEQS---RQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKS 1315
Cdd:COG3096 506 SQQALAQRLQ-----------QLRAQLAELEQRLRQQQnaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1316 QLTSQLEEARRTADEEARERQTVAAQAKNYqHEAEQLQESLEeeiEGKNEILRQLSKANADIQQWKARfEGEGLLKADEL 1395
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAW-LAAQDALERLR---EQSGEALADSQEVTAAMQQLLER-EREATVERDEL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1396 EDAKRRQAQKINELQEALDAANSKNASLektKSRLVGDL-----DDAQVD-----------------VERANGVASALEK 1453
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDPRLLAL---AERLGGVLlseiyDDVTLEdapyfsalygparhaivVPDLSAVKEQLAG 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1454 KQ-------------KGFDkiidewrkktDDL--AAELDGA------QRDLRNT---STDLFkAKNAQEELAEVvegLRR 1509
Cdd:COG3096 727 LEdcpedlyliegdpDSFD----------DSVfdAEELEDAvvvklsDRQWRYSrfpEVPLF-GRAAREKRLEE---LRA 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1510 ENKSLSQEIKDLTdqlgeggrsvHEMQKIiRRLEIEKEEL--QHALDEAEAALEAEEsKVLRAQvevsqiRSEIEKRIqe 1587
Cdd:COG3096 793 ERDELAEQYAKAS----------FDVQKL-QRLHQAFSQFvgGHLAVAFAPDPEAEL-AALRQR------RSELEREL-- 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1588 keEEFENTRKNHARALESMQASLETEAK--GKAELLRiKKKLEGDINELEIALDHANKANADAQKN-------------L 1652
Cdd:COG3096 853 --AQHRAQEQQLRQQLDQLKEQLQLLNKllPQANLLA-DETLADRLEELREELDAAQEAQAFIQQHgkalaqleplvavL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1653 KRYQEQVRELQLQVEEEQRNGADTREQFFN----AEKRATLLQSEKEELLVAN-----------EAAERARKQAEYEAAD 1717
Cdd:COG3096 930 QSDPEQFEQLQADYLQAKEQQRRLKQQIFAlsevVQRRPHFSYEDAVGLLGENsdlneklrarlEQAEEARREAREQLRQ 1009
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1718 ARDQANEANAQVSSLTSAKR-------KLEGEIQAIHADLDETlneykaAEERskkaiadatrlAEELRQEQEHSQHVDR 1790
Cdd:COG3096 1010 AQAQYSQYNQVLASLKSSRDakqqtlqELEQELEELGVQADAE------AEER-----------ARIRRDELHEELSQNR 1072
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1791 LRKGleQQLKEIQVRldEAEaaalkggkkvIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRE 1858
Cdd:COG3096 1073 SRRS--QLEKQLTRC--EAE----------MDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARD 1126
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1085-1848 |
4.98e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1085 LENNLKKKESELHSVSSRLEDEQALVSKLQRqikdGQSRISELEEELENERQSRSKADRAKSDLQRELEElgekldeqgg 1164
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQF----ENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKE---------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1165 ATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGG---LRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLA 1241
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAfeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1242 AQLDQETSGKLNNEKlakqfelQLTELQSKADEQSRQLQDFTSLKG----RLHSENGDLVRQLEDAESQVNQLTRLKSQL 1317
Cdd:pfam05483 243 SLLLIQITEKENKMK-------DLTFLLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1318 TSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKanadiqqwkaRFEGegllKADELED 1397
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQ----------RLEK----NEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1398 AKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDlddaqvdverangvasalekkqkgfDKIIDEwRKKTDDLAAELD 1477
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEELKKILAED-------------------------EKLLDE-KKQFEKIAEELK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1478 GAQRDLrntsTDLFKAKNAQEELAEV-VEGLRRENKSLSQEIKDLtdqlgeggrsvhemqkiirRLEIEKEELQHALDEA 1556
Cdd:pfam05483 436 GKEQEL----IFLLQAREKEIHDLEIqLTAIKTSEEHYLKEVEDL-------------------KTELEKEKLKNIELTA 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1557 EAALEAEESKvlraqvEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEI 1636
Cdd:pfam05483 493 HCDKLLLENK------ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1637 ALDHANK-------ANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATllqSEKEELLVANEAAERARK 1709
Cdd:pfam05483 567 KLDKSEEnarsieyEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS---AENKQLNAYEIKVNKLEL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1710 QAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQ----EHS 1785
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdkiiEER 723
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1786 QHVDRLRKGLEQQLKEIQVRLdEAEAAALKggkkviAKLEQRVRELESELDGEQRRFQDANKN 1848
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAAL-EIELSNIK------AELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
894-1714 |
6.19e-08 |
|
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: 58.13 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 894 TSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLS---ELNDQLADNEDRTADVQRAKKKIEAEVE----ALKKQIQDL 966
Cdd:TIGR00606 227 TSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSkimKLDNEIKALKSRKKQMEKDNSELELKMEkvfqGTDEQLNDL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 967 EmslRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQE-EINR-KLMEDLQSEEDKGNHQNKVKAKLEQTLDDLE 1044
Cdd:TIGR00606 307 Y---HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLvEQGRlQLQADRHQEHIRARDSLIQSLATRLELDGFE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1045 DSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKD----- 1119
Cdd:TIGR00606 384 RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFvikel 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1120 -----GQSRISELEEELENERQSRSKADR----------------AKSDLQRELEELGEKLDEQGGATAAQVEVNKKREA 1178
Cdd:TIGR00606 464 qqlegSSDRILELDQELRKAERELSKAEKnsltetlkkevkslqnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKD 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1179 ELAKLRRdLEEANMNHENQLGGLR-------------KKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLd 1245
Cdd:TIGR00606 544 KMDKDEQ-IRKIKSRHSDELTSLLgyfpnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1246 QETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSlKGRLHSEngdLVRQLEDAES-------QVNQLTRLKSQLT 1318
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG-ATAVYSQ---FITQLTDENQsccpvcqRVFQTEAELQEFI 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1319 SQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGK----NEILRQLSKANADIQQWKARF-EGEGLLKA- 1392
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKekeiPELRNKLQKVNRDIQRLKNDIeEQETLLGTi 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1393 -DELEDAKRRQAQK--INELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERangvasalEKKQKGFDKI---IDEWR 1466
Cdd:TIGR00606 778 mPEEESAKVCLTDVtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK--------QEKQHELDTVvskIELNR 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1467 KKTDD---LAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQlgeggrsVHEMQKIIRRLE 1543
Cdd:TIGR00606 850 KLIQDqqeQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQ 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1544 IEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHaraLESMQASLEteakgkaELLRI 1623
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNAQLE-------ECEKH 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1624 KKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEelLVANEA 1703
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID--LIKRNH 1070
|
890
....*....|.
gi 17509401 1704 AERARKQAEYE 1714
Cdd:TIGR00606 1071 VLALGRQKGYE 1081
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
899-1438 |
7.40e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 899 NLESTKTQLSDAEERLAkleaQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDL---EMSLRKAES 975
Cdd:PRK04863 514 QLQQLRMRLSELEQRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArerRMALRQQLE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 976 EKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLER-EKRAR 1054
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERlSQPGG 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1055 ADLDKQKRKVE--------------------------GELKIAQENIDESGRQRH-----DLENNLKKKESELHSVSSRL 1103
Cdd:PRK04863 670 SEDPRLNALAErfggvllseiyddvsledapyfsalyGPARHAIVVPDLSDAAEQlagleDCPEDLYLIEGDPDSFDDSV 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1104 EDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKadRAKsDLQRELEELGEKLDE----------------QGGATA 1167
Cdd:PRK04863 750 FSVEELEKAVVVKIADRQWRYSRFPEVPLFGRAAREK--RIE-QLRAEREELAERYATlsfdvqklqrlhqafsRFIGSH 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1168 AQVEVNKKREAELAKLRR----------DLEEANMNH-------ENQLGGLRK-----------KHTDAVAELTDQLDQL 1219
Cdd:PRK04863 827 LAVAFEADPEAELRQLNRrrveleralaDHESQEQQQrsqleqaKEGLSALNRllprlnlladeTLADRVEEIREQLDEA 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1220 NKAKAKVEKdKAQAVRDAEDLAAQLDQETSgklNNEKLAKQFElQLTELQSKADEQSRQLQDFTSLkgRLHSENGDLVRQ 1299
Cdd:PRK04863 907 EEAKRFVQQ-HGNALAQLEPIVSVLQSDPE---QFEQLKQDYQ-QAQQTQRDAKQQAFALTEVVQR--RAHFSYEDAAEM 979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1300 LEDAESQVNQL-TRLKsqltsQLEEARRTADEEARERQTVAAQAKNYQHEAEQLqesleeeIEGKNEILRQLSKANADIQ 1378
Cdd:PRK04863 980 LAKNSDLNEKLrQRLE-----QAEQERTRAREQLRQAQAQLAQYNQVLASLKSS-------YDAKRQMLQELKQELQDLG 1047
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1379 qwkarfegeglLKADEleDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQ 1438
Cdd:PRK04863 1048 -----------VPADS--GAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
911-1339 |
8.01e-08 |
|
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: 57.67 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 911 EERLAKLEAQQKDASKQLSELNDQLADN-------------EDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEK 977
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 978 QSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQ-NKVKAKLEQTLDDLEDSLEREKRARAD 1056
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEqDLQDVRLHLQQCSQELALKLTALHALQ 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1057 LDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQ 1136
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1137 SRSKADRAKSDLQRELEELG-EKLDEQGGATAA---QVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAEL 1212
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQArTVLKARTEAHFNnneEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1213 TDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFElQLTELQSKADEQSRQLQDFTSLKGrlhSE 1292
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKLNGINQIKI---QF 888
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1293 NGDLVRQLEdAESQVNQLTRLKSQ----LTSQLEEARRTADEEARERQTVA 1339
Cdd:TIGR00618 889 DGDALIKFL-HEITLYANVRLANQsegrFHGRYADSHVNARKYQGLALLVA 938
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
888-1338 |
1.13e-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: 57.04 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 888 KLVEEKTSLFTNLESTKTQLSDAEERLAKL-------EAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALK 960
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqitekENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 961 KQIQDLEMSLRKAESEKqskdhqiRSLQDEMQQQDEAIAKLNKEKKHQ-EEINR-----------------KLMEDLQSE 1022
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQ-------KALEEDLQIATKTICQLTEEKEAQmEELNKakaahsfvvtefeattcSLEELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1023 EDK-GNHQNKVK---AKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQEN------IDESGRQRHDLENNLKKK 1092
Cdd:pfam05483 369 QQRlEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKkqfekiAEELKGKEQELIFLLQAR 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1093 ESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQggatAAQVEV 1172
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH----QEDIIN 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1173 NKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKL 1252
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1253 NNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLK----SQLTSQLEEARRTA 1328
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkiseEKLLEEVEKAKAIA 684
|
490
....*....|
gi 17509401 1329 DEEARERQTV 1338
Cdd:pfam05483 685 DEAVKLQKEI 694
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
965-1858 |
1.16e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 965 DLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEkkhqeeinrkLMEDLQSEEDkgnHQNKVKAKLEQTlddle 1044
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD----------LEQDYQAASD---HLNLVQTALRQQ----- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1045 dslEREKRARADLDKQKRKVEgELKIAQENIDEsgrQRHDLENnlkkkeselhsvssRLEDEQALVSKLQRQIKDGQSRI 1124
Cdd:PRK04863 348 ---EKIERYQADLEELEERLE-EQNEVVEEADE---QQEENEA--------------RAEAAEEEVDELKSQLADYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1125 SELEEELENERQSRSKADRAKSDLQR---ELEELGEKLDEqggATAAQVEVNKKREAELAKLRrDLEEANMNHENQLGGL 1201
Cdd:PRK04863 407 DVQQTRAIQYQQAVQALERAKQLCGLpdlTADNAEDWLEE---FQAKEQEATEELLSLEQKLS-VAQAAHSQFEQAYQLV 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1202 RKkhtdaVAELTDQLDQLNKAKAKV---EKDKAQAVRdAEDLAAQLdQETSGKLNN----EKLAKQFELQL-------TE 1267
Cdd:PRK04863 483 RK-----IAGEVSRSEAWDVARELLrrlREQRHLAEQ-LQQLRMRL-SELEQRLRQqqraERLLAEFCKRLgknlddeDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1268 LQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQ-LTSQ--LEEARRTADEEARERQTVAAQAKN 1344
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwLAAQdaLARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1345 YQHEAEQLQESLEEEIEGKNEILRQLSK-------ANADIQQWKARFEGEGL--LKAD-ELEDA--------KRRQAQKI 1406
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIERlsqpggsEDPRLNALAERFGGVLLseIYDDvSLEDApyfsalygPARHAIVV 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1407 NELqealDAANSKNASLEKTKSRLV---GD---LDDAQVDV-ERANGVASALEKKQKGFDKIIDE---WRKKTDDLAAEL 1476
Cdd:PRK04863 716 PDL----SDAAEQLAGLEDCPEDLYlieGDpdsFDDSVFSVeELEKAVVVKIADRQWRYSRFPEVplfGRAAREKRIEQL 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1477 DgAQRDLRNTstdlfkaknAQEELAEVVEGLRRENKSLSQ----------------EIKDLTDQLGEGGRSVHEmqkiir 1540
Cdd:PRK04863 792 R-AEREELAE---------RYATLSFDVQKLQRLHQAFSRfigshlavafeadpeaELRQLNRRRVELERALAD------ 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1541 rleIEKEELQHALDEAEAALEAEESKVLRAQVEVSQiRSEIEKRIQEKEEEFEntrknharALESMQASLETEAKGKAEL 1620
Cdd:PRK04863 856 ---HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLA-DETLADRVEEIREQLD--------EAEEAKRFVQQHGNALAQL 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1621 LRIKKKLEGDinelEIALDHANKANADAQKNLKRYQEQVRELQLQVEeeqrngadtREQFFNAEKRATLLQSEKE--ELL 1698
Cdd:PRK04863 924 EPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ---------RRAHFSYEDAAEMLAKNSDlnEKL 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1699 VAN-EAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETlnEYKAAEERSKKAIADATRLAEE 1777
Cdd:PRK04863 991 RQRlEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL--GVPADSGAEERARARRDELHAR 1068
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1778 LRQEQEHsqhvdrlRKGLEQQLKEIQVRLDEaeaaalkggkkviakLEQRVRELESELDGEQRRFQDANKNLGRADRRVR 1857
Cdd:PRK04863 1069 LSANRSR-------RNQLEKQLTFCEAEMDN---------------LTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVK 1126
|
.
gi 17509401 1858 E 1858
Cdd:PRK04863 1127 D 1127
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
899-1438 |
1.19e-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: 57.27 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 899 NLESTKTQLSDAEERLAkleaQQKDASKQLSELNDQLADNEDRTADVqrakkkiEAEVEALKKQIQDLEMSLRKAeSEKQ 978
Cdd:COG3096 513 RLQQLRAQLAELEQRLR----QQQNAERLLEEFCQRIGQQLDAAEEL-------EELLAELEAQLEELEEQAAEA-VEQR 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 979 SkdhqirslqdEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQ----NKVKAKLEQTLDDL-EDSLEREK-- 1051
Cdd:COG3096 581 S----------ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAladsQEVTAAMQQLLERErEATVERDEla 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1052 RARADLDKQKRKV-------EGELKIAQE--------------NIDES-------GRQRH-----DLENNLKKkeseLHS 1098
Cdd:COG3096 651 ARKQALESQIERLsqpggaeDPRLLALAErlggvllseiyddvTLEDApyfsalyGPARHaivvpDLSAVKEQ----LAG 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1099 VSSRLED---------------------EQALVSKL-QRQIKdgQSRISELEEELENERQSRSKAdraksdLQRELEELG 1156
Cdd:COG3096 727 LEDCPEDlyliegdpdsfddsvfdaeelEDAVVVKLsDRQWR--YSRFPEVPLFGRAAREKRLEE------LRAERDELA 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1157 EKLDE----------------QGGATAAQVEVNKKREAELAKLRRDLEEANMNHEN-----------------QLGGLRK 1203
Cdd:COG3096 799 EQYAKasfdvqklqrlhqafsQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQhraqeqqlrqqldqlkeQLQLLNK 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1204 -----------KHTDAVAELTDQLDQLNKAKAKVEKdKAQAVRDAEDLAAQLDQEtsgKLNNEKLAKQFElQLTELQSKA 1272
Cdd:COG3096 879 llpqanlladeTLADRLEELREELDAAQEAQAFIQQ-HGKALAQLEPLVAVLQSD---PEQFEQLQADYL-QAKEQQRRL 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1273 DEQSRQLQDftsLKGRLHSENgdlvrqLEDAESQVNQLTRLKSQLTSQLEEArrtadEEARERQTVAAQAKNYQH-EAEQ 1351
Cdd:COG3096 954 KQQIFALSE---VVQRRPHFS------YEDAVGLLGENSDLNEKLRARLEQA-----EEARREAREQLRQAQAQYsQYNQ 1019
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1352 LQESLEEEIEGKNEILRQLskanadiqqwKARFEGEGLlKADEleDAKRRQAQKINELQEALDAANSKNASLEKTKSRLV 1431
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQEL----------EQELEELGV-QADA--EAEERARIRRDELHEELSQNRSRRSQLEKQLTRCE 1086
|
....*..
gi 17509401 1432 GDLDDAQ 1438
Cdd:COG3096 1087 AEMDSLQ 1093
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1217-1901 |
1.30e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1217 DQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQsKADEQSRQLQDFTSLKGRLHSENGDL 1296
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1297 VRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEA-------------RERQTVAAQAKNYQHEAEQLQESLEeeIEGK 1363
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRARKAAPLAAHIKAvtqieqqaqrihtELQSKMRSRAKLLMKRAAHVKQQSS--IEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1364 NEILRQLSKANADIQQW--KARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRlVGDLDDAQVDV 1441
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT-IDTRTSAFRDL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1442 ERANGVASALEKKQKGFDKIIDEW-RKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQ------EELAEVVEGLRRENKSL 1514
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEqihlqeTRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1515 SQEIKDLT-------DQLGEGGRSVHEMQKIIRR---LEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSeiekR 1584
Cdd:TIGR00618 503 PCPLCGSCihpnparQDIDNPGPLTRRMQRGEQTyaqLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ----C 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1585 IQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQL 1664
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1665 QVEEEQRNGADTREQFFNAEKRA-TLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEI 1743
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLAlQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1744 QAihadLDETLNEYKA-AEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAeaaalkggKKVIA 1822
Cdd:TIGR00618 739 DA----LNQSLKELMHqARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL--------KTLEA 806
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1823 KLEQRVRELESELDGEQRRFQDANKNLgraDRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLN 1901
Cdd:TIGR00618 807 EIGQEIPSDEDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1313-1927 |
1.52e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1313 LKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEeeIEGKNEILRQLSKANADIQQWKARFEGEGLLKA 1392
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPE--FTKLQQEFNTLESAELRLSHLHFGYKSDETLIA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1393 DELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEK----KQKGFDKIIDEWRKK 1468
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadieTAAADQEQLPSWQSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1469 TDDLAAELD---GAQRDLrNTSTDLFKAkNAQEELAEVVEGL-------RRENKSLSQEIKDLTDQLGEGGRSVHEMQK- 1537
Cdd:pfam12128 356 LENLEERLKaltGKHQDV-TAKYNRRRS-KIKEQNNRDIAGIkdklakiREARDRQLAVAEDDLQALESELREQLEAGKl 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1538 --------IIRRLEIEK---------EELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHA 1600
Cdd:pfam12128 434 efneeeyrLKSRLGELKlrlnqatatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1601 RALE-----------------SMQASLETEAKG----------KAELLR--------------------IKKKLEG-DIN 1632
Cdd:pfam12128 514 RLEErqsaldelelqlfpqagTLLHFLRKEAPDweqsigkvisPELLHRtdldpevwdgsvggelnlygVKLDLKRiDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1633 E-------LEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAE 1705
Cdd:pfam12128 594 EwaaseeeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1706 RARKQaeyeaadardqanEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRqeqehS 1785
Cdd:pfam12128 674 AERKD-------------SANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL-----K 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1786 QHVDRLRKGLEQQLKEIQVRLDEaEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDA--------NKNLGRADR--- 1854
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKR-DLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRlat 814
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1855 RVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLS 1927
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGS 887
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1681-1878 |
1.55e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1681 FNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAA 1760
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1761 E---ERSKKAIADATRLAEELRQE--------QEHSQHVDRLRKGLEQQLKEIQVRLDE--AEAAALKGGKKVIAKLEQR 1827
Cdd:COG4942 96 RaelEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1828 VRELESELDGEQRRFQDA----NKNLGRADRRVRELQFQVDEDKKNFERLQDLID 1878
Cdd:COG4942 176 LEALLAELEEERAALEALkaerQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
949-1662 |
2.66e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 949 KKKIEAEVEALKKQIQ----DLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINR--KLMEDLQSE 1022
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1023 EDKGNHQNKVKAKLEQTLDdledslerekraradldkQKRKVEgELKIAQENIDESGRQRHDLENNLKKKESELHSVSSR 1102
Cdd:TIGR00618 269 IEELRAQEAVLEETQERIN------------------RARKAA-PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1103 LEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKadRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKreaELAK 1182
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI--REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK---ELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1183 LRRDLEEANMNHENQ---LGGLRKKHTDAVAELtDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAK 1259
Cdd:TIGR00618 405 LQREQATIDTRTSAFrdlQGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1260 QFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVrQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVA 1339
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDID-NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1340 AQAKNYQHEaeqlQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANsK 1419
Cdd:TIGR00618 563 EQMQEIQQS----FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-C 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1420 NASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKiidewrkktddlAAELDGAQRDLRNTSTDLFKAKNAQE- 1498
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR------------QLALQKMQSEKEQLTYWKEMLAQCQTl 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1499 --ELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLeiEKEELQHALDEAEAALEAEESKVLRAQvEVSQ 1576
Cdd:TIGR00618 706 lrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ--ARTVLKARTEAHFNNNEEVTAALQTGA-ELSH 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1577 IRSEIEKRIQ----------EKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANA 1646
Cdd:TIGR00618 783 LAAEIQFFNRlreedthllkTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730
....*....|....*.
gi 17509401 1647 DAQKNLKRYQEQVREL 1662
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKL 878
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1189 |
3.47e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 850 KAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQkDASK--- 926
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL-EAGKcpe 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 927 -----QLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEmSLRKAESEKQSKDHQIRSLQDEMQQQD------ 995
Cdd:PRK02224 457 cgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRetieek 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 996 -EAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKqkrkvegelkiAQEN 1074
Cdd:PRK02224 536 rERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-----------IADA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1075 IDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQrqikdgQSRISeleeeleNERQSRSKADRAKSDLQRELEE 1154
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD------EARIE-------EAREDKERAEEYLEQVEEKLDE 671
|
330 340 350
....*....|....*....|....*....|....*
gi 17509401 1155 LGEKLDEQGGATAAqVEVNKKREAELAKLRRDLEE 1189
Cdd:PRK02224 672 LREERDDLQAEIGA-VENELEELEELRERREALEN 705
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1397-1830 |
3.74e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1397 DAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLD--DAQVDVERANGVASALEKKQKGFDKIIDEWRKKtddlAA 1474
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEER----LE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1475 ELDGAQRDLRNTSTDLFKAKNAQEELAEV--------VEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEiek 1546
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1547 EELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEE--------------EFENTRKNHARALESMQASLET 1612
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1613 EAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRN------GADTREQFFNAEKR 1686
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeaGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1687 ATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQvssltsakrKLEGEIQAIHADLDETLNEYKAAEERSKK 1766
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE---------ELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1767 AIADATrlAEELRQEQEHsqhvdrlrkgLEQQLKEIqvrldEAEAAALKGGKKVIAKLEQRVRE 1830
Cdd:COG4717 465 LEEDGE--LAELLQELEE----------LKAELREL-----AEEWAALKLALELLEEAREEYRE 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
856-1257 |
3.98e-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: 55.41 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 856 EELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQL 935
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 936 ADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEeinrkl 1015
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE------ 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1016 mEDLQSEEDKGNhqnkvkaKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESE 1095
Cdd:TIGR04523 468 -TQLKVLSRSIN-------KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1096 LHSVSSRLE--DEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEqggataaqvevn 1173
Cdd:TIGR04523 540 ISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE------------ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1174 kkREAELAKLRRDLEEANMNHEnQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQ--ETSGK 1251
Cdd:TIGR04523 608 --KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDiiELMKD 684
|
....*.
gi 17509401 1252 LNNEKL 1257
Cdd:TIGR04523 685 WLKELS 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
856-1331 |
4.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 856 EELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSL-FTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQ 934
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 935 LADNEDRTADVQR----AKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQ-------DEMQQQDEAIAK--- 1000
Cdd:COG4913 375 LPASAEEFAALRAeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipARLLALRDALAEalg 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1001 ---------------LNKEKKHQEEINR-----------------------------------KLMEDLQSEEDKGNHQN 1030
Cdd:COG4913 455 ldeaelpfvgelievRPEEERWRGAIERvlggfaltllvppehyaaalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPD 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1031 ----KVKAK-------LEQTL---------DDLEDsLEREKRA------------RADLDKQKRkVEGELKIAQENIdes 1078
Cdd:COG4913 535 slagKLDFKphpfrawLEAELgrrfdyvcvDSPEE-LRRHPRAitragqvkgngtRHEKDDRRR-IRSRYVLGFDNR--- 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1079 gRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQikdgqsriseleEELENERQSRSKADRAKSDLQRELEELGEK 1158
Cdd:COG4913 610 -AKLAALEAELAELEEELAEAEERLEALEAELDALQER------------REALQRLAEYSWDEIDVASAEREIAELEAE 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1159 LDEqggATAAQVEVnKKREAELAKLRRDLEEAnmnhENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVE-KDKAQAVRDA 1237
Cdd:COG4913 677 LER---LDASSDDL-AALEEQLEELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELR 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1238 EDLAAQLDQEtSGKLNNEKLAKQFELQLTELQSKADEQSRQLQD-FTSLKGRLHSENGDLVRQLEDAESQVNQLTRLK-- 1314
Cdd:COG4913 749 ALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLESLPEYLALLDRLEed 827
|
570 580 590
....*....|....*....|....*....|....*...
gi 17509401 1315 ---------------------SQLTSQLEEARRTADEE 1331
Cdd:COG4913 828 glpeyeerfkellnensiefvADLLSKLRRAIREIKER 865
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
905-1065 |
4.54e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 905 TQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAkkkieAEVEALKKQIQDLEMSLRKAESEKQSKDHQI 984
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 985 RSLQDEMQQQDEAIaklnkekkhQEEINRkLMEDLQSEEDKGNHQnkvKAKLEQTLDDLEDSLEREKRARADLDKQKRKV 1064
Cdd:COG3206 294 IALRAQIAALRAQL---------QQEAQR-ILASLEAELEALQAR---EASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
.
gi 17509401 1065 E 1065
Cdd:COG3206 361 E 361
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
904-1099 |
4.86e-07 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 54.86 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 904 KTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADV--QRAKKKIEAeVEALKKQIQDLEMSLRKAESEKQSKD 981
Cdd:pfam09726 464 KQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATAARAvaLAAASRGEC-TESLKQRKRELESEIKKLTHDIKLKE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 982 HQIRSLQDEMQQqdeaiakLNKEKKHQEEiNRKLMEDLQSEEDKGNHqnkvkakleqtlddLEDSLEREKRARADLDKQK 1061
Cdd:pfam09726 543 EQIRELEIKVQE-------LRKYKESEKD-TEVLMSALSAMQDKNQH--------------LENSLSAETRIKLDLFSAL 600
|
170 180 190
....*....|....*....|....*....|....*...
gi 17509401 1062 RKVEGELKIAQENIdesgRQRHDLENNLKKKESELHSV 1099
Cdd:pfam09726 601 GDAKRQLEIAQGQI----YQKDQEIKDLKQKIAEVMAV 634
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1573-1954 |
5.17e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1573 EVSQIRSEIEkRIQEKEEEFENTRKNHARALESMQASLETeakgkaellrikkklegdINELEIALDHANKANADAQKNL 1652
Cdd:PRK02224 214 ELAELDEEIE-RYEEQREQARETRDEADEVLEEHEERREE------------------LETLEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1653 KRYQEQVRELQLQVEE--EQRNGADTREQFFNAEKRATL-----LQSEKEELL-----------VANEAAERARKQA--- 1711
Cdd:PRK02224 275 EELAEEVRDLRERLEEleEERDDLLAEAGLDDADAEAVEarreeLEDRDEELRdrleecrvaaqAHNEEAESLREDAddl 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1712 EYEAADARDQANEANAQVSSLTSAKRKLEGEIqaihADLDETLNEYKAAEERSKKAIADATRLAEELRQEQehsqhvDRL 1791
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEI----EELEEEIEELRERFGDAPVDLGNAEDFLEELREER------DEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1792 R---KGLEQQLKEIQVRLDEAEAAaLKGGK--------------KVIAKLEQRVRELESELDgeqrrfqdanknlgradr 1854
Cdd:PRK02224 425 RereAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvETIEEDRERVEELEAELE------------------ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1855 rvrELQFQVDEDKKNFERLQDLIdklqqklktqkkqveEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSR 1934
Cdd:PRK02224 486 ---DLEEEVEEVEERLERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420
....*....|....*....|
gi 17509401 1935 ASASVAPGLQSSASAAVIRS 1954
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEA 567
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1449-1873 |
5.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1449 SALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLtDQLGEG 1528
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1529 GRSVHEMQKIIRRLEIEKEELQHALDEAEAaleaeeskVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQA 1608
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1609 SLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQ------------------------------ 1658
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1659 ---VRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSA 1735
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1736 KRKLegEIQAIHADLDETLNEYKAAEErskkaiADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALk 1815
Cdd:COG4717 360 EEEL--QLEELEQEIAALLAEAGVEDE------EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL- 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1816 ggKKVIAKLEQRVRELESELD---GEQRRFQDANKNLGRaDRRVRELQFQVDEDKKNFERL 1873
Cdd:COG4717 431 --EEELEELEEELEELEEELEelrEELAELEAELEQLEE-DGELAELLQELEELKAELREL 488
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
853-1166 |
7.00e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 853 KEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKlvEEKTSLFTNLESTKTQLSDAEERLAKLeaQQKDASKQLSELN 932
Cdd:pfam17380 303 QEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMERERELERIRQEERKRELERI--RQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 933 DQladnEDRTADVQRAKKKIEAEVEALKKQiQDLEMSLRKAESEKQSKDHQIRSLQDEMQQqdeaiaklnKEKKHQEEIN 1012
Cdd:pfam17380 379 EL----ERLQMERQQKNERVRQELEAARKV-KILEEERQRKIQQQKVEMEQIRAEQEEARQ---------REVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1013 RKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKV-EGELKIAQENIDESGRQRHDLENNLKK 1091
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1092 KESELHSVSSRLEDEQalvsKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGAT 1166
Cdd:pfam17380 525 RQKAIYEEERRREAEE----ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATT 595
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1260-1876 |
7.20e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1260 QFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRtadEEARERQTva 1339
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK---LEEKIREL-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1340 aqaknyqheaeqlqeslEEEIEGKNEILRQLSKANADIQ--QWKA-------RFEGEGLLKADELEDAKRRQAQKINELQ 1410
Cdd:PRK03918 265 -----------------EERIEELKKEIEELEEKVKELKelKEKAeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1411 EALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKgfdkiIDEWRKKTDDLaaELDGAQRDLRNtstdl 1490
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE-----LERLKKRLTGL--TPEKLEKELEE----- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1491 fkAKNAQEELAEVVEGLRRENKSLSQEIKDLTDqlgeggrSVHEMQKIIRRLEIEKEELQHALDEAEAAleaeeskvlRA 1570
Cdd:PRK03918 396 --LEKAKEEIEEEISKITARIGELKKEIKELKK-------AIEELKKAKGKCPVCGRELTEEHRKELLE---------EY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1571 QVEVSQIRSEIeKRIQEKEEEFENTRKNharalesmqasLETEAKGKAELLRIKKKLEgDINELEIALDHANKAnaDAQK 1650
Cdd:PRK03918 458 TAELKRIEKEL-KEIEEKERKLRKELRE-----------LEKVLKKESELIKLKELAE-QLKELEEKLKKYNLE--ELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1651 NLKRYqEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADardqanEANAQVS 1730
Cdd:PRK03918 523 KAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE------ELEERLK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1731 SLTSAKRKLEgEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQeqehsqhvdrlrkgLEQQLKEIQVRLDEAE 1810
Cdd:PRK03918 596 ELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE--------------LRKELEELEKKYSEEE 660
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1811 aaalkggkkvIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDL 1876
Cdd:PRK03918 661 ----------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
995-1454 |
8.69e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 995 DEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAqen 1074
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1075 idESGRQRHDLENNLKKKESELHsvssRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAK-SDLQRELE 1153
Cdd:COG4717 129 --PLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1154 ELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVekdKAQA 1233
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI---AGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1234 VRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRL 1313
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1314 KSQLTSQLEEARRTA---------DEEARERQTVAAQAKNYQHEAEQLQesleeeiegkneilRQLSKANADIQQWKARF 1384
Cdd:COG4717 360 EEELQLEELEQEIAAllaeagvedEEELRAALEQAEEYQELKEELEELE--------------EQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1385 EGEGLL-KADELEDAKRRQAQKINELQEALDAANSKNASLEKTksrlvGDLDDAQVDVERANGVASALEKK 1454
Cdd:COG4717 426 DEEELEeELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
996-1424 |
1.72e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 996 EAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEdSLEREKRARaDLDKQKRKVEGELKIAQ--- 1072
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLL-PLYQELEALEAELAELPerl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1073 ENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQikdgqsRISELEEELENERQSRSKADRAKSDLQREL 1152
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1153 EELGEKLDEQGGATAAQVEVNKKREAE-----------LAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNK 1221
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1222 AKAKVEKDKAQAVRDAEDLAAQLDQ-ETSGKLNNEKLAKQFEL--QLTELQSKADEQSRQLQ------DFTSLKGRLHSE 1292
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAAlGLPPDLSPEELLELLDRieELQELLREAEELEEELQleeleqEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1293 NGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESleeeiEGKNEILRQLSK 1372
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE-----EELEELREELAE 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1373 ANADIQQwkarfegegLLKADELEDAKRRQAQKINELQEALDAANSKNASLE 1424
Cdd:COG4717 458 LEAELEQ---------LEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
934-1096 |
1.91e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 934 QLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLnkEKKHQEEINR 1013
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1014 KLMEDLQSEEDKgnhQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKE 1093
Cdd:COG1579 89 KEYEALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
...
gi 17509401 1094 SEL 1096
Cdd:COG1579 166 EEL 168
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
895-1871 |
2.99e-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: 52.75 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 895 SLFTNLES-TKTQLSDAEERLAKLEAQQKDASKQLSEL-NDQLADNEDRTADVQRAKKKIEAEVEALKKQIQ-DLEMSLR 971
Cdd:TIGR01612 675 ALYNELSSiVKENAIDNTEDKAKLDDLKSKIDKEYDKIqNMETATVELHLSNIENKKNELLDIIVEIKKHIHgEINKDLN 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 972 KAESEKQSKDHQIRS-LQDEMQQQDEaiakLNKEKKHQEEINRKLmedlqseEDKGNHQNkvkAKLEQTLDDLEDSLERE 1050
Cdd:TIGR01612 755 KILEDFKNKEKELSNkINDYAKEKDE----LNKYKSKISEIKNHY-------NDQINIDN---IKDEDAKQNYDKSKEYI 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1051 KRARADLDkQKRKVEGELKIAQENIDESGRQRHDLENNLKKKeselhsVSSRLEDEQALVSKLQRQIKDGQSRIseleeE 1130
Cdd:TIGR01612 821 KTISIKED-EIFKIINEMKFMKDDFLNKVDKFINFENNCKEK------IDSEHEQFAELTNKIKAEISDDKLND-----Y 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1131 LENERQSRSKADRAKSDLQRELEELG--EKLDEQGGATAAQVEVNKKREAELAKLRRDLEEaNMNHENQLGGLRKKHTDA 1208
Cdd:TIGR01612 889 EKKFNDSKSLINEINKSIEEEYQNINtlKKVDEYIKICENTKESIEKFHNKQNILKEILNK-NIDTIKESNLIEKSYKDK 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1209 VAE-LTDQLDQLNKAKAKV-----EKDKAQAVRDAEDLAAQLdqetsGKLNNEKLAKQF---ELQLTELQSKADEQSRQL 1279
Cdd:TIGR01612 968 FDNtLIDKINELDKAFKDAslndyEAKNNELIKYFNDLKANL-----GKNKENMLYHQFdekEKATNDIEQKIEDANKNI 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1280 QD-----FTSLKG------RLHSENGDLVRQ--LEDAESQVNQLTRLKSQLTSQ------LEEARRTADEEARERQTVAA 1340
Cdd:TIGR01612 1043 PNieiaiHTSIYNiideieKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYnfddfgKEENIKYADEINKIKDDIKN 1122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1341 QAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADE----LEDAKRRQAQKINELQEALDAA 1416
Cdd:TIGR01612 1123 LDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIEnivtKIDKKKNIYDEIKKLLNEIAEI 1202
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1417 NSKNASLEKTKS------RLVGDLDDAQVDVER--ANGVASALEKKQKGFDKIIDEWRKKTDDLAAELD-GAQRDLRNTS 1487
Cdd:TIGR01612 1203 EKDKTSLEEVKGinlsygKNLGKLFLEKIDEEKkkSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDiKAEMETFNIS 1282
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1488 TDLFK-----AKNAQEELAEV-------VEGLRREN------KSLSQEIKDLTDQLGEGGRSVHEM------------QK 1537
Cdd:TIGR01612 1283 HDDDKdhhiiSKKHDENISDIrekslkiIEDFSEESdindikKELQKNLLDAQKHNSDINLYLNEIaniynilklnkiKK 1362
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1538 IIRRLEIEKEELQHALDEAEAALEAEES--KVLRAQVEVSQIRSEIEKRIQEKE-----------------EE------F 1592
Cdd:TIGR01612 1363 IIDEVKEYTKEIEENNKNIKDELDKSEKliKKIKDDINLEECKSKIESTLDDKDidecikkikelknhilsEEsnidtyF 1442
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1593 ENTRKNHARALESMQaSLETEAKGKAELLRIKKK-----LEGDINELEIALDHANKANADAQKNlKRYQEQVRELqlqVE 1667
Cdd:TIGR01612 1443 KNADENNENVLLLFK-NIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKN-AKAIEKNKEL---FE 1517
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1668 EEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAErARKQAEYEAADARDQANEanaqvssLTSAKRKLEGEIqaih 1747
Cdd:TIGR01612 1518 QYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKD-AHKKFILEAEKSEQKIKE-------IKKEKFRIEDDA---- 1585
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1748 adldetlneykAAEERSKKAIADATRLAEELRQE-------QEHSQHVDRLRKGLEQQLKEIQVRLDEAEaaaLKGGKKV 1820
Cdd:TIGR01612 1586 -----------AKNDKSNKAAIDIQLSLENFENKflkisdiKKKINDCLKETESIEKKISSFSIDSQDTE---LKENGDN 1651
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1821 IAKLEQRvreLESeLDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFE 1871
Cdd:TIGR01612 1652 LNSLQEF---LES-LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE 1698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1601-1865 |
4.05e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1601 RALESMQASLETEAKGKAELLRIKKKLEGDineLEIALDHANKA-NA-DAQKNLKRYQEQVRELQLQVEEEQRNGADTRE 1678
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQD---YQAASDHLNLVqTAlRQQEKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1679 QFFNAEKRATLLQSEKEELLV---------------------ANEAAERARKQ---AEYEAADARDQANEANAQVSSLTS 1734
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSqladyqqaldvqqtraiqyqqAVQALEKARALcglPDLTPENAEDYLAAFRAKEQQATE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1735 AKRKLEGEIqaihADLDETLNEYKAAEERSKKAIADATRLA------EELRQEQEHSQHVDRLrKGLEQQLKEIQVRLDE 1808
Cdd:COG3096 456 EVLELEQKL----SVADAARRQFEKAYELVCKIAGEVERSQawqtarELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQ 530
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1809 AEAAA--LKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDE 1865
Cdd:COG3096 531 QQNAErlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
912-1280 |
4.41e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 912 ERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAEsekqskdhQIRSLQDEM 991
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE--------KIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 992 qqqDEAIAKLNKEKKHQEEINRKLMEdlqSEEDKGNHQNKVK------AKLEQTLDDLE-------DSLEREKRARA--- 1055
Cdd:COG3096 357 ---EELTERLEEQEEVVEEAAEQLAE---AEARLEAAEEEVDslksqlADYQQALDVQQtraiqyqQAVQALEKARAlcg 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1056 --DLDKQkrKVEGELKIAQENIDESGRQRHDLENNLkkkeselhSVSS--RLEDEQALvsKLQRQIKDGQSRISELEEEL 1131
Cdd:COG3096 431 lpDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKL--------SVADaaRRQFEKAY--ELVCKIAGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1132 ENERQSRSK---ADRAKSdLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKlRRDLEEANMNHENQLGGLRKKHTDA 1208
Cdd:COG3096 499 ELLRRYRSQqalAQRLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1209 VAELTDQLDQLNKAKAKVEK--DKAQAVRDAEDLAAQLdQETSGK---------------LNNEKLAKQFELQLTELQSK 1271
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKElaARAPAWLAAQDALERL-REQSGEaladsqevtaamqqlLEREREATVERDELAARKQA 655
|
....*....
gi 17509401 1272 ADEQSRQLQ 1280
Cdd:COG3096 656 LESQIERLS 664
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1208-1861 |
4.60e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1208 AVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLA-KQFELQLtelqSKADEQSRQLQDFTSLK 1286
Cdd:pfam12128 266 GYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvAKDRSEL----EALEDQHGAFLDADIET 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1287 GRLHSENGDLVR-QLEdaesqvNQLTRLKSQLTSQLE-EARRTADEEARERQTVAAQAKNYQHEAEQlqesleeeiegKN 1364
Cdd:pfam12128 342 AAADQEQLPSWQsELE------NLEERLKALTGKHQDvTAKYNRRRSKIKEQNNRDIAGIKDKLAKI-----------RE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1365 EILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKnaslektkSRLVGDLDDAQVDVERA 1444
Cdd:pfam12128 405 ARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT--------PELLLQLENFDERIERA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1445 NgvaSALEKKQKGFDKIIDEWRKktddLAAELDGAQRDLRNTSTDLFKAKNAQEELAEV--------VEGLRRENKSLSQ 1516
Cdd:pfam12128 477 R---EEQEAANAEVERLQSELRQ----ARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtlLHFLRKEAPDWEQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1517 EI---------------KDLTDQLGEGGRSVHEMQKIIRRLEIEK-----EELQHALDEAEAALEAEESKVLRAQVEVSQ 1576
Cdd:pfam12128 550 SIgkvispellhrtdldPEVWDGSVGGELNLYGVKLDLKRIDVPEwaaseEELRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1577 IRSEIEKriQEKEEEF-----ENTRKNHARALESMQAslETEAKGKAELLRIKKKlegdiNELEIALDHANKANADAQKN 1651
Cdd:pfam12128 630 ANGELEK--ASREETFartalKNARLDLRRLFDEKQS--EKDKKNKALAERKDSA-----NERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1652 -LKRYQEQVRELQLQVEEEQRngadtreqffnaekratllqsEKEELLVANEAAERARKQAEYEAADARDQANEanaqvs 1730
Cdd:pfam12128 701 wLEEQKEQKREARTEKQAYWQ---------------------VVEGALDAQLALLKAAIAARRSGAKAELKALE------ 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1731 slTSAKRKLEGEiqaihaDLDE-TLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHvdrlRKGLEQQLKEIQVRLDEA 1809
Cdd:pfam12128 754 --TWYKRDLASL------GVDPdVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQE----TWLQRRPRLATQLSNIER 821
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1810 EAAALKGG-KKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQF 1861
Cdd:pfam12128 822 AISELQQQlARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1715-1962 |
4.68e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1715 AADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEhsqHVDRLRKG 1794
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1795 LEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQ 1874
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1875 DLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRASASVAPGLQSSASAAVIRS 1954
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*...
gi 17509401 1955 PSRARASD 1962
Cdd:COG3883 248 GAGAAGAA 255
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1013-1299 |
5.45e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.59 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1013 RKLMEDL-QSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRAradldKQKRKVEGEL-KIAQE---NIDESGRQRHDLEN 1087
Cdd:PRK10929 26 KQITQELeQAKAAKTPAQAEIVEALQSALNWLEERKGSLERA-----KQYQQVIDNFpKLSAElrqQLNNERDEPRSVPP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1088 NLKKK--ESELHSVSSRLEDEQALVSKLQ---RQIKDGQSRISeleeelenerQSRSKADRAKSDLQRELEELGEKLD-- 1160
Cdd:PRK10929 101 NMSTDalEQEILQVSSQLLEKSRQAQQEQdraREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTpl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1161 EQGGATAAQVEVNKKR----EAELAKLrrdleeaNMNHENQLGGLR-----KKHTDAVAELTDQLDQLNkakAKVEKDKA 1231
Cdd:PRK10929 171 AQAQLTALQAESAALKalvdELELAQL-------SANNRQELARLRselakKRSQQLDAYLQALRNQLN---SQRQREAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1232 QAVRDAEDLAaqldqETSGKLNNEkLAKQFELQlTELqSKADEQSRQLQDFTSLKGRLHSENGDLVRQ 1299
Cdd:PRK10929 241 RALESTELLA-----EQSGDLPKS-IVAQFKIN-REL-SQALNQQAQRMDLIASQQRQAASQTLQVRQ 300
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
917-1435 |
6.25e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 917 LEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVE-----------------ALKKQIQDLEMSLRKAESEKQS 979
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNnamddynnlksalnelsSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 980 ---KDHQIRSLQDEMQQ-------------------------QDEAIAKLNKEKKHQEEINRKLmEDLQSEEDKGNHQNK 1031
Cdd:PRK01156 268 eleKNNYYKELEERHMKiindpvyknrnyindyfkykndienKKQILSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1032 VKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVS 1111
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1112 KLQRQIKDGQSRISELEEELENERQ-----------SRSKADRAKSDLQRELEELGEKLDEqggataAQVEVnKKREAEL 1180
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMEMLNGqsvcpvcgttlGEEKSNHIINHYNEKKSRLEEKIRE------IEIEV-KDIDEKI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1181 AKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNneKLAKQ 1260
Cdd:PRK01156 500 VDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLN--ALAVI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1261 FELQLTELQSKADEQSRQLQDftsLKGRLHsengDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAA 1340
Cdd:PRK01156 578 SLIDIETNRSRSNEIKKQLND---LESRLQ----EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRG 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1341 QAKNYQHEAeqlqESLEEEIEGKNEILRQLSKANADIQQWKARFEgEGLLKADELEDAKRRQAQKINELQEALDAANSKN 1420
Cdd:PRK01156 651 KIDNYKKQI----AEIDSIIPDLKEITSRINDIEDNLKKSRKALD-DAKANRARLESTIEILRTRINELSDRINDINETL 725
|
570
....*....|....*
gi 17509401 1421 ASLEKTKsRLVGDLD 1435
Cdd:PRK01156 726 ESMKKIK-KAIGDLK 739
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
926-1248 |
6.41e-06 |
|
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: 51.01 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 926 KQLSELNDQLADNEDRTA--DVQRAKK---KIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAK 1000
Cdd:pfam06160 153 KQLAEIEEEFSQFEELTEsgDYLEAREvleKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1001 LNKEKKHQ--EEINRKLMEDLQSEEDKGNHQNKvkAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENides 1078
Cdd:pfam06160 233 LNVDKEIQqlEEQLEENLALLENLELDEAEEAL--EEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1079 grqrhdleNNLKKKESELHSVSSRL-EDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGE 1157
Cdd:pfam06160 307 --------NKELKEELERVQQSYTLnENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1158 KLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQ-LGGLRKKHTDAVAELTDQLDQLNKA--KAKVEKDKAQA- 1233
Cdd:pfam06160 379 EQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKSnLPGLPESYLDYFFDVSDEIEDLADElnEVPLNMDEVNRl 458
|
330
....*....|....*
gi 17509401 1234 VRDAEDLAAQLDQET 1248
Cdd:pfam06160 459 LDEAQDDVDTLYEKT 473
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1590-1908 |
6.95e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1590 EEFENTRKNHARALESMQASLETEAKGKAELLrikkklegdinelEIALDHANKAnaDAQKNLKRYQEQVRELQLqveEE 1669
Cdd:COG3206 107 EDPLGEEASREAAIERLRKNLTVEPVKGSNVI-------------EISYTSPDPE--LAAAVANALAEAYLEQNL---EL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1670 QRNGADTREQFFNAEkratlLQSEKEELlvanEAAERARK--QAEYEAADARDQANEANAQVSSLTSakrklegEIQAIH 1747
Cdd:COG3206 169 RREEARKALEFLEEQ-----LPELRKEL----EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELES-------QLAEAR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1748 ADLDETLNEYKAAEERSKKAIADATRLAEelrqeqehsqhvDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAkLEQR 1827
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQ------------SPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-LRAQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1828 VRELESELDGE-QRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLidklQQKLKTQKKQVEEAEELANLNLQKYK 1906
Cdd:COG3206 300 IAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLE 375
|
..
gi 17509401 1907 QL 1908
Cdd:COG3206 376 EA 377
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1177-1346 |
8.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1177 EAELAKLRRDLEEAnmnhENQLGGLRKKHTDAVAE-----LTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQ--ETS 1249
Cdd:COG3206 181 EEQLPELRKELEEA----EAALEEFRQKNGLVDLSeeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgpDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1250 GKLNNEKLAKQFELQLTELQSKADEQSRQLQD-----------FTSLKGRLHSENGDLVRQLED----AESQVNQLTRLK 1314
Cdd:COG3206 257 PELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialraqIAALRAQLQQEAQRILASLEAeleaLQAREASLQAQL 336
|
170 180 190
....*....|....*....|....*....|..
gi 17509401 1315 SQLTSQLEEARRTADEEARERQTVAAQAKNYQ 1346
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVARELYE 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1450-1843 |
9.91e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1450 ALEKKQKGFDKIIDEWRKKTDDLA------AELDGAQRDLRNTSTDLFKAKNAQEELAEVVEgLRRENKSLSQEIKDLTD 1523
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEeleeelEELEAELEELREELEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1524 QLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARAL 1603
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1604 ESMQASLETEAKGKAE-----------LLRIKKKLEGDINE-----------LEIALDHANKANADAQKNLKRYQEQVRE 1661
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTiagvlflvlglLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1662 LQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTS------- 1734
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraaleq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1735 --AKRKLEGEIQAIHADLDETLNEYKAAEErskkaIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEaa 1812
Cdd:COG4717 394 aeEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE-- 466
|
410 420 430
....*....|....*....|....*....|.
gi 17509401 1813 alkgGKKVIAKLEQRVRELESELDGEQRRFQ 1843
Cdd:COG4717 467 ----EDGELAELLQELEELKAELRELAEEWA 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1472-1723 |
1.05e-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: 50.15 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1472 LAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQH 1551
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1552 ALDEAEAALEAEE---SKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLE 1628
Cdd:COG4942 91 EIAELRAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1629 GDINELEialdhankanadaqKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERAR 1708
Cdd:COG4942 171 AERAELE--------------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*
gi 17509401 1709 KQAEYEAADARDQAN 1723
Cdd:COG4942 237 AAAAERTPAAGFAAL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1618-1778 |
1.06e-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: 48.77 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1618 AELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNA--EKRATLLQSEKE 1695
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1696 ellvaneAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIAD-ATRL 1774
Cdd:COG1579 100 -------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREElAAKI 172
|
....
gi 17509401 1775 AEEL 1778
Cdd:COG1579 173 PPEL 176
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
945-1073 |
1.07e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.53 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 945 VQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKkhqEEINRKLMEDLQSEed 1024
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK---EEILEKAREEAEEI-- 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1025 kgnhQNKVKAKLEQTLDDLEDSLERE---KRARADLDKQKRKVEGELKIAQE 1073
Cdd:COG1193 577 ----LREARKEAEELIRELREAQAEEeelKEARKKLEELKQELEEKLEKPKK 624
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1633-1843 |
1.11e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.46 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1633 ELEIALDHANKANADAQKNLKRYQEQVREL---QLQVEEEQRNgADTREQFFNAEKRATLLQsEKEELLVANEAA----- 1704
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELeaaALQPGEEEEL-EEERRRLSNAEKLREALQ-EALEALSGGEGGaldll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1705 ERARKQAEyEAADARDQANEANAQVSS----LTSAKRKLEGEIQAIHAD------LDETLNEYKAAEERSKKAIADATRL 1774
Cdd:COG0497 247 GQALRALE-RLAEYDPSLAELAERLESalieLEEAASELRRYLDSLEFDperleeVEERLALLRRLARKYGVTVEELLAY 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1775 AEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAeAAAL-KGGKKVIAKLEQRVRELESELDGEQRRFQ 1843
Cdd:COG0497 326 AEELRAELAELENSDERLEELEAELAEAEAELLEA-AEKLsAARKKAAKKLEKAVTAELADLGMPNARFE 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1163-1429 |
1.12e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1163 GGATAAQVEVNKKREAELAKLRRDLEEANmNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAA 1242
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1243 QLDQetsgklNNEKLAKQFElQLTELQSKADEQSRQlqdfTSLKGRLHSEN-GDLVRQLEDAESQVNQLTRLKSQLTSQL 1321
Cdd:COG4942 91 EIAE------LRAELEAQKE-ELAELLRALYRLGRQ----PPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1322 EEARRTADEEARERQTVAAQAKnyqhEAEQLQESLEEEIEGKNEILRQLSKANADIQQwkarfegegllKADELEDAKRR 1401
Cdd:COG4942 160 AELAALRAELEAERAELEALLA----ELEEERAALEALKAERQKLLARLEKELAELAA-----------ELAELQQEAEE 224
|
250 260
....*....|....*....|....*...
gi 17509401 1402 QAQKINELQEALDAANSKNASLEKTKSR 1429
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
941-1195 |
1.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 941 RTADVQRAKKKIEAEVEALKKQIQDLemslRKAESEKQSK--DHQIRSLQDEMQQQDEAIAKLNKEKKhqeeinrklMED 1018
Cdd:COG3206 143 TSPDPELAAAVANALAEAYLEQNLEL----RREEARKALEflEEQLPELRKELEEAEAALEEFRQKNG---------LVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1019 LQSEEDKgnhqnkvkakLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRH--DLENNLKKKESEL 1096
Cdd:COG3206 210 LSEEAKL----------LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1097 HSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAK-SDLQRELEELGEKLDEQGgataaqvevnkK 1175
Cdd:COG3206 280 AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAReASLQAQLAQLEARLAELP-----------E 348
|
250 260
....*....|....*....|
gi 17509401 1176 REAELAKLRRDLEEANMNHE 1195
Cdd:COG3206 349 LEAELRRLEREVEVARELYE 368
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1466-1878 |
1.19e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1466 RKKTDDLAAELdgaQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIR-RLEI 1544
Cdd:PRK04863 281 RRVHLEEALEL---RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERyQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1545 EKEELQhaldeaeaaleaeeskvLRAQVEVSQ----IRSEIEKRIQEKEEEFENTRK---NHARALESMQ--ASLETEAK 1615
Cdd:PRK04863 358 EELEER-----------------LEEQNEVVEeadeQQEENEARAEAAEEEVDELKSqlaDYQQALDVQQtrAIQYQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1616 gkaELLRIKKKLEGdineleiaLDHANKANADA-QKNLKRYQEQVRELQLQVEEEQRNGADTREQFfnaEKRATLLQSek 1694
Cdd:PRK04863 421 ---QALERAKQLCG--------LPDLTADNAEDwLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF---EQAYQLVRK-- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1695 eelLVANEAAERARKQAEYEAADARDQANEAnAQVSSLTSAKRKLEGEIQAiHADLDETLNEYKAAEERSKKAIADATRL 1774
Cdd:PRK04863 485 ---IAGEVSRSEAWDVARELLRRLREQRHLA-EQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1775 AEELRQEQEHSQ----HVDRLRKGLEQQLKEIQVRLDEAEAAALK--GGKKVIAKL-EQRVRELESELDGEQRRFQDAnk 1847
Cdd:PRK04863 560 QEELEARLESLSesvsEARERRMALRQQLEQLQARIQRLAARAPAwlAAQDALARLrEQSGEEFEDSQDVTEYMQQLL-- 637
|
410 420 430
....*....|....*....|....*....|.
gi 17509401 1848 nlgradRRVRELQFQVDEDKKNFERLQDLID 1878
Cdd:PRK04863 638 ------ERERELTVERDELAARKQALDEEIE 662
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1469-1949 |
1.21e-05 |
|
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: 50.74 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1469 TDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKdLTDQLGEGGRSVHEMQKIIRRLEIEKEE 1548
Cdd:TIGR00618 207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1549 LQHALDEAEAALEAeeskvlRAQVEVSQIRSEIEKRIQEKEEEFENTRKnHARALESMQASLETEAKGKAELLRIKKKLE 1628
Cdd:TIGR00618 286 INRARKAAPLAAHI------KAVTQIEQQAQRIHTELQSKMRSRAKLLM-KRAAHVKQQSSIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1629 GDINELEIALDHANKANADAQ----------------KNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQS 1692
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQhihtlqqqkttltqklQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1693 EKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKlEGEIQAIHADLDETLNEYKAAEERSKKAIADAT 1772
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1773 RLAEE--------LRQEQEHSQHVDRLRKgLEQQLKEI--QVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRF 1842
Cdd:TIGR00618 518 QDIDNpgpltrrmQRGEQTYAQLETSEED-VYHQLTSErkQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1843 QDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELAnLNLQKYKQLTHQL---EDAEERA 1919
Cdd:TIGR00618 597 QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ-LTLTQERVREHALsirVLPKELL 675
|
490 500 510
....*....|....*....|....*....|
gi 17509401 1920 DQAENSLSKMRSKSRASASVAPGLQSSASA 1949
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1034-1334 |
1.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1034 AKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHdlennLKKKESELhsvsSRLEDEQALVSKL 1113
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-----IAELEAEL----ERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1114 QRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLD--EQGGATAAQVEVNKKREAELAKLRRDLEEAN 1191
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaEDLARLELRALLEERFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1192 MnhENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQetsgkLNNEKLAkQFELQLTELQsk 1271
Cdd:COG4913 771 L--EERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDR-----LEEDGLP-EYEERFKELL-- 840
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1272 adeQSRQLQDFTSLKGRLHSENGDLVRQLEDaesqVNQ-LTRLKSQLTSQLE-EARRTADEEARE 1334
Cdd:COG4913 841 ---NENSIEFVADLLSKLRRAIREIKERIDP----LNDsLKRIPFGPGRYLRlEARPRPDPEVRE 898
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1397-1619 |
1.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1397 DAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDE-----------W 1465
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelraeL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1466 RKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLgeggrsvHEMQKIIRRLEIE 1545
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1546 KEELQhaldEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNhARALESMQASLETEAKGKAE 1619
Cdd:COG4942 173 RAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
648-682 |
1.42e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 17509401 648 SGSFMTV------SMLYRESLNNLMTMLNKTHPHFIRCIIP 682
Cdd:cd01363 130 FGKFIEIlldiagFEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1697-1961 |
1.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1697 LLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAE 1776
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1777 ELRQeqehsqhvdrLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAkleqrvreleseldgeqrrfqdANKNLGRADRRV 1856
Cdd:COG4942 91 EIAE----------LRAELEAQKEELAELLRALYRLGRQPPLALLL----------------------SPEDFLDAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1857 RELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRAS 1936
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*
gi 17509401 1937 ASVAPGLQSSASAAVIRSPSRARAS 1961
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERT 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
869-1081 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 869 EDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRA 948
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 949 KKKIEAEVEALK-----KQIQDLemsLRKAESEKQSKDHQirslQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEE 1023
Cdd:COG3883 95 LYRSGGSVSYLDvllgsESFSDF---LDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1024 DKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQ 1081
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1582-1935 |
1.73e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1582 EKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEG----DINELEIALDHANKANADAQKNLKRYQE 1657
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1658 QVRELQLQVEEEQRNGADTREQFfnaekrATLLQSEKEELlvanEAAERARKQAEYEAADARDQANEANAQVSSLTSAKR 1737
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEA------AALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1738 KLEGEIQAIHADLDETLN-------------EYKAAEERSKKAI------------------ADATRL------------ 1774
Cdd:COG4913 437 NIPARLLALRDALAEALGldeaelpfvgeliEVRPEEERWRGAIervlggfaltllvppehyAAALRWvnrlhlrgrlvy 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1775 --------------------------------------------------AEELRQEQ-------------EHSQHVDRL 1791
Cdd:COG4913 517 ervrtglpdperprldpdslagkldfkphpfrawleaelgrrfdyvcvdsPEELRRHPraitragqvkgngTRHEKDDRR 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1792 R---------------KGLEQQLKEIQVRLDEAEAAalkggkkvIAKLEQRVRELESELDGEQR--RFQDANKNLGRADR 1854
Cdd:COG4913 597 RirsryvlgfdnraklAALEAELAELEEELAEAEER--------LEALEAELDALQERREALQRlaEYSWDEIDVASAER 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1855 RVRELQ---FQVDEDKKNFERLQDLIDKLQQKlktqkkqVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRS 1931
Cdd:COG4913 669 EIAELEaelERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
....
gi 17509401 1932 KSRA 1935
Cdd:COG4913 742 LARL 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1096-1343 |
2.82e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1096 LHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQggataaqvevnkk 1175
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1176 rEAELAKLRRDLEEAnmnhENQLGGLRkkhtDAVAELTDQLDQLNKAKAKVE----KDKAQAVRDAEDLAAQLDQetsgk 1251
Cdd:COG4942 82 -EAELAELEKEIAEL----RAELEAQK----EELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPA----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1252 lnNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEE 1331
Cdd:COG4942 148 --RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|..
gi 17509401 1332 ARERQTVAAQAK 1343
Cdd:COG4942 226 EALIARLEAEAA 237
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1231-1950 |
2.95e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1231 AQAVRDAEDLAAQLDQETSGKLnnEKLAKQFELqLTELQSKADEQSRQL----QDFTSLKGRLHSENGDLvRQLEDAESQ 1306
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSR--RQLAAEQYR-LVEMARELAELNEAEsdleQDYQAASDHLNLVQTAL-RQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1307 VNQLTRLKSQLTSQlEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEgkneilRQLSKANADIQQWKARFEG 1386
Cdd:PRK04863 354 QADLEELEERLEEQ-NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD------VQQTRAIQYQQAVQALERA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1387 EGLLKADEL--EDAKRRQAQKINELQEALDAANS---KNASLEKTKSR------LVGDLDDaQVDVERANGVASALEK-- 1453
Cdd:PRK04863 427 KQLCGLPDLtaDNAEDWLEEFQAKEQEATEELLSleqKLSVAQAAHSQfeqayqLVRKIAG-EVSRSEAWDVARELLRrl 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1454 -KQKGFDKIIDEWRKKTDDLAAELDgAQRDLRNTSTDLFKAKNAQEELAEVVEGLRREnksLSQEIKDLTDQLGEGGRSV 1532
Cdd:PRK04863 506 rEQRHLAEQLQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1533 HEMQKIIRRLEIEKEELQ--------------------HALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEF 1592
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAarapawlaaqdalarlreqsGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1593 ENTRKNHARALESMQA-----------------SLE----TEAK-GKA-------ELLRIKKKLEG------DINELEIA 1637
Cdd:PRK04863 662 ERLSQPGGSEDPRLNAlaerfggvllseiyddvSLEdapyFSALyGPArhaivvpDLSDAAEQLAGledcpeDLYLIEGD 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1638 LDHANKANADAQKNLKRYQEQVRELQL---QVEEEQRNGADTREqffnaeKRATLLQSEKEEL--LVANEAAERARKQAE 1712
Cdd:PRK04863 742 PDSFDDSVFSVEELEKAVVVKIADRQWrysRFPEVPLFGRAARE------KRIEQLRAEREELaeRYATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1713 YEAADARDQANEA-------NAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERskkaiadatrlaeeLRQEQEHS 1785
Cdd:PRK04863 816 HQAFSRFIGSHLAvafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEG--------------LSALNRLL 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1786 QHVDRL-RKGLEQQLKEIQVRLDEAEAAA--LKGGKKVIAKLEQRV---RELESELDGEQRRFQDANKNLGRADRRVREL 1859
Cdd:PRK04863 882 PRLNLLaDETLADRVEEIREQLDEAEEAKrfVQQHGNALAQLEPIVsvlQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL 961
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1860 QfQVDEDKKNFerlqdlidklqqklktqkkQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRASASV 1939
Cdd:PRK04863 962 T-EVVQRRAHF-------------------SYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQV 1021
|
810
....*....|.
gi 17509401 1940 APGLQSSASAA 1950
Cdd:PRK04863 1022 LASLKSSYDAK 1032
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1325 |
3.22e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 858 LEKINDKVKALEDslakeekLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQlad 937
Cdd:pfam05483 263 LEESRDKANQLEE-------KTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 938 NEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQE----EINR 1013
Cdd:pfam05483 333 KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEveleELKK 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1014 ----------------KLMEDLQSEE----------DKGNHQNKVKAKLEQT--------LDDLEDSLEREKRARADLDK 1059
Cdd:pfam05483 413 ilaedeklldekkqfeKIAEELKGKEqelifllqarEKEIHDLEIQLTAIKTseehylkeVEDLKTELEKEKLKNIELTA 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1060 QKRKVEGELK-IAQENID---ESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQ--------------------- 1114
Cdd:pfam05483 493 HCDKLLLENKeLTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqkgdevkckldkse 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1115 ---RQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVnkkREAELAKLRRDLEEAN 1191
Cdd:pfam05483 573 enaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNA---YEIKVNKLELELASAK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1192 MNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEK----DKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTE 1267
Cdd:pfam05483 650 QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL 729
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1268 LQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEAR 1325
Cdd:pfam05483 730 YKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1726-1930 |
3.43e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1726 NAQVSSLTSAKRKLEGEIQAIHADLDET---LNEYKAA------EERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLE 1796
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAeaaLEEFRQKnglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1797 QQLKEIQVRLDEAEAAAlkggkkVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVD-EDKKNFERLQD 1875
Cdd:COG3206 247 AQLGSGPDALPELLQSP------VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1876 LIDKLQQKLKTQKKQVEEAE-ELANLN--LQKYKQLTHQLEDAEERADQAENSLSKMR 1930
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEaRLAELPelEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
901-1118 |
3.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 901 ESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQrakkkIEAEVEALKKQIQDLEMSLRKAESEKQSK 980
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 981 DHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRklMEDLQSEEdkgnhqnkvkAKLEQTLDDLEDSLEREKRARADLDKQ 1060
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQ--LAELEAEL----------AELSARYTPNHPDVIALRAQIAALRAQ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1061 KRKVEGELKIAQENIDESGRQRhdlENNLKKKESELHSVSSRLEDEQALVSKLQRQIK 1118
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAR---EASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
949-1268 |
3.76e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 949 KKKIEAEVEALKK----QIQDLEmslrkaeseKQSKDHQIRSLQDEMQQQDEAIAKLNK--EKKHQEEINRKLMEDLQSE 1022
Cdd:PRK05771 15 KSYKDEVLEALHElgvvHIEDLK---------EELSNERLRKLRSLLTKLSEALDKLRSylPKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1023 EdkgnhqnkVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQ--ENIDEsgrqrhDLENnlkkkESELHSVS 1100
Cdd:PRK05771 86 E--------LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDL------DLSL-----LLGFKYVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1101 srledeqALVSKLQRQIKDGQSRISELEEELENeRQSRSK-------ADRAKSDLQRELEELG-EKLDEQGGATAAqvEV 1172
Cdd:PRK05771 147 -------VFVGTVPEDKLEELKLESDVENVEYI-STDKGYvyvvvvvLKELSDEVEEELKKLGfERLELEEEGTPS--EL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1173 NKKREAELAKLRRDLEEAnmnhENQLGGLRKKHTDAVAELTDQLDQ-LNKAKAKVE---KDKAQAV------RDAEDLAA 1242
Cdd:PRK05771 217 IREIKEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIeLERAEALSKflkTDKTFAIegwvpeDRVKKLKE 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17509401 1243 QLDQETSG------------------KLNNEKLAKQFELqLTEL 1268
Cdd:PRK05771 293 LIDKATGGsayvefvepdeeeeevptKLKNPKFIKPFES-LTEM 335
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1297-1718 |
3.84e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1297 VRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGK------------N 1364
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPErleeleerleelR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1365 EILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERA 1444
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1445 NgvasALEKKQKGFDKIIDEwrkktdDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEG-LRRENKSLSQEIKDLTD 1523
Cdd:COG4717 240 A----LEERLKEARLLLLIA------AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLlLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1524 QLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEesKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARAL 1603
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL--QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1604 ESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQknLKRYQEQVRELQLQVEEEQRNGADTREQFFNA 1683
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|....*
gi 17509401 1684 EKRATLLQSEKEELLVANEAAERARKQAEYEAADA 1718
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
807-1049 |
3.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 807 LKDRKRRMEQRAGLLIVQRNVRSWCTLRTWEWFKLYGKVKPMLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESS 886
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 887 AKLVEEKTSLFTNLESTKTQLSDAEERlakLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDL 966
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDR---LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 967 EMSLRKAESEKQSKDH-QIRSLQDEMQQQDEAIAKLNKEK-----KHQEEINRKLMEdlQSEEDKGNHQNKVKAKLE--- 1037
Cdd:COG4913 786 EEELERAMRAFNREWPaETADLDADLESLPEYLALLDRLEedglpEYEERFKELLNE--NSIEFVADLLSKLRRAIReik 863
|
250
....*....|..
gi 17509401 1038 QTLDDLEDSLER 1049
Cdd:COG4913 864 ERIDPLNDSLKR 875
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
899-1320 |
4.19e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 899 NLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADV----QRAKKKIEAE-------VEALKKQIQDLE 967
Cdd:PRK04778 99 RFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyRELRKSLLANrfsfgpaLDELEKQLENLE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 968 MSLRKAESEKQSKDH-----QIRSLQDEMQQQDEAIaklnkekkhqEEInRKLMEDLQSEedkgnhqnkvkakLEQTLDD 1042
Cdd:PRK04778 179 EEFSQFVELTESGDYveareILDQLEEELAALEQIM----------EEI-PELLKELQTE-------------LPDQLQE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1043 LEDSLEREKRARADLDKQkrKVEGELKIAQENIDESGRQRHDLEnnLKKKESELHSVSSRLEDeqaLVSKLQRQIKDGQS 1122
Cdd:PRK04778 235 LKAGYRELVEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQ---LYDILEREVKARKY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1123 riseLEEELENERQSRSKADRAKSDLQRELEELGEK--LDEQggataaQVEVNKKREAELAKLRRDLEEANMNHENQlgg 1200
Cdd:PRK04778 308 ----VEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSytLNES------ELESVRQLEKQLESLEKQYDEITERIAEQ--- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1201 lRKKHTDAVAELTDQLDQLNKAKAKVEK--DKAQAVRDAE----DLAAQLDQETSG------KLNNEKLAKQFELQLTEL 1268
Cdd:PRK04778 375 -EIAYSELQEELEEILKQLEEIEKEQEKlsEMLQGLRKDElearEKLERYRNKLHEikryleKSNLPGLPEDYLEMFFEV 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1269 QSKADEQSRQLQdftslKGRLHSEngDLVRQLEDAESQVNQLTRLKSQLTSQ 1320
Cdd:PRK04778 454 SDEIEALAEELE-----EKPINME--AVNRLLEEATEDVETLEEETEELVEN 498
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
851-987 |
4.94e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 851 AGKEaEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEktslftnLESTKTQLSDAEERLAKLEAQQKDASKQLSE 930
Cdd:PRK09039 49 SGKD-SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS-------LSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 931 LNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSL 987
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1579-1776 |
5.11e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1579 SEIEKRIQEKEEEFENTRKNharaLESMQASLEtEAKGKAEllrikkKLEGDINELEIALDHANKANADAQKNLKRYQEQ 1658
Cdd:COG3883 19 QAKQKELSELQAELEAAQAE----LDALQAELE-ELNEEYN------ELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1659 VRElqlQVEEEQRNGADTR--EQFFNAE------KRATLL--------------QSEKEELLVANEAAERARKQAEYEAA 1716
Cdd:COG3883 88 LGE---RARALYRSGGSVSylDVLLGSEsfsdflDRLSALskiadadadlleelKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1717 DARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAE 1776
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
926-1066 |
6.26e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 47.36 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 926 KQLSELNDQLADNEDrTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESekqskdhQIRSLQDEMQQQDEAIAKLNKE- 1004
Cdd:cd22656 94 AEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVD-------KLTDFENQTEKDQTALETLEKAl 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1005 ----KKHQEEINRKLMEDLQSEEDKGNHQNKVKAK-----LEQTLDDLEDSLEREKRARADLDKQKRKVEG 1066
Cdd:cd22656 166 kdllTDEGGAIARKEIKDLQKELEKLNEEYAAKLKakideLKALIADDEAKLAAALRLIADLTAADTDLDN 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
901-1017 |
6.51e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 901 ESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTAD-VQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQS 979
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17509401 980 --KDHQirsLQDEMQQQDEAIAKLNKEKKHQEEINRKLME 1017
Cdd:PRK00409 603 svKAHE---LIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1458-1949 |
6.98e-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: 48.19 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1458 FDKIIDEWRKKTDDLAAELDGAQR-------DLRNTSTDL-FKAKNAQEELAEVVEGLRRENKSlsQEikDLTDQLGEgg 1529
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNElhekqkfYLRQSVIDLqTKLQEMQMERDAMADIRRRESQS--QE--DLRNQLQN-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1530 rSVHEMQKIiRRLEIEKEELQHALDEAEAALEAEESKVLRaqvEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQAS 1609
Cdd:pfam15921 150 -TVHELEAA-KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ---EIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1610 LETEAKGKAELLRikkkleGDINELEIALDhANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTrEQFFNAEKRATL 1689
Cdd:pfam15921 225 ILRELDTEISYLK------GRIFPVEDQLE-ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLT-EKASSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1690 LQSEKEELlvaneaAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIqaihadldetlneykaaEERSKKAIA 1769
Cdd:pfam15921 297 IQSQLEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKI-----------------EELEKQLVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1770 DATRLAEELRQEQEHSQHvdrlRKGLEQQLKeiqvrldeaeaaalkggkKVIAKLEQRVRELESELDGEQRRFQDANKNL 1849
Cdd:pfam15921 354 ANSELTEARTERDQFSQE----SGNLDDQLQ------------------KLLADLHKREKELSLEKEQNKRLWDRDTGNS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1850 GRADRRVRELqfqvDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEE--RADQAENSLS 1927
Cdd:pfam15921 412 ITIDHLRREL----DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlRKVVEELTAK 487
|
490 500
....*....|....*....|....
gi 17509401 1928 KM--RSKSRASASVAPGLQSSASA 1949
Cdd:pfam15921 488 KMtlESSERTVSDLTASLQEKERA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1231-1479 |
7.92e-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: 47.07 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1231 AQAVRDAEDLAAQLDQetsgklnNEKLAKQFELQLTELQSKADEQSRQLQDftslkgrLHSENGDLVRQLEDAESQVNQL 1310
Cdd:COG4942 16 AAQADAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAA-------LERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1311 TRLKSQLTSQLEEARRtadEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGeglL 1390
Cdd:COG4942 82 EAELAELEKEIAELRA---ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE---L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1391 KAD--ELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKK 1468
Cdd:COG4942 156 RADlaELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|.
gi 17509401 1469 TDDLAAELDGA 1479
Cdd:COG4942 236 AAAAAERTPAA 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
887-1025 |
8.20e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 887 AKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLadNEDRTADVQRAkkkIEAEVEALKKQIQDL 966
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL--GNVRNNKEYEA---LQKEIESLKRRISDL 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 967 EMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDK 1025
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1034-1182 |
9.58e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1034 AKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESgRQRHDLENNLKkkesELHSVSSRLEdeqalvsKL 1113
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-EEQLGNVRNNK----EYEALQKEIE-------SL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1114 QRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAK 1182
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1580-1927 |
1.01e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1580 EIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQV 1659
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1660 RELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKL 1739
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1740 EGEIQAIHADLDETLNEykAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKK 1819
Cdd:COG4372 163 QEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1820 VIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELAN 1899
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340
....*....|....*....|....*...
gi 17509401 1900 LNLQKYKQLTHQLEDAEERADQAENSLS 1927
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLV 348
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1152-1604 |
1.24e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1152 LEELGEKLDEQGGATAAQVEVNKKreaELAKLRRDLEEAnmnhenqlgglrKKHTDAVAELTDQLDQLNKAKAKVEKDKA 1231
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEA------------EEKEEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1232 QAVRDAEDLAAQLD--------QETSGKLNN-EKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDL----VR 1298
Cdd:COG4717 113 ELREELEKLEKLLQllplyqelEALEAELAElPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1299 QLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGkneILRQLSKANADIQ 1378
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA---ALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1379 QWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGF 1458
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1459 DKIIDEWRKKTDDLAAEldgaqrDLRNTSTDLFKAKNAQ--EELAEVVEGLRRENKsLSQEIKDLTDQLGEGGRSVHEMQ 1536
Cdd:COG4717 350 QELLREAEELEEELQLE------ELEQEIAALLAEAGVEdeEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1537 KiirrlEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEK-----RIQEKEEEFENTRKNHARALE 1604
Cdd:COG4717 423 E-----ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQleedgELAELLQELEELKAELRELAE 490
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
890-1423 |
1.39e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 890 VEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMS 969
Cdd:pfam05557 47 SDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 970 LRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLME--------------------------DLQSEE 1023
Cdd:pfam05557 127 LQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefeiqsqeqdseivknskselaripELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1024 DKGNHQNKV-------KAKLEQTLDDLEDSLEREKRAR---ADLDKQKRKVEGELKiAQENIDESG----RQRHDLENNL 1089
Cdd:pfam05557 207 ERLREHNKHlnenienKLLLKEEVEDLKRKLEREEKYReeaATLELEKEKLEQELQ-SWVKLAQDTglnlRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1090 KKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELeelgekldeqggataaq 1169
Cdd:pfam05557 286 EQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV----------------- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1170 VEVNKKREAELAKLRR-DLEEANMNHENQLgglrkkhTDAVAELTDQLDqlnKAKAKVEKDKAQAVRDAEDLAAQLDQET 1248
Cdd:pfam05557 349 LLLTKERDGYRAILESyDKELTMSNYSPQL-------LERIEEAEDMTQ---KMQAHNEEMEAQLSVAEEELGGYKQQAQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1249 SGKLnneklakqfELQLTELQSKADEQSRQLQDFTSLKgrlhsengdlvRQLEDAESQVNQLTRLKSQLTSQLEEARRTA 1328
Cdd:pfam05557 419 TLER---------ELQALRQQESLADPSYSKEEVDSLR-----------RKLETLELERQRLREQKNELEMELERRCLQG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1329 DEEARERQTVAAQaKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADeledakrrqaQKINE 1408
Cdd:pfam05557 479 DYDPKKTKVLHLS-MNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNF----------KEVLD 547
|
570
....*....|....*
gi 17509401 1409 LQEALDAANSKNASL 1423
Cdd:pfam05557 548 LRKELESAELKNQRL 562
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1631-1816 |
1.49e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1631 INELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEeqrngadtreqffnAEKRATL-LQSEKEELlvANEAAERaRK 1709
Cdd:COG1842 32 IRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK--------------WEEKARLaLEKGREDL--AREALER-KA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1710 QAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKA-------IADATRLAEELRQEQ 1782
Cdd:COG1842 95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNealsgidSDDATSALERMEEKI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17509401 1783 EH----SQHVDRLRKG--LEQQLKEIQVRLD-EAEAAALKG 1816
Cdd:COG1842 175 EEmearAEAAAELAAGdsLDDELAELEADSEvEDELAALKA 215
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1508-1812 |
1.60e-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: 46.66 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1508 RRENKSLSQEIKDLTDQLgEGGRSVHEMQKIiRRLEIEK--------EELQHALDEAEAALEAEESKVLRAQVEVSQIRS 1579
Cdd:pfam17380 295 KMEQERLRQEKEEKAREV-ERRRKLEEAEKA-RQAEMDRqaaiyaeqERMAMERERELERIRQEERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1580 EIEKRIQEKEEEFENTRKNHaralesmQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQV 1659
Cdd:pfam17380 373 EISRMRELERLQMERQQKNE-------RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1660 RELQLQVEEEQ-RNGADTREQFFNAEKRATLLQSEKEellvaneaaERARKQAEYEAADARDQANEANAQVSSLTSAKRK 1738
Cdd:pfam17380 446 REMERVRLEEQeRQQQVERLRQQEEERKRKKLELEKE---------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRK 516
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1739 -LEGEIQAIHADLDETLNEYKAAEERSK-KAIADATRLAEELRQEQEHSQHVDRLRKGLE--QQLKEIQVRLDEAEAA 1812
Cdd:pfam17380 517 lLEKEMEERQKAIYEEERRREAEEERRKqQEMEERRRIQEQMRKATEERSRLEAMEREREmmRQIVESEKARAEYEAT 594
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1666-1934 |
1.63e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1666 VEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAE-YEAADARDQANEAnaqvSSLTSAKRKLEGEIQ 1744
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAErYQALLKEKREYEG----YELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1745 AIHADLDETlneykaaeersKKAIADATRLAEELRQEQEhsqhvdRLRKGLEQQLKEIQvRLDEAEAAALKggKKV---- 1820
Cdd:TIGR02169 241 AIERQLASL-----------EEELEKLTEEISELEKRLE------EIEQLLEELNKKIK-DLGEEEQLRVK--EKIgele 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1821 --IAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELA 1898
Cdd:TIGR02169 301 aeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270
....*....|....*....|....*....|....*.
gi 17509401 1899 NLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSR 1934
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
950-1344 |
1.68e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 950 KKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQ---DEAIAKLNKEKKHQEEINRKLMEDLQSEEDKG 1026
Cdd:COG5185 96 TKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVeklDEIADIEASYGEVETGIIKDIFGKLTQELNQN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1027 NHQNKVKAkleqTLDDLEDSLEREKRARADLDKQKRKVEGELkiaQENIDESGRQRHDLENNLKKKESELHSVSSRLEDE 1106
Cdd:COG5185 176 LKKLEIFG----LTLGLLKGISELKKAEPSGTVNSIKESETG---NLGSESTLLEKAKEIINIEEALKGFQDPESELEDL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1107 QALVSKLQRQIKDGQSrisELEEELENERQSRSKADRAKSDLQRELEELGEKLDEqggataaqvevnKKREAELAKLRRD 1186
Cdd:COG5185 249 AQTSDKLEKLVEQNTD---LRLEKLGENAESSKRLNENANNLIKQFENTKEKIAE------------YTKSIDIKKATES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1187 LEE--ANMNHENQLGGLRKKHTDAVAELTDQLDQLNKA------KAKVEKDKAQAVRDAEDLAAQLDQEtsgKLNNEKLA 1258
Cdd:COG5185 314 LEEqlAAAEAEQELEESKRETETGIQNLTAEIEQGQESltenleAIKEEIENIVGEVELSKSSEELDSF---KDTIESTK 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1259 KQFELQLTELQSKADEQSRQLQDftsLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTV 1338
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILATLED---TLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEE 467
|
....*.
gi 17509401 1339 AAQAKN 1344
Cdd:COG5185 468 AYDEIN 473
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1150-1549 |
1.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1150 RELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEA-----NMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKA 1224
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1225 KVE--KDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQ-----LTELQSKADEQSRQLQDFTSLKGRLHSENGDLV 1297
Cdd:COG4717 154 RLEelRELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaeeLEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1298 RQLEDAESQvNQLTRLKSQL--TSQLEEARRTADEEARERQTVAAQAK-------NYQHEAEQLQESLEEEIEGKNEILR 1368
Cdd:COG4717 234 NELEAAALE-ERLKEARLLLliAAALLALLGLGGSLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1369 QLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANS-KNASLEKTKSRLVgdlddAQVDVERANGV 1447
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALL-----AEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1448 ASALEKKQKgFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTD-----LFKAKNAQEELAEVVEGLRRENKSLSQEIKDLt 1522
Cdd:COG4717 388 RAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEeleeeLEELEEELEELEEELEELREELAELEAELEQL- 465
|
410 420
....*....|....*....|....*..
gi 17509401 1523 dqlgEGGRSVHEMQKIIRRLEIEKEEL 1549
Cdd:COG4717 466 ----EEDGELAELLQELEELKAELREL 488
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
906-1522 |
2.43e-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: 46.35 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 906 QLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKkIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQir 985
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKA-LQTVIEMKDTKISSLERNIRDLEDEVQMLKTN-- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 986 slqdemqqqdeaiAKLNKEKkHQEEInrKLMEDLQSeedkgnHQNKVKAKLEQtlddledslerekraradLDKQKRKVE 1065
Cdd:pfam10174 263 -------------GLLHTED-REEEI--KQMEVYKS------HSKFMKNKIDQ------------------LKQELSKKE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1066 GELKIAQENIDESGRQRHD-------LENNLKKKE-------SELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEEL 1131
Cdd:pfam10174 303 SELLALQTKLETLTNQNSDckqhievLKESLTAKEqraailqTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1132 ENERQSRSKADRAKSDLQRELEELGEKLDEQGGataaQVEVNKKREAELAKLRRD-------LEEANMNHENQLGGLRKK 1204
Cdd:pfam10174 383 RDLKDMLDVKERKINVLQKKIENLQEQLRDKDK----QLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQ 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1205 HTDAVAELTDQLDQLNKaKAKVEKDKAQAVRdaedlAAQLDQETSgklnneklakqfelqLTELQSKADEQ-SRQLQDFT 1283
Cdd:pfam10174 459 REREDRERLEELESLKK-ENKDLKEKVSALQ-----PELTEKESS---------------LIDLKEHASSLaSSGLKKDS 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1284 SLKgrlhsengdlvrQLEDA-ESQVNQLTRLKSQL--TSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEI 1360
Cdd:pfam10174 518 KLK------------SLEIAvEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLL 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1361 ----EGKNE--------------ILRQLSKANADIQQWKARFEGEGLLKADELEDAKRR--------QAQKINELQEALD 1414
Cdd:pfam10174 586 gilrEVENEkndkdkkiaeleslTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRednladnsQQLQLEELMGALE 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1415 AANSKnasLEKTKSRLVG--------DLDDAQVDVERANGVASALEKKQKGFDKIIDEwrKKTDDLAAELDGAQRdlrnt 1486
Cdd:pfam10174 666 KTRQE---LDATKARLSStqqslaekDGHLTNLRAERRKQLEEILEMKQEALLAAISE--KDANIALLELSSSKK----- 735
|
650 660 670
....*....|....*....|....*....|....*.
gi 17509401 1487 stdlfkaKNAQEElaevVEGLRRENKSLSQEIKDLT 1522
Cdd:pfam10174 736 -------KKTQEE----VMALKREKDRLVHQLKQQT 760
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1393-1946 |
2.45e-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: 46.17 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1393 DELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDL 1472
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1473 AaELDGAQRDLRNTSTDLFKAK--------NAQEELAEVVEGLRRENKSLS------QEIKDLTDQLGEGGRSVHEMQKI 1538
Cdd:TIGR04523 155 E-KLNNKYNDLKKQKEELENELnllekeklNIQKNIDKIKNKLLKLELLLSnlkkkiQKNKSLESQISELKKQNNQLKDN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1539 IRRLEIEKEELQhaldeaeaaleaeeSKVLRAQVEVSQIRSE---IEKRIQEKEEEFENTRK---NHARALESMQASLET 1612
Cdd:TIGR04523 234 IEKKQQEINEKT--------------TEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1613 EAKGKAEllRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQS 1692
Cdd:TIGR04523 300 LNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1693 EKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHA---DLDETLNEYKAAEERSKKAIA 1769
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKEtiiKNNSEIKDLTNQDSVKELIIK 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1770 DATRLAEELRQE-QEHSQHVDRLRKGLEQQLKEIQVRLDEaeaaaLKGGKKVIAKLEQRVRELESELDGEQRRFQDANKN 1848
Cdd:TIGR04523 458 NLDNTRESLETQlKVLSRSINKIKQNLEQKQKELKSKEKE-----LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1849 LGRADRRVRELQFQVDEDK--KNFERLQDLIDKLQQK-------LKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERA 1919
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
570 580
....*....|....*....|....*..
gi 17509401 1920 DQAENSLSKMRSKSRASASVAPGLQSS 1946
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1545-1858 |
2.53e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1545 EKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALES---MQASLETEAKGKAELL 1621
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykeLSASSEELSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1622 RIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQrngaDTREQFfnaekRATLLQSEKEELLVAN 1701
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE----AERKQL-----QAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1702 EAAERARKQAEYEAADARDQaNEANAQVSSLTSAKRKlEGEIQAIHADLdETLNEYKAAEERSKKAIADATRLAEELRQE 1781
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQ-DTITTLTQKLTTAHRK-EAENEALLEEL-RSLQERLNASERKVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 1782 QEHSQHVDRLrkgleqQLKEIQVRLDEAeAAALKGGKkviAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRE 1858
Cdd:pfam07888 270 TQAELHQARL------QAAQLTLQLADA-SLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
904-1154 |
2.67e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 904 KTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSkdhQ 983
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA---Q 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 984 IRSLQdemQQQDEAIaklnKEKKHQ--------EEINRKlmEDLQSEEdkgNHQNKVKaklEQTLDDLedslereKRARA 1055
Cdd:PRK11637 123 ERLLA---AQLDAAF----RQGEHTglqlilsgEESQRG--ERILAYF---GYLNQAR---QETIAEL-------KQTRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1056 DLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQikdgQSRIseleeeleneR 1135
Cdd:PRK11637 181 ELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRAN----ESRL----------R 246
|
250 260
....*....|....*....|
gi 17509401 1136 QSRSKADR-AKSDLQRELEE 1154
Cdd:PRK11637 247 DSIARAEReAKARAEREARE 266
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
954-1333 |
2.67e-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: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 954 AEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEInRKLMEDLQSEedkgnhqnkvK 1033
Cdd:pfam05622 7 EEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLL-QKQLEQLQEE----------N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1034 AKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENnLKKKESELHSVSSRLEDeqalVSKL 1113
Cdd:pfam05622 76 FRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDK-VKKLEATVETYKKKLED----LGDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1114 QRQIKDGQSRISELEEELENERQSRSKADRAKSDLQ---RELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRD---- 1186
Cdd:pfam05622 151 RRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLEtykRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEkerl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1187 ------LEEAN---------MNHENQLGGLRKKHTDAV---------AELTDQLDQL-NKAKAKVEKDKAQAVRDAEDLA 1241
Cdd:pfam05622 231 iierdtLRETNeelrcaqlqQAELSQADALLSPSSDPGdnlaaeimpAEIREKLIRLqHENKMLRLGQEGSYRERLTELQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1242 AQLDQ--------ETSGKLNNEKLaKQFELQLTELQSKADEQSRQLQDFTSLKGRL----------HSENGDLVRQLEDA 1303
Cdd:pfam05622 311 QLLEDanrrknelETQNRLANQRI-LELQQQVEELQKALQEQGSKAEDSSLLKQKLeehleklheaQSELQKKKEQIEEL 389
|
410 420 430
....*....|....*....|....*....|
gi 17509401 1304 ESQVNQLTRLKsqlTSQLEEARRTADEEAR 1333
Cdd:pfam05622 390 EPKQDSNLAQK---IDELQEALRKKDEDMK 416
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1643-1836 |
2.84e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1643 KANADAQKNLKRY-QEQVRELQL-QVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARD 1720
Cdd:PRK09510 72 KSAKRAEEQRKKKeQQQAEELQQkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1721 QAN---------EANAQVSSLTSAKRKLEGEIQAihadldetlneyKAAEERSKKAIADATRLAEELRQEQ---EHSQHV 1788
Cdd:PRK09510 152 EAKraaaaakkaAAEAKKKAEAEAAKKAAAEAKK------------KAEAEAAAKAAAEAKKKAEAEAKKKaaaEAKKKA 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17509401 1789 DRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELD 1836
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLD 267
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1762-1937 |
2.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1762 ERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAalkggkKVIAKLEQRVRELESELDGEQRR 1841
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1842 FQDANKNLgradRRVRELQFQVDEDKKNFERLQDLIDKLQQKL-KTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERAD 1920
Cdd:COG4717 148 LEELEERL----EELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*..
gi 17509401 1921 QAENSLSKMRSKSRASA 1937
Cdd:COG4717 224 ELEEELEQLENELEAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1734-1874 |
3.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1734 SAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKgLEQQLKEIQVRLDEAEA-- 1811
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEErl 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509401 1812 AALKGGKKVIAKLEQRVRELESELDGEQR--------RFQDANKNLGRADRRVRELQFQVDEDKKNFERLQ 1874
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1207-1450 |
3.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1207 DAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQ----DF 1282
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1283 TSLKGRLHSEN-GDLVRQLedaeSQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIE 1361
Cdd:COG3883 103 SYLDVLLGSESfSDFLDRL----SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1362 GKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDV 1441
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
....*....
gi 17509401 1442 ERANGVASA 1450
Cdd:COG3883 259 AGSAGAAGA 267
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
849-1105 |
3.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 849 LKAGKEAE-ELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLEstktqlsDAEERLAKLEAQQKDASKQ 927
Cdd:PRK02224 501 AEDLVEAEdRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE-------EKREAAAEAEEEAEEAREE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 928 LSELNDQLADNEDR------TADVQRAKKKIEAEVEALKKQIQDLemslrkAESEKQSKDHqirsLQDEMQQQDEAIAKL 1001
Cdd:PRK02224 574 VAELNSKLAELKERieslerIRTLLAAIADAEDEIERLREKREAL------AELNDERRER----LAEKRERKRELEAEF 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1002 NKEKkhqeeinrklMEDLQSEedkgnhqnkvKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELkiaqENIDESGRQ 1081
Cdd:PRK02224 644 DEAR----------IEEARED----------KERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL----EELEELRER 699
|
250 260
....*....|....*....|....
gi 17509401 1082 RHDLENNLKKKESeLHSVSSRLED 1105
Cdd:PRK02224 700 REALENRVEALEA-LYDEAEELES 722
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
887-1206 |
3.35e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 887 AKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDL 966
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 967 EMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDS 1046
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1047 LEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISE 1126
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1127 LEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHT 1206
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1295-1484 |
3.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1295 DLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKAN 1374
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1375 ADIQQWKARFEGEGLLKADELEDAKRR----------QAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQ------ 1438
Cdd:COG4942 111 RALYRLGRQPPLALLLSPEDFLDAVRRlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEeeraal 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17509401 1439 -VDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLR 1484
Cdd:COG4942 191 eALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1070-1337 |
3.78e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1070 IAQENIDESGRQRHDLennLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAksdlQ 1149
Cdd:pfam07888 31 LLQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK----Y 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1150 RELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKD 1229
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1230 KAQAVR---DAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLH----------SENGDL 1296
Cdd:pfam07888 184 EEELRSlskEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNaserkveglgEELSSM 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17509401 1297 VRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEE----ARERQT 1337
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGrarwAQERET 308
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1055-1247 |
3.88e-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: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1055 ADLDKQKRKVEGELKIAQENIDEsgrqrhdLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRIseleeELENE 1134
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-----KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1135 RQSRSKADRAKSDLQRELEELgekldeqggataaqvevnKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTD 1214
Cdd:COG1579 81 QLGNVRNNKEYEALQKEIESL------------------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
170 180 190
....*....|....*....|....*....|...
gi 17509401 1215 QLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQE 1247
Cdd:COG1579 143 KKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1535-1929 |
4.11e-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: 45.73 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1535 MQKIIRRLEI--EKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLET 1612
Cdd:pfam02463 140 QGGKIEIIAMmkPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1613 EAKGKAELLRIKKKLEGDINELEIAldhanKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQffnAEKRATLLQS 1692
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQE-----LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK---KLQEEELKLL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1693 EKEEllvanEAAERARKQAEYEAADARDQANEANAQvssltsaKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADAT 1772
Cdd:pfam02463 292 AKEE-----EELKSELLKLERRKVDDEEKLKESEKE-------KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1773 RLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKV--IAKLEQRVRELESELDGEQRRFQDANKNLG 1850
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAqlLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1851 RADRRVRELQfqvdedkKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKM 1929
Cdd:pfam02463 440 ELKQGKLTEE-------KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
948-1191 |
4.32e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.60 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 948 AKKKIEAEVEALKKQIQDLEMSlRKAESEKQSKDHQIRSLQDEMQQQDEAIA----KLNKEKKHQEEINRKLMEDLQSEE 1023
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQDDAA-QNALADKERAEADRQRLEQEKQQQLAAISgsqsQLESTDQNALETNGQAQRDAILEE 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1024 dkGNHQNKVKAKLEQTLDDLEDSLE---------REKRARADLDKQKRKVEGELKIAQENIDESgRQRHdLENNLKKKES 1094
Cdd:NF012221 1615 --SRAVTKELTTLAQGLDALDSQATyagesgdqwRNPFAGGLLDRVQEQLDDAKKISGKQLADA-KQRH-VDNQQKVKDA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1095 elhsvssrLEDEQALVSKLQRQIKDGQSRISeleeelenerQSRSKADRAKSD-LQRELEelGEKLDEQGGATAAQVEVN 1173
Cdd:NF012221 1691 --------VAKSEAGVAQGEQNQANAEQDID----------DAKADAEKRKDDaLAKQNE--AQQAESDANAAANDAQSR 1750
|
250
....*....|....*...
gi 17509401 1174 KKREAELAKLRRDLEEAN 1191
Cdd:NF012221 1751 GEQDASAAENKANQAQAD 1768
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1135-1894 |
4.41e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1135 RQSRSKADRAKSDLQRELEELGEKLDEQGGAtaaqvEVNKKREAELAKLRRDLEEANMNHENQLgglrKKHTDAVAELTD 1214
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEA-----ESDLEQDYQAASDHLNLVQTALRQQEKI----ERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1215 QLDQLNKA-------KAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQsKADEQSrQLQDFT--SL 1285
Cdd:PRK04863 363 RLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE-RAKQLC-GLPDLTadNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1286 KGRLHSengdLVRQLEDAESQVNQL-TRL------KSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEE 1358
Cdd:PRK04863 441 EDWLEE----FQAKEQEATEELLSLeQKLsvaqaaHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1359 EIEGKNEILRQLSKANADIQQWKARFE---GEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTksrlvgdLD 1435
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRAERLLAEFCkrlGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ-------LE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1436 DAQVDVERangvasaLEKKQKgfdkiidEWRKKTDDLAA--ELDGAQRDLRNTSTDLFKAKNAQE-ELAEVVEGLRRENK 1512
Cdd:PRK04863 590 QLQARIQR-------LAARAP-------AWLAAQDALARlrEQSGEEFEDSQDVTEYMQQLLERErELTVERDELAARKQ 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1513 SLSQEIKDLTD----------QLGE--GGRSVHE--------------------MQKI-IRRLEIEKEELQHALD----- 1554
Cdd:PRK04863 656 ALDEEIERLSQpggsedprlnALAErfGGVLLSEiyddvsledapyfsalygpaRHAIvVPDLSDAAEQLAGLEDcpedl 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1555 ---------------EAEAALEAEESKVLRAQVEVSQIRSEI-------EKRIQEKEEEFENTRKNHARALESMQaslet 1612
Cdd:PRK04863 736 yliegdpdsfddsvfSVEELEKAVVVKIADRQWRYSRFPEVPlfgraarEKRIEQLRAEREELAERYATLSFDVQ----- 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1613 eakgkaELLRIKKKLEGDINE-LEIALDhANKANADAQKNLKRyQEQVRELQLQVEEEQRNgadtREQFFNAEKRATLLQ 1691
Cdd:PRK04863 811 ------KLQRLHQAFSRFIGShLAVAFE-ADPEAELRQLNRRR-VELERALADHESQEQQQ----RSQLEQAKEGLSALN 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1692 SEKEE--LLVANEAAERARkqaeyEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHAD---LDETLNEYKAAEERSKK 1766
Cdd:PRK04863 879 RLLPRlnLLADETLADRVE-----EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDpeqFEQLKQDYQQAQQTQRD 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1767 AIADATRLAEeLRQEQEH-------------SQHVDRLRKGLEQ----------QLKEIQVRLDEAEA--AALKGGKKVi 1821
Cdd:PRK04863 954 AKQQAFALTE-VVQRRAHfsyedaaemlaknSDLNEKLRQRLEQaeqertrareQLRQAQAQLAQYNQvlASLKSSYDA- 1031
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1822 akLEQRVRELESELD---------GEQR---RFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKK 1889
Cdd:PRK04863 1032 --KRQMLQELKQELQdlgvpadsgAEERaraRRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
....*
gi 17509401 1890 QVEEA 1894
Cdd:PRK04863 1110 QVVNA 1114
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1662-1860 |
4.48e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1662 LQLQVEEEQRNGADTREQFfnaekRATLLQSEkeellvaneaAERARKQAEYEaadaRDQANEANAQvssltsakrkLEG 1741
Cdd:pfam07111 481 LELEQLREERNRLDAELQL-----SAHLIQQE----------VGRAREQGEAE----RQQLSEVAQQ----------LEQ 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1742 EIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQE-----HSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKG 1816
Cdd:pfam07111 532 ELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqaLQEKVAEVETRLREQLSDTKRRLNEARREQAKA 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17509401 1817 gkKVIAKLEQRVRELESELDGEQRRFQD-ANKNLG-RADRRVRELQ 1860
Cdd:pfam07111 612 --VVSLRQIQHRATQEKERNQELRRLQDeARKEEGqRLARRVQELE 655
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
902-1018 |
4.52e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.00 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 902 STKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKD 981
Cdd:pfam08614 47 PQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKR 126
|
90 100 110
....*....|....*....|....*....|....*..
gi 17509401 982 HQIRSLQDEMQQqdeaiakLNKEKKHQEEINRKLMED 1018
Cdd:pfam08614 127 KLNQDLQDELVA-------LQLQLNMAEEKLRKLEKE 156
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1602-1833 |
4.79e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.45 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1602 ALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVREL--QLQVEEEQRNGADTREQ 1679
Cdd:TIGR02794 34 GAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELeqRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1680 FFNAEKRATLL--QSEKEELLVANEAAER-----ARKQAEYEA-----ADARDQANEANAQVSSLTSAKRKLEGEIQAIH 1747
Cdd:TIGR02794 114 AEEKQKQAEEAkaKQAAEAKAKAEAEAERkakeeAAKQAEEEAkakaaAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1748 ADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKG--GKKVIAKLE 1825
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDkyAAIIQQAIQ 273
|
....*...
gi 17509401 1826 QRVRELES 1833
Cdd:TIGR02794 274 QNLYDDPS 281
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1450-1835 |
5.32e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1450 ALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGG 1529
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1530 RSVHEMQKIIRRLeiekeelqhaldeaeaaleaeESKVLRAQVEVSQIRSEIEKR-IQEKEEEFENtrknharalESMQA 1608
Cdd:pfam07888 129 ARIRELEEDIKTL---------------------TQRVLERETELERMKERAKKAgAQRKEEEAER---------KQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1609 SLEteaKGKAELLRIKKKLEGDINELEIALDHANK-ANADAQKNLKRYQEQVRELQLQVEEEQRNGadTREQFFNAEKRA 1687
Cdd:pfam07888 179 KLQ---QTEEELRSLSKEFQELRNSLAQRDTQVLQlQDTITTLTQKLTTAHRKEAENEALLEELRS--LQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1688 TLLQSEKEELlvaneAAERARKQAEYEaaDARDQANEANAQVSSLTSAKRklegEIQAIHADLDETLNEYKAAEERSKKA 1767
Cdd:pfam07888 254 EGLGEELSSM-----AAQRDRTQAELH--QARLQAAQLTLQLADASLALR----EGRARWAQERETLQQSAEADKDRIEK 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 1768 IADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESEL 1835
Cdd:pfam07888 323 LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1602-1744 |
5.33e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1602 ALESMQASLEtEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRElqlqveeeqrnGADTREQFF 1681
Cdd:COG1566 84 ALAQAEAQLA-AAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKK-----------GAVSQQELD 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1682 NAEKRATLLQSEKeellvanEAAERARKQAEyEAADARDQANEANAQVSSLTSAKRKLEGEIQ 1744
Cdd:COG1566 152 EARAALDAAQAQL-------EAAQAQLAQAQ-AGLREEEELAAAQAQVAQAEAALAQAELNLA 206
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
909-1022 |
5.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 909 DAEERLAKLEAQQKdASKQLSELNdqlADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQ 988
Cdd:PRK12704 52 EAIKKEALLEAKEE-IHKLRNEFE---KELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110
....*....|....*....|....*....|....*....
gi 17509401 989 DEMQQQDEAIAKLNKEKKH-----QEEINRKLMEDLQSE 1022
Cdd:PRK12704 128 KKEEELEELIEEQLQELERisgltAEEAKEILLEKVEEE 166
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1569-1771 |
6.34e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.93 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1569 RAQVEVSQIRSEIEKRIQEK-EEEFENTRKNHARALESMqASLETEakgKAELLRIKKKLEGDINELEIALDHANKANAD 1647
Cdd:PLN03188 1078 RALAEKQKHELDTEKRCAEElKEAMQMAMEGHARMLEQY-ADLEEK---HIQLLARHRRIQEGIDDVKKAAARAGVRGAE 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1648 AqKNLKRYQEQVRELQLQVEEEQRngadtreqFFNAEKRA--TLLQSEKE------ELLVANEAAERARKQAEYEAADAR 1719
Cdd:PLN03188 1154 S-KFINALAAEISALKVEREKERR--------YLRDENKSlqAQLRDTAEavqaagELLVRLKEAEEALTVAQKRAMDAE 1224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1720 DQANEANAQVSSLtsaKRKLEGEIQaihadldeTLNEYKAAEERSKKAIADA 1771
Cdd:PLN03188 1225 QEAAEAYKQIDKL---KRKHENEIS--------TLNQLVAESRLPKEAIRPA 1265
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
900-1025 |
7.58e-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: 44.29 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 900 LESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLadnEDRTADVQRAKKKIEAEVeALKKQIQDLEMSLRKAESEKQS 979
Cdd:pfam05622 306 LTELQQLLEDANRRKNELETQNRLANQRILELQQQV---EELQKALQEQGSKAEDSS-LLKQKLEEHLEKLHEAQSELQK 381
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 17509401 980 KDHQIRSLQ-DEMQQQDEAIAKLnkekkhqEEINRKLMEDLQSEEDK 1025
Cdd:pfam05622 382 KKEQIEELEpKQDSNLAQKIDEL-------QEALRKKDEDMKAMEER 421
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1206-1457 |
7.67e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1206 TDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQetsgklNNEKLAKQfELQLTELQSKADEQSRQLQDftsL 1285
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA------LERRIAAL-ARRIRALEQELAALEAELAE---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1286 KGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNE 1365
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1366 ILRQLSKANADIQQWKARfegegllkADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDV-ERA 1444
Cdd:COG4942 169 LEAERAELEALLAELEEE--------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAaAAA 240
|
250
....*....|...
gi 17509401 1445 NGVASALEKKQKG 1457
Cdd:COG4942 241 ERTPAAGFAALKG 253
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
964-1415 |
7.89e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 964 QDLEMSLRKAESEKQSKdhqirslQDEMQQQDEAIAKLNKEkkhQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDL 1043
Cdd:pfam12128 600 EELRERLDKAEEALQSA-------REKQAAAEEQLVQANGE---LEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1044 EDSLEREKR----ARADLDKQKRKVEGELKIAQENIDESGRqrhdlENNLKKKESELHSVSSRLEDEQALVSKLQRQIKD 1119
Cdd:pfam12128 670 NKALAERKDsaneRLNSLEAQLKQLDKKHQAWLEEQKEQKR-----EARTEKQAYWQVVEGALDAQLALLKAAIAARRSG 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1120 GQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLdeqggataaqvEVNKKREAELAKLRRDLEEANMNHENQLG 1199
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI-----------ERIAVRRQEVLRYFDWYQETWLQRRPRLA 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1200 GLRKKHTDAVAELTDQLDQLnKAKAKVEKDKAQAVRDA-EDLAAQLDQETSG-KLNNEKLAKQFELQ-LTELQSKADEQS 1276
Cdd:pfam12128 814 TQLSNIERAISELQQQLARL-IADTKLRRAKLEMERKAsEKQQVRLSENLRGlRCEMSKLATLKEDAnSEQAQGSIGERL 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1277 RQLQDFtslKGRLHSENGDLVRQLEDAESQVNQLTRlksqltSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESL 1356
Cdd:pfam12128 893 AQLEDL---KLKRDYLSESVKKYVEHFKNVIADHSG------SGLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWF 963
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1357 EEEIEGKNEILRQLSKANA-DIQQWkarfegegllkADELEDAKRRQAQKINELQEALDA 1415
Cdd:pfam12128 964 DVRVPQSIMVLREQVSILGvDLTEF-----------YDVLADFDRRIASFSRELQREVGE 1012
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1650-1878 |
8.08e-04 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1650 KNLKRYQEQVRELQLQVEEEQR---------NGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARD 1720
Cdd:pfam07902 78 KSLEEMLSQLKELNLELTDTKNsnlwskiklNNNGMLREYHNDTIKTEIVESAEGIATRISEDTDKKLALINETISGIRR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1721 QANEANAQVSS------------LTSAKRKLEGEIQAIHADL----DETLNEYKAAEERSKKAIADA--TRLaEELRQEQ 1782
Cdd:pfam07902 158 EYQDADRQLSSsyqagieglkatMASDKIGLQAEIQASAQGLsqryDNEIRKLSAKITTTSSGTTEAyeSKL-DDLRAEF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1783 EHSQHvdRLRKGLEQQLKEIQvrldEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQ 1862
Cdd:pfam07902 237 TRSNQ--GMRTELESKISGLQ----STQQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQDAEKNYSSLTQTVKGLQST 310
|
250 260
....*....|....*....|
gi 17509401 1863 VDEDKKN----FERLQDLID 1878
Cdd:pfam07902 311 VSDPNSKlesrITQLAGLIE 330
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1770-1951 |
8.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1770 DATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNL 1849
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1850 GRADRRVRELQFQVDEDKknFERLQDLidklqqklktqKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKM 1929
Cdd:COG4913 319 DALREELDELEAQIRGNG--GDRLEQL-----------EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180
....*....|....*....|..
gi 17509401 1930 RSKSRASASVAPGLQSSASAAV 1951
Cdd:COG4913 386 RAEAAALLEALEEELEALEEAL 407
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1078-1586 |
8.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1078 SGRQRHDLENNLKKKESELHSVSSRLEDEQALV---SKLQRQIKDGQSRISELEEELENERQSRSKAD--RAKSDLQREL 1152
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1153 EELGEKLDEQggatAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQ 1232
Cdd:COG4717 142 AELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1233 AVRDAEDLAAQLDQetsgkLNNEKLAKQFELQLTELQSKADEQSRQL---QDFTSLKGRLHSENGDLVRQLEDAESQVNQ 1309
Cdd:COG4717 218 AQEELEELEEELEQ-----LENELEAAALEERLKEARLLLLIAAALLallGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1310 LTRLKSQLTSQLEEARRTADEEARERQtvaaqaknyqheaeqlqesleeeiegkneilrqlskanaDIQQWKARFEGEGL 1389
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEE---------------------------------------ELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1390 LKADELEDAKRRQAQKINELQEALDAANS-KNASLEKTKSRLVgdlddAQVDVERANGVASALEKKQKgFDKIIDEWRKK 1468
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALL-----AEAGVEDEEELRAALEQAEE-YQELKEELEEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1469 TDDLAAELDGAQRDLRNTSTD-----LFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQlgeggrsvHEMQKIIRRLE 1543
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEeleeeLEELEEELEELEEELEELREELAELEAELEQLEED--------GELAELLQELE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 17509401 1544 IEKEELQhaldeaeaaLEAEESKVLRAQVEV-SQIRSEIEKRIQ 1586
Cdd:COG4717 480 ELKAELR---------ELAEEWAALKLALELlEEAREEYREERL 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1566-1713 |
8.63e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1566 KVLRAQVEVSQIRSEIEKRIQEKEEEF---ENTRKNHARALESMQASLEteaKGKAELLRIKKKLEGDINELEIALDHAN 1642
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKELRERRNELqklEKRLLQKEENLDRKLELLE---KREEELEKKEKELEQKQQELEKKEEELE 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1643 KANADAQKNLKRY----QEQVRELQL-QVEEEqrngadtreqffnAEKRATLLQSEKEEllvanEAAERARKQAEY 1713
Cdd:PRK12704 135 ELIEEQLQELERIsgltAEEAKEILLeKVEEE-------------ARHEAAVLIKEIEE-----EAKEEADKKAKE 192
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1215-1492 |
9.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1215 QLDQLNKAKAKVEKDKAQAVRDAEDLA-AQLDQETSGKLNNEKLAKQfelQLTELQSKADEQSRQLQDFTSLKGRLHSEN 1293
Cdd:PHA02562 167 EMDKLNKDKIRELNQQIQTLDMKIDHIqQQIKTYNKNIEEQRKKNGE---NIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1294 GDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTAD--EEARERQTVAAQaknyqheaeqlqesleeeIEGKNEILRQLS 1371
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQ------------------ISEGPDRITKIK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1372 KANADIQQwkarfegegllKADELEDAKRRQAQKINELQEALDAANSKNASLEKTK---SRLVGDLDDAQVDVERANG-- 1446
Cdd:PHA02562 306 DKLKELQH-----------SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqslITLVDKAKKVKAAIEELQAef 374
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17509401 1447 --VASALEKKQKGFDKIIdewrKKTDDLAAEldgaqRDLRNTSTDLFK 1492
Cdd:PHA02562 375 vdNAEELAKLQDELDKIV----KTKSELVKE-----KYHRGIVTDLLK 413
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1181-1471 |
9.54e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1181 AKLRRDLEEANMNHENQlgglrkkHTDAVAELTDQLDQLNKAKAKVEKdkAQAVRDAEDLAAQLDQETSGKLNNEK---- 1256
Cdd:PRK10929 26 KQITQELEQAKAAKTPA-------QAEIVEALQSALNWLEERKGSLER--AKQYQQVIDNFPKLSAELRQQLNNERdepr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1257 ------LAKQFELQLTELQSKADEQSRQLQdftslkgrlhsENGDLVRQLEDAESQVNQltrlksqltsQLEEARRTADE 1330
Cdd:PRK10929 97 svppnmSTDALEQEILQVSSQLLEKSRQAQ-----------QEQDRAREISDSLSQLPQ----------QQTEARRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1331 EARERQ------TVAAQAKNYQHEAEQLQESLEEeiegkNEI-LRQLSKANadiQQWKARFegegllkadELEDAKRRQA 1403
Cdd:PRK10929 156 IERRLQtlgtpnTPLAQAQLTALQAESAALKALV-----DELeLAQLSANN---RQELARL---------RSELAKKRSQ 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1404 QKINELQEALDAANS---KNA--SLEKTK--SRLVGDLDDAQVDVERANGVAS-ALEKKQKGFDKIIDEWRKKTDD 1471
Cdd:PRK10929 219 QLDAYLQALRNQLNSqrqREAerALESTEllAEQSGDLPKSIVAQFKINRELSqALNQQAQRMDLIASQQRQAASQ 294
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1136-1347 |
1.07e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1136 QSRSKADRAKSDLQRELEELGEKLDEQGGATAAQV-------------------EVNKKR--EAELAKLRRDLEEANMNH 1194
Cdd:pfam00038 40 KKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQleldnlrlaaedfrqkyedELNLRTsaENDLVGLRKDLDEATLAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1195 ---ENQ-------LGGLRKKHTDAVAELTDQLDQlnkAKAKVEKDKAQAVRDAEDLA---AQLDQETsgKLNNEKLAKQF 1261
Cdd:pfam00038 120 vdlEAKieslkeeLAFLKKNHEEEVRELQAQVSD---TQVNVEMDAARKLDLTSALAeirAQYEEIA--AKNREEAEEWY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1262 ELQLTELQSKADEQSRQLQ----DFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARE--- 1334
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRsakeEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAElqe 274
|
250
....*....|....
gi 17509401 1335 -RQTVAAQAKNYQH 1347
Cdd:pfam00038 275 tRQEMARQLREYQE 288
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
888-1107 |
1.08e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 888 KLVEEKTSLFTNLEST-------KTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEAL- 959
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKtnelkseKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELi 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 960 ----------KKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEA-----IAKLNKEKKHQEEINRKLMEDLQSEED 1024
Cdd:TIGR00606 930 ssketsnkkaQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntvNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1025 KGNHQNKVKAKLeqTLDDLEDSLEREKRARADLDKQKRKVE-----GELKIAQENIDESGRQRHDLENNLKKKESELHSV 1099
Cdd:TIGR00606 1010 QKIQERWLQDNL--TLRKRENELKEVEEELKQHLKEMGQMQvlqmkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHF 1087
|
....*...
gi 17509401 1100 SSRLEDEQ 1107
Cdd:TIGR00606 1088 KKELREPQ 1095
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
856-1105 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 856 EELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNL----ESTKTQLSDAEERLAKLEAQQKDASKQLSEL 931
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELveeaKTIKAEIEELTDELLNLVMDIEDPSAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 932 NDQLADNEDRTADVQRAKKKIE--AEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQE 1009
Cdd:PHA02562 261 NTAAAKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1010 EINRKLmedlqsEEDKGNHQNKVKAkleqtLDDLEDSLEREKRARADldkqkrkVEGELKIAQENIDESGRQRHDlennL 1089
Cdd:PHA02562 341 ELKNKI------STNKQSLITLVDK-----AKKVKAAIEELQAEFVD-------NAEELAKLQDELDKIVKTKSE----L 398
|
250
....*....|....*.
gi 17509401 1090 KKKESELHSVSSRLED 1105
Cdd:PHA02562 399 VKEKYHRGIVTDLLKD 414
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
912-1119 |
1.25e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 912 ERLAKLEAQQKDASKQLSELNDQLADNEDRTADVqrakkkiEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEM 991
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKA-------EAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 992 QQQDEAIAKL-NKEKKHQEEINR---KLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLdkqkRKVEGE 1067
Cdd:pfam00261 74 DESERGRKVLeNRALKDEEKMEIleaQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKI----VELEEE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1068 LKIAQENI------DESGRQRHDL-ENNLKKKESELHSVSSRLEDEQALVSKLQRQIKD 1119
Cdd:pfam00261 150 LKVVGNNLksleasEEKASEREDKyEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1668-1931 |
1.34e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1668 EEQRNGADTREQFFNAEKRATLLQS-------EKEELLVANEAAERARKQAEYEAADARDQaneanaqvssLTSAKRKLE 1740
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRAELLQNrleeclqERAELLQAQEAANRQREKEKERYKRDREQ----------WERQRRELE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1741 GEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEE----LRQEQEHSQHVDRLR---KGLEQQLKEIQVRLDEAEAAA 1813
Cdd:pfam07888 80 SRVAELKEELRQSREKHEELEEKYKELSASSEELSEEkdalLAQRAAHEARIRELEediKTLTQRVLERETELERMKERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1814 lkggKKVIAKLeqrvRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEE 1893
Cdd:pfam07888 160 ----KKAGAQR----KEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 17509401 1894 AEELanlnLQKYKQLTHQLEDAEERADQAENSLSKMRS 1931
Cdd:pfam07888 232 NEAL----LEELRSLQERLNASERKVEGLGEELSSMAA 265
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1361-1928 |
1.41e-03 |
|
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: 43.56 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1361 EGKNEILRQLSKANADIQQWKARFEGEGLLKADELED------AKRRQAQKIN------------ELQEALDAANSKNA- 1421
Cdd:pfam05483 74 EGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQEnrkiieAQRKAIQELQfenekvslkleeEIQENKDLIKENNAt 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1422 -------------SLEKTKSRLVGDLDDAQVDVERANGVasalEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTST 1488
Cdd:pfam05483 154 rhlcnllketcarSAEKTKKYEYEREETRQVYMDLNNNI----EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1489 DLFKAKNAQEELAEV--VEGLRRENKslsqeIKDLTDQLGEGGRSVHEMQKiirRLEIEKEELQHALDEAEAALEAEESK 1566
Cdd:pfam05483 230 EYKKEINDKEKQVSLllIQITEKENK-----MKDLTFLLEESRDKANQLEE---KTKLQDENLKELIEKKDHLTKELEDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1567 VLRAQVEVS---------QIRSE-IEKRIQEKEEEFENTrkNHARALESMQAS-LETEAKGKAELLRI-KKKLEGDINEL 1634
Cdd:pfam05483 302 KMSLQRSMStqkaleedlQIATKtICQLTEEKEAQMEEL--NKAKAAHSFVVTeFEATTCSLEELLRTeQQRLEKNEDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1635 EIALDHANKANADAQKNLKRYQEQVRELQ--LQVEEEQRNGADTREQFfnaEKRATLLQSEKEELLVANEAAERARKQAE 1712
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEelKKILAEDEKLLDEKKQF---EKIAEELKGKEQELIFLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1713 YEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEykaaeerSKKAIADATRLAEELRQEQEHsqhVDRLR 1792
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE-------NKELTQEASDMTLELKKHQED---IINCK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1793 KGLEQQLKEIQvRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFER 1872
Cdd:pfam05483 527 KQEERMLKQIE-NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1873 LQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSK 1928
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
913-1247 |
1.74e-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: 43.20 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 913 RLAKLEAQQKDASKQL----SELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQ 988
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLrgqvAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 989 DEMQ-----------QQDEAIAKLNKEKKHQEEINRKLMEDLQSEED-KGNHQNKVK-AKLEQTLD---------DLEDS 1046
Cdd:pfam07111 401 EQLKfvvnamsstqiWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTiKGLMARKVAlAQLRQESCpppppappvDADLS 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1047 LEREKraradLDKQKRKVEGELKIAQENI-DESGRQRHDLEnnlkKKESELHSVSSRLEDEqalvskLQRQIKDGQSRIS 1125
Cdd:pfam07111 481 LELEQ-----LREERNRLDAELQLSAHLIqQEVGRAREQGE----AERQQLSEVAQQLEQE------LQRAQESLASVGQ 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1126 ELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQggataaQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKH 1205
Cdd:pfam07111 546 QLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEK------VAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQ 619
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17509401 1206 TDAVAElTDQLDQLNKAKAKVEKDKAQAV--------RDAEDLAAQLDQE 1247
Cdd:pfam07111 620 HRATQE-KERNQELRRLQDEARKEEGQRLarrvqeleRDKNLMLATLQQE 668
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
928-1264 |
1.81e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 928 LSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKK- 1006
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1007 --HQEEINRKLMEDLqsEEDkgnhqnkVKAKLEQTLdDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHD 1084
Cdd:pfam07888 120 llAQRAAHEARIREL--EED-------IKTLTQRVL-ERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1085 LENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAksdlQRELEELGEKLDEQGG 1164
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS----ERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1165 AtaaqvevnkkreaelaklrRDLEEANMnHENQLgglrkkhtdAVAELTDQLDQLNKAkakVEKDKAQAVRDAEDL--AA 1242
Cdd:pfam07888 266 Q-------------------RDRTQAEL-HQARL---------QAAQLTLQLADASLA---LREGRARWAQERETLqqSA 313
|
330 340
....*....|....*....|..
gi 17509401 1243 QLDQETSGKLNNEKLAKQFELQ 1264
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQ 335
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
855-1010 |
1.82e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 855 AEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLftnlestKTQLSDAEERLAKLEAQQKDAS--KQLSELN 932
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-------ELEIEEVEARIKKYEEQLGNVRnnKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509401 933 DQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEmslRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEE 1010
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
936-1550 |
1.91e-03 |
|
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: 43.17 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 936 ADNEDRTADVQRAKKKIEAEVEALKK-QIQDLEMSLRKAESEKQSKD-----HQIRSLQDEMQQQDEAIAKLNKEKKHQE 1009
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAIQElQFENEKVSLKLEEEIQENKDlikenNATRHLCNLLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1010 EINRKLMEDLQSEEDK---GNHQNKVKA---KLEQTLDdLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRH 1083
Cdd:pfam05483 179 EETRQVYMDLNNNIEKmilAFEELRVQAenaRLEMHFK-LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1084 DLENNLKKKESELHSVS--SRLEDE--QALVSK---LQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELG 1156
Cdd:pfam05483 258 DLTFLLEESRDKANQLEekTKLQDEnlKELIEKkdhLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1157 EKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLR---KKHTDAVAELTD-------QLDQLNKAKAKV 1226
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmelQKKSSELEEMTKfknnkevELEELKKILAED 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1227 EK---DKAQAVRDAEDLAAQlDQETSGKLN-NEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLED 1302
Cdd:pfam05483 418 EKlldEKKQFEKIAEELKGK-EQELIFLLQaREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1303 AESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQES----LEEEIEGKNEILRQLSKA--NAD 1376
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDElesvREEFIQKGDEVKCKLDKSeeNAR 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1377 IQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALdaaNSKNASLEKTKSRLVGDLDDAQVDVeraNGVASALEKKQK 1456
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL---HQENKALKKKGSAENKQLNAYEIKV---NKLELELASAKQ 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1457 GFDKIIDEWRKKTDD-------LAAELDGAqRDLRNTSTDLFKA--KNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGE 1527
Cdd:pfam05483 651 KFEEIIDNYQKEIEDkkiseekLLEEVEKA-KAIADEAVKLQKEidKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL 729
|
650 660
....*....|....*....|...
gi 17509401 1528 GGRSVHEMQKIIRRLEIEKEELQ 1550
Cdd:pfam05483 730 YKNKEQEQSSAKAALEIELSNIK 752
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
971-1310 |
2.18e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 971 RKAESEKQSKDHQIRSLQDEMQQQDEaiaklnkEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLERE 1050
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKE-------EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1051 KraradLDKQKRKVEgelKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLE---DEQALVSKLQRQIKDGQSRISEL 1127
Cdd:pfam17380 354 R-----QEERKRELE---RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1128 EEELENERQSRSKadRAKSDLQRELEELGEKLDEQggataaQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTd 1207
Cdd:pfam17380 426 RAEQEEARQREVR--RLEEERAREMERVRLEEQER------QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1208 avaeLTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELqltELQSKADEQSRQLQDFTSLKG 1287
Cdd:pfam17380 497 ----LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM---EERRRIQEQMRKATEERSRLE 569
|
330 340
....*....|....*....|...
gi 17509401 1288 RLHSENgDLVRQLEDAESQVNQL 1310
Cdd:pfam17380 570 AMERER-EMMRQIVESEKARAEY 591
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
904-1103 |
2.35e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 904 KTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQrakkkieAEVEALKKQIQDLEMSLRkaeSEKQSKDHQ 983
Cdd:PRK11281 120 TLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQ-------AALYANSQRLQQIRNLLK---GGKVGGKAL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 984 IRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQnkvKAKLEQTLDDLEDSLerekraradldKQKRK 1063
Cdd:PRK11281 190 RPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTAR---IQRLEHQLQLLQEAI-----------NSKRL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17509401 1064 VEGELKIAQ-ENIDESGRQRHdleNNLKKKESEL-HSVSSRL 1103
Cdd:PRK11281 256 TLSEKTVQEaQSQDEAARIQA---NPLVAQELEInLQLSQRL 294
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1145-1694 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1145 KSDLQRELEELGEKLDEQGgATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGG---LRKKHTDAVAELTDQLDQLNK 1221
Cdd:pfam13166 29 KTTLSRLLRSLELGEPHPK-FANGKFEWTNGQPLDIRVFNRDFVEENLSEQGEIKPiftLGEESIEIQEKIAKLKKEIKD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1222 AKAKVEKDKAQAvrdaEDLAAQLDQETSGKLNN--EKLAKQFELQLTElqskadeqsrqlqDFTSLKGrlhsENGDLVRQ 1299
Cdd:pfam13166 108 HEEKLDAAEANL----QKLDKEKEKLEADFLDEcwKKIKRKKNSALSE-------------ALNGFKY----EANFKSRL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1300 LEDAES-QVNQLTRLksqLTSQLEEARRTADEEARERqTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKaNADIQ 1378
Cdd:pfam13166 167 LREIEKdNFNAGVLL---SDEDRKAALATVFSDNKPE-IAPLTFNVIDFDALEKAEILIQKVIGKSSAIEELIK-NPDLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1379 QWKArfEGEGLLKAD-----------------ELEDA-KRRQAQKINELQEALDaansknaSLEKTKSRLVGDLDDAqvd 1440
Cdd:pfam13166 242 DWVE--QGLELHKAHldtcpfcgqplpaerkaALEAHfDDEFTEFQNRLQKLIE-------KVESAISSLLAQLPAV--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1441 verangvaSALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKaknaqeelaevveglRRENKSLSQEIKD 1520
Cdd:pfam13166 310 --------SDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFK---------------SIELDSVDAKIES 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1521 LTDQLGEGGRSVHEMQKIIRRLEIEKEELqhaldeaeaaleaeesKVLRAQVEVSQIRSEIEKRIQEKeeefentrknha 1600
Cdd:pfam13166 367 INDLVASINELIAKHNEITDNFEEEKNKA----------------KKKLRLHLVEEFKSEIDEYKDKY------------ 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1601 RALESMQASLETEAKGKAELLrikKKLEGDINELEIALDHANKANADAQKNLKRYQEQvrELQLQVEEEQRNGADTREQf 1680
Cdd:pfam13166 419 AGLEKAINSLEKEIKNLEAEI---KKLREEIKELEAQLRDHKPGADEINKLLKAFGFG--ELELSFNEEGKGYRIIRKG- 492
|
570
....*....|....
gi 17509401 1681 fNAEKRATLLQSEK 1694
Cdd:pfam13166 493 -GSQAAETLSEGER 505
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1744-1862 |
2.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1744 QAIHADLDeTLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQ---QLKEIQVRLDEAEAAALKGGKKV 1820
Cdd:PRK11281 39 ADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQapaKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17509401 1821 IAKLEqrVRELESELDGEQRRFQDANKNLGRADRRVRELQFQ 1862
Cdd:PRK11281 118 LSTLS--LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ 157
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
953-1238 |
2.86e-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: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 953 EAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLN--KEKKHQEEInRKLMEDLQSEEDKGNHQN 1030
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANllADETLADRL-EELREELDAAQEAQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1031 KVKAKLEQtLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENID--ESGRQR------HDLENNLKKKESELHSVSSR 1102
Cdd:COG3096 914 QHGKALAQ-LEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalSEVVQRrphfsyEDAVGLLGENSDLNEKLRAR 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1103 LEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQvevnkkreaelak 1182
Cdd:COG3096 993 LEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARI------------- 1059
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17509401 1183 LRRDLEEANMNHENQLGGLRKKHTDAVAEltdqLDQLNKAKAKVEKDKAQAVRDAE 1238
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRCEAE----MDSLQKRLRKAERDYKQEREQVV 1111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1044-1243 |
2.91e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1044 EDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKD---G 1120
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErarA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1121 QSRISELEEELENERQSRSKAD------------RAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLE 1188
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1189 EANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQ 1243
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1266-1499 |
3.14e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.90 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1266 TELQSKADEQSRQL-QDFTSLKGRLHSENGDLVRQLEDAESQvNQLTRL-KSQltSQLEEARRTADEEARERQTVAAQAk 1343
Cdd:NF012221 1538 SESSQQADAVSKHAkQDDAAQNALADKERAEADRQRLEQEKQ-QQLAAIsGSQ--SQLESTDQNALETNGQAQRDAILE- 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1344 nyqhEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGeGLLK-------------ADELEDAKRRQAQKINELQ 1410
Cdd:NF012221 1614 ----ESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAG-GLLDrvqeqlddakkisGKQLADAKQRHVDNQQKVK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1411 EALDAANSKNASLEKTKSRLVGDLDDAQVDVERangvasaleKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDL 1490
Cdd:NF012221 1689 DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEK---------RKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAE 1759
|
....*....
gi 17509401 1491 FKAKNAQEE 1499
Cdd:NF012221 1760 NKANQAQAD 1768
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1735-1937 |
3.32e-03 |
|
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: 42.75 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1735 AKRKLEGEIQAIhADLDETLNEYKAAEERSKKAIADATRLAEELRQEqehsqhVDRLRKGLEQQLK--EIQVRLDEAEAA 1812
Cdd:TIGR02169 154 ERRKIIDEIAGV-AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQ------LERLRREREKAERyqALLKEKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1813 ALKGGKKV----IAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQfqvdedkknfERLQDLIDKLQQKLKTQK 1888
Cdd:TIGR02169 227 ELLKEKEAlerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN----------KKIKDLGEEEQLRVKEKI 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17509401 1889 KQVEEAEELANLNLQKYKQlthQLEDAEERADQAENSLSKMRSKSRASA 1937
Cdd:TIGR02169 297 GELEAEIASLERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELE 342
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
907-1194 |
3.53e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 907 LSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAK-------KKIEAEVEALKKQIQDLEMSLRKAESE-KQ 978
Cdd:PLN02939 109 AAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARlqaledlEKILTEKEALQGKINILEMRLSETDARiKL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 979 SKDHQIRSlqdemQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNK--------VKAKLEQtLDDLEDSLERE 1050
Cdd:PLN02939 189 AAQEKIHV-----EILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMllkddiqfLKAELIE-VAETEERVFKL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1051 KRARADLDKQKRKVEGELKIAQENIDESGRQRHD-LENNLKKKESELHSVSSRLEdEQALVSKLQRQIKDGQSRISELEE 1129
Cdd:PLN02939 263 EKERSLLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVE-KAALVLDQNQDLRDKVDKLEASLK 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 1130 ELENERQSRSKADRaksdLQRELEELGEKLDEQGGATAAQVEVNKKREAE----LAKLRRDLEEANMNH 1194
Cdd:PLN02939 342 EANVSKFSSYKVEL----LQQKLKLLEERLQASDHEIHSYIQLYQESIKEfqdtLSKLKEESKKRSLEH 406
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1067-1343 |
3.72e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1067 ELKIAQENIDESGR-------QRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELeeelenerQSRS 1139
Cdd:PRK11637 48 QLKSIQQDIAAKEKsvrqqqqQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKL--------EQQQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1140 KAdraksdlQRELeeLGEKLD---EQGGATAAQV----EVNKKREAELAklrrdleeanmnhenQLGGLRKKHTDAVAEL 1212
Cdd:PRK11637 120 AA-------QERL--LAAQLDaafRQGEHTGLQLilsgEESQRGERILA---------------YFGYLNQARQETIAEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1213 TDQLDQLNKAKAKVEKDKAQavrDAEDLAAQldQETSGKLNNEKLAKQfeLQLTELQSKADEQSRQLqdftslkgrlhse 1292
Cdd:PRK11637 176 KQTREELAAQKAELEEKQSQ---QKTLLYEQ--QAQQQKLEQARNERK--KTLTGLESSLQKDQQQL------------- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1293 ngdlvrqledAESQVNQlTRLKSQLTSQLEEARRTADEEARERQTVAA---QAK 1343
Cdd:PRK11637 236 ----------SELRANE-SRLRDSIARAEREAKARAEREAREAARVRDkqkQAK 278
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
926-1081 |
3.81e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 926 KQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEK 1005
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSII 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1006 KHQEEINRKLME------DLQSEEDKGN-HQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKR--KVEGELKIAQENID 1076
Cdd:PRK01156 667 PDLKEITSRINDiednlkKSRKALDDAKaNRARLESTIEILRTRINELSDRINDINETLESMKKikKAIGDLKRLREAFD 746
|
....*
gi 17509401 1077 ESGRQ 1081
Cdd:PRK01156 747 KSGVP 751
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
853-1056 |
4.28e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 853 KEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQ----------LSDAEERLAKLEAQQK 922
Cdd:pfam05667 332 QREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQykvkkktldlLPDAEENIAKLQALVD 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 923 DASKQLSELNDQLadNEDRTADVQ--RAKKKI----EAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQqqde 996
Cdd:pfam05667 412 ASAQRLVELAGQW--EKHRVPLIEeyRALKEAksnkEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE---- 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509401 997 aiaKLNKE-----------------KKHQEEINRKLME--DLQSEedkgnhQNKVKAKLEQTLDDLEDSLEREkrARAD 1056
Cdd:pfam05667 486 ---RLPKDvsrsaytrrileivkniKKQKEEITKILSDtkSLQKE------INSLTGKLDRTFTVTDELVFKD--AKKD 553
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
903-969 |
4.41e-03 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 39.65 E-value: 4.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 903 TKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMS 969
Cdd:pfam06810 16 PKAKFDEVNTERDTLKEQLATRDKQLKDLKKVAKDNEELQKQIDELQAKNKDAEADYEAKIADLKFD 82
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1299-1519 |
4.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1299 QLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQ 1378
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1379 QWKARFEGEG----LLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKK 1454
Cdd:COG3883 104 YLDVLLGSESfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1455 QKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIK 1519
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
894-1043 |
5.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 894 TSLFTNLESTKTQLSDAEERLAKLEAQ-----------QK---DASKQLSELNDQLADNEDRTADVQRA-KKKIEAEVEA 958
Cdd:PRK11281 124 RQLESRLAQTLDQLQNAQNDLAEYNSQlvslqtqperaQAalyANSQRLQQIRNLLKGGKVGGKALRPSqRVLLQAEQAL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 959 LKKQI-------------QDLEMSLRKAESEKQSK-DHQIRSLQD---------------EMQQQDEAI-AKLNKEKKHQ 1008
Cdd:PRK11281 204 LNAQNdlqrkslegntqlQDLLQKQRDYLTARIQRlEHQLQLLQEainskrltlsektvqEAQSQDEAArIQANPLVAQE 283
|
170 180 190
....*....|....*....|....*....|....*....
gi 17509401 1009 EEINRKLMEDLQSEEDKGN---HQN-KVKakleQTLDDL 1043
Cdd:PRK11281 284 LEINLQLSQRLLKATEKLNtltQQNlRVK----NWLDRL 318
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1638-1849 |
5.20e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1638 LDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAAD 1717
Cdd:pfam00261 10 LDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1718 ARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELR-----------QEQEHSQ 1786
Cdd:pfam00261 90 DEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKvvgnnlksleaSEEKASE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17509401 1787 HVDRlrkgLEQQLKEIQVRLDEAEAAALKGGKKViAKLEQRVRELESELDGEQRRFQDANKNL 1849
Cdd:pfam00261 170 REDK----YEEQIRFLTEKLKEAETRAEFAERSV-QKLEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1139-1783 |
5.95e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1139 SKADRAKS-DLQRELEEL---GEKLDEQGGATAAQVEVNKKREAElaklrRDLEEANMNHENQLGglrKKHTDAvaeltD 1214
Cdd:NF041483 428 TKEYRAKTvELQEEARRLrgeAEQLRAEAVAEGERIRGEARREAV-----QQIEEAARTAEELLT---KAKADA-----D 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1215 QLDQlnKAKAKVEKDKAQAVRDAEDLAAQLDQETS-GKLNNEKLAKQFELQLTELQSKADEQSRQLqdftslkgRLHSEN 1293
Cdd:NF041483 495 ELRS--TATAESERVRTEAIERATTLRRQAEETLErTRAEAERLRAEAEEQAEEVRAAAERAAREL--------REETER 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1294 GDLVRQLEDAEsqvnQLTRLKSQLTSQL---EEARRTADEEA-RERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRq 1369
Cdd:NF041483 565 AIAARQAEAAE----ELTRLHTEAEERLtaaEEALADARAEAeRIRREAAEETERLRTEAAERIRTLQAQAEQEAERLR- 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1370 lSKANADIQQwkARFEGEGL--------------LKADELEDAKRRQAQKI-------NELQEALDAANSKNASLEKTKS 1428
Cdd:NF041483 640 -TEAAADASA--ARAEGENVavrlrseaaaeaerLKSEAQESADRVRAEAAaaaervgTEAAEALAAAQEEAARRRREAE 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1429 RLVGDLDdAQVDVERANG-------VASA---LEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLfkAKNAQE 1498
Cdd:NF041483 717 ETLGSAR-AEADQERERAreqseelLASArkrVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGL--QEQAEE 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1499 ELA-------EVVEGLRRENKSLSQEIKdlTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQ 1571
Cdd:NF041483 794 EIAglrsaaeHAAERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEAAKALAERTVSEAIAEAERLRSDA 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1572 VEVSQ-IRSEIEKRIQEKEEEFENTRK------NHARALESMQA-SLETEAKGKAELLRIKKKLEGDINELEiALDHANK 1643
Cdd:NF041483 872 SEYAQrVRTEASDTLASAEQDAARTRAdaredaNRIRSDAAAQAdRLIGEATSEAERLTAEARAEAERLRDE-ARAEAER 950
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1644 ANADAQKNLKRYQEQVrelqlqVEEEQRNGADTREQFFNAEKRATLLQSEKEELLV-ANEAAERARKQAEYEAADARDQA 1722
Cdd:NF041483 951 VRADAAAQAEQLIAEA------TGEAERLRAEAAETVGSAQQHAERIRTEAERVKAeAAAEAERLRTEAREEADRTLDEA 1024
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1723 NEANAQVSSltSAKRKLEGEIQAIHADLDETLNEykaAEERSKKAIADATRLAEEL----RQEQE 1783
Cdd:NF041483 1025 RKDANKRRS--EAAEQADTLITEAAAEADQLTAK---AQEEALRTTTEAEAQADTMvgaaRKEAE 1084
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1360-1851 |
6.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1360 IEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKrrqaQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQV 1439
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK----SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1440 ---DVERANGVASalEKKQKGFDKIIDEWRKKTD--DLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRR--ENK 1512
Cdd:PRK01156 275 ykeLEERHMKIIN--DPVYKNRNYINDYFKYKNDieNKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRydDLN 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1513 SLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEF 1592
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1593 ENTRKNHARALESMqASLETEAK--------GKAELLRIKK-------KLEGDINELEIALDHANKANADAQKNLKR--- 1654
Cdd:PRK01156 433 RALRENLDELSRNM-EMLNGQSVcpvcgttlGEEKSNHIINhynekksRLEEKIREIEIEVKDIDEKIVDLKKRKEYles 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1655 --------YQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVA-NEAAERARKQAEYEAADA-RDQANE 1724
Cdd:PRK01156 512 eeinksinEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSkRTSWLNALAVISLIDIETnRSRSNE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1725 ANAQVSSLTSAKRKLEGEIQAIHA-------DLDETLNEYkaaeERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQ 1797
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSyidksirEIENEANNL----NNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP 667
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1798 QLKEIQVRLDEAE------AAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGR 1851
Cdd:PRK01156 668 DLKEITSRINDIEdnlkksRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1696-1871 |
6.10e-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: 41.58 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1696 ELLVANEAAERARKQAEYEAADARDQANEANAQVSSLT---SAKRK----------LEGEIQAIHADLDETL------NE 1756
Cdd:pfam13166 304 AQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRralEAKRKdpfksieldsVDAKIESINDLVASINeliakhNE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1757 YKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRkGLEQQLKEIQVRLDEAEAAalkggkkvIAKLEQRVRELESELD 1836
Cdd:pfam13166 384 ITDNFEEEKNKAKKKLRLHLVEEFKSEIDEYKDKYA-GLEKAINSLEKEIKNLEAE--------IKKLREEIKELEAQLR 454
|
170 180 190
....*....|....*....|....*....|....*
gi 17509401 1837 GEQRRFQDANKNLGRADRrvRELQFQVDEDKKNFE 1871
Cdd:pfam13166 455 DHKPGADEINKLLKAFGF--GELELSFNEEGKGYR 487
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1758-1930 |
6.24e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.99 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1758 KAAEER----SKKAIADATRLAEelrqeQEHSQHVDRLRKgLEQQLKEIQVR---LD-EAEAAALKGgkkVIAKLEQRVR 1829
Cdd:COG3524 161 AESEELvnqlSERAREDAVRFAE-----EEVERAEERLRD-AREALLAFRNRngiLDpEATAEALLQ---LIATLEGQLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1830 ELESELDgEQRRFQDANknlgraDRRVRELQFQVDedkknfeRLQDLIDKLQQKLKTQkkqvEEAEELANLnLQKYKQLT 1909
Cdd:COG3524 232 ELEAELA-ALRSYLSPN------SPQVRQLRRRIA-------ALEKQIAAERARLTGA----SGGDSLASL-LAEYERLE 292
|
170 180
....*....|....*....|.
gi 17509401 1910 HQLEDAEERADQAENSLSKMR 1930
Cdd:COG3524 293 LEREFAEKAYTSALAALEQAR 313
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
912-1191 |
6.67e-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: 41.55 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 912 ERLAKLEAQQKDASKQLSE--LNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQI--RSL 987
Cdd:pfam05667 210 ERNAAELAAAQEWEEEWNSqgLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFsgSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 988 QDEMQQQDEAIAKLNKEKKHQEEIN--RKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLERekraradLDKQKRKVE 1065
Cdd:pfam05667 290 TDTGLTKGSRFTHTEKLQFTNEAPAatSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQE-------LEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1066 GELKIAQENIDESGRQRHDLENNLKKKESELHsvssRLEDEQALVSKLQRQIKDGQSRI--------SELEEELENERQS 1137
Cdd:pfam05667 363 SSIKQVEEELEELKEQNEELEKQYKVKKKTLD----LLPDAEENIAKLQALVDASAQRLvelagqweKHRVPLIEEYRAL 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17509401 1138 RSKADRAKSDLQRELEELgEKLDEQGGATAAQVevnKKREAELAKLRRDLEEAN 1191
Cdd:pfam05667 439 KEAKSNKEDESQRKLEEI-KELREKIKEVAEEA---KQKEELYKQLVAEYERLP 488
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1688-1829 |
6.76e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1688 TLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDEtlnEYKAAEERSKKA 1767
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---EAQQAIKEAKKE 585
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509401 1768 IADATRLAEELRQEQEHSQHvdrlrkglEQQLKEIQVRLDEA----EAAALKGGKKVIA-KLEQRVR 1829
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVK--------AHELIEARKRLNKAnekkEKKKKKQKEKQEElKVGDEVK 644
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1184-1951 |
6.88e-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: 41.48 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1184 RRDLEEANMNHENQLGGLRKKHTDA---VAELTDQLDQLNKAkakvEKDKAQAVRDAEDLAAQLDQETSgklNNEKLAkQ 1260
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEqyrLVEMARELEELSAR----ESDLEQDYQAASDHLNLVQTALR---QQEKIE-R 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1261 FELQLTELQSKADEQSRQLQDftslkgrLHSENGDLVRQLEDAESQVNqltRLKSQLTS-------------QLEEARRt 1327
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEE-------AAEQLAEAEARLEAAEEEVD---SLKSQLADyqqaldvqqtraiQYQQAVQ- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1328 ADEEARER----QTVAAQAKNYQHEAEQLQESLEEEIEGkneiLRQ-LSKANADIQQWKARFEgegLLK--ADELEdakR 1400
Cdd:COG3096 421 ALEKARALcglpDLTPENAEDYLAAFRAKEQQATEEVLE----LEQkLSVADAARRQFEKAYE---LVCkiAGEVE---R 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1401 RQAQKinELQEALDAANSKNASLEKTKSrLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEwRKKTDDLAAELDGAQ 1480
Cdd:COG3096 491 SQAWQ--TARELLRRYRSQQALAQRLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1481 RDLrntstdlfkaknaQEELAEVVE---GLRRENKSLSQEIKDLTDQLGEGgrsvHEMQKIIRRLEiekeELQHALDEAE 1557
Cdd:COG3096 567 EEL-------------EEQAAEAVEqrsELRQQLEQLRARIKELAARAPAW----LAAQDALERLR----EQSGEALADS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1558 AALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFEntRKNHARALESmqasleteakgkAELLRIKKKLEG----DINE 1633
Cdd:COG3096 626 QEVTAAMQQLLEREREATVERDELAARKQALESQIE--RLSQPGGAED------------PRLLALAERLGGvllsEIYD 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1634 lEIALDHA--------NKANADAQKNLKRYQEQVRELQ-----LQVEEEQRNGADtrEQFFNAE--KRATLLQSEKEELL 1698
Cdd:COG3096 692 -DVTLEDApyfsalygPARHAIVVPDLSAVKEQLAGLEdcpedLYLIEGDPDSFD--DSVFDAEelEDAVVVKLSDRQWR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1699 VAN--EAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLegeiQAIHADLDETLNEYKAaeerskkaIADATRLAE 1776
Cdd:COG3096 769 YSRfpEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKL----QRLHQAFSQFVGGHLA--------VAFAPDPEA 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1777 ELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAeAAALKGGKKVIAK--------LEQRVRELESELDG--EQRRFQDAN 1846
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQL-KEQLQLLNKLLPQanlladetLADRLEELREELDAaqEAQAFIQQH 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1847 -KNLGRADRRVRELQ---FQVDEDKKNFERLQDLIDKLQQKLKTQKKQV--------EEAEELANLNLQKYKQLTHQLED 1914
Cdd:COG3096 916 gKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVqrrphfsyEDAVGLLGENSDLNEKLRARLEQ 995
|
810 820 830
....*....|....*....|....*....|....*..
gi 17509401 1915 AEERADQAENSLSKMRSKSRASASVAPGLQSSASAAV 1951
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQ 1032
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1135-1323 |
7.05e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1135 RQSRSKADRAKSDLQRELEELGEKLD-EQGGATAAQvevnkkreAELAKLRRDLEEANMNHEnQLGGLRKKHTDAVAELT 1213
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLSlERQGNQDLQ--------DSVANLRASLSAAEAERS-RLQALLAELAGAGAAAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1214 DQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQetsgkLNNEKLAKQFELQLTELQSKadEQSRQLQdftslkgrlhsen 1293
Cdd:PRK09039 116 GRAGELAQELDSEKQVSARALAQVELLNQQIAA-----LRRQLAALEAALDASEKRDR--ESQAKIA------------- 175
|
170 180 190
....*....|....*....|....*....|.
gi 17509401 1294 gDLVRQLEDAESQ-VNQLTRLKSQLTSQLEE 1323
Cdd:PRK09039 176 -DLGRRLNVALAQrVQELNRYRSEFFGRLRE 205
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
842-1003 |
7.15e-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: 40.82 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 842 YGKVKPMLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKL--EA 919
Cdd:cd22656 93 YAEILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 920 QQKDASKQLSELNDQLADNEDRTAdvqrakKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIA 999
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYA------AKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIP 246
|
....
gi 17509401 1000 KLNK 1003
Cdd:cd22656 247 ALEK 250
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1659-1934 |
7.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1659 VRELQLQVEEEQRNgADTREQFFNAEKR--ATLLQSEKEELLVANEAAER--ARKQA-EYEAADARDQANEANAQVSSLT 1733
Cdd:pfam01576 17 VKERQQKAESELKE-LEKKHQQLCEEKNalQEQLQAETELCAEAEEMRARlaARKQElEEILHELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1734 SAKRKLEGEIQaihaDLDETLNEYKAAEERSK--KAIADAT--RLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEA 1809
Cdd:pfam01576 96 NEKKKMQQHIQ----DLEEQLDEEEAARQKLQleKVTTEAKikKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1810 EAAAlKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKK 1889
Cdd:pfam01576 172 EEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17509401 1890 QVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSR 1934
Cdd:pfam01576 251 RLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR 295
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1338-1548 |
7.53e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1338 VAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAAN 1417
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1418 SKNASLEKTKSRLVGDLDDAQV--------------DVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDL 1483
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509401 1484 RNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEE 1548
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1459-1635 |
7.64e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1459 DKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGgRSVHEMQKI 1538
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1539 IRRLEIEKEElqhaldeaeaaleaeeskvlraqvevsqiRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKA 1618
Cdd:COG1579 95 QKEIESLKRR-----------------------------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170
....*....|....*..
gi 17509401 1619 ELLRIKKKLEGDINELE 1635
Cdd:COG1579 146 ELDEELAELEAELEELE 162
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1082-1306 |
8.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1082 RHDLENNLKK-KESELHS-----VSSRLEDEQALVSKLQRQIKDgqsriseleeeLENERQSRSKADRAKSDLQRELEEL 1155
Cdd:PRK11281 38 EADVQAQLDAlNKQKLLEaedklVQQDLEQTLALLDKIDRQKEE-----------TEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1156 GEKLDEQ-----GGATAAQVEVN-KKREAELAKLRRDLEEANmnheNQLGGLRKKHTDAVAELTD---QLDQLNKAKAKV 1226
Cdd:PRK11281 107 KDDNDEEtretlSTLSLRQLESRlAQTLDQLQNAQNDLAEYN----SQLVSLQTQPERAQAALYAnsqRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1227 EKDKAQAVRDAED--------LAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSL---KGRLHSENgd 1295
Cdd:PRK11281 183 KVGGKALRPSQRVllqaeqalLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAinsKRLTLSEK-- 260
|
250
....*....|.
gi 17509401 1296 lvrQLEDAESQ 1306
Cdd:PRK11281 261 ---TVQEAQSQ 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1737-1872 |
8.07e-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: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1737 RKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRlaeELRQEQEHSQHVDRLRKGLEQQL------KEIQVRLDEAE 1810
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEK---EIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALQKEIE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509401 1811 AAALKggkkvIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFER 1872
Cdd:COG1579 100 SLKRR-----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
848-1190 |
9.96e-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: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 848 MLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEErlaKLEAQQKDA--- 924
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ---ALDVQQTRAiqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 925 ---------SKQLSELNDQLADNedrtadvqrakkkIEAEVEALKKQIQDLEMSLRKAEsekqskdHQIRSLQDEMQQQD 995
Cdd:COG3096 416 qqavqalekARALCGLPDLTPEN-------------AEDYLAAFRAKEQQATEEVLELE-------QKLSVADAARRQFE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 996 EAIAKLNK-----EKKHQEEINRKLMEDLQSEEdkgnHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKI 1070
Cdd:COG3096 476 KAYELVCKiagevERSQAWQTARELLRRYRSQQ----ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 1071 AQEnidesgrqrhdLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRIseleeeleneRQSRSKADR---AKSD 1147
Cdd:COG3096 552 AEE-----------LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI----------KELAARAPAwlaAQDA 610
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 17509401 1148 LQRELEELGEKLDEQGGATAA-QVEVNKKREA-----ELAKLRRDLEEA 1190
Cdd:COG3096 611 LERLREQSGEALADSQEVTAAmQQLLEREREAtverdELAARKQALESQ 659
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1017 |
9.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 847 PMLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASK 926
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509401 927 QLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDL------------EMSLRKAESEKQSKDhqirsLQDEMQQQ 994
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEERYDFLSEQRED-----LEEARETL 814
|
170 180
....*....|....*....|....*...
gi 17509401 995 DEAIAKLNKEKKHQ-----EEINRKLME 1017
Cdd:COG1196 815 EEAIEEIDRETRERfletfDAVNENFQE 842
|
|
| |
