|
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, ... |
95-776 |
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: 1198.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDkaqVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK---GTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDaQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKP-LGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKprpPKGKQA 573
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKK---PKPKKS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 574 EAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVaaaakdgkkaVGKKKGKSASFM 653
Cdd:cd01377 474 EAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSS-DPLVASLFKDYEESGGG----------GGKKKKKGGSFR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 654 TVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVL 733
Cdd:cd01377 543 TVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSIL 622
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 734 AADAAKAGKdpkDAGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd01377 623 APNAIPKGF---DDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-776 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1009.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 83 TEDMANLTFLNDASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMT 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 163 NDRENQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKkskkdkaqVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRF 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 243 GKFIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQ-AEVTIDGV 321
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNP-KDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 322 DDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPR 401
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 402 VKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVN 481
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 482 EKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHP 560
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 561 NFQKPRPpkgkQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDvaaAAKDGKK 640
Cdd:pfam00063 470 HFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSS-DPLLAELFPDYETAES---AAANESG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 641 AVGKKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNR 720
Cdd:pfam00063 542 KSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 721 MPFLDFKQRYavlAADAAKAGKDPKDAGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:pfam00063 622 ITFQEFVQRY---RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-788 |
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: 965.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 76 NPPKYEKTEDMANLTFLNDASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 156 EAYRNMTNDRENQSMLITGESGAGKTENTKKVISYFAMVGAsqqsnkkkskKDKAQVSLEDQIVQTNPVLEAFGNAKTVR 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG----------SNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 236 NNNSSRFGKFIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQA- 314
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 315 EVTIDGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEG-ELACKLYCVESEKF 393
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEElSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 394 INALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFE 473
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKD-GSTYFIGVLDIYGFEIFEVNSFE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 474 QLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLN 552
Cdd:smart00242 389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 553 dQHLGKHPNFQKPRppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVa 632
Cdd:smart00242 468 -QHHKKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSK-NPLIASLFPSGVSNAGS- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 633 aaakdgkkavgkkkgkSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRI 712
Cdd:smart00242 541 ----------------KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRI 604
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 713 CRKGFPNRMPFLDFKQRYavlaADAAKAGKDPKDAGEK-ISAALIKDGSLKQEEFQCGLTKVFFKAGVLAHLEELRD 788
Cdd:smart00242 605 RRAGFPYRLPFDEFLQRY----RVLLPDTWPPWGGDAKkACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-776 |
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: 928.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKG----SLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQ-KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKQAE 574
Cdd:cd14909 396 LEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 575 AHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKanKG-NQLMADLWADYATQEdvaaaaKDGKKAVGKKKGKSASFM 653
Cdd:cd14909 476 AHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFK--KSqNKLLIEIFADHAGQS------GGGEQAKGGRGKKGGGFA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 654 TVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVL 733
Cdd:cd14909 548 TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKIL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 734 AADAAKAGKDPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14909 628 NPAGIQGEEDPKKAAEIILESI----ALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-776 |
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: 866.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQV--SLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNT 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 253 GGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDE 332
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 333 AFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKG 412
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 413 QNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQdLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHM 492
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTK-LPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 493 FVLEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKQ 572
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 573 AEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVaaaaKDGKKAVGKKKGKSASF 652
Cdd:cd14927 480 YEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQ-NKLLATLYENYVGSDST----EDPKSGVKEKRKKAASF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 653 MTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAV 732
Cdd:cd14927 555 QTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 17561652 733 LAADA--AKAGKDPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14927 635 LNPSAipDDKFVDSRKATEKLLGSL----DIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-776 |
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: 834.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGKG------SLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14934 155 KLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14934 235 DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQdLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14934 315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTK-MQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKQAE 574
Cdd:cd14934 394 LEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 575 AHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKanKGNQLMADLWadyatqedvaaAAKDGKKAVGKKKGKSASFMT 654
Cdd:cd14934 474 AHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQ--KSSLGLLALL-----------FKEEEAPAGSKKQKRGSSFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 655 VSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLA 734
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17561652 735 ADAAKAGKDPKdagEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14934 621 PNVIPQGFVDN---KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-776 |
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: 830.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKG--TLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQdLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTK-LPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEA 575
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGR-AEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEdvaaaakDGKKAVGKKKGKSASFMTV 655
Cdd:cd14913 478 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVG-LYQKSSNRLLAHLYATFATAD-------ADSGKKKVAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14913 550 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 629
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14913 630 SAIPEGQfiDSKKACEKLLASI----DIDHTQYKFGHTKVFFK 668
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
23-1140 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 797.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 23 TTKKFDSKKNVWVADPEEGFIAAEIKSS---KGDTVVVVTSKGVEK-TIKKDDAQQ--MNPPKYEKTEDMANLTFLNDAS 96
Cdd:COG5022 2 STTNAEVGSGCWIPDEEKGWIWAEIIKEafnKGKVTEEGKKEDGESvSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 97 VLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGES 176
Cdd:COG5022 82 VLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 177 GAGKTENTKKVISYFAMVGAsqqsnkkksKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGKV 256
Cdd:COG5022 162 GAGKTENAKRIMQYLASVTS---------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 257 AGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAEVT-IDGVDDKEEMLITDEAFD 335
Cdd:COG5022 233 CGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNP-KDYIYLSQGGCDkIDGIDDAKEFKITLDALK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQrPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:COG5022 312 TIGIDEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:COG5022 391 EQALAIRDSLAKALYSNLFDWIVDRINKSLDHSA-AASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFgLDLQACIELIEK--PLGIVSMLDEECIVPKASDLTLASKLNDQ-HLGKHPNFQKPRppkgkQ 572
Cdd:COG5022 470 EQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSR-----F 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 573 AEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEdvaaaakdgkkavgkkkgKSASF 652
Cdd:COG5022 544 RDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKAST-NEFVSTLFDDEENIE------------------SKGRF 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 653 MTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAV 732
Cdd:COG5022 605 PTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRI 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 733 LAADAAKAGKDPKDAGEK-ISAALIKDGSLKQEEFQCGLTKVFFKAGVLAHLEELRDEALGKIMAKFQCACRHYLAQCEY 811
Cdd:COG5022 685 LSPSKSWTGEYTWKEDTKnAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRY 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 812 KRKLDQKVGLIVLQRNIRAWCTLRSWSWFKLFGRVKPLIKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARle 891
Cdd:COG5022 765 LQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSL-- 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 892 aeKQALLIQleqeRDSSAEGEERSAKLLAQKADLEK---QMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLE 968
Cdd:COG5022 843 --KAEVLIQ----KFGRSLKAKKRFSLLKKETIYLQsaqRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLS 916
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 969 TtikkqesekqakdhqirSLQDEIQSQDEVISKLnkeKKHQEEVNRKLLEDIQAEE-DKVNHLNKTKAKLESTLDELEDT 1047
Cdd:COG5022 917 S-----------------DLIENLEFKTELIARL---KKLLNNIDLEEGPSIEYVKlPELNKLHEVESKLKETSEEYEDL 976
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1048 LEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQViKKKDIELSSIQ-------SRLEDEQSLvAKLQRQIKE 1120
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL-KELPVEVAELQsaskiisSESTELSIL-KPLQKLKGL 1054
|
1130 1140
....*....|....*....|
gi 17561652 1121 LLARIQELEEELDAERNSRS 1140
Cdd:COG5022 1055 LLLENNQLQARYKALKLRRE 1074
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-776 |
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: 786.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSkkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLG-------ALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSdAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQdLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAK-LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKgKQAE 574
Cdd:cd14929 392 LEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDK-KKFE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 575 AHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVaaaakdgKKAVGKKKGKSASFMT 654
Cdd:cd14929 471 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSS-NRLLASLFENYISTDSA-------IQFGEKKRKKGASFQT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 655 VSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY--AV 732
Cdd:cd14929 543 VASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYciLN 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 17561652 733 LAADAAKAGKDPKDAGEKISAALIKDGSlkqeEFQCGLTKVFFK 776
Cdd:cd14929 623 PRTFPKSKFVSSRKAAEELLGSLEIDHT----QYRFGITKVFFK 662
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-776 |
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: 785.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRN-EMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGASQQSNKKKSKKdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAS-----SIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 GKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTF----VSQAEVTIDGVDDKEEMLI 329
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 330 TDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREE--QAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTE 407
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 408 WVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDF-FIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQ 486
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTsFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 487 FFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKP 565
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH-GSHPRFFSK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 566 RppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKAnkgnqlmadlwadyatqedvaaaakdgkkavgkk 645
Cdd:cd00124 474 K----RKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS---------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 646 kgkSASFmtvsmmyRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLD 725
Cdd:cd00124 516 ---GSQF-------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDE 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 17561652 726 FKQRYAVLAADAAKAGKDPKDAGEKISAALIKDGSlkqEEFQCGLTKVFFK 776
Cdd:cd00124 586 FLKRYRILAPGATEKASDSKKAAVLALLLLLKLDS---SGYQLGKTKVFLR 633
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-776 |
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: 760.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKG--TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEA 575
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGK-PEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEdvaaaakDGKKAVGKKKGKSASFMTV 655
Cdd:cd14917 478 HFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSS-LKLLSNLFANYAGAD-------APIEKGKGKAKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14917 550 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 629
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14917 630 AAIPEGQfiDSRKGAEKLLSSL----DIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-776 |
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: 755.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKG-TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKQaEA 575
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQ-EA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEdvaaaaKDGKKAVGKKKGKSASFMTV 655
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVG-LYQKSSLKLMATLFSTYASAD------TGDSGKGKGGKKKGSSFQTV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14916 552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14916 632 AAIPEGQfiDSRKGAEKLLGSL----DIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-776 |
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: 753.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 97 VLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 177 GAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGKV 256
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQG--TLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 257 AGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFDI 336
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 337 MKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNLD 416
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 417 QVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLE 496
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 497 QEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEAH 576
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 577 LAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEdvaaaakDGKKAVGKKKGKSASFMTVS 656
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVG-LYQKSAMKTLASLFSTYASAE-------ADSGAKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 657 MMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAAD 736
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17561652 737 AAKAGK--DPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14918 631 AIPEGQfiDSKKASEKLLASI----DIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-776 |
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: 749.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEA 575
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-VEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEdvaaaaKDGKKAVGKKKGKSASFMTV 655
Cdd:cd14910 480 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVVG-LYQKSSMKTLALLFSGAAAAE------AEEGGGKKGGKKKGSSFQTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14910 553 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALIKDgslkQEEFQCGLTKVFFK 776
Cdd:cd14910 633 SAIPEGQfiDSKKASEKLLGSIDID----HTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-776 |
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: 747.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVgASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATI-AVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEA 575
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGK-AEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEdvaaaAKDGKKAVGKKKGKSASFMTV 655
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVG-LYQKSSLKLLSFLFSNYAGAE-----AGDSGGSKKGGKKKGSSFQTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14923 553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALIKDgslkQEEFQCGLTKVFFK 776
Cdd:cd14923 633 SAIPEGQfiDSKNASEKLLNSIDVD----REQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-776 |
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: 746.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEA 575
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGK-AEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANkGNQLMADLWADYATQEDvaaaAKDGKKAVGKKKGKSASFMTV 655
Cdd:cd14912 480 HFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKS-AMKTLAYLFSGAQTAEG----ASAGGGAKKGGKKKGSSFQTV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14912 555 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14912 635 SAIPEGQfiDSKKASEKLLASI----DIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-776 |
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: 741.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNL 415
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 416 DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVL 495
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 496 EQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKqAEA 575
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-AEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 576 HLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEdvaaaaKDGKKAVGKKKGKSASFMTV 655
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVG-LYQKSGMKTLAFLFSGGQTAE------AEGGGGKKGGKKKGSSFQTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 656 SMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAA 735
Cdd:cd14915 553 SALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 17561652 736 DAAKAGK--DPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14915 633 SAIPEGQfiDSKKASEKLLGSI----DIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-776 |
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: 731.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE----LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14920 157 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPL---GIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRPPKGk 571
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 qaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADY-ATQEDVAAAAKDGKKAVGKKKGKSA 650
Cdd:cd14920 474 --KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS-DRFVAELWKDVdRIVGLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 651 SFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17561652 731 avlaaDAAKAGKDPKD--AGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14920 631 -----EILTPNAIPKGfmDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-776 |
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: 724.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVS-----LEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNPAvligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 250 FNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAEVTIDGVDDKEEMLI 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV-KSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 330 TDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWV 409
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 410 NKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFN 489
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 490 HHMFVLEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKprppK 569
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMK----T 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 570 GKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADyatQEDVAAAAKDGKKAVGKKKGKS 649
Cdd:cd14911 475 DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ-DPFVVNIWKD---AEIVGMAQQALTDTQFGARTRK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 650 ASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQR 729
Cdd:cd14911 551 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17561652 730 YavlaaDAAKAGKDPKD--AGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14911 631 Y-----ELLTPNVIPKGfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-776 |
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: 687.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPL---GIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRPPKGk 571
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 qaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVAAAAKDGKKAVGKKKGKSAS 651
Cdd:cd14932 478 --DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQST-DKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 652 FMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYa 731
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY- 633
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 17561652 732 vlaaDAAKAGKDPKD--AGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14932 634 ----EILTPNAIPKGfmDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-776 |
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: 677.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSM-MIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNkkkskkdkaqVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGE----------TQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDF-FIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMF 493
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 494 VLEQEEYKREGIQWEFIDFgLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGK-HPNFQKPRPPKGKq 572
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 573 aeahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQlmadlwadyatqedvaaaakdgkkavgkkkgksasf 652
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK------------------------------------ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 653 MTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAV 732
Cdd:cd01380 510 KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRV 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 17561652 733 LAADAAKAGKDPKDAGEKISAALIKDgslkQEEFQCGLTKVFFK 776
Cdd:cd01380 590 LLPSKEWLRDDKKKTCENILENLILD----PDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-776 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 648.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPL---GIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRPPKGK 571
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 qaeAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVAAAAKDGKKAV-GKKKGKSA 650
Cdd:cd14921 475 ---TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASS-DKFVADLWKDVDRIVGLDQMAKMTESSLpSASKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 651 SFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14921 551 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17561652 731 avlaaDAAKAGKDPKD--AGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14921 631 -----EILAANAIPKGfmDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-776 |
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: 640.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKkdkaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGE-------LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14919 154 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPL---GIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRPPKGK 571
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 qaeAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVAAAAKDGKKAVGKK-KGKSA 650
Cdd:cd14919 472 ---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS-DKFVSELWKDVDRIIGLDQVAGMSETALPGAfKTRKG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 651 SFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14919 548 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17561652 731 avlaaDAAKAGKDPKD--AGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14919 628 -----EILTPNSIPKGfmDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-776 |
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: 639.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRpIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLEN-YNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPL---GIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRPPKGk 571
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 qaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVAAAAKDGKKAVGKKKGKSAs 651
Cdd:cd15896 478 --EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQST-DKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGM- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 652 FMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYa 731
Cdd:cd15896 554 FRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY- 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 17561652 732 vlaaDAAKAGKDPKD--AGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd15896 633 ----EILTPNAIPKGfmDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-776 |
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: 613.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGvDDKEEMLITDEAF 334
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQETLESL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14930 235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFGLDLQACIELIEKPL---GIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRppkGK 571
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVA-QEQGGHPKFQRPR---HL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 QAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVAAAAKDGKKAVGKKKGKSAs 651
Cdd:cd14930 471 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQST-DRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGM- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 652 FMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYA 731
Cdd:cd14930 549 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 17561652 732 VLAADAAKAG-KDPKDAGEKISAALIKDGSLkqeeFQCGLTKVFFK 776
Cdd:cd14930 629 ILTPNAIPKGfMDGKQACEKMIQALELDPNL----YRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-776 |
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: 613.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYlGKRRNEmPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQsnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS-------------GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAE-VTIDGVDDKEEMLITDEAF 334
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSA-SEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFqkprppKGKQA 573
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLK-QHLKSNSCF------KGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 574 EAhLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGN--QLMADLWADYATQEDVAAAAKDGKKAVGkkkgksas 651
Cdd:cd01383 458 GA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQlpQLFASKMLDASRKALPLTKASGSDSQKQ-------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 652 fmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYa 731
Cdd:cd01383 529 --SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRY- 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17561652 732 vlaadaakAGKDPKDAGEK-----ISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd01383 606 --------GFLLPEDVSASqdplsTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-776 |
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: 593.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQsnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAV--KGLREKLFLtRPIKEYTFVSQAE-VTIDGVDDKEEMLITDE 332
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQSGcIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 333 AFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELA-CKLYCVESEKFINALLKPRVKVgtewvnK 411
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKIvAKLLGVDPDKLKKALTIRQINV------R 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 412 GQNLD---QVNWAV---GALAKALFARMFSWLIRRCNKTLDA-QDLSRdfFIGVLDIAGFEIFDLNSFEQLWINFVNEKL 484
Cdd:cd14883 302 GNVTEiplKVQEARdnrDAMAKALYSRTFAWLVNHINSCTNPgQKNSR--FIGVLDIFGFENFKVNSFEQLCINYTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 485 QQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIEK-PLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQ 563
Cdd:cd14883 380 HKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 564 KPRPPKGKQAeahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKaNKGNQLMADLwADYATQEDVaAAAKDGKKAVG 643
Cdd:cd14883 458 KPDRRRWKTE---FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMS-RSKNKFVKEL-FTYPDLLAL-TGLSISLGGDT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 644 KKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPF 723
Cdd:cd14883 532 TSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 17561652 724 LDFKQRYavlaADAAKAGKDPKDAGEKISA-ALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14883 612 KEFVDRY----LCLDPRARSADHKETCGAVrALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-776 |
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: 577.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQsnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAE-VTIDGVDDKEEMLITDEA 333
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDA-SDYYYLTQGNcLTCEGRDDAAEFADIRSA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 334 FDIMKFTATEKSELFAITAGIMHMGELKFKQRPRE--EQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNK 411
Cdd:cd01381 227 MKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 412 GQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL---DAQDLSRDfFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFF 488
Cdd:cd01381 307 PLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRT-SIGVLDIFGFENFEVNSFEQLCINFANENLQQFF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 489 NHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKPRp 567
Cdd:cd01381 386 VRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPK- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 568 pkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWA-DYATQEDVAAAAKdgkkavgkkk 646
Cdd:cd01381 463 ---SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSK-NKFLKQLFNeDISMGSETRKKSP---------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 647 gksasfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDF 726
Cdd:cd01381 529 -------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 17561652 727 KQRYAV-LAADAAKAGKDPKDAGEKISAALIkdgsLKQEEFQCGLTKVFFK 776
Cdd:cd01381 602 VERYRVlVPGIPPAHKTDCRAATRKICCAVL----GGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-776 |
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: 570.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVE---------RVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAFD 335
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 336 IMKFTATEKSELFAITAGIMHMGELKFKQrprEEQ--AELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEW---VN 410
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEgnAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 411 KGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNH 490
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 491 hmFVL--EQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECI-VPKASDLTLASKLNdQHLGKHPNFQKPR 566
Cdd:cd01378 390 --LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLtAGDATDQTFLQKLN-QLFSNHPHFECPS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 567 PPKGkQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLkANKGNQLMADLWADyATQEDVAAAAKdgkkavgkkk 646
Cdd:cd01378 466 GHFE-LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELM-QSSSNPFLRSLFPE-GVDLDSKKRPP---------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 647 gksasfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDF 726
Cdd:cd01378 533 -------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKF 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17561652 727 KQRYAVLAADAAKAGKDPKDAGekiSAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd01378 606 LERYKLLSPKTWPAWDGTWQGG---VESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-776 |
6.65e-179 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 557.68 E-value: 6.65e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGASQQSNKKkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR---------SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 GKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAE-VTIDGVDDKEEMLITDE 332
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDP-KQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 333 AFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEG---ELACKLYCVESEKFINALLKPRVKVGTEWV 409
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEfhlKAAAELLMCDEKALEDALCKRVIVTPDGII 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 410 NKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLdAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFN 489
Cdd:cd01384 311 TKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSI-GQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 490 HHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQhLGKHPNFQKPrpp 568
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKP--- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 569 kgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDvaaaakdgkkavgkkkGK 648
Cdd:cd01384 465 --KLSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASK-CPFVAGLFPPLPREGT----------------SS 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 649 SASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQ 728
Cdd:cd01384 526 SSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLD 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17561652 729 RYAVLAADAAKAGKDPKDAGEKISAALIKDGslkqeeFQCGLTKVFFK 776
Cdd:cd01384 606 RFGLLAPEVLKGSDDEKAACKKILEKAGLKG------YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-776 |
6.83e-168 |
|
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: 527.97 E-value: 6.83e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGASQQSnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG------------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 GKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLfLTRPIkeytfvsqaevtidgVDDKEEMLITDEA 333
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPL---------------LDDVGDFIRMDKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 334 FDIMKFTATEKSELFAITAGIMHMGELKFKQRPREE----QAELEEGKEGELACKLYCVESEKFINALLKpRVKVGTEWV 409
Cdd:cd01382 213 MKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 410 NKGQ------NLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSrdFFIGVLDIAGFEIFDLNSFEQLWINFVNEK 483
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSS--YFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 484 LQQFFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQHLgKHPNF 562
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 563 QKPRPPKGKQ------AEAHLaIVHYAGTVRYNVKGWLEKNKDPLNDTaVTVLKANKGNQLMADLWADYATQEDVAAAAK 636
Cdd:cd01382 448 SIPRKSKLKIhrnlrdDEGFL-IRHFAGAVCYETAQFIEKNNDALHAS-LESLICESKDKFIRSLFESSTNNNKDSKQKA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 637 DGKkavgkkkgksaSFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKG 716
Cdd:cd01382 526 GKL-----------SFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGG 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 717 FPNRMPFLDFKQRYavlaadaaKAGKDPKDAGEK---ISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd01382 595 FPSRTSFHDLYNMY--------KKYLPPKLARLDprlFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-776 |
2.19e-160 |
|
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: 507.39 E-value: 2.19e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQsnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTN-------------GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPikeYTFVSQAE-VTIDGVDDKEEMLITDEA 333
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA---YGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 334 FDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACK---LYCVESEKFINALLKPRVKVgtewvn 410
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEI------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 411 KGQNL-------DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEK 483
Cdd:cd14872 299 KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 484 LQQFFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIEK-PLGIVSMLDEECIVPKASDLTLASKLNDQHLGKhpNF 562
Cdd:cd14872 379 LQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAK--ST 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 563 QKPRPPKGKQAEahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKAnKGNQLMADLWADYATQEdvaaaakdgkkav 642
Cdd:cd14872 456 FVYAEVRTSRTE--FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSS-SKNKLIAVLFPPSEGDQ------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 643 gkkkgkSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMP 722
Cdd:cd14872 520 ------KTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYS 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 17561652 723 FLDFKQRYavLAADAAKAGKDPKDAGEKISaALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14872 594 HERFLKRY--RFLVKTIAKRVGPDDRQRCD-LLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-776 |
2.87e-160 |
|
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: 507.78 E-value: 2.87e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNEMPPHLFAVSDEAY----RNMTNDRENQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 170 MLITGESGAGKTENTKKVISYFAMV------GASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARItsgfaqGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 244 KFIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIkEYTFVSQAEVTIDGVDD 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPV-EYFYLRGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 324 KEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREE-QAELEEGKEGELACKLYCVESEKFINALLKPRV 402
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 403 KVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNE 482
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPD-DKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 483 KLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-----KPlGIVSMLDeECIVPKAS--DLTLASKLNDQH 555
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 556 ------------LGKHPNFQKPRPPKGKQaeahLAIVHYAGTVRYNVKGWLEKNKDPLNDTavtvlkankgnqlMADLWA 623
Cdd:cd14890 476 grksgsggtrrgSSQHPHFVHPKFDADKQ----FGIKHYAGDVIYDASGFNEKNNETLNAE-------------MKELIK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 624 dyatqedvaaaakdgkkavgkKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTC 703
Cdd:cd14890 539 ---------------------QSRRSIREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKY 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 704 NGVLEGIRICRKGFPNRMPFLDFKQRYAVLAADAakagkdpkDAGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14890 598 SGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA--------ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-776 |
1.34e-159 |
|
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: 505.83 E-value: 1.34e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEM---PPHLFAVSDEAYRNMTNDR----EN 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 168 QSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 248 IHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIysdaVKGL----REKLFLTrPIKEYTFVSQAE-VTIDGVD 322
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQL----LAGLdaneNAALELT-PAESFLFLNQGNcVEVDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 323 DKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQR--PREEQAELEEGKEGELACKLYCVESEKFINALLKp 400
Cdd:cd14892 236 DATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVT- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 401 RVKVGTewvnKGQNL------DQVNWAVGALAKALFARMFSWLIRRCNK---------TLDAQDLSRDFFIGVLDIAGFE 465
Cdd:cd14892 315 QTTSTA----RGSVLeikltaREAKNALDALCKYLYGELFDWLISRINAchkqqtsgvTGGAASPTFSPFIGILDIFGFE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 466 IFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIEK-PLGIVSMLDEECIVP-KAS 543
Cdd:cd14892 391 IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 544 DLTLASKLNDQHLGKHPNFQKPRppkgkQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgnqlmadlwa 623
Cdd:cd14892 470 DKQLLTIYHQTHLDKHPHYAKPR-----FECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS---------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 624 dyatqedvaaaakdgkkavgkkkgksasfmtvsmMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTC 703
Cdd:cd14892 535 ----------------------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIY 580
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 704 NGVLEGIRICRKGFPNRMPFLDFKQRYAVLAADAAKAGKDPKDAGEKISAAL---IKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14892 581 SGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTARKKceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-776 |
1.02e-158 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 503.17 E-value: 1.02e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVgasqQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVI----SQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 GKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAE-VTIDGVDDKEEMLITDE 332
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTP-ENYHYLNQSGcVEDKTISDQESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 333 AFDIMKFTATEKSELFAITAGIMHMGELKFKQrprEEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKG 412
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 413 QNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlsrDF-FIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHH 491
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKE---DFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 492 MFVLEQEEYKREGIQWEFIDFgLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKPRppkgk 571
Cdd:cd14873 390 IFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR----- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 572 QAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNqLMADLWadyatqEDVAAAAKDGKKAVGKKKGKSas 651
Cdd:cd14873 463 VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFD-FIYDLF------EHVSSRNNQDTLKCGSKHRRP-- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 652 fmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYa 731
Cdd:cd14873 534 --TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRY- 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 17561652 732 vlaADAAKAGKDPKDAGEKISAALIK-DGSLKqeEFQCGLTKVFFK 776
Cdd:cd14873 611 ---KVLMRNLALPEDVRGKCTSLLQLyDASNS--EWQLGKTKVFLR 651
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1933 |
7.11e-156 |
|
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: 510.10 E-value: 7.11e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEV 1012
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 NRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKK 1092
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 KDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIE 1172
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 LNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQR 1252
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1253 QNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQE 1332
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1333 TRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSrAEELEETRRKLTHKVQEMQE 1412
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1413 QLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETF 1492
Cdd:pfam01576 560 QLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1493 RLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQ 1572
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1573 IEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKS 1652
Cdd:pfam01576 720 VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1653 MKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQE----KEDLAIiyeqSERTRRQAELELAEVKDSVNELSN 1728
Cdd:pfam01576 800 LKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAEllqlQEDLAA----SERARRQAQQERDELADEIASGAS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1729 SNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLD 1808
Cdd:pfam01576 876 GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1809 EAEAAGIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTY 1888
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL 1035
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 17561652 1889 KRQIEDAESLASGNLAKYRQLQHVVEDAQERADAAENALQKLRLK 1933
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-774 |
8.43e-154 |
|
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: 489.68 E-value: 8.43e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESV--CQMYLGKRR----NEMPPHLFAVSDEAYRNMTNDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETkeAYYEHGERRaageRKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 167 --NQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 244
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERE----NVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 245 FIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTrPIKEYTFVSQAEVTI--DGVD 322
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLT-HVEEYKYLNSSQCYDrrDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 323 DKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELA-CKLYCVESEKFINALLKPR 401
Cdd:cd14901 236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAaCDLLGLDMDVLEKTLCTRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 402 VKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL---DAQDLSRdfFIGVLDIAGFEIFDLNSFEQLWIN 478
Cdd:cd14901 316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaysESTGASR--FIGIVDIFGFEIFATNSLEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 479 FVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQhLG 557
Cdd:cd14901 394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 558 KHPNFQKprpPKGKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQLMAdlwadyatqedvaaaakd 637
Cdd:cd14901 472 KHASFSV---SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 638 gkkavgkkkgksasfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGF 717
Cdd:cd14901 531 ----------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 718 PNRMPFLDFKQRYA--VLAADAAKAGKDPKDAGEKISAALIKDGSLKQEEFQCGLTKVF 774
Cdd:cd14901 595 PVRFPHDAFVHTYSclAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-776 |
2.43e-153 |
|
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: 488.82 E-value: 2.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLgKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGASQQSNKKKskkdkaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNT- 252
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL---------VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 253 --------GGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFL------------TRPIK------ 306
Cdd:cd14888 151 kskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeendeklakgadAKPISidmssf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 307 ------EYTFVSqAEVTIDGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFK-QRPREEQAELEEGKEG 379
Cdd:cd14888 231 ephlkfRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAVVSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 380 --ELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIG 457
Cdd:cd14888 310 dlEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 458 VLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELI-EKPLGIVSMLDEE 536
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 537 CIVPKASDLTLASKLNDQHLGkHPNFQKPrppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQ 616
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKHKG-HKRFDVV-----KTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK-NP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 617 LMADLWADYatqedvaaaakdgKKAVGKKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANL 696
Cdd:cd14888 542 FISNLFSAY-------------LRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRIS 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 697 VLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYavlaadaakagkdpkdagekiSAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14888 609 VNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDY---------------------RILLNGEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-776 |
2.30e-151 |
|
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: 484.19 E-value: 2.30e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALSQKGYGS-----------GVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAE-VTIDGVDDKEEMLITDEA 333
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNQSDcYTLEGEDEKYEFERLKQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 334 FDIMKFTATEKSELFAITAGIMHMGELKFKQRP--REEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNK 411
Cdd:cd01385 229 MEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLIL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 412 GQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLS---RDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFF 488
Cdd:cd01385 309 PYKLPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLeeaKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 489 NHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKPrp 567
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH-KDNKYYEKP-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 568 pkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKG-----------------NQLMADLWADYATQED 630
Cdd:cd01385 465 ---QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFRAMAAFREA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 631 VAAAAKDGKKAVGKKKGKSASF----------MTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQ 700
Cdd:cd01385 542 GRRRAQRTAGHSLTLHDRTTKSllhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQ 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 701 LTCNGVLEGIRICRKGFPNRMPFLDFKQRYavlaadaakAGKDPKDAG---EKISAALIKDgSLKQEEFQCGLTKVFFK 776
Cdd:cd01385 622 LRYTGMLETVRIRRSGYSVRYTFQEFITQF---------QVLLPKGLIsskEDIKDFLEKL-NLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-776 |
4.25e-149 |
|
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: 476.96 E-value: 4.25e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGAsqqsnkkkskkdkaqvSLED----QIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 249
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG----------------GLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 250 FNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVkgLREKLFL-TRPIKEYTFVSQAEVtIDGVDDKEEML 328
Cdd:cd14903 145 FDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPD--VEERLFLdSANECAYTGANKTIK-IEGMSDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 329 ITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQ--AELEEGKEGELACKLYCVESEKFINALLKPRVKVGT 406
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEksAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 407 EWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDfFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQ 486
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMAN-HIGVLDIFGFEHFKHNSFEQFCINYANEKLQQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 487 FFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPR 566
Cdd:cd14903 381 KFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 567 PPKgkqaeAHLAIVHYAGTVRYNVKGWLEKNKDP-LNDTAVTVLKANKgnQLMADLWADYATQEDVAAAAKDGKKAVGKK 645
Cdd:cd14903 460 TSR-----TQFTIKHYAGPVTYESLGFLEKHKDAlLPDLSDLMRGSSK--PFLRMLFKEKVESPAAASTSLARGARRRRG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 646 KGKSASfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLD 725
Cdd:cd14903 533 GALTTT--TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEE 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 17561652 726 FKQRYAVLAADAAKAGKDPKDAGEkisaALIKDGSLKQ-EEFQCGLTKVFFK 776
Cdd:cd14903 611 FLDKFWLFLPEGRNTDVPVAERCE----ALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-776 |
2.32e-147 |
|
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: 470.99 E-value: 2.32e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR------------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSdavkGLRE-------KLFLTRP---IKEYTFVSQAEVTIDGVDDKE 325
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYA----GLAEdkklakyKLPENKPpryLQNDGLTVQDIVNNSGNREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 326 EMLitDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEG----KEGELACKLYCVESEKFINALLKPR 401
Cdd:cd01379 226 EEI--EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSRisnpEALNNVAKLLGIEADELQEALTSHS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 402 VKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRD--FFIGVLDIAGFEIFDLNSFEQLWINF 479
Cdd:cd01379 304 VVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDepLSIGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 480 VNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFG-----LDLqacieLIEKPLGIVSMLDEECIVPKASDLTLASKLNDQ 554
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 555 HlgKHPNFQKPrppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMAdlwadyatqedvaaa 634
Cdd:cd01379 459 I--KSKYYWRP-----KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSE-NPLVR--------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 635 akdgkkavgkkkgksasfMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICR 714
Cdd:cd01379 516 ------------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRR 577
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 715 KGFPNRMPFLDFKQRYAVLAADAAKAGKDPKDAGEKIsaaLIKdgsLKQEEFQCGLTKVFFK 776
Cdd:cd01379 578 QGFSHRILFADFLKRYYFLAFKWNEEVVANRENCRLI---LER---LKLDNWALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-776 |
1.30e-145 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 466.47 E-value: 1.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKR-RNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGASQQSnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS------------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 GKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPikEYTFVSQAEVTIDGV-DDKEEM----L 328
Cdd:cd14897 149 GQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDP--DCHRILRDDNRNRPVfNDSEELeyyrQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 329 ITDEAFDIMK---FTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVG 405
Cdd:cd14897 227 MFHDLTNIMKligFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 406 TEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL----DAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVN 481
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 482 EKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLASKLNDqHLGKHP 560
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 561 NFQkprPPKGKQAEahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKaNKGNQLMADLWADYatqedvaaaakdgkk 640
Cdd:cd14897 465 RYV---ASPGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLL-NSNNEFISDLFTSY--------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 641 avgkkkgksasfmtvsmmYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNR 720
Cdd:cd14897 524 ------------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 721 MPFLDFKQRYavlaaDAAKAGKDPKDAGEKISAALIKDgSLKQEEFQCGLTKVFFK 776
Cdd:cd14897 586 IKYEDFVKRY-----KEICDFSNKVRSDDLGKCQKILK-TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-776 |
2.48e-145 |
|
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: 466.54 E-value: 2.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVgasqqsnkkkskKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNtGG 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV------------NQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd01387 148 VIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELFAITAGIMHMGELKFKQRPRE---EQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNK 411
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 412 GQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDA--QDLSRdffIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFN 489
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSgtQDTLS---IAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 490 HHMFVLEQEEYKREGIQWEFIDFgLDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKPRPP 568
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 569 kgkqaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDvaaaakdgkkaVGKKKGK 648
Cdd:cd01387 463 -----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSR-TRVVAHLFSSHRAQTD-----------KAPPRLG 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 649 SASFM-------TVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRM 721
Cdd:cd01387 526 KGRFVtmkprtpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 722 PFLDFKQRYavlAADAAKAGKDPKDAGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd01387 606 PFQVFIDRY---RCLVALKLPRPAPGDMCVSLLSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-730 |
5.45e-140 |
|
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: 450.53 E-value: 5.45e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYL-----------GKRRNEMPPHLFAVSDEAYRNM-- 161
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLlsfearssstrNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 162 --TNDRENQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSleDQIVQTNPVLEAFGNAKTVRNNNS 239
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIA--AKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 240 SRFGKFIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKlfltrpikeytfvsqaevtid 319
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR--------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 320 gvDDKEEMLitdEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEG-------KEGELACKLYCVESEK 392
Cdd:cd14900 219 --DMYRRVM---DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSdlapssiWSRDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 393 FINALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDF----FIGVLDIAGFEIFD 468
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHgglhFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 469 LNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELI-EKPLGIVSMLDEECIVPKASDLTL 547
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 548 ASKLNdQHLGKHPNFQKPRPPKGKqaeAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKankgnqlmadlwadYAT 627
Cdd:cd14900 453 ASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV--------------YGL 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 628 QedvaaaakdgkkavgkkkgksasfmtvsmmYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVL 707
Cdd:cd14900 515 Q------------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVM 564
|
650 660
....*....|....*....|...
gi 17561652 708 EGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14900 565 EAVRVARAGFPIRLLHDEFVARY 587
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-730 |
8.28e-134 |
|
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: 434.84 E-value: 8.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRN--------EMPPHLFAVSDEAYRNMTNDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 166 ENQSMLITGESGAGKTENTK-------KVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKyamkfltQLSQQEQNSEEVLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 239 SSRFGKFIRIHFN-TGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKE--YTFVSQAE 315
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGdrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 316 -VTIDGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQR--PREEQAELEEGKEGELACKLYCVESEK 392
Cdd:cd14907 241 cYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 393 FINALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFF-------IGVLDIAGFE 465
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQLfqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 466 IFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEF--IDFgLDLQACIELIEK-PLGIVSMLDEECIVPKA 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 543 SDLTLASKLNDQHlGKHPNFQKPRppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLkANKGNQLMADLW 622
Cdd:cd14907 480 TDEKLLNKIKKQH-KNNSKLIFPN----KINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCI-QNSKNRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 623 ADyatqedvaaAAKDGKKAVGKKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLT 702
Cdd:cd14907 554 SG---------EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIR 624
|
650 660
....*....|....*....|....*...
gi 17561652 703 CNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14907 625 YLGVLESIRVRKQGYPYRKSYEDFYKQY 652
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-776 |
2.71e-127 |
|
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: 415.84 E-value: 2.71e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 97 VLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNM----TNDRENQSMLI 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 173 TGESGAGKTENTKKVISYFamvgasqqsnkkkSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNT 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQI-------------MELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 253 GgKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSqaevtiDGVDDKEEM----L 328
Cdd:cd14889 150 G-HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDP-GKYRYLN------NGAGCKREVqywkK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 329 ITDE---AFDIMKFTATEKSELFAITAGIMHMGELKFKqrPREEQAELEEGKEG---ELACKLYCVESEKFINALLKPRV 402
Cdd:cd14889 222 KYDEvcnAMDMVGFTEQEEVDMFTILAGILSLGNITFE--MDDDEALKVENDSNgwlKAAAGQFGVSEEDLLKTLTCTVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 403 KVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQ-DLSRDFF-IGVLDIAGFEIFDLNSFEQLWINFV 480
Cdd:cd14889 300 FTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKdDSSVELReIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 481 NEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIEL-IEKPLGIVSMLDEECIVPKASDLTLASKLNdQHLGKH 559
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLN-IHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 560 PNFQKPRPPKGKqaeahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTvLKANKGNQLMADLWADYATQEDVaAAAKDGK 639
Cdd:cd14889 458 SYYGKSRSKSPK-----FTVNHYAGKVTYNASGFLEKNRDTIPASIRT-LFINSATPLLSVLFTATRSRTGT-LMPRAKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 640 KAVGKKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPN 719
Cdd:cd14889 531 PQAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSW 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 720 RMPFLDFKQRYavlaadaAKAGKDPKDAGEKISA-ALIKDGSLKqeEFQCGLTKVFFK 776
Cdd:cd14889 611 RPSFAEFAERY-------KILLCEPALPGTKQSClRILKATKLV--GWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-776 |
3.41e-127 |
|
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: 415.21 E-value: 3.41e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYS--MMIYTYSGLFCVVINPYKRLPiysESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRE---NQS 169
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 170 MLITGESGAGKTENTKKVISYFAMVGA------SQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVggkkasGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 244 KFIRIHFNTGG-KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQ-AEVTIDGV 321
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSP-EDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 322 DDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREE----QAELEEGKEGELACKLYCVESEKFINAL 397
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 398 LKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDaQDLSRDFFIGVLDIAGFEIFDL-NSFEQLW 476
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG-HDPDPLPYIGVLDIFGFESFETkNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 477 INFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLASKLNDQH 555
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 556 lGKHPNFQKPRPpkgKQAEAHLAIVHYAGTVRYNVKGWLEKNkdplNDTavtvlkankgnqLMADLwadyatqedvaaaa 635
Cdd:cd14891 475 -KRHPCFPRPHP---KDMREMFIVKHYAGTVSYTIGSFIDKN----NDI------------IPEDF-------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 636 kdgkkavgkkkgksASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRK 715
Cdd:cd14891 521 --------------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKV 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 716 GFPNRMPFLDFKQRYAVLAADAAKAGKDPKDAgeKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14891 587 GLPTRVTYAELVDVYKPVLPPSVTRLFAENDR--TLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-730 |
5.76e-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: 407.37 E-value: 5.76e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYS----ESVCQMYLGKRRNEMP-----PHLFAVSDEAYRNMTND- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGkeilESYRQEGLLRSQGIESpqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 165 RENQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAqVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 244
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGK-LSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 245 FIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPI-------KEYTFVSQAEV- 316
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGItgglqlpNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 317 TIDGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGE---LACKLYCVESEKF 393
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 394 INALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAqDLSRDF--FIGVLDIAGFEIFDLNS 471
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINW-ENDKDIrsSVGVLDIFGFECFAHNS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 472 FEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVP-KASDLTLAS 549
Cdd:cd14908 399 FEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYAS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 550 KLNDQHLGK----HPNFQKPRPPKGKQAEAHLAIVHYAGTVRYNVK-GWLEKNKDPLNDTAvtvlkankgnqlmadlwad 624
Cdd:cd14908 478 RLYETYLPEknqtHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVEtTFCEKNKDEIPLTA------------------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 625 yatqedvaaaakdgkkavgkkkgksASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCN 704
Cdd:cd14908 539 -------------------------DSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYG 593
|
650 660
....*....|....*....|....*.
gi 17561652 705 GVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14908 594 GVLEAVRVARSGYPVRLPHKDFFKRY 619
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-730 |
2.23e-122 |
|
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: 403.89 E-value: 2.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMY--------LGKRRNEMPPHLFAVSDEAYRNM-TND 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLlKPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 165 RENQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDkaqVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 244
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDA---VEIGKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 245 FIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTR-----PIKEYtFVSQAEVTID 319
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKggkyeLLNSY-GPSFARKRAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 320 GVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEG---ELACKLYCVESEKFINA 396
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 397 LLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFF--------IGVLDIAGFEIFD 468
Cdd:cd14902 317 LSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISdedeelatIGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 469 LNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVPKASDLTL 547
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQAL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 548 ASKLNDQHLGkhpnfqkprppkgkqaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQLMADLWADyat 627
Cdd:cd14902 476 STKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADE--- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 628 QEDVAAAAKDGKKAVGKKKGKSASfmtVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVL 707
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660
....*....|....*....|...
gi 17561652 708 EGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-776 |
6.08e-121 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 399.71 E-value: 6.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPiysesvcQMY-LGKRRNEMP------PHLFAVSDEAYRNM------- 161
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYdLHKYREEMPgwtalpPHVFSIAEGAYRSLrrrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 162 TNDRENQSMLITGESGAGKTENTKKVISYFAMVGasqQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSR 241
Cdd:cd14895 75 GASKKNQTILVSGESGAGKTETTKFIMNYLAESS---KHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 242 FGKFIRIHF-----NTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFL-TRPIKEYTFVS--Q 313
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLeLLSAQEFQYISggQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 314 AEVTIDGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGEL------------ 381
Cdd:cd14895 232 CYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASAPCrlasaspssltv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 382 ------ACKLYCVESEKFINALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL---------- 445
Cdd:cd14895 312 qqhldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 446 DAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGLDlQACIELIE- 524
Cdd:cd14895 392 KAANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEq 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 525 KPLGIVSMLDEECIVPKASDLTLASKLNdQHLGKHPNFQKPRPpkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDT 604
Cdd:cd14895 471 RPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASRT---DQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 605 AVTVLkANKGNQLMADLWADYATQEDvaaAAKDGKKAVGKKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPN 684
Cdd:cd14895 547 LFSVL-GKTSDAHLRELFEFFKASES---AELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 685 ELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAADAAKAGKdpkDAGEKISAalikdgsLKQE 764
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDA---TASALIET-------LKVD 692
|
730
....*....|..
gi 17561652 765 EFQCGLTKVFFK 776
Cdd:cd14895 693 HAELGKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-776 |
3.30e-119 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 392.61 E-value: 3.30e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASqqsnkkkskkdkaqvSLEDQIVQTN---PVLEAFGNAKTVRNNNSSRFGKFIRIHFN 251
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQD---------------QTEDRLRQPEdvlPILESFGHAKTILNANASRFGQVLRLHLQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 252 TgGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAEV-TIDGVDDKEEMLIT 330
Cdd:cd14896 146 H-GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGP-ETYYYLNQGGAcRLQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 331 DEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPRE--EQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEW 408
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 409 VNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLD-AQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQF 487
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLApPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 488 FNHHMFVLEQEEYKREGIQWEFIDfGLDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLASKLNDQHlGKHPNFQKPR 566
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 567 PPKgkqaeAHLAIVHYAGTVRYNVKGWLEKNKDPLnDTAVTVLKANKGNQLMADLWADYATQEDVAAAAKdgkkavgkkk 646
Cdd:cd14896 462 LPL-----PVFTVRHYAGTVTYQVHKFLNRNRDQL-DPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 647 gksasfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDF 726
Cdd:cd14896 526 -------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17561652 727 KQRYAVLAADAAKAGKDPKDAGEKISAALIKDGSLkqeeFQCGLTKVFFK 776
Cdd:cd14896 599 LARFGALGSERQEALSDRERCGAILSQVLGAESPL----YHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
27-829 |
5.20e-119 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 397.86 E-value: 5.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 27 FDSKKN------VWV-------ADPEEGFIAAEI-KSSKGDTVVVVTS---KGVEKTIKKDDAQQMNPP-KYEKTEDMAN 88
Cdd:PTZ00014 24 FDKSGNvlkgfyVWTdkapavkEDPDLMFAKCLVlPGSTGEKLTLKQIdppTNSTFEVKPEHAFNANSQiDPMTYGDIGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 89 LTFLNDASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYL-GKRRNEMPPHLFAVSDEAYRNMTNDREN 167
Cdd:PTZ00014 104 LPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 168 QSMLITGESGAGKTENTKKVISYFAmvgasqqsnkkKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 247
Cdd:PTZ00014 184 QTIIVSGESGAGKTEATKQIMRYFA-----------SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 248 IHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDDKEEM 327
Cdd:PTZ00014 253 LQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 328 LITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQA-----ELEEGKEGELACKLYCVESEKFINALLKPRV 402
Cdd:PTZ00014 332 EEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTdaaaiSDESLEVFNEACELLFLDYESLKKELTVKVT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 403 KVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNE 482
Cdd:PTZ00014 412 YAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPG-GFKVFIGMLDIFGFEVFKNNSLEQLFINITNE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 483 KLQQFFNHHMFVLEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQhLGKHPNF 562
Cdd:PTZ00014 491 MLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKY 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 563 QKPRppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWadyatqEDVAAAAKDGkkav 642
Cdd:PTZ00014 570 KPAK----VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASP-NPLVRDLF------EGVEVEKGKL---- 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 643 gkkkgksASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMP 722
Cdd:PTZ00014 635 -------AKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 723 FLDFKQRYA-VLAADAAKAGKDPKDAGEKisaaLIKDGSLKQEEFQCGLTKVFFKAGVLAHLEELRDEALgkimAKFQCA 801
Cdd:PTZ00014 708 FAEFLSQFKyLDLAVSNDSSLDPKEKAEK----LLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKL----AAWEPL 779
|
810 820 830
....*....|....*....|....*....|..
gi 17561652 802 CR---HYLAQCEYKRKLDQKVGLIV-LQRNIR 829
Cdd:PTZ00014 780 VSvleALILKIKKKRKVRKNIKSLVrIQAHLR 811
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-776 |
7.54e-119 |
|
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: 391.61 E-value: 7.54e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLIT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAMVGASQQSnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKD------------KTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 GKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTrPIKEYTFV--SQAEVTIDGVDDKEEMLITD 331
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLD-PNCQYQYLgdSLAQMQIPGLDDAKLFASTQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 332 EAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPrEEQAELEEGKEGELACKLYCVESEKFINALL-------KPRVKV 404
Cdd:cd14904 228 KSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCnrsvvtrNESVTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 405 GTEWVNKGQNLDqvnwavgALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKL 484
Cdd:cd14904 307 PLAPVEAEENRD-------ALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 485 QQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKL--NDQHLGKHPNF 562
Cdd:cd14904 380 QQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIrtNHQTKKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 563 QKPrppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPL-NDTAVTVLKANKgnQLMADLWadyatqEDVAAAAKDGKKA 641
Cdd:cd14904 459 DFP-----KVKRTQFIINHYAGPVTYETVGFMEKHRDTLqNDLLDLVLLSSL--DLLTELF------GSSEAPSETKEGK 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 642 VGKKKGKSASFMTvsmMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRM 721
Cdd:cd14904 526 SGKGTKAPKSLGS---QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRL 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 722 PFLDFKQRYAVLAADAAKAgkdpKDAGEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14904 603 TPKELATRYAIMFPPSMHS----KDVRRTCSVFMTAIGRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-776 |
7.39e-118 |
|
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: 388.58 E-value: 7.39e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYlgkrRN-----EMPPHLFAVSDEAYRNMTNDRENQS 169
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKY----RDapdltKLPPHVFYTARRALENLHGVNKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 170 MLITGESGAGKTENTKKVISYFAmvgasqqsnkkKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 249
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFA-----------SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 250 FNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDDKEEMLI 329
Cdd:cd14876 146 VASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHL-LGLKEYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 330 TDEAFDIMKFTATEKSELFAITAGIMHMGELKF--KQRPREEQA---ELEEGKEGELACKLYCVESEKFINALLKPRVKV 404
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAaaiSNESLEVFKEACSLLFLDPEALKRELTVKVTKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 405 GTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKL 484
Cdd:cd14876 305 GGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPG-GFKNFMGMLDIFGFEVFKNNSLEQLFINITNEML 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 485 QQFFNHHMFVLEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQhLGKHPNFQk 564
Cdd:cd14876 384 QKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFK- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 565 prPPKGKQaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQedvaaaakdgkkavgk 644
Cdd:cd14876 462 --PAKVDS-NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQAST-NPVVKALFEGVVVE---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 645 kKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFL 724
Cdd:cd14876 522 -KGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFE 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 17561652 725 DF-KQRYAVLAADAAKAGKDPKDAGEKisaaLIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14876 601 EFlYQFKFLDLGIANDKSLDPKVAALK----LLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-774 |
6.95e-114 |
|
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: 377.65 E-value: 6.95e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRR-NEMPPHLFAVSDEAYRNMTNDRE--NQSM 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 171 LITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF 250
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER----IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 251 NTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPiKEYTFVSQAEVTIDGvDDKEemlIT 330
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEG-AAFSWLPNPERNLEE-DCFE---VT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 331 DEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAeleegkegelaCKL--YCVESEKFINALLK-------PR 401
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQP-----------CQPmdDTKESVRTSALLLKlpedhllET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 402 VKVGTEWVNKGQNL-------DQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQ 474
Cdd:cd14880 301 LQIRTIRAGKQQQVfkkpcsrAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 475 LWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLND 553
Cdd:cd14880 381 LCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 554 QHLGKHPNFQKPRPPKgkqaEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQLMADLWAD--YATQEDV 631
Cdd:cd14880 460 SALAGNPCLGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANpeEKTQEEP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 632 AAAAKdgkkavgkkkgksASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIR 711
Cdd:cd14880 536 SGQSR-------------APVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIH 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 712 ICRKGFPNRMPFLDFKQRYAVLAADAAKAGKDPKDAGEKisaalikdgSLKQEEFQCGLTKVF 774
Cdd:cd14880 603 ISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGPHSPYPA---------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-730 |
1.84e-108 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 363.92 E-value: 1.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRN-EMPPHLFAVSDEAYRNMTNDRENQSMLI 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 173 TGESGAGKTENTKKVISYfaMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF-N 251
Cdd:cd14906 81 SGESGSGKTEASKTILQY--LINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 252 TGGKVAGADIEHYLLEKSRvIKQAPGER--SYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVSQAEVTIDGV-------- 321
Cdd:cd14906 159 SDGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnkn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 322 -------DDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQ---RPREEQAELEEGKEGELACKLYCVESE 391
Cdd:cd14906 238 snhnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdsdFSKYAYQKDKVTASLESVSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 392 KFINALLKPRVKVGTEWVNKGQNLD--QVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDF----------FIGVL 459
Cdd:cd14906 318 VFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLaggsnkknnlFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 460 DIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELIE-KPLGIVSMLDEECI 538
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 539 VPKASDLTLASKLNDQHlgkhpnFQKPRPPKGKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNdTAVTVLKANKGNQLM 618
Cdd:cd14906 477 MPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLY-SDVEDLLLASSNFLK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 619 ADLWADYATqedvaaaakdgkkAVGKKKGKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVL 698
Cdd:cd14906 550 KSLFQQQIT-------------STTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670
....*....|....*....|....*....|..
gi 17561652 699 NQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRY 648
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-730 |
3.25e-104 |
|
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: 351.71 E-value: 3.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMY-------LGKR---RNEMPPHLFAVSDEAYRNMTN 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRvtsTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 164 DRENQSMLITGESGAGKTENTKKVISYFAMVGA-----SQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 239 SSRFGKFIRIHF-NTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSD----AVKGLREKLFLTRPIKEYTFVSQ 313
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 314 AEVTI--DGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRP--REEQAELEEGKEG---------- 379
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 380 ELACKLYCVESEKFINALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL--------DAQDLS 451
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwGADESD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 452 RDF------FIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE- 524
Cdd:cd14899 401 VDDeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 525 KPLGIVSMLDEECIVPKASDLTLASK--LNDQHLGKHPNFqkpRPPKGKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLN 602
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKyyLEFEKKNSHPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 603 DTAVTVLkANKGNQLMADLWADYATQEDVAAAAKDGKKAVGKKKGKSA-SFMTVSMMYRESLNKLMHMLHQTHPHFIRCI 681
Cdd:cd14899 557 ESAAQLL-AGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAiAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17561652 682 IPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-726 |
2.92e-102 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 344.10 E-value: 2.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRY------YSMMiytysGLFCVVINPYKRLPIYSESVCQMYLGKRRNEM-PPHLFAVSDEAYRNM-TNDRE 166
Cdd:cd14875 1 ATLLHCIKERFeklhqqYSLM-----GEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 167 NQSMLITGESGAGKTENTKKVISYfamVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 246
Cdd:cd14875 76 NQSVVISGESGSGKTENAKMLIAY---LGQLSYMHSSNTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 247 RIHFN-TGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEY-------TFVSQAevtI 318
Cdd:cd14875 153 KLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG---V 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 319 DG--VDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQrPREEQAELEEGKEGELACKLYCVESEKFINA 396
Cdd:cd14875 230 DGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLREC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 397 LLkprVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQ-DLSRDFFIGVLDIAGFEIFDLNSFEQL 475
Cdd:cd14875 309 FL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQgDCSGCKYIGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 476 WINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIE-KPLGIVSMLDEECIVPKASDLTLASKLNDQ 554
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 555 HLGKHPNFQKPRPPKGKQaeahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLkANKGNQLMADLWADYATQEDVAAa 634
Cdd:cd14875 465 WANKSPYFVLPKSTIPNQ----FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECV-SNSTDEFIRTLLSTEKGLARRKQ- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 635 akdgkkavgkkkgksasfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICR 714
Cdd:cd14875 539 -------------------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650
....*....|..
gi 17561652 715 KGFPNRMPFLDF 726
Cdd:cd14875 600 QGYPVRRPIEQF 611
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-776 |
4.73e-98 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 331.47 E-value: 4.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRN-----EMPPHLFAVSDEAYRNMTNDRENQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 169 SMLITGESGAGKTENTKKVISYFAMVGASQQSnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST------------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 249 HFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIysdaVKGL---REKLFLTRPIKEYTFVSQAEV-TIDGVDDK 324
Cdd:cd14886 149 LVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQC----IKGLspeEKKSLGFKSLESYNFLNASKCyDAPGIDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 325 EEMLITDEAFDIMkFTATEKSELFAITAGIMHMGELKFKQRPR---EEQAELEEGKEGELACKLYCVESEKFINALLKPR 401
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 402 VKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDfFIGVLDIAGFEIFDLNSFEQLWINFVN 481
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARP-WIGILDIYGFEFFERNTYEQLLINYAN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 482 EKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGlDLQACIELIEKP-LGIVSMLDEECIVPKASDLTLASKLNdqhlgKHP 560
Cdd:cd14886 383 ERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSCK-----SKI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 561 NFQKPRPPKGKQAEahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDvaaaakdgkk 640
Cdd:cd14886 457 KNNSFIPGKGSQCN--FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGST-NPIVNKAFSDIPNEDG---------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 641 avgkkkGKSASFmtVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNR 720
Cdd:cd14886 524 ------NMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYN 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 721 MPFLDFKQRYAVLAADAAKAGKDPKDAGEKISAALIKDGsLKQEEFQCGLTKVFFK 776
Cdd:cd14886 596 DTFEEFFHRNKILISHNSSSQNAGEDLVEAVKSILENLG-IPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-776 |
4.49e-90 |
|
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: 308.67 E-value: 4.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYL---GKRRNEMPPHLFAVSDEAYRNMTNDRENQSML 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 172 ITGESGAGKTENTKKVISYFAmvgasqqsnkkkSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFN 251
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 252 TGGK-VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRpIKEYTFVSQAE----VTIDGVDDKEE 326
Cdd:cd14878 149 ERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNN-LCAHRYLNQTMredvSTAERSLNREK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 327 MLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGT 406
Cdd:cd14878 228 LAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 407 EWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQD---LSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEK 483
Cdd:cd14878 308 DMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDeqkSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 484 LQQFFNHHMFVLEQEEYKREGIQWEFIdFGLDLQACIE--LIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKHPN 561
Cdd:cd14878 388 MHHYINEVLFLQEQTECVQEGVTMETA-YSPGNQTGVLdfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 562 FQKPRPPKG------KQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWadyatqedvaaaa 635
Cdd:cd14878 467 AVYSPMKDGngnvalKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSE-NVVINHLF------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 636 kdgkkavgkkkgkSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRK 715
Cdd:cd14878 533 -------------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 716 GFPNRMPFLDFKQRYAVLAADAAKAGKDpKDAGEKISAALIKdgsLKQEEFQCGLTKVFFK 776
Cdd:cd14878 600 GYPVRLSFSDFLSRYKPLADTLLGEKKK-QSAEERCRLVLQQ---CKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-730 |
2.62e-86 |
|
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: 294.88 E-value: 2.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRlpIYSESVCQMYLgKRRNEMPPHLFAVSDEAYRNMTNdRENQSMLITGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQsnkkkskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNtgGK 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYsdAVKGLReklfLTRPIKEYTFVSQAEVTIDGVDDKEEMLITD-EAF 334
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFC--ASKRLN----IKNDFIDTSSTAGNKESIVQLSEKYKMTCSAmKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATEKSELfaitaGIMHMGELKFKQrprEEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWVNKGQN 414
Cdd:cd14898 217 GIANFKSIEDCLL-----GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 415 LDQVNWAVGALAKALFARMFSWLIRRCNKTLDAqdlSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFV 494
Cdd:cd14898 289 LKQARTIRNSMARLLYSNVFNYITASINNCLEG---SGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 495 LEQEEYKREGIQWEFIDFgLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKhpnfqkprppKGKQAE 574
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGF----------INTKAR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 575 AHLAIVHYAGTVRYNVKGWLEKNKDplndtavtvlkanKGNQLM--ADLWADYATQEDVAAaakdgkkavgkkkgksasf 652
Cdd:cd14898 435 DKIKVSHYAGDVEYDLRDFLDKNRE-------------KGQLLIfkNLLINDEGSKEDLVK------------------- 482
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 653 mtvsmMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRY 730
Cdd:cd14898 483 -----YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERY 555
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-776 |
2.42e-82 |
|
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: 286.90 E-value: 2.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGAsqqsnkkkskKDKAQVSLEdQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAG----------SVGGVLSVE-KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTF----VSQAEvtiDGVDDKEEMLIT 330
Cdd:cd01386 150 QLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFgivpLQKPE---DKQKAAAAFSKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 331 DEAFDIMKFTATEKSELFAITAGIMHMG--------ELKFKQRPREEQAeleegkegELACKLYCVESEKFINALLKPRV 402
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGaagatkaaSAGRKQFARPEWA--------QRAAYLLGCTLEELSSAIFKHHL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 403 K---------VGTEWVNKGQNLDQVNWAVGAL---AKALFARMFSWLIRRCNKTLDAQDLSRDfFIGVLDIAGFEifdlN 470
Cdd:cd01386 299 SggpqqsttsSGQESPARSSSGGPKLTGVEALegfAAGLYSELFAAVVSLINRSLSSSHHSTS-SITIVDTPGFQ----N 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 471 ----------SFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGLDLQACIELIEKPL------------- 527
Cdd:cd01386 374 pahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrded 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 528 --GIVSMLDEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKQAEaHLAIVHYAGT--VRYNVKGWLEKNK-DPLN 602
Cdd:cd01386 454 rrGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEGPL-QFVLGHLLGTnpVEYDVSGWLKAAKeNPSA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 603 DTAVTVLKANKgNQLMAdlwadyatqedvaaaakdgkkavgkkKGKSASFMTVSMmyreSLNKLMHMLHQTHPHFIRCII 682
Cdd:cd01386 533 QNATQLLQESQ-KETAA--------------------------VKRKSPCLQIKF----QVDALIDTLRRTGLHFVHCLL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 683 PN------ELKKAG------MIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAADAAKAGKDP------ 744
Cdd:cd01386 582 PQhnagkdERSTSSpaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNsevade 661
|
730 740 750
....*....|....*....|....*....|..
gi 17561652 745 KDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd01386 662 RKAVEELLEEL----DLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-776 |
2.11e-80 |
|
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: 282.31 E-value: 2.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSM--------MIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrnCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 167 NQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKskkdkaqvSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQ--------GLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 247 RIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFltrPIKEYTFVSQAEVTIdgvddkee 326
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS---AGEGDPESTDLRRIT-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 327 mlitdEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYCVE----------------- 389
Cdd:cd14887 222 -----AAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADrshssevkclssglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 390 ----------------------SEKFINALLKPRVKVgtewVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL-- 445
Cdd:cd14887 297 easrkhlktvarllglppgvegEEMLRLALVSRSVRE----TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqr 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 446 -----------DAQDLSRDFFIGVLDIAGFEIF---DLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFI- 510
Cdd:cd14887 373 sakpsesdsdeDTPSTTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDc 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 511 -DFGLDLQACIELIEKPLGIVSML------DEECIVPKASDLTLASKLNDQHLGKHPNFQ-------------------- 563
Cdd:cd14887 453 sAFPFSFPLASTLTSSPSSTSPFSptpsfrSSSAFATSPSLPSSLSSLSSSLSSSPPVWEgrdnsdlfyeklnkniinsa 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 564 --KPRPPKGKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKAnkgnqlmadlwADYATQEDVAAAAKDGKKA 641
Cdd:cd14887 533 kyKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----------CSTYTRLVGSKKNSGVRAI 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 642 VGKKKGKSASFmtvsmmyRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRM 721
Cdd:cd14887 602 SSRRSTLSAQF-------ASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRL 674
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 722 PFLDFKQRYAVLAADAAKAGKDPKDAGEKISAALikdgSLKQEEFQCGLTKVFFK 776
Cdd:cd14887 675 PYVELWRRYETKLPMALREALTPKMFCKIVLMFL----EINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-712 |
4.65e-80 |
|
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: 278.82 E-value: 4.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLpiysESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFaMVGASQQSNkkkskkdkaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14937 77 ESGSGKTEASKLVIKYY-LSGVKEDNE------------ISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKlFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDEAF 334
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNK-YKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 335 DIMKFTATeKSELFAITAGIMHMGELKFKQ-----RPREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGTEWV 409
Cdd:cd14937 223 DKMNMHDM-KDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 410 NKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDaQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFN 489
Cdd:cd14937 302 EIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 490 HHMFVLEQEEYKREGIQWEFIDFGLDlQACIELIEKPLGIVSMLDEECIVPKASDLTLASKLNDQhLGKHPNFQKPRppk 569
Cdd:cd14937 381 YIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNK-FSKHEKYASTK--- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 570 gKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQEDVAAAAkdgkkavgkkkgks 649
Cdd:cd14937 456 -KDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSN-NKLVRSLYEDVEVSESLGRKN-------------- 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 650 asfmTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRI 712
Cdd:cd14937 520 ----LITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI 578
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-722 |
2.22e-78 |
|
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: 275.25 E-value: 2.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYLGKRRNE-------MPPHLFAVSDEAYRNMTNDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 167 NQSMLITGESGAGKTENTKKVISYFAMVgasqqsnkkksKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 246
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 247 RIHFNT---------GGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQ-IYSDAVKGLREKLfLTRPIKEYTFVSQAE- 315
Cdd:cd14884 150 LLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQvLRGLSDEDLARRN-LVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 316 -----------VTIDGVDDKEEMLITDE--------AFDIMKFTATEKSELFAITAGIMHMGELKFKqrpreeqaeleeg 376
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEknfvallhGLHYIKYDERQINEFFDIIAGILHLGNRAYK------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 377 kegeLACKLYCVESEKFINALLKPRVKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDF-- 454
Cdd:cd14884 296 ----AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESdn 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 455 ---------FIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQW--EFIDFGLDLQACIELI 523
Cdd:cd14884 372 ediysineaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 524 EKPLGIVSMLdEECIVPKASDLTLASKLND----QHLGKH------PNFQKPRPPKGKQAEAHLAIVHYAGTVRYNVKGW 593
Cdd:cd14884 452 FRRLDDITKL-KNQGQKKTDDHFFRYLLNNerqqQLEGKVsygfvlNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 594 LEKNKDPLNDTAVTVLKANKGNQLmadlwadyatqedvaaaakdgkkAVGKKKGKSASFMTVSMMYRESLNKLMHMLHQT 673
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFL-----------------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQST 587
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 17561652 674 HPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMP 722
Cdd:cd14884 588 DMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-775 |
1.99e-76 |
|
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: 268.26 E-value: 1.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 92 LNDASVLHNLRQRYYSMMIYTY---SGLfcVVINPYKRLPIYS-------ESVCQMYLGKRRNEMPPHLFAVSDEAYRNM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSdaslgeyGSEYYDTTSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 162 TNDRENQSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKkskkdkaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSR 241
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTK----------LSSQISAAEFVLDSFGNAKTLTNPNASR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 242 FGKFIRIHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLTRPIKEYTFVS------QAE 315
Cdd:cd14879 149 FGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASygchplPLG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 316 VtidGVDDKEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRP--REEQAELEEGKEGELACKLYCVESEKF 393
Cdd:cd14879 229 P---GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 394 INALlkpRVK---VGTEWVN-----KG--QNLDQvnwavgaLAKALFARMFSWLIRRCNKTLDAQDLSRDFFIGVLDIAG 463
Cdd:cd14879 306 ETSL---TYKtklVRKELCTvfldpEGaaAQRDE-------LARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 464 FEIFD---LNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFgLDLQACIELI-EKPLGIVSMLDEEC-I 538
Cdd:cd14879 376 FQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 539 VPKASDLTLASKLnDQHLGKHPNFQKPRPPKGKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKAnkgnqlm 618
Cdd:cd14879 455 MPKKTDEQMLEAL-RKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRG------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 619 adlwadyATQEdvaaaakdgkkavgkkkgksasfmtvsmmyRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVL 698
Cdd:cd14879 527 -------ATQL------------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVK 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 699 NQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYavlaadaakAGKDPKDAGEKISAALIKDGSLKQEEFQCGLTKVFF 775
Cdd:cd14879 570 AQIRSLGLPELAARLRVEYVVSLEHAEFCERY---------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-775 |
2.70e-63 |
|
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: 231.78 E-value: 2.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 98 LHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRR----------NEMPPHLFAVSDEAYRNMTNDREN 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 168 QSMLITGESGAGKTENTKKVISYFAMVGASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 248 IHFNTGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVK--GLREKLFLTRPIKEYTFVSQAE-----VTIDG 320
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNKCVNEFVMLKQADplatnFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 321 VDDKEEMlitdEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRP---REEQAELEEGKEGELACKLYCVESEKFINAL 397
Cdd:cd14893 244 RDYRDLM----SSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPeggKSVGGANSTTVSDAQSCALKDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 398 L--KPRV------------KVGTEWVN--KGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTL----DAQDLSRDFF-- 455
Cdd:cd14893 320 LevEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIns 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 456 --IGVLDIAGFEIFD--LNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWE-------FIDFGLDLQACIELIE 524
Cdd:cd14893 400 qgVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLFE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 525 -KPLGIVSMLDEECIVPKASDLTLASKL---NDQHLG-KHPN----FQKPRPPKGKQAEAHLAIVHYAGTVRYNVKGWLE 595
Cdd:cd14893 480 dKPFGIFDLLTENCKVRLPNDEDFVNKLfsgNEAVGGlSRPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 596 KNKDPLNDTAVTVLKANKGNQLMADLWADYA----------TQEDVAAAAKDGKKAVGKKKGKSASFMTVSMMYRESlNK 665
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAVGAAQMAaassekaakqTEERGSTSSKFRKSASSARESKNITDSAATDVYNQA-DA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 666 LMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQRYAVLAADaakagkdpK 745
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH--------R 710
|
730 740 750
....*....|....*....|....*....|
gi 17561652 746 DAGEKISAALIKDGSLKQEEFQCGLTKVFF 775
Cdd:cd14893 711 GTLESLLRSLSAIGVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-776 |
3.42e-62 |
|
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: 225.91 E-value: 3.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 95 ASVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYlgkrrnemppHLFAVSDEAYRNMTNDRENQSMLI-T 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 174 GESGAGKTENTKKVISYFAmvgasqqsnkkkSKKDKAQVSLEDQIVQTnpVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT------------SQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 254 gKVAGADIEHYL-LEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKlFLTRPIKEYTFVSQAEVTIDGVDDKEEMLITDE 332
Cdd:cd14874 137 -VLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAK-FGIKGLQKFFYINQGNSTENIQSDVNHFKHLED 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 333 AFDIMKFTATEKSELFAITAGIMHMGELKFKQR--PREEQAELEEGKEGELACKLYC--VESEKFINALLkPRVKVGTEw 408
Cdd:cd14874 215 ALHVLGFSDDHCISIYKIISTILHIGNIYFRTKrnPNVEQDVVEIGNMSEVKWVAFLleVDFDQLVNFLL-PKSEDGTT- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 409 VNKGQNLDQVNwavgALAKALFARMFSWLIRRCNktLDAQDLSRDFFIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFF 488
Cdd:cd14874 293 IDLNAALDNRD----SFAMLIYEELFKWVLNRIG--LHLKCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 489 NHHMFVLEQEEYKREGIQWEF-IDFGLDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLASKLNDQHLGKhPNFQKPR 566
Cdd:cd14874 367 VKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR-SSYGKAR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 567 ppkgKQAEAHLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKgNQLMADLWADYATQedvaaaakdgkkavgkkk 646
Cdd:cd14874 446 ----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSK-NPIIGLLFESYSSN------------------ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 647 gKSASFMTVSMMYRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDF 726
Cdd:cd14874 503 -TSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17561652 727 KQRYAVLAADAAKAGKDPKdagEKISAALIKDGSLKQEEFQCGLTKVFFK 776
Cdd:cd14874 582 ARQYRCLLPGDIAMCQNEK---EIIQDILQGQGVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
94-730 |
6.45e-61 |
|
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: 221.91 E-value: 6.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 94 DAsVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPiysesvCQMYLGKRRNEMP-PHLFAVSDEAYRNMTNDRENQSMLI 172
Cdd:cd14881 1 DA-VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRSSPLaPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 173 TGESGAGKTENTKKVI-SYFAMVGASQQSNKKKskkdkaqvsledQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFn 251
Cdd:cd14881 74 SGTSGSGKTYASMLLLrQLFDVAGGGPETDAFK------------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 252 TGGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLT-RPIKEYTFVSQAevtidgvDDKEemlit 330
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgYSPANLRYLSHG-------DTRQ----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 331 DEAFDIMKFTATEKS---------ELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELAcKLYCVESEKFINALLKPR 401
Cdd:cd14881 209 NEAEDAARFQAWKAClgilgipflDVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVA-ALLGVSGAALFRGLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 402 VKVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCN--KTLDAQDLSR--DFFIGVLDIAGFEIFDLNSFEQLWI 477
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHatDGFIGILDMFGFEDPKPSQLEHLCI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 478 NFVNEKLQQFFNHHMFVLEQEEYKREGIQWEF-IDFgLDLQACIELIEK-PLGIVSMLDEECiVPKASDLTLASKLNDQH 555
Cdd:cd14881 368 NLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVEC-SPRGTAESYVAKIKVQH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 556 LGkHPNFQKPRPPKGKQaeahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQLMADLWADYATQedvaaaa 635
Cdd:cd14881 446 RQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFATHTQDFHTR------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 636 kdgkkavgkkkgksasfmtvsmmyresLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRK 715
Cdd:cd14881 514 ---------------------------LDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAG 566
|
650
....*....|....*
gi 17561652 716 GFPNRMPFLDFKQRY 730
Cdd:cd14881 567 GYPHRMRFKAFNARY 581
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-601 |
3.94e-60 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 220.73 E-value: 3.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLP-IYSESVCQMYlgKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFAMVGASQQSNkkkskkdkaqvsLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGG 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSKY------------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 255 KVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIysdaVKGLREK---LFLTRPIKEYTFVSQ-AEVTIDGVDDKEEMLIT 330
Cdd:cd14905 148 EIQGAKLYSYFLDENRVTYQNKGERNFHIFYQF----LKGITDEekaAYQLGDINSYHYLNQgGSISVESIDDNRVFDRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 331 DEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPREEQAELEEGKEGELACKLYcvESEKFINALLKPRVKVGTEWVn 410
Cdd:cd14905 224 KMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIESLSHNITF--DSTKLENILISDRSMPVNEAV- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 411 kgQNLDqvnwavgALAKALFARMFSWLIRRCNKTLDAQDLSRDffIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNH 490
Cdd:cd14905 301 --ENRD-------SLARSLYSALFHWIIDFLNSKLKPTQYSHT--LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 491 HMFVLEQEEYKREGIQWEFIDFGLDLQACIELIEKplgIVSMLDEECIVPKASDLTLASKLNDqHLGKHPNFQKpRPPKg 570
Cdd:cd14905 370 TVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFGK-KPNK- 443
|
490 500 510
....*....|....*....|....*....|.
gi 17561652 571 kqaeahLAIVHYAGTVRYNVKGWLEKNKDPL 601
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEI 468
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
5.77e-53 |
|
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: 183.70 E-value: 5.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 117 FCVVINPYKRLPIYSESVC-QMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGESGAGKTENTKKVISYFAMV- 194
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVa 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 195 --GASQQSNKKKSKKDKAQVSLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 248
Cdd:cd01363 81 fnGINKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-776 |
5.91e-49 |
|
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: 186.48 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRRNEMPPHLFAVSDEAYRNMTNDRENQSMLITGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 176 SGAGKTENTKKVISYFAMVGASQQSNKKkskkdkaqvsledQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTGGK 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG-------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 256 VAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYS--DAVKGLRE-------KLFLTRPIKEYTFVSQAEVTIDGVDDKEE 326
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEynlkagrNYRYLRIPPEVPPSKLKYRRDDPEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 327 MLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQrpREEQAELEEGKEGELACKLYCVESEKFINALLKPRVKVGT 406
Cdd:cd14882 229 YKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 407 EWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLdaqDLSRDFF-----IGVLDIAGFEIFDLNSFEQLWINFVN 481
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM---SFPRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 482 EKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGLDLQACIELIEKPLGIVSMLDEECIVPKASDLTLASklndqhlgkhpn 561
Cdd:cd14882 384 EQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIMDR------------ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 562 FQKPRPPKGKQAEAH-LAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQLMAdLWADYATQEdvaaaakdgkk 640
Cdd:cd14882 452 IKEKHSQFVKKHSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKL-MFTNSQVRN----------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 641 avgkkkgksasFMTVSMMYRESLNKLMHMLHQTH----PHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLEGIRICRKG 716
Cdd:cd14882 520 -----------MRTLAATFRATSLELLKMLSIGAnsggTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKG 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 717 FPNRMPFLDFKQRYAVLAADAAKAGKDPKDAGEKIsaaLIKdgsLKQEEFQCGLTKVFFK 776
Cdd:cd14882 589 FSYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLL---LIR---LKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-728 |
4.42e-43 |
|
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: 170.02 E-value: 4.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 96 SVLHNLRQRYYSMMIYTYSGLFCVVINPYKRLPIYSESVCQMYLGKRR-NEMPPHLFAVSDEAYRNMTNDRENQSMLITG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 175 ESGAGKTENTKKVISYFA--MVGASQQSNKKKSKKDKAQVSLEDQIVQ---------TNPVLEAFGNAKTVRNNNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqVKGSRRLPTNLNDQEEDNIHNEENTDYQfnmsemlkhVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 244 KFIRIHFNTgGKVAGADIEHYLLEKSRVIKQAPGERSYHIFYQIYSDAVKGLREKLFLtRPIKEYTFVSQAEVTIDGVDD 323
Cdd:cd14938 162 KFCTIHIEN-EEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL-KNIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 324 KEEMLITDEAFDIMKFTATEKSELFAITAGIMHMGELKFKQRPR---------------------------EEQAELEEG 376
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRkksllmgknqcgqninyetilselensEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 377 KEGELACKLYCVESEKFINALLKPRVkVGTEWVNKGQNLDQVNWAVGALAKALFARMFSWLIRRCNKTLDAQDLSRDF-- 454
Cdd:cd14938 320 KNLLLACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 455 FIGVLDIAGFEIFDLNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYKREGIQWEFIDFGLD-LQACIELIEKPLGIVSML 533
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 534 DEECIVPKASDLTLASKLNDQHLGKHPNFQKPRPPKGKQAEahLAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANk 613
Cdd:cd14938 479 LENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT--FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 614 GNQLMADLWADYATQ------EDVAAAAKDGKKAVGKKKGKSASFMTVSMMyRESLNKLMHMLHQTHPHFIRCIIPNELK 687
Cdd:cd14938 556 ENEYMRQFCMFYNYDnsgnivEEKRRYSIQSALKLFKRRYDTKNQMAVSLL-RNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17561652 688 KA-GMIDANLVLNQLTCNGVLEGIRICRKGFPNRMPFLDFKQ 728
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS 676
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
853-1544 |
7.88e-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: 126.71 E-value: 7.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEV 1012
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 NRKLLEDIQAEEDK-----VNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEEL----NRHK 1083
Cdd:TIGR02168 423 IEELLKKLEEAELKelqaeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerlqENLE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1084 HEQEQV--IKKKDIELSSIQSRL--------EDEQSLVAKLQRQIKELLAR--------IQELEE---------ELDAER 1136
Cdd:TIGR02168 503 GFSEGVkaLLKNQSGLSGILGVLselisvdeGYEAAIEAALGGRLQAVVVEnlnaakkaIAFLKQnelgrvtflPLDSIK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1137 NSRSKAEKARNEMQME--------LEELGDRLDEAGG--------------ATQAQIELNKK------------------ 1176
Cdd:TIGR02168 583 GTEIQGNDREILKNIEgflgvakdLVKFDPKLRKALSyllggvlvvddldnALELAKKLRPGyrivtldgdlvrpggvit 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1177 ------------REAELAKLRQDLEDAainsETSMAALRKkhndAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQS 1244
Cdd:TIGR02168 663 ggsaktnssileRRREIEELEEKIEEL----EEKIAELEK----ALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1245 ADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEE 1324
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1325 LKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEeLEETRRKLT 1404
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLR 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1405 HKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLekkqkgFDKVLDEWRRKCEALVAEVEQSQRET 1484
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL------QERLSEEYSLTLEEAEALENKIEDDE 967
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1485 RAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQlgeggksVHDLQKMRRRLE 1544
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQ-------KEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1663 |
1.76e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.55 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 862 LEKKFKVLEEEKTQEERKRkdmEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEE 941
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYK---ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 942 KNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQ 1021
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1022 AEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSiq 1101
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1102 SRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLD---------EAGGATQAQIE 1172
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslerlqenlEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 LNKKR----------------------EAELAKLRQDLEDAAINSETSMAALRKKHND---AVAELSDQLDT-IQKMRGK 1226
Cdd:TIGR02168 513 KNQSGlsgilgvlselisvdegyeaaiEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvTFLPLDSIKGTeIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1227 LEREKNDKQREVDELQQSAD-------------VEAKQRQNCERMAKQLEAQLTDMTLKsDEQARLIQELTMGKNKVHNE 1293
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPklrkalsyllggvLVVDDLDNALELAKKLRPGYRIVTLD-GDLVRPGGVITGGSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1294 NQDLNRQLEDAEAqlcalnrikqqqhsQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSK 1373
Cdd:TIGR02168 672 ILERRREIEELEE--------------KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1374 ANSEIQQWrakfegegvsraeelEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLE 1453
Cdd:TIGR02168 738 LEAEVEQL---------------EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1454 KKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSV 1533
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1534 HDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQ----- 1608
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEalenk 962
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1609 -VSLETESRGRAELLKTKKKLEGDVNELEIA--------LDHSNKLNVDGQKSMKKLQDTIREL 1663
Cdd:TIGR02168 963 iEDDEEEARRRLKRLENKIKELGPVNLAAIEeyeelkerYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1031-1837 |
3.80e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.93 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1031 NKTKAKLEST---LDELEDTLEREKRGRQDCEKQRRKVEgelkIAQELIEELNRHKHEqeqvIKKKDIElsSIQSRLEDE 1107
Cdd:TIGR02168 175 KETERKLERTrenLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELA----LLVLRLE--ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1108 QSLVAKLQRQIKELLARIQELEEELDAernsrskAEKARNEMQMELEELGDRLDEAggatqaQIELNKKrEAELAKLRQD 1187
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKELYAL------ANEISRL-EQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1188 LEDAAINSEtsmaalrkkhndavaELSDQLDTIQKMRGKLEREKNDKQREVDELQqsadveaKQRQNCERMAKQLEAQLT 1267
Cdd:TIGR02168 311 LANLERQLE---------------ELEAQLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1268 DMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQslhsqvsnyQ 1347
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL---------Q 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1348 LECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFegegVSRAEELEETRRKLtHKVQEMQEQLENANQKIGTLEKN 1427
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQAL----DAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKN 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1428 KQRLAHDL----------------------EDAQ----VDADRANSIASSLEKKQKGFDK--VLDEWR-RKCEALVAEVE 1478
Cdd:TIGR02168 515 QSGLSGILgvlselisvdegyeaaieaalgGRLQavvvENLNAAKKAIAFLKQNELGRVTflPLDSIKgTEIQGNDREIL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1479 QSQRETRAAA---------------------------TETFRLRNQLEE--------------SGEQT-EAVKRENKALA 1516
Cdd:TIGR02168 595 KNIEGFLGVAkdlvkfdpklrkalsyllggvlvvddlDNALELAKKLRPgyrivtldgdlvrpGGVITgGSAKTNSSILE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1517 --QELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKE-EEF 1593
Cdd:TIGR02168 675 rrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqLSK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1594 ENTRKNHSRTIESMQvsLETESRGRAELLKTKKKLEGDVNELEIALDhSNKLNVDGQKsmKKLQDTIRELQYQVEEEQRS 1673
Cdd:TIGR02168 755 ELTELEAEIEELEER--LEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELR--AELTLLNEEAANLRERLESL 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1674 LSESRDhanlAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSnslllatKRKVEGDLQLLQSEIEE 1753
Cdd:TIGR02168 830 ERRIAA----TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE-------RASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1754 AMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKGGKRQLAKLDMRIHELE 1833
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....
gi 17561652 1834 TELE 1837
Cdd:TIGR02168 979 NKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
968-1765 |
1.01e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 968 ETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDT 1047
Cdd:TIGR02168 210 EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1048 LEREKRGRQDCEKQ-------RRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKE 1120
Cdd:TIGR02168 290 LYALANEISRLEQQkqilrerLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1121 LLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMA 1200
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1201 ALRKKHNDAVAElsdQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCE---RMAKQLEAQLTDMT------- 1270
Cdd:TIGR02168 450 EELQEELERLEE---ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQSGLSgilgvls 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1271 --LKSDEQARL---------IQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQhsqleelkrtLDQETRERQSL 1339
Cdd:TIGR02168 527 elISVDEGYEAaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE----------IQGNDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1340 HSQVSNYQLECEQFRESLE-------------EEQDAKTDVQRQLSKANSEI----QQWRAKF-----EGEGVSRAEELE 1397
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGYRIVtldgDLVRPGGvitggSAKTNSSILERR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1398 ETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRansiassLEKKQKGFDKVLDEWRRKCEALVAEV 1477
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-------LSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1478 EQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLgeggksvhdlqkmrrrleiekEELQQALDEA 1557
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL---------------------KALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1558 ECALEAEEAKVMRAQIEVSQIRSEI---EKRLQEKEEEFENTRKNHSR---TIESMQVSLETESRGRAELLKTKKKLEGD 1631
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIaatERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEA 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1632 VNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESR-DHANLAERRSQVLQQEKEDLAIIYEQSERTRR 1710
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1711 QAELELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAmSDAKTSDEKA 1765
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDL-TEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1122-1930 |
9.03e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.69 E-value: 9.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1122 LARIQELEEELDAERNS----RSKAEKARnEMQMELEEL-----GDRLDEAggatQAQIELNKKREAELAKLRQDLEDAA 1192
Cdd:TIGR02168 188 LDRLEDILNELERQLKSlerqAEKAERYK-ELKAELRELelallVLRLEEL----REELEELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1193 INSETSMAALRKKHNdavaELSDQLDTIQKMRGKLEREKNDKQREVDELQQSadveakqRQNCERMAKQLEAQLTDMTLK 1272
Cdd:TIGR02168 263 QELEEKLEELRLEVS----ELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1273 SDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQ 1352
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1353 FRESLEEEQDAKTDVQRQLSKANSEIQQwrakfegegvSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLA 1432
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQ----------AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1433 HDLEDAQVDADRANSIASSLEKKQKGFDKVLD--EWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESgEQTEAVKR 1510
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLKnqSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV-ENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1511 ENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKV--MRAQIEVSQ-IRSEIEKRLQ 1587
Cdd:TIGR02168 561 AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyLLGGVLVVDdLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1588 EKEEEFENTRKNH------SRTIESMQVSLETESRGR--AELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDT 1659
Cdd:TIGR02168 641 LRPGYRIVTLDGDlvrpggVITGGSAKTNSSILERRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1660 IRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSnsnslllATKRK 1739
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-------AQIEQ 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1740 VEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKgGK 1819
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1820 RQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQI-EDAESL 1898
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLT 952
|
810 820 830
....*....|....*....|....*....|..
gi 17561652 1899 ASGNLAKYRQLQHVVEDAQERADAAENALQKL 1930
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
999-1636 |
3.73e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 999 ISKLnKEKKHQ-----EEVNRKL--LEDIQAE-EDKVNHLNKTKAKLES--TLDELEDTLEREKRGRQDcekqrRKVEGE 1068
Cdd:COG1196 167 ISKY-KERKEEaerklEATEENLerLEDILGElERQLEPLERQAEKAERyrELKEELKELEAELLLLKL-----RELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1069 LKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNE 1148
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1149 MQMELEELGDRLDEAggatQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKmrgkLE 1228
Cdd:COG1196 321 LEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE----AL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1229 REKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQL 1308
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1309 calnrikQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQdaktdvQRQLSKANSEIQQWRAKFEGE 1388
Cdd:COG1196 473 -------ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG------LRGLAGAVAVLIGVEAAYEAA 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 GVSRAEELEetrrklthkVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDkVLDEWRR 1468
Cdd:COG1196 540 LEAALAAAL---------QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-LVASDLR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1469 KCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKE 1548
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1549 ELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSR---TIESMQVSLETESRGRAELLKTK 1625
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEeeeLLEEEALEELPEPPDLEELEREL 769
|
650
....*....|.
gi 17561652 1626 KKLEGDVNELE 1636
Cdd:COG1196 770 ERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
860-1416 |
5.80e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 5.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 860 EALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDE 939
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 940 EEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLED 1019
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1020 IQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSS 1099
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1100 IQSRLEDEQSLVAKLQRQIKELLARIQELEE-ELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIElnkkrE 1178
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-----A 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1179 AELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSdqldtIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERM 1258
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP-----LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1259 AKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQS 1338
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1339 LHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEG---EGVSRAEELEETRRKLTHKVQEMQEQLE 1415
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElleEEALEELPEPPDLEELERELERLEREIE 777
|
.
gi 17561652 1416 N 1416
Cdd:COG1196 778 A 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1049-1813 |
2.22e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 108.62 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1049 EREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIelssiQSRLED-EQSLVAK----LQRQIKELLA 1123
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAL-----LKEKREyEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1124 RIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELN-KKREAELAKLRQDLEDAAINSETSMAAL 1202
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1203 RKkhndAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMA----------KQLEAQLTDMTLK 1272
Cdd:TIGR02169 325 AK----LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetrdelKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1273 SDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNrikqqqhSQLEELKRTLDQETRERQSLHSQVSNYQLECEQ 1352
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE-------EEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1353 FRESLEEEQDAKTDVQRQLSKANSEIQQWRAKfEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNkqRLA 1432
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN--RLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1433 HDLEDAQVDADRA-----------------NSIASS-------LEKKQKGFDKVLDEWRRKCEALVAEVEQS-------- 1480
Cdd:TIGR02169 551 NVVVEDDAVAKEAiellkrrkagratflplNKMRDErrdlsilSEDGVIGFAVDLVEFDPKYEPAFKYVFGDtlvvedie 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1481 ----------------------------QRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKS 1532
Cdd:TIGR02169 631 aarrlmgkyrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1533 VHDLQKMRRRLEIEKEELQQALDEaecaleaeeakvmraqieVSQIRSEIEKRLQEKEEEFENtrknhsrtIESMQVSLE 1612
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEK------------------LKERLEELEEDLSSLEQEIEN--------VKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1613 TEsrgRAELLKTKKKLEGDVNELEIALDHSNKLNVdgQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQ 1692
Cdd:TIGR02169 765 AR---IEELEEDLHKLEEALNDLEARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1693 QEKEDLAIiyEQSERTRRQAEL---------ELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDE 1763
Cdd:TIGR02169 840 EQRIDLKE--QIKSIEKEIENLngkkeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 17561652 1764 KAKKAIMDASKLADELrSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAA 1813
Cdd:TIGR02169 918 RLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1295-1933 |
3.39e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1295 QDLNRQLEDAEAQLCALNriKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKA 1374
Cdd:TIGR02168 216 KELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1375 NSEIqqwrAKFEgegvSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEK 1454
Cdd:TIGR02168 294 ANEI----SRLE----QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1455 KQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQEL-----KDIADQLGEG 1529
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1530 GKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEeakvmRAQIEVSQIRSEIEKRLQEKEEEFENTRKN---------- 1599
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAA-----ERELAQLQARLDSLERLQENLEGFSEGVKAllknqsglsg 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1600 -HSRTIESMQV------SLETESRGRAELLKT-------------KKKLEGDVNELEIALDHSNKLNVDGQ--------- 1650
Cdd:TIGR02168 521 iLGVLSELISVdegyeaAIEAALGGRLQAVVVenlnaakkaiaflKQNELGRVTFLPLDSIKGTEIQGNDReilkniegf 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1651 --------KSMKKLQDTIRELQYQV------EEEQRSLSESRDHANL------------------AERRSQVLQQEKE-- 1696
Cdd:TIGR02168 601 lgvakdlvKFDPKLRKALSYLLGGVlvvddlDNALELAKKLRPGYRIvtldgdlvrpggvitggsAKTNSSILERRREie 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1697 DLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLA 1776
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1777 DELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAA------GIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVL 1850
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalreALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1851 RNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDAESLASGNLAKYRQLQHVVEDAQERADAAENALQKL 1930
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
...
gi 17561652 1931 RLK 1933
Cdd:TIGR02168 921 REK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1299-1893 |
8.46e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1299 RQLEDAEAQLCALNRIKQQQHSQLEELKR---------TLDQETRERQSLHsqvsnYQLECEQFRESLEEEQDAKTDVQR 1369
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERqaekaeryrELKEELKELEAEL-----LLLKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1370 QLSKANSEIQQWRAkfegegvsRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIA 1449
Cdd:COG1196 254 ELEELEAELAELEA--------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1450 SSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEG 1529
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1530 GKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQV 1609
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1610 SLETESRGRAeLLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQ 1689
Cdd:COG1196 486 LAEAAARLLL-LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1690 VLQQEKEDLAIIY--EQSERTRRQAELELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDA----KTSDE 1763
Cdd:COG1196 565 YLKAAKAGRATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAlrraVTLAG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1764 KAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKGGKRQLAKLDMRIHELETELEGENRRH 1843
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 17561652 1844 AETQKVLRNKDRKCRELQFQVDEDKKSQERMYDL---IEKLQQKIKTYKRQIE 1893
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEppdLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
939-1479 |
2.03e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 939 EEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLE 1018
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1019 DIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELS 1098
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1099 SIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAggatQAQIELNKKRE 1178
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA----AEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1179 AELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGK----LEREKNDKQR--------------EVDE 1240
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRglagavavligveaAYEA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1241 LQQSADVEAKQRQNCERMAKQLEAQLtdmTLKSDEQARL--IQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQ 1318
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIE---YLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1319 HSQLEELK-RTLDQETRERQSLHSQVSNYQL-ECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEEL 1396
Cdd:COG1196 616 YVLGDTLLgRTLVAARLEAALRRAVTLAGRLrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1397 EETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAE 1476
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
...
gi 17561652 1477 VEQ 1479
Cdd:COG1196 776 IEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1273-1933 |
2.66e-22 |
|
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: 105.14 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1273 SDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQsLHSQVSNYQL---- 1348
Cdd:TIGR02168 153 KPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELallv 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1349 -ECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEgegvsraeELEETRRKLTHKVQEMQEQLENANQKIGTLEKN 1427
Cdd:TIGR02168 232 lRLEELREELEELQEELKEAEEELEELTAELQELEEKLE--------ELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1428 KQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEA 1507
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1508 VKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIR-------- 1579
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElerleeal 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1580 SEIEKRLQEKEEEFENTRKNHSR------TIESMQVSLETESRGRAELLKTKKKLEGDV----------NELEIALD--- 1640
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEaal 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1641 --HSNKLNVDGQKSMKKLQ----------------DTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEK------- 1695
Cdd:TIGR02168 544 ggRLQAVVVENLNAAKKAIaflkqnelgrvtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllg 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1696 -----EDLA---------------------------IIYEQSERTR----------RQAELELAEVKDSVNELSNSNSLL 1733
Cdd:TIGR02168 624 gvlvvDDLDnalelakklrpgyrivtldgdlvrpggVITGGSAKTNssilerrreiEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1734 LATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEA- 1812
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAe 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1813 -----AGIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKT 1887
Cdd:TIGR02168 784 ieeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 17561652 1888 YKRQIEDAESLASGNLAKYRQLQHVVEDAQERADAAENALQKLRLK 1933
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
853-1380 |
4.47e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEV 1012
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 NRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKK 1092
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 KDIELSSIQSRLEDEQSlvAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIE 1172
Cdd:COG1196 503 YEGFLEGVKAALLLAGL--RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 LNKKREAELAKLRQDLEDAAINSETSMAA-LRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQ 1251
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLReADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1252 RQNCERMAKQLEAQLTDMTLKSDEQARLIQEltmgknkvhnENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQ 1331
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEE----------ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 17561652 1332 ETRERQSLHSQVSNYQLECEQFRESLEEEQDAKtDVQRQLSKANSEIQQ 1380
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
875-1596 |
5.19e-22 |
|
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: 104.38 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 875 QEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQManmndqlcDEEEKNAALTKQKKKIE 954
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--------EKAERYQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 955 QdneglkktvSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAE-EDKVNHLNKT 1033
Cdd:TIGR02169 225 G---------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1034 KAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRhkhEQEQVIKKKDielsSIQSRLEDEQSLVAK 1113
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER---EIEEERKRRD----KLTEEYAELKEELED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1114 LQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGD---RLDEAGGATQAQIELNKKREAELAKLRQDLED 1190
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEelqRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1191 AAINSETSMAALRKKHNDAVAELSDQLDTIQKmrgkLEREKNDKQREVDELQQSADV-EAKQRQNC-------------- 1255
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEAEAQARAsEERVRGGRaveevlkasiqgvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1256 ----------ERMAKQLE----AQLTDMTLKSDEQA-RLIQELTMGK---------NKVHNENQDLNRQLEDAEAQLcAL 1311
Cdd:TIGR02169 525 gtvaqlgsvgERYATAIEvaagNRLNNVVVEDDAVAkEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGF-AV 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1312 NRIKQQQH---------------SQLEELKR--------TLDQE-----------TRERQSLHSQVSNYQLECEQFRESL 1357
Cdd:TIGR02169 604 DLVEFDPKyepafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGElfeksgamtggSRAPRGGILFSRSEPAELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1358 EEEQDAKTDVQRQLSKANSEIQQWRAKFE------GEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRL 1431
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSdasrkiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1432 AHDLEDAQVDA-------------------DRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETF 1492
Cdd:TIGR02169 764 EARIEELEEDLhkleealndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1493 RLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECA--LEAEEAKVMR 1570
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQieKKRKRLSELK 923
|
810 820
....*....|....*....|....*..
gi 17561652 1571 AQIEVSQIR-SEIEKRLQEKEEEFENT 1596
Cdd:TIGR02169 924 AKLEALEEElSEIEDPKGEDEEIPEEE 950
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
850-1524 |
1.57e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.91 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 850 IKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDM-EAENAR-LEAEKQALLI-QLEQERDSSAEGEERSAKLLAQKADLE 926
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDArKAEAARkAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 927 KQMANMNDQLCDEEEKNAALTKQKKKIEQDNeglKKTVSDLETTIKKQESEKQAKDHQIRSLqDEIQSQDEVISKLNKEK 1006
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEE---ARKADELKKAEEKKKADEAKKAEEKKKA-DEAKKKAEEAKKADEAK 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1007 KHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQ 1086
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1087 EQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERnsrsKAEKARnemqmELEELGDRLDEAGGA 1166
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK----KAEEAK-----KAEEAKKKAEEAKKA 1472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1167 TQAQIELNKKREAELAKLRQDlEDAAINSETSMAALRKKHNDAV-----AELSDQLDTIQKMRGKLEREKNDKQREVDEL 1241
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAkkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1242 QQSADV-EAKQRQNCERMAKQLEAQltDMTLKSDEQARLIQELTMGKNKVHNENQDLNR--QLEDAEAQLCALNRIKQQQ 1318
Cdd:PTZ00121 1552 KKAEELkKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeEAKKAEEAKIKAEELKKAE 1629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1319 H--SQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQwrAKFEGEGVSRAEEL 1396
Cdd:PTZ00121 1630 EekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA--LKKEAEEAKKAEEL 1707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1397 EETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAE 1476
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 17561652 1477 VEQSQR-ETRAAATETFRLRNQLEESG-EQTEAVKRENKALAQELKDIAD 1524
Cdd:PTZ00121 1788 EDEKRRmEVDKKIKDIFDNFANIIEGGkEGNLVINDSKEMEDSAIKEVAD 1837
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
857-1593 |
3.67e-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: 101.68 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 857 EEFEALEKKFKVLEEEKTQE-ERKRKDMEAENARLEaekqalliqleqerdssAEGEERSAKLLAQKADLEKQMANMNDQ 935
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRlEEIEQLLEELNKKIK-----------------DLGEEEQLRVKEKIGELEAEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 936 LCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKqakdhqiRSLQDEIQSQDEVISKLNKEKKHQEEVNRK 1015
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR-------DKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1016 LLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREkrgrqdcEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDI 1095
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRL-------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1096 ELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLD-------------- 1161
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvge 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1162 --------EAGGATQA-----------QIELNKKREA------ELAKLRQD-------LEDAAINSETSMAALRKKHNDA 1209
Cdd:TIGR02169 536 ryataievAAGNRLNNvvveddavakeAIELLKRRKAgratflPLNKMRDErrdlsilSEDGVIGFAVDLVEFDPKYEPA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1210 VAE------LSDQLDTIQKMRGK-----LEREKNDKQREV----DELQQSADVEAKQRQNCERMAKQLEAqltdmtLKsD 1274
Cdd:TIGR02169 616 FKYvfgdtlVVEDIEAARRLMGKyrmvtLEGELFEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEG------LK-R 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1275 EQARLIQELTMGKNKVH---NENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECE 1351
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1352 QFRESLEEEQDAKTDVQRQLSKanSEIQQWRAKFE------GEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLE 1425
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSkleeevSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1426 KNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQT 1505
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1506 EAVKRENKALAQELKDIADQLGEgGKSVHDLQKMRRRLEIEKEELQ-------QALDEAECALEAEEAKVMRAQIEVSQI 1578
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
810
....*....|....*
gi 17561652 1579 RSEIEKRLQEKEEEF 1593
Cdd:TIGR02169 1006 LERIEEYEKKKREVF 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1140-1905 |
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 17561652 1140 SKAEKARNEmqmeLEELGDRLDEAggatqaQIELNKKREaELAKLRQDLEDAainsETSMAALRKKHNDAVAELSDQLDT 1219
Cdd:TIGR02169 170 RKKEKALEE----LEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1220 IQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTlkSDEQARLiqeltmgknkvhnenqdlNR 1299
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG--EEEQLRV------------------KE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1300 QLEDAEAQLCALNRikqqqhsQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQrqlskanSEIQ 1379
Cdd:TIGR02169 295 KIGELEAEIASLER-------SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1380 QWRAKFEgEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGF 1459
Cdd:TIGR02169 361 ELKEELE-DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1460 DKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRE-NKALAQelKDIADQLGEGGKSVHDLQK 1538
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRElAEAEAQ--ARASEERVRGGRAVEEVLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1539 MRRR--------LEIEKEELQQAL--------------DEAECALEAEEAKVMRA---------QIEVSQIRSEIEKR-- 1585
Cdd:TIGR02169 518 ASIQgvhgtvaqLGSVGERYATAIevaagnrlnnvvveDDAVAKEAIELLKRRKAgratflplnKMRDERRDLSILSEdg 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1586 -------LQEKEEEFENTRKNHSRT---IESMQ-----------VSLETE-----------SRGRAELLKTKKKLEGDVN 1633
Cdd:TIGR02169 598 vigfavdLVEFDPKYEPAFKYVFGDtlvVEDIEaarrlmgkyrmVTLEGElfeksgamtggSRAPRGGILFSRSEPAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1634 ELEIALDhsnklnvDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAE 1713
Cdd:TIGR02169 678 RLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1714 LELAEVKDSVNELsnsnslllatkRKVEGDLQLLQSEIEEAMSD--AKTSDEKAKKAIMDASKLADELRSEQEHASNLNQ 1791
Cdd:TIGR02169 751 QEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1792 SkktlesqVKDLQMRLDEAEAAgIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQ 1871
Cdd:TIGR02169 820 K-------LNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
810 820 830
....*....|....*....|....*....|....
gi 17561652 1872 ERMYDLIEKLQQKIKTYKRQIEDAESLASGNLAK 1905
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1109-1924 |
4.06e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.22 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1109 SLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDeaggatqaqielnkkreaelaKLRQDL 1188
Cdd:TIGR02169 149 SMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE---------------------RLRRER 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1189 EDAainsETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTD 1268
Cdd:TIGR02169 208 EKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1269 MTlkSDEQARliqeltmgknkvhnenqdLNRQLEDAEAQLCALNRikqqqhsQLEELKRTLDQETRERQSLHSQVSNYQL 1348
Cdd:TIGR02169 284 LG--EEEQLR------------------VKEKIGELEAEIASLER-------SIAEKERELEDAEERLAKLEAEIDKLLA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1349 ECEQFRESLEEEQDAKTDVQrqlskanSEIQQWRAKFEgEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNK 1428
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLT-------EEYAELKEELE-DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1429 QRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAV 1508
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1509 KRE-NKALAQelKDIADQLGEGGKSVHDLQKMRRR--------LEIEKEELQQAL--------------DEAECALEAEE 1565
Cdd:TIGR02169 489 QRElAEAEAQ--ARASEERVRGGRAVEEVLKASIQgvhgtvaqLGSVGERYATAIevaagnrlnnvvveDDAVAKEAIEL 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1566 AKVMRA---------QIEVSQIRSEIEKR---------LQEKEEEFENTRKNHSRT---IESMQ-----------VSLET 1613
Cdd:TIGR02169 567 LKRRKAgratflplnKMRDERRDLSILSEdgvigfavdLVEFDPKYEPAFKYVFGDtlvVEDIEaarrlmgkyrmVTLEG 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1614 E-----------SRGRAELLKTKKKLEGDVNELEIALDhsnklnvDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHAN 1682
Cdd:TIGR02169 647 ElfeksgamtggSRAPRGGILFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1683 LAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSLLLATKRKVEGDL-----QLLQSEIEEAMSD 1757
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1758 AKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDE--AEAAGIKGGKR----QLAKLDMRIHE 1831
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEeleeELEELEAALRD 879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1832 LETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDAESLaSGNLAKYRQLQH 1911
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQA 958
|
890
....*....|...
gi 17561652 1912 VVEDAQERADAAE 1924
Cdd:TIGR02169 959 ELQRVEEEIRALE 971
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
966-1583 |
3.30e-19 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 94.98 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 966 DLETTIKKQESEKQAKDH--QIRSLQDEIQSQDEVISKLNKEKKHQE-EVNRKLLEDIQAEedkvnhlnktKAKLESTLD 1042
Cdd:COG4913 243 ALEDAREQIELLEPIRELaeRYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAE----------LARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1043 ELEDTLEREKRGRQDCEKQRRKVEGE-LKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKEL 1121
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1122 LARIQELEEELDAER----NSRSKAEKARNEMQMELEELGDR---LDEAGGATQAQI--ELNKKRE-----AELAKLRQD 1187
Cdd:COG4913 393 LEALEEELEALEEALaeaeAALRDLRRELRELEAEIASLERRksnIPARLLALRDALaeALGLDEAelpfvGELIEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1188 LED--AAINSETSMAALR----KKHNDAVAELSDQLDTIQKMR----------------------GKLEREKNDKQREVD 1239
Cdd:COG4913 473 EERwrGAIERVLGGFALTllvpPEHYAAALRWVNRLHLRGRLVyervrtglpdperprldpdslaGKLDFKPHPFRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1240 -ELQQSAD---VEAKQRQNCERMAKQLEAQLTDM--TLKSDEQARLIQELTMGKNkvhNEnqdlnRQLEDAEAQLCALNR 1313
Cdd:COG4913 553 aELGRRFDyvcVDSPEELRRHPRAITRAGQVKGNgtRHEKDDRRRIRSRYVLGFD---NR-----AKLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1314 IKQQQHSQLEELKRTLDQeTRERQSLHSQVSNYQLEcEQFRESLEEEQDAKTDVQRQLSKANSEIqqwrakfegegvsra 1393
Cdd:COG4913 625 ELAEAEERLEALEAELDA-LQERREALQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDDL--------------- 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1394 EELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQkgfdkvLDEWRR--KCE 1471
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL------LEERFAaaLGD 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1472 ALVAEVEQS-QRETRAAATETFRLRNQLEesgEQTEAVKRENKALAQElkdiadqLGEGGKSVHDLQKMRRRLEIE---- 1546
Cdd:COG4913 762 AVERELRENlEERIDALRARLNRAEEELE---RAMRAFNREWPAETAD-------LDADLESLPEYLALLDRLEEDglpe 831
|
650 660 670
....*....|....*....|....*....|....*...
gi 17561652 1547 -KEELQQALDEAECALEAEEAKVMRAQIEvsQIRSEIE 1583
Cdd:COG4913 832 yEERFKELLNENSIEFVADLLSKLRRAIR--EIKERID 867
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
865-1825 |
8.33e-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: 8.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 865 KFKVLEEEKTQEERKRKDMEAENARLEaEKQALLIQLEQ-------ERDSSAEGEERS-----AKLL----AQKADLEKQ 928
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQ-EIRSILVDFEEasgkkiyEHDSMSTMHFRSlgsaiSKILreldTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 929 MANMNDQLcdEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIkkqeSEKQAKDHQIRSLQDEIQSQDEVIsklNKEKKH 1008
Cdd:pfam15921 240 IFPVEDQL--EALKSESQNKIELLLQQHQDRIEQLISEHEVEI----TGLTEKASSARSQANSIQSQLEII---QEQARN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1009 QEEVNRKLLEDiqaeedkvnhlnktkakLESTLDELEDTLEREKRGRQDcekQRRKVEGELKIAQElieELNRHKHEQEQ 1088
Cdd:pfam15921 311 QNSMYMRQLSD-----------------LESTVSQLRSELREAKRMYED---KIEELEKQLVLANS---ELTEARTERDQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1089 vikkkdieLSSIQSRLEDE-QSLVAKLQRQIKELlariqeleeELDAERNSRSKAEKARNEMQME--LEELGDRLDEAgg 1165
Cdd:pfam15921 368 --------FSQESGNLDDQlQKLLADLHKREKEL---------SLEKEQNKRLWDRDTGNSITIDhlRRELDDRNMEV-- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1166 atqaqielnKKREAELAKLRQDLEDaaiNSETSMAALRKKHN--DAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQ 1243
Cdd:pfam15921 429 ---------QRLEALLKAMKSECQG---QMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1244 SADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQarlIQELTMGKNKvHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLE 1323
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEITKLRSRVDLK---LQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1324 ELKRTLDQETR-------ERQSLHSQVSNYQLECEQFReSLEEEQDAKTdvqRQLSKANSEIQQWRAKFEGEGVSR---A 1393
Cdd:pfam15921 573 NMTQLVGQHGRtagamqvEKAQLEKEINDRRLELQEFK-ILKDKKDAKI---RELEARVSDLELEKVKLVNAGSERlraV 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1394 EELEETRRKLTHKVQEMQEQLENANQKIGTLEKN-----------KQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKV 1462
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseemettTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1463 LDEWRRKCEALVAEVEQSQRETRAaatetfrLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRR 1542
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQF-------LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1543 LEIEKEELQQALDEAECALEAEEAKVMRAQIEvsQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETesrgraell 1622
Cdd:pfam15921 802 LKEKVANMEVALDKASLQFAECQDIIQRQEQE--SVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFT--------- 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1623 KTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEE------------------------QRSLSESR 1678
Cdd:pfam15921 871 RTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEptvqlskaedkgrapslgalddrvRDCIIESS 950
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1679 DHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELE-----LAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEE 1753
Cdd:pfam15921 951 LRSDICHSSSNSLQTEGSKSSETCSREPVLLHAGELEdpsscFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEG 1030
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1754 AMsdAKTSDEKAKKAIMDASKLADE----LRSEQEHASNLNQSKKTLESQVKDLQMRlDEAEAAGIKGGKRQLAKL 1825
Cdd:pfam15921 1031 SI--GSSSQYRSAKTIHSPDSVKDSqslpIETTGKTCRKLQNRLESLQTLVEDLQLK-NQAMSSMIRNQEKRIQKV 1103
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
856-1465 |
2.11e-18 |
|
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: 92.01 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 856 NEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAE---KQALLIQLEQERDSSaegEERSAKLLAQKADLEKQMANM 932
Cdd:TIGR04523 74 NNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEiknDKEQKNKLEVELNKL---EKQKKENKKNIDKFLTEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEV 1012
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 NRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKK 1092
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 K-DIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEEL----GDRLDEAGGAT 1167
Cdd:TIGR04523 311 ElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIKNLE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1168 QAQIELNKKREaELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQkmrgKLEREKNDKQREVDELQQSADV 1247
Cdd:TIGR04523 391 SQINDLESKIQ-NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK----DLTNQDSVKELIIKNLDNTRES 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1248 EAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKR 1327
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1328 TL--DQETRERQSLHSQVSNYQLECEQFRE---SLEEEQDAKTDVQRQLSKANSEIqqwrakfegegVSRAEELEETRRK 1402
Cdd:TIGR04523 546 ELnkDDFELKKENLEKEIDEKNKEIEELKQtqkSLKKKQEEKQELIDQKEKEKKDL-----------IKEIEEKEKKISS 614
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 1403 LTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDE 1465
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
950-1550 |
2.97e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 91.66 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 950 KKKIEQDNEGLKKTvSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEvnrkLLEDIQAEEDKVNH 1029
Cdd:PRK03918 175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1030 LNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEgELKIAQELIEELNRHKHEQEQvikkkdiELSSIQSRLEDEQS 1109
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLD-------ELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1110 LVAKLQRQIKELLARIQELEEeldaernsrskAEKARNEMQMELEELGDRLDEAGGATQAQIELNKkreaeLAKLRQDLE 1189
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEE-----------LKKKLKELEKRLEELEERHELYEEAKAKKEELER-----LKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1190 DAAINSETSMAALRKKhndavaELSDQLDTIQKMRGKLEREKNDKQREVDELQqsadveaKQRQNCERMAKQLEaqltdm 1269
Cdd:PRK03918 386 PEKLEKELEELEKAKE------EIEEEISKITARIGELKKEIKELKKAIEELK-------KAKGKCPVCGRELT------ 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1270 tlkSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQ------HSQLEELKRT-----------LDQE 1332
Cdd:PRK03918 447 ---EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseliklKELAEQLKELeeklkkynleeLEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1333 TRERQSLHSQVSNYQLECEQFRESLEEEQD---AKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQE 1409
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1410 MQEqLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEwrrkcealvAEVEQSQRETRAAAT 1489
Cdd:PRK03918 604 YLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EEYEELREEYLELSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1490 ETFRLRNQLEESGEQTEAVKRENKALAQELKDIAdqlgEGGKSVHDLQKMRRRLEIEKEEL 1550
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEERE----KAKKELEKLEKALERVEELREKV 730
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1720 |
3.91e-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: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 854 KKNEEFEALEKKFKVLEEEKTQEE-RKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDneglkktVSDLETTIKKQESEKQAKDHQirslqdEIQSQDEVISKLNKEKKHQEEV 1012
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQ-------EIEKEEEKLAQVLKENKEEEK------EKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 NRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKK 1092
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 KDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKarnemqmelEELGDRLDEAGGATQAQIE 1172
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE---------EEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 LNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQ--KMRGKLEREKNDKQREVD----------E 1240
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKesKARSGLKVLLALIKDGVGgriisahgrlG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1241 LQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHS 1320
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1321 QLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETR 1400
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1401 RKLTHkvqemQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQS 1480
Cdd:pfam02463 693 EILRR-----QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1481 QRET----RAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDE 1556
Cdd:pfam02463 768 ELSLkekeLAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1557 AECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELE 1636
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1637 IALDHSN----KLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQA 1712
Cdd:pfam02463 928 EILLKYEeepeELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
....*...
gi 17561652 1713 ELELAEVK 1720
Cdd:pfam02463 1008 IRAIIEET 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
851-1455 |
4.27e-18 |
|
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: 91.39 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 851 KGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMA 930
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 931 NMNDQLcdeeeknAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKK--- 1007
Cdd:pfam01576 535 EDAGTL-------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfd 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1008 ------------HQEEVNR-------------KLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQR 1062
Cdd:pfam01576 608 qmlaeekaisarYAEERDRaeaeareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1063 RKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLE-DEQSLVAKLQRQIKELLARIQELEEELDAERNSRSK 1141
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQ 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1142 AEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAInSETSMAALRKKHNDAVAELSDQLDTIQ 1221
Cdd:pfam01576 768 AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA-SRDEILAQSKESEKKLKNLEAELLQLQ 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1222 KMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQL 1301
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1302 EDAEAQLCALNRIKQQQHSQLEELKRTLDQ-ETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQ 1380
Cdd:pfam01576 927 AAERSTSQKSESARQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1381 WRAKFEGEGvSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKK 1455
Cdd:pfam01576 1007 VLLQVEDER-RHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
889-1442 |
5.06e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.87 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 889 RLEAEKQALLIQLEQERDssaegEERSAKLLAQKADLEKQMANMNDQL--CDEEEKNAALTKQK-KKIEQDNEGLKKTVS 965
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIE-----EKEEKDLHERLNGLESELAELDEEIerYEEQREQARETRDEaDEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 966 DLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLnkekkhqEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELE 1045
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1046 DTLEREkrgRQDCEKQRRKVEGELKIAQELiEELNRHKHEQEQVIKKkdiELSSIQSRLEDEQSLVAKLQRQIKELLARI 1125
Cdd:PRK02224 328 DRLEEC---RVAAQAHNEEAESLREDADDL-EERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1126 -------QELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQA--------------QIELNKKREAELAKL 1184
Cdd:PRK02224 401 gdapvdlGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1185 RQDLEDAainsETSMAALRKKHNDAV--AELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQL 1262
Cdd:PRK02224 481 EAELEDL----EEEVEEVEERLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1263 EAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNR------QLEDAEAQLCALNRiKQQQHSQLEELKRTLDQETRER 1336
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLRE-KREALAELNDERRERLAEKRER 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1337 QSlhsqvsnyQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFE------GEGVSRAEELEETRRKLTHkVQEM 1410
Cdd:PRK02224 636 KR--------ELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDdlqaeiGAVENELEELEELRERREA-LENR 706
|
570 580 590
....*....|....*....|....*....|..
gi 17561652 1411 QEQLENANQKIGTLEKNKQRLAHDLEDAQVDA 1442
Cdd:PRK02224 707 VEALEALYDEAEELESMYGDLRAELRQRNVET 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
854-1683 |
6.53e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 854 KKNEEFEALEKKFKVLEE-EKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQD----EVISKLNKEKKH 1008
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaEEAKKDAEEAKK 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1009 QEEVnRKLLEDIQAEEDKVNHLNK----TKAKLESTLDELEDTLEREKRGRQDCEKQRRKVE------GELKIAQELIEE 1078
Cdd:PTZ00121 1245 AEEE-RNNEEIRKFEEARMAHFARrqaaIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkkaEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1079 LNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKAR--NEMQMELEEL 1156
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1157 GDRLDEAGGATQAQIELNK-KREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQlDTIQKMRGKLEREKNDKQ 1235
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK-KAEEAKKADEAKKKAEEA 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1236 REVDELQQSADvEAKQRqnCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIK 1315
Cdd:PTZ00121 1483 KKADEAKKKAE-EAKKK--ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1316 QQQHSQLEELKRtldQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEiqqwraKFEGEGVSRAee 1395
Cdd:PTZ00121 1560 AEEKKKAEEAKK---AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA------KIKAEELKKA-- 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1396 lEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGfdkvlDEWRRKCEALVA 1475
Cdd:PTZ00121 1629 -EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1476 EVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALD 1555
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1556 EAECAleaeeakvmraqiEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNEL 1635
Cdd:PTZ00121 1783 EELDE-------------EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAF 1849
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 17561652 1636 EialDHSNKLNVDGQKSMKKLQDTIRElQYQVEEEQRSLSESRDHANL 1683
Cdd:PTZ00121 1850 E---KHKFNKNNENGEDGNKEADFNKE-KDLKEDDEEEIEEADEIEKI 1893
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
924-1869 |
4.70e-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: 88.10 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 924 DLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDL--------ETTIKKQESEKQAKDHQIRSLQDEIQSQ 995
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLaeliidleELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 996 DEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQEL 1075
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1076 IEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEEldaernsrskAEKARNEMQMELEE 1155
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE----------EEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1156 LGDRLDEAGGATQAQIELNKKREAELAKLRQDledaaINSETSMAALRKKHNDAVAELSDQLDTIQKMrgkLEREKNDKQ 1235
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEE-----EKEAQLLLELARQLEDLLKEEKKEELEILEE---EEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1236 REVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMgknkvhneNQDLNRQLEDAEAQLCALNRIK 1315
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ--------KLEERSQKESKARSGLKVLLAL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1316 QQQHsqleeLKRTLDQETRERQSLHSQVSNYqleceqfresleeEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEE 1395
Cdd:pfam02463 516 IKDG-----VGGRIISAHGRLGDLGVAVENY-------------KVAISTAVIVEVSATADEVEERQKLVRALTELPLGA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1396 LEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVA 1475
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1476 EVEQSQRETRAAAtETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQAld 1555
Cdd:pfam02463 658 LAEKSEVKASLSE-LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-- 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1556 eaecALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNEL 1635
Cdd:pfam02463 735 ----NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1636 EIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELE 1715
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1716 LAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKT 1795
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1796 LESQVKdlqmrldeaeaagikggkrqlaklDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKK 1869
Cdd:pfam02463 971 ELGKVN------------------------LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
926-1522 |
4.99e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.38 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 926 EKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKE 1005
Cdd:TIGR04523 53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1006 KKHQEEVNRKLLEDIQAEED-------KVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIE- 1077
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQk 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1078 ---------ELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNE 1148
Cdd:TIGR04523 213 nkslesqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1149 MQMELEELGDrldeaggatQAQIELNKKREAELAKLRQDLEDaaINSETSmaalrkKHNDAVAELSDQLDTIQKMRGKLE 1228
Cdd:TIGR04523 293 LKSEISDLNN---------QKEQDWNKELKSELKNQEKKLEE--IQNQIS------QNNKIISQLNEQISQLKKELTNSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1229 REKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQL 1308
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1309 CALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQwrakfege 1388
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE-------- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 gvsraeeLEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANsiassLEKKQKGFDKVLDEWRR 1468
Cdd:TIGR04523 508 -------LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQ 575
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1469 KCEALVAEVEQSQRETRAAATETFRLRNQLEESG-------EQTEAVKRENKALAQELKDI 1522
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEkkissleKELEKAKKENEKLSSIIKNI 636
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1083-1869 |
5.40e-17 |
|
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: 87.87 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1083 KHEQEQVIKKKDIELSSIQSRLEDEQSLVAK----LQRQIKELLARIQELEEELDA----ERNSRSKAEKARNEMQMELE 1154
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAmadiRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1155 EL-------GDRLDEAGGATQAQIELNKKREAELAKLRQ---DLEDAA---INSETSMAALR-KKHNDAVAELSDQLDT- 1219
Cdd:pfam15921 153 ELeaakclkEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvDFEEASgkkIYEHDSMSTMHfRSLGSAISKILRELDTe 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1220 IQKMRGKLEREKNDKQREVDELQQSADVEAKQRQN-CERMAKQLEAQLTDMTLKSD---EQARLIQ-ELTMGKNKVHNEN 1294
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASsarSQANSIQsQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1295 QDLNRQLEDAEAQLcalnrikQQQHSQLEELKRTLDQETRErqslhsqvsnyqleceqfresleeeqdaktdVQRQLSKA 1374
Cdd:pfam15921 313 SMYMRQLSDLESTV-------SQLRSELREAKRMYEDKIEE-------------------------------LEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1375 NSEIQQWRakfegegvSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAhdledaqvDADRANSIasslek 1454
Cdd:pfam15921 355 NSELTEAR--------TERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW--------DRDTGNSI------ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1455 kqkgfdkVLDEWRRKCEALVAEVEQSQRETRAAATETfrlRNQLEesgEQTEAVKRENKALaQELKDIADQLgEGGKSVh 1534
Cdd:pfam15921 413 -------TIDHLRRELDDRNMEVQRLEALLKAMKSEC---QGQME---RQMAAIQGKNESL-EKVSSLTAQL-ESTKEM- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1535 dLQKMRRRLEIEK---EELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEefENTRKNHSRTIESMQVSL 1611
Cdd:pfam15921 477 -LRKVVEELTAKKmtlESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH--LKNEGDHLRNVQTECEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1612 ETESRGRAELLKT-KKKLEgdvNELEIALDH---SNKLNVDGQKSMKKLQDTIRELQyqveeEQRSLSESRDhANLAERR 1687
Cdd:pfam15921 554 KLQMAEKDKVIEIlRQQIE---NMTQLVGQHgrtAGAMQVEKAQLEKEINDRRLELQ-----EFKILKDKKD-AKIRELE 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1688 SQVLQQEKEDLAIIYEQSERTRRQAELE------LAEVKDSVNELS--------------NSNSLLLATKRKVEGDLQLL 1747
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVKDIKqerdqlLNEVKTSRNELNslsedyevlkrnfrNKSEEMETTTNKLKMQLKSA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1748 QSEIEEAMSDAKT---SDEKAKKAIMDASK-----------LADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAE-- 1811
Cdd:pfam15921 705 QSELEQTRNTLKSmegSDGHAMKVAMGMQKqitakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAte 784
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1812 ----AAGIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKK 1869
Cdd:pfam15921 785 knkmAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-714 |
4.05e-16 |
|
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: 84.79 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 218 IVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNTG-----GKVAGADIEHYLLEKSRVIKQA------PGERSYHIFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFGlhpweFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 287 IysdaVKGLREKLFLTRPIKEY----------TFVSQAEVTIDGVDDKEEMLITD--------EAFDIMKFTATEKSELF 348
Cdd:cd14894 329 M----VAGVNAFPFMRLLAKELhldgidcsalTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIF 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 349 AITAGIMHMGELKFKQRPREEQAELEEGKEGELACK----LYCVESEKFINALLKPRVKVGTEWVNKGQNLD--QVNWAV 422
Cdd:cd14894 405 KVLSAVLWLGNIELDYREVSGKLVMSSTGALNAPQKvvelLELGSVEKLERMLMTKSVSLQSTSETFEVTLEkgQVNHVR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 423 GALAKALFARMFSWLIRRCNKTLDAQDLSRD----------------FFIGVLDIAGFEIFDLNSFEQLWINFVNEKLqq 486
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNEATKMSALSTDgnkhqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL-- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 487 fFNHHMFVLEQEEYKREGIqwefidFGLDLQACIELI-EKPLGIVSMLDEECIVPKASDLTLA-----SKLNDQHLGKHP 560
Cdd:cd14894 563 -YAREEQVIAVAYSSRPHL------TARDSEKDVLFIyEHPLGVFASLEELTILHQSENMNAQqeekrNKLFVRNIYDRN 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 561 NFQKPRPPKG-KQAEAH---------LAIVHYAGTVRYNVKGWLEKNKDPLNDTAVTVLKANKGNQLMADLwadyatQED 630
Cdd:cd14894 636 SSRLPEPPRVlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML------NES 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 631 VAAAAKDGKKAVGKKKGKSASFMTVSMM--YRESLNKLMHMLHQTHPHFIRCIIPNELKKAGMIDANLVLNQLTCNGVLE 708
Cdd:cd14894 710 SQLGWSPNTNRSMLGSAESRLSGTKSFVgqFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789
|
....*.
gi 17561652 709 GIRICR 714
Cdd:cd14894 790 QMEICR 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
997-1863 |
1.28e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 83.24 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 997 EVISKLNKEKKHQ-EEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELE-------DTLEREKRGRQDCEKQRRKVEGE 1068
Cdd:pfam15921 74 EHIERVLEEYSHQvKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQmerdamaDIRRRESQSQEDLRNQLQNTVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1069 LKIAQELIEELNRHKHEQEQVIKKKDIE----LSSIQSRLEDEQ----------------------SLVAKLQR----QI 1118
Cdd:pfam15921 154 LEAAKCLKEDMLEDSNTQIEQLRKMMLShegvLQEIRSILVDFEeasgkkiyehdsmstmhfrslgSAISKILReldtEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1119 KELLARIQELEEELDAERNsrskaeKARNEMQMELEELGDRLDEAggATQAQIELNKKREaELAKLRQDLEDAAINSETS 1198
Cdd:pfam15921 234 SYLKGRIFPVEDQLEALKS------ESQNKIELLLQQHQDRIEQL--ISEHEVEITGLTE-KASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1199 MAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQqsadveakqrqncermaKQLEAQLTDMTLKSDEQAR 1278
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELE-----------------KQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1279 LIQEltmgKNKVHNENQDLNRQLEDAEAQLcalnRIKQQQHSQL-----------EELKRTLDQETRERQSLHSQVSNYQ 1347
Cdd:pfam15921 368 FSQE----SGNLDDQLQKLLADLHKREKEL----SLEKEQNKRLwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1348 LECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRA---KFEGEGVSRAEELEETRRK---LTHKVQEMQEQLENANQKI 1421
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTvsdLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1422 GTLEKNKQRLAHDLEDAQVDADRANSIAS---SLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQL 1498
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTeceALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1499 EesgeqteavkrENKALAQELKDIADQlgeGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQI 1578
Cdd:pfam15921 600 N-----------DRRLELQEFKILKDK---KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1579 RSEiekrLQEKEEEFENTRKNHSRTIESMQVsleTESRGRAELLKTKKKLEGDVNEL---EIALDHSNKLNVDGQKSMKK 1655
Cdd:pfam15921 666 RNE----LNSLSEDYEVLKRNFRNKSEEMET---TTNKLKMQLKSAQSELEQTRNTLksmEGSDGHAMKVAMGMQKQITA 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1656 LQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKE-----------DLAIIYEQSERTRRQ-AELELAEVKDSV 1723
Cdd:pfam15921 739 KRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvateknkmagELEVLRSQERRLKEKvANMEVALDKASL 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1724 NELSNSNSLLLATKRKVEGDLQlLQSEIEEAMSDAKTSDEKAKKAIMDASKLA---DELRSEQEHASNL-NQSKKT---L 1796
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLKLQ-HTLDVKELQGPGYTSNSSMKPRLLQPASFTrthSNVPSSQSTASFLsHHSRKTnalK 897
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1797 ESQVKDLQMRLDEAEA------------AGIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQ 1863
Cdd:pfam15921 898 EDPTRDLKQLLQELRSvineeptvqlskAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSR 976
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
864-1800 |
1.73e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.17 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 864 KKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKN 943
Cdd:TIGR00606 192 RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 944 AALTKQKKKIEQDNEGLKK--------TVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKH--QEEVN 1013
Cdd:TIGR00606 272 KALKSRKKQMEKDNSELELkmekvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEllVEQGR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1014 RKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKK 1093
Cdd:TIGR00606 352 LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1094 DIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEelgdrldeaggatQAQIEL 1173
Cdd:TIGR00606 432 RDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-------------NSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1174 NKKREAELAKLRQDLEDAAINSETSMAALrkkhNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQsadvEAKQRQ 1253
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQL----NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS----LLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1254 NCERMAKQLEAQLTDMTLKSDEQARL---IQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRiKQQQHSQLEELKRTLD 1330
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDRLAKLnkeLASLEQNKNHINNELESKEEQLSSYEDKLFDVCG-SQDEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1331 QETRERQSLHSQVSNYqlecEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEM 1410
Cdd:TIGR00606 650 KSSKQRAMLAGATAVY----SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1411 QEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWR--RKCEALVAEVEQSQRETR--- 1485
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKdve 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1486 ------AAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAEC 1559
Cdd:TIGR00606 806 rkiaqqAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1560 ALEAEEAKVMRAQ---IEVSQIRSEI-------EKRLQEKEEEFenTRKNHSRTIESMQVSLETESRGRAELLKT---KK 1626
Cdd:TIGR00606 886 FEEQLVELSTEVQsliREIKDAKEQDspletflEKDQQEKEELI--SSKETSNKKAQDKVNDIKEKVKNIHGYMKdieNK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1627 KLEGDVNELEIALDHSNKLNV---DGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYE 1703
Cdd:TIGR00606 964 IQDGKDDYLKQKETELNTVNAqleECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKE 1043
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1704 QSERTRRQAELELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEamSDAKTSDEKAKKAIMdaskladELRSEQ 1783
Cdd:TIGR00606 1044 MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMI-------VMRTTE 1114
|
970
....*....|....*..
gi 17561652 1784 EHASNLNQSKKTLESQV 1800
Cdd:TIGR00606 1115 LVNKDLDIYYKTLDQAI 1131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
851-1245 |
4.15e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.22 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 851 KGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENarLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMA 930
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKN--QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 931 NMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQE 1010
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1011 EVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKqrrkvegELKIAQELIEELNRHKHEQEQVI 1090
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK-------ELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1091 KKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDaernsRSKAEKARNEMQMELEELGDRLDEAGGATQAQ 1170
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1171 IELNKKREAELAKLRQDLEdaainsetsmaalrkKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSA 1245
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIE---------------EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1218-1973 |
8.00e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1218 DTIQKMRGKLEREKNDKQREVDElqQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDL 1297
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1298 NRQLEDA---EAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYqlECEQFRESLEEEQDAKTDVQrQLSKA 1374
Cdd:PTZ00121 1169 ARKAEDAkkaEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA--EDAKKAEAVKKAEEAKKDAE-EAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1375 NSEiqqwRAKFEGEGVSRAEELEETRRKLTHKVQEMQ--EQLENANQKIGTLEKNKQRLAHDLEDAQVDADRAnsiassl 1452
Cdd:PTZ00121 1246 EEE----RNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA------- 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1453 eKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKR---ENKALAQELKDIADQLgeg 1529
Cdd:PTZ00121 1315 -KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKKAEEK--- 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1530 gKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQV 1609
Cdd:PTZ00121 1391 -KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1610 SLETESRGRAELLKTKKKLEGDVNELEIALDHSNKlnvdgQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQ 1689
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1690 VlqqekedlaiiyEQSERTRRQAELELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAM----SDAKTSDEKA 1765
Cdd:PTZ00121 1545 K------------KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyeEEKKMKAEEA 1612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1766 KKAiMDASKLADELRSEQEHASNLNQSKKTLESQVKDL-QMRLDEAEAAGIKGGKRQLAKLDMRIHELETELEGENRRHA 1844
Cdd:PTZ00121 1613 KKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1845 ETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDAESLA------SGNLAKYRQLQHVVEDAQE 1918
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeakkdEEEKKKIAHLKKEEEKKAE 1771
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1919 RADAAENALQKLRLKGRSTSGVFGPRGLAHSMSTTGVNMRRGGSRGAFLDEDFAE 1973
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
890-1591 |
9.22e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.40 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 890 LEAEKQALLIQLEQERDSSAEGEersAKLLAQKADLEKQMANmnDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLET 969
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGK---AELLTLRSQLLTLCTP--CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 970 TIKKQE--SEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRklledIQAEEDKVNHLNKTKAKLESTLDELEDT 1047
Cdd:TIGR00618 248 KREAQEeqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP-----LAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1048 LEREKRGRQDCEKQRRKVEGELKIAQELI--EELNRHKHEQEQVIK----KKDIELSSIQSRLEDEQSLVAKLQ--RQIK 1119
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqEIHIRDAHEVATSIReiscQQHTLTQHIHTLQQQKTTLTQKLQslCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1120 ELLARIQELEEELDAERNSRsKAEKARNEMQMELEELGDRLDEAGGATQAQIElnKKREAELAKLRQDLEDaainsetsm 1199
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQCE--KLEKIHLQESAQSLKE--------- 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1200 aalRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVD--------ELQQSADVEAKQRQNC--ERMAKQLEAQLTDM 1269
Cdd:TIGR00618 471 ---REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCgscihpnpARQDIDNPGPLTRRMQrgEQTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1270 TLKSDEQARLIQELtmgKNKVHNENQDL-------NRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQ 1342
Cdd:TIGR00618 548 YHQLTSERKQRASL---KEQMQEIQQSFsiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1343 VSNYQ--LECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFE----GEGVSRAEELEETRRKLTHKVQEMQEQLEN 1416
Cdd:TIGR00618 625 QDLQDvrLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1417 ANQKIGTLEKNKQRLAHDLEDAqvdadrANSIASSLEKKQKGFDKVLDEWRRKC-EALVAEVEQSQRETRAAATETFRLr 1495
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENA------SSSLGSDLAAREDALNQSLKELMHQArTVLKARTEAHFNNNEEVTAALQTG- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1496 NQLEESGEQTEAVKRENKALAQELKDIADQLGEggKSVHDLQKmrrrLEIEKEELQQALDEAECALEAEEAKvmraQIEV 1575
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ--EIPSDEDI----LNLQCETLVQEEEQFLSRLEEKSAT----LGEI 847
|
730
....*....|....*.
gi 17561652 1576 SQIRSEIEKRLQEKEE 1591
Cdd:TIGR00618 848 THQLLKYEECSKQLAQ 863
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
28-71 |
2.48e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 68.61 E-value: 2.48e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 17561652 28 DSKKNVWVADPEEGFIAAEIKSSKGDTVVVVTSKGVEKTIKKDD 71
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDD 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
971-1662 |
4.55e-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: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 971 IKKQESEKQAKDHQIRSLQDEIqsqdeviskLNKEKKHqeevnRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLER 1050
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNEL---------KNKEKEL-----KNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1051 EKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEE 1130
Cdd:TIGR04523 94 NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1131 ELDAERNSRSKAEKARNEMQMELEELGDRLDeaggATQAQIELNKKREAELAklrqDLEDAAINSETSMAALRKKHNDAV 1210
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLS----NLKKKIQKNKSLESQIS----ELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1211 AELSDQLDTIQKMRGKLEREKNDKQREVDELQQSAdveaKQRQNCERMAKQLEAQLTDmtLKSDEQARLIqeltmgkNKV 1290
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN----KKIKELEKQLNQLKSEISD--LNNQKEQDWN-------KEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1291 HNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLhsqvsnyqleceqfRESLEEEQDAKTDVQRQ 1370
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK--------------QRELEEKQNEIEKLKKE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1371 LSKANSEIQQwrakfegegvsraeeLEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIAS 1450
Cdd:TIGR04523 379 NQSYKQEIKN---------------LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1451 SLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGG 1530
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1531 KSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAK--VMRAQIEVSQIR----------SEIEKRLQEKEEEFENTRK 1598
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeIDEKNKEIEELKqtqkslkkkqEEKQELIDQKEKEKKDLIK 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1599 NhsrtIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLnvdgQKSMKKLQDTIRE 1662
Cdd:TIGR04523 604 E----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE----VKQIKETIKEIRN 659
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1465 |
4.60e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFE--ALEKKFKVLEEEKTQEERKRKDmeaENARLEAEKQALLIQLEQERDSSAEGEERSAKllaQKADLEKQMA 930
Cdd:PTZ00121 1314 AKKADEAKkkAEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK---KKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 931 NMNDQlCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLettikKQESEKQAKDHQIRSLQDEIQSQDEvISKLNKEKKHQE 1010
Cdd:PTZ00121 1388 EEKKK-ADEAKKKAEEDKKKADELKKAAAAKKKADEA-----KKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1011 EVNRKLLEDIQAEEDKVNHLNKTKAklestlDELEDTLEREKRGRQDCEK--QRRKVEGELKIAQELIEELNRHKHEQeq 1088
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKA------DEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEE-- 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1089 viKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSR-----SKAEKARNEMQMEL--EELGDRLD 1161
Cdd:PTZ00121 1533 --AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeaKKAEEARIEEVMKLyeEEKKMKAE 1610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1162 EAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLdtiqKMRGKLEREKNDKQREVDEL 1241
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE----AKKAEEDKKKAEEAKKAEED 1686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1242 QQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAeaqlcalnRIKQQQHSQ 1321
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--------KKDEEEKKK 1758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1322 LEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAK------TDVQRQLSKANSEIQQWRAKFEGE----GVS 1391
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKdifdnfANIIEGGKEGNLVINDSKEMEDSAikevADS 1838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1392 RAEELEETRRKLTHKVQEMQEQLE------NANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDE 1465
Cdd:PTZ00121 1839 KNMQLEEADAFEKHKFNKNNENGEdgnkeaDFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDK 1918
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1119-1793 |
5.42e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1119 KELLARIQELEEELDAERNSRSKAEKARNEMQM--ELEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAInse 1196
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1197 TSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKND-KQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDE 1275
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1276 QARLIQELtmgknkvhneNQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRE 1355
Cdd:COG4913 378 SAEEFAAL----------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1356 SLEEEqdaktdvqrqLSKANSEI-------------QQWRAKFEG----------------EGVSRAEEleetRRKLTHK 1406
Cdd:COG4913 448 ALAEA----------LGLDEAELpfvgelievrpeeERWRGAIERvlggfaltllvppehyAAALRWVN----RLHLRGR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1407 VQEMQEQLENANQKIGTLEKN-----------------KQRLAHDLEDAQVD-------ADRANSIA----SSLEKKQKG 1458
Cdd:COG4913 514 LVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFDYVCVDspeelrrHPRAITRAgqvkGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1459 F-DKVLDEW------RRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKR---------ENKALAQELKDI 1522
Cdd:COG4913 594 DrRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1523 ADQLGEGGKSVHDLQKMRRRLEIEKEELQQAldeaecaleaeeakvMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSR 1602
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEEL---------------EEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1603 TIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNvdgQKSMKKLQDTIRELQYQ---------------- 1666
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL---NRAEEELERAMRAFNREwpaetadldadleslp 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1667 -VEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELS-NSNSLL-LATKRKVEGD 1743
Cdd:COG4913 816 eYLALLDRLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPfGPGRYLrLEARPRPDPE 895
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 17561652 1744 LQLLQSEIEEAMSDAKTSDE---KAKKAIMDAskLADELRSEQEHASNLNQSK 1793
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEelsEARFAALKR--LIERLRSEEEESDRRWRAR 946
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
920-1812 |
1.11e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 920 AQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDhqirslqdeiqsqdevi 999
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED----------------- 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1000 SKLNKEKKHQEEVnRKLLEDIQAEEDKvnhlnktkaklestldelEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEEL 1079
Cdd:PTZ00121 1127 ARKAEEARKAEDA-RKAEEARKAEDAK------------------RVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1080 NRhkheQEQVIKKKDIELSSIQSRLEDEqslvaklqRQIKEllARIQELEEELDAERnsrsKAEKARnemqmeleelgdr 1159
Cdd:PTZ00121 1188 RK----AEELRKAEDARKAEAARKAEEE--------RKAEE--ARKAEDAKKAEAVK----KAEEAK------------- 1236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1160 ldeaggatqaqielNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRgklEREKNDKQREVD 1239
Cdd:PTZ00121 1237 --------------KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE---EKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1240 ELQQSAdvEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQH 1319
Cdd:PTZ00121 1300 EKKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1320 SQLEELKRTLdQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEiqqwRAKFEGEGVSRAEELEet 1399
Cdd:PTZ00121 1378 KKADAAKKKA-EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD----EAKKKAEEAKKADEAK-- 1450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1400 rrklthKVQEMQEQLENANQKigTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQ 1479
Cdd:PTZ00121 1451 ------KKAEEAKKAEEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1480 SQRETRAAatetfrlrnqlEESGEQTEAVKRENKALAQELKDiADQLGEgGKSVHDLQKMRRRLEIEKEELQQAlDEAEC 1559
Cdd:PTZ00121 1523 KADEAKKA-----------EEAKKADEAKKAEEKKKADELKK-AEELKK-AEEKKKAEEAKKAEEDKNMALRKA-EEAKK 1588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1560 ALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHS-RTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIA 1638
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1639 LDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAE 1718
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1719 VKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAM--SDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTL 1796
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELdeEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
890 900
....*....|....*....|
gi 17561652 1797 ESQVKDL----QMRLDEAEA 1812
Cdd:PTZ00121 1829 DSAIKEVadskNMQLEEADA 1848
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
857-1336 |
1.52e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 857 EEFEALEKKFKVLEEEKTQEERKRKdmEAENARLEAEKQALLIQLEQERDSSAEGEERSAK--LLAQKADLEKQMANMND 934
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAAaeLAAQLEELEEAEEALLE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 935 QLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLnKEKKHQEEVNR 1014
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1015 KLLEDIQAEED------KVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRR--KVEGELKIAQELIEELNRHKH-- 1084
Cdd:COG1196 494 LLLLEAEADYEgflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnIVVEDDEVAAAAIEYLKAAKAgr 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1085 -EQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEA 1163
Cdd:COG1196 574 aTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1164 GGATQAQIELNKKREAELAKLRQDLEDAAINSETsMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQ 1243
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAER-LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1244 SADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELT-----MGK---------NKVHNENQDLNRQLEDAEAqlc 1309
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEreieaLGPvnllaieeyEELEERYDFLSEQREDLEE--- 809
|
490 500
....*....|....*....|....*..
gi 17561652 1310 ALNrikqqqhsQLEELKRTLDQETRER 1336
Cdd:COG1196 810 ARE--------TLEEAIEEIDRETRER 828
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1310-1931 |
1.62e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1310 ALNRIKQQQHSQLEELKRTLDQetRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEgeg 1389
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE--- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1390 vsRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEwrrk 1469
Cdd:PRK02224 252 --ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE---- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1470 cealvaeVEQSQRETRAAATETfrlRNQLEesGEQTEAVKRENKAlaQELKDIADQLGEggksvhDLQKMRRRLEIEKEE 1549
Cdd:PRK02224 326 -------LRDRLEECRVAAQAH---NEEAE--SLREDADDLEERA--EELREEAAELES------ELEEAREAVEDRREE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1550 LqqaldeaecaleaeeakvmraqievsqirSEIEKRLQEKEEEFENTrknhsrtiesmQVSLETESRGRAELLKTKKKLE 1629
Cdd:PRK02224 386 I-----------------------------EELEEEIEELRERFGDA-----------PVDLGNAEDFLEELREERDELR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1630 GDVNELEIALdhsnklnvdgqksmKKLQDTIRELQYQVEEEQ-----RSLSESRDHANLAERRSQVLQQEKEDLAIIYEQ 1704
Cdd:PRK02224 426 EREAELEATL--------------RTARERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1705 SERTRRQAELE-LAEVKDSVNELSNSNSL---LLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAimdASKLADELR 1780
Cdd:PRK02224 492 EEVEERLERAEdLVEAEDRIERLEERREDleeLIAERRETIEEKRERAEELRERAAELEAEAEEKREA---AAEAEEEAE 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1781 SEQEHASNLNQSKKTLESQVKDLQmRLDEAEAAgikggkrqLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCREL 1860
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLE-RIRTLLAA--------IADAEDEIERLREKREALAELNDERRERLAEKRERKREL 639
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1861 QFQVDEDKksqermydlIEKLQQKIKTYKRQIEDAESlasgnlaKYRQLQHVVEDAQERADAAENALQKLR 1931
Cdd:PRK02224 640 EAEFDEAR---------IEEAREDKERAEEYLEQVEE-------KLDELREERDDLQAEIGAVENELEELE 694
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
913-1147 |
1.87e-13 |
|
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: 74.42 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 913 ERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEI 992
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 993 QSQDEVISKLNKekKHQEEVNRKLLEDIQAEEDkVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIA 1072
Cdd:COG4942 100 EAQKEELAELLR--ALYRLGRQPPLALLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1073 QELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARN 1147
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
855-1487 |
2.26e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 75.85 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 855 KNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDssaegeersakllaqKADLEKQMANMND 934
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKD---------------KMDKDEQIRKIKS 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 935 QLCDEEEKNAALTKQKKKieqdneglkktvsdLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNR 1014
Cdd:TIGR00606 557 RHSDELTSLLGYFPNKKQ--------------LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1015 KLLEDI------QAEEDKVNHL-------NKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNR 1081
Cdd:TIGR00606 623 SYEDKLfdvcgsQDEESDLERLkeeieksSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1082 -------HKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELE 1154
Cdd:TIGR00606 703 klrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1155 ELGDRLDEAGGATQAQIEL--NKKREAELAKlrqdlEDAAINSETSMAALRKKhndaVAELSDQLDTIQKMRGKLEREKN 1232
Cdd:TIGR00606 783 SAKVCLTDVTIMERFQMELkdVERKIAQQAA-----KLQGSDLDRTVQQVNQE----KQEKQHELDTVVSKIELNRKLIQ 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1233 DKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALN 1312
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1313 RIKQQQHSQLEELKRTLDQETRERQSLHSQVsnyQLECEQFRESLEEEQD----AKTDVQRQLSKANSEIQQWRAKFEGE 1388
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNtvnaQLEECEKHQEKINEDMRLMRQDIDTQ 1010
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 GV-SRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSiaSSLEKKQKGFDKvldewr 1467
Cdd:TIGR00606 1011 KIqERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNH--VLALGRQKGYEK------ 1082
|
650 660
....*....|....*....|
gi 17561652 1468 rkcEALVAEVEQSQRETRAA 1487
Cdd:TIGR00606 1083 ---EIKHFKKELREPQFRDA 1099
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1001-1438 |
5.68e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.03 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1001 KLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKiAQELIEELN 1080
Cdd:COG4717 57 ELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1081 RHKHEQEQVIKKKDielssiqsRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKAR-NEMQMELEELGDR 1159
Cdd:COG4717 136 ALEAELAELPERLE--------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1160 LDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQK----------------- 1222
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1223 -MRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELtmgknkvhnenQDLNRQL 1301
Cdd:COG4717 288 lLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL-----------QELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1302 EDAEAQLcALNRIKQQQHSQLEELKRTLDQETRERqslhsqvsnyqleCEQFREsLEEEQDAKTDVQRQLSKANSEIQQW 1381
Cdd:COG4717 357 EELEEEL-QLEELEQEIAALLAEAGVEDEEELRAA-------------LEQAEE-YQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1382 RAKFEGEGV-SRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNK--QRLAHDLEDA 1438
Cdd:COG4717 422 LEALDEEELeEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEEL 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1663-1935 |
7.64e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1663 LQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSLLLAtkrkveg 1742
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1743 DLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAgIKGGKRQL 1822
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-LAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1823 AKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDAESLASGN 1902
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|...
gi 17561652 1903 LAKYRQLQHVVEDAQERADAAENALQKLRLKGR 1935
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1062-1605 |
1.52e-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: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1062 RRKVEGELKIAQELIEELNRHKHE----QEQV-----IKKKDIELSSIQSRLEDEQSLVAKL-----QRQIKELLARIQE 1127
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEAledaREQIellepIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1128 LEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGAT----QAQIELNKKREAELAKLRQDLEDAAI-------NSE 1196
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAalglplpASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1197 TSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQS-ADVEAKQR---QNCERMAKQLEAQLTdmtlK 1272
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiASLERRKSnipARLLALRDALAEALG----L 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1273 SDEQARLIQELTmgknKVHNENQD----LNRQL-----------EDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQ 1337
Cdd:COG4913 456 DEAELPFVGELI----EVRPEEERwrgaIERVLggfaltllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1338 SLHSQVSNYQLECEQFRESLEEEQDAKTDVQRqlskanseiqqwrakfegegVSRAEELEETRRKLT--------HKVQE 1409
Cdd:COG4913 532 DPDSLAGKLDFKPHPFRAWLEAELGRRFDYVC--------------------VDSPEELRRHPRAITragqvkgnGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1410 MQEQLE---------NANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLD-EWRRKcealvaEVEQ 1479
Cdd:COG4913 592 KDDRRRirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEySWDEI------DVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1480 SQRETRAAATEtfrlRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAEC 1559
Cdd:COG4913 666 AEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 17561652 1560 ALEAEEAKV---MRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIE 1605
Cdd:COG4913 742 LARLELRALleeRFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
883-1521 |
1.87e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.83 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 883 MEAENARLE-----AEKQALLIQLEQERDSSAEGEERSAKLL-AQKADLEKQMANMN-------DQLCDEEEKNAALTKQ 949
Cdd:pfam05483 204 VQAENARLEmhfklKEDHEKIQHLEEEYKKEINDKEKQVSLLlIQITEKENKMKDLTflleesrDKANQLEEKTKLQDEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 950 KKKIEQDNEGLKKTVSDLETTIKKQESEKQAkdhqirsLQDEIQSQDEVISKLNKEKKHQEEvnrkllediQAEEDKVNH 1029
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKA-------LEEDLQIATKTICQLTEEKEAQME---------ELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1030 lNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEqvikkkdIELSSIQSRLEDEQS 1109
Cdd:pfam05483 348 -SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE-------VELEELKKILAEDEK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1110 LVAKlQRQIKELLARIQELEEELDAERNSRSKaekarnemqmELEELGDRLDEAGGATQAQIELNKKREAELAKlrQDLE 1189
Cdd:pfam05483 420 LLDE-KKQFEKIAEELKGKEQELIFLLQAREK----------EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK--EKLK 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1190 DAAINSETSMAALRKKhnDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDM 1269
Cdd:pfam05483 487 NIELTAHCDKLLLENK--ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1270 TLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLE 1349
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1350 CEQFRESLEEEQDaktdvqrqlskanseiqqwrakfegegvSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQ 1429
Cdd:pfam05483 645 LASAKQKFEEIID----------------------------NYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1430 RLAHDLEDaqvdadransIASSLEKKQKGFDKVLDEwRRKCEALVAEVEQSQRETRAA-ATETFRLRNQLEESGEQTEAV 1508
Cdd:pfam05483 697 RCQHKIAE----------MVALMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKAAlEIELSNIKAELLSLKKQLEIE 765
|
650
....*....|...
gi 17561652 1509 KRENKALAQELKD 1521
Cdd:pfam05483 766 KEEKEKLKMEAKE 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
846-1375 |
2.24e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 846 VKPLIKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKllAQKADL 925
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 926 EKQMANMNDQLCDEEEKNAaltKQKKKIEQDNEGLKKTVSDletTIKKQESEKQAKDHQirsLQDEIQSQDEVisKLNKE 1005
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAA---EAKKKADEAKKAEEAKKAD---EAKKAEEAKKADEAK---KAEEKKKADEL--KKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1006 KKHQEEVnRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELieelnrhkhE 1085
Cdd:PTZ00121 1557 LKKAEEK-KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL---------K 1626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1086 QEQVIKKKDIELssiQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGG 1165
Cdd:PTZ00121 1627 KAEEEKKKVEQL---KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1166 ATQaqieLNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDavAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSA 1245
Cdd:PTZ00121 1704 AEE----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED--KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1246 DVEAKQRQNCERMAKQLEAQLTDMTLKSDEQarLIQEltmgKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHS-QLEE 1324
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFA--NIIE----GGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAdAFEK 1851
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1325 LKRTLDQETRERQSLHSQVSNYQLECEQFRESLEE----EQDAKTDVQRQLSKAN 1375
Cdd:PTZ00121 1852 HKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEadeiEKIDKDDIEREIPNNN 1906
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
844-1339 |
2.48e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 844 GRVKPLIKGSKKN-EEF----EALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQAL---LIQLEQERDSSAEGEERS 915
Cdd:PRK03918 168 GEVIKEIKRRIERlEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 916 AKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQ------DNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQ 989
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 990 DEIQSQDEVISKLNKEKKHQEEVNRK---LLEDIQAEED---KVNHLNKTKAKLES-TLDELEDTLEREKRGRQDCEKQR 1062
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRleeLEERHELYEEakaKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1063 RKVEGEL----KIAQEL---IEELNRHK------------HEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKEL-- 1121
Cdd:PRK03918 408 SKITARIgelkKEIKELkkaIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELek 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1122 --------------LARIQELEEEL------DAERNSR--SKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKR-- 1177
Cdd:PRK03918 488 vlkkeseliklkelAEQLKELEEKLkkynleELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLde 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1178 -EAELAKLRQDLEDAAINS----ETSMAALRKKHNDAVaelsdqldTIQKMRGKLEREKNDKQREVDELQQSADVEAKQR 1252
Cdd:PRK03918 568 lEEELAELLKELEELGFESveelEERLKELEPFYNEYL--------ELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1253 QNCERMAKQLEAQLTDMTLKSDEQARliqeltmgknkvhNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQE 1332
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEYEELR-------------EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
....*..
gi 17561652 1333 TRERQSL 1339
Cdd:PRK03918 707 EKAKKEL 713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1533-1937 |
3.04e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1533 VHDLQKMRRRLEIEKE------ELQQALDEAECALEAEEAKVMRAQIEvsQIRSEIEkRLQEKEEEFENTRKNHSRTIES 1606
Cdd:COG1196 195 LGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELE--ELEAELE-ELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1607 MQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAER 1686
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1687 RSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAK 1766
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1767 KAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKggkrQLAKLDMRIHELETELEGENRRHAET 1846
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1847 QKVLRNKDrkcrelqfqvdedKKSQERMYDLIEKLQQKIKTYKRQIEDAESLAsgnlakyrqLQHVVEDAQERADAAENA 1926
Cdd:COG1196 508 EGVKAALL-------------LAGLRGLAGAVAVLIGVEAAYEAALEAALAAA---------LQNIVVEDDEVAAAAIEY 565
|
410
....*....|.
gi 17561652 1927 LqKLRLKGRST 1937
Cdd:COG1196 566 L-KAAKAGRAT 575
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1031-1289 |
4.36e-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: 70.18 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1031 NKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSL 1110
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1111 VAKLQRQIKELLARIQELEE--ELDAERNSRSKAEKARNEMQMEleelgdrldeaggatqaqiELNKKREAELAKLRQDL 1188
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqpPLALLLSPEDFLDAVRRLQYLK-------------------YLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1189 EDaainsetsMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTD 1268
Cdd:COG4942 160 AE--------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|.
gi 17561652 1269 MTLKSDEQARLIQELTMGKNK 1289
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALK 252
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
853-1336 |
6.20e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEK--------------QALLIQLEQERDSSAEGEERSAKL 918
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDeelrdrleecrvaaQAHNEEAESLREDADDLEERAEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 919 LAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEV 998
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 999 ISKlnkekkhqeevNRKLLED------IQAEEDkvnhlnktkAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIA 1072
Cdd:PRK02224 442 VEE-----------AEALLEAgkcpecGQPVEG---------SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1073 QELIeelnrhkhEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQME 1152
Cdd:PRK02224 502 EDLV--------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1153 LEELGDRLDEaggatqaqielNKKREAELAKLRQDLEDAAiNSETSMAALRKKHnDAVAELSDQldtiqkMRGKLeREKN 1232
Cdd:PRK02224 574 VAELNSKLAE-----------LKERIESLERIRTLLAAIA-DAEDEIERLREKR-EALAELNDE------RRERL-AEKR 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1233 DKQREVDELQQSADVEAKQ--RQNCERMAKQLEAQLTDMTLKSDEqarLIQELTMGKNKVhNENQDLNRQLEDAEAQLCA 1310
Cdd:PRK02224 634 ERKRELEAEFDEARIEEARedKERAEEYLEQVEEKLDELREERDD---LQAEIGAVENEL-EELEELRERREALENRVEA 709
|
490 500
....*....|....*....|....*.
gi 17561652 1311 LNRIKQQQhSQLEELKRTLDQETRER 1336
Cdd:PRK02224 710 LEALYDEA-EELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1175-1894 |
6.75e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.82 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1175 KKREAELAKLRQDLEDAA---INSETSMAALRKKHNDAVAELSDQLDTIQKMRGKL----EREKNDKQREVDELQQSADV 1247
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEekiNNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLskinSEIKNDKEQKNKLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1248 EAKQRQNCERMAK------QLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAeaqlcalnrikQQQHSQ 1321
Cdd:TIGR04523 130 EKQKKENKKNIDKflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI-----------KNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1322 LEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQwrakfegegvsraeeLEETRR 1401
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ---------------LKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1402 KLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLED--AQVDADRANSIASSLEKKQKGFDKV---LDEWRRKCEALVAE 1476
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnNQKEQDWNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1477 VEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDiadqlgeggksvhdlqkmrrrLEIEKEELQQALDE 1556
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN---------------------LESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1557 AECALEAEEAKVMRAQIEVSQIRSEIEKRLQEkeeefentrknhsrtiesmqvsletesrgRAELLKTKKKLEGDVNELE 1636
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKET-----------------------------IIKNNSEIKDLTNQDSVKE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1637 IALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSesrdhanlaerrsqvlQQEKEDLAIIYEQSertrrQAELEL 1716
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK----------------SKEKELKKLNEEKK-----ELEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1717 AEVKDSVNELSNSNSLLLATKRKVEGDLQLLQSEIEEamsdaktsdekaKKAIMDASKLADELRSEQEHASNLNQSKKTL 1796
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK------------DDFELKKENLEKEIDEKNKEIEELKQTQKSL 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1797 ESQVKDLQMRLDEAEAAgIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYD 1876
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKE-KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
730
....*....|....*...
gi 17561652 1877 LIEKLQQKIKTYKRQIED 1894
Cdd:TIGR04523 660 KWPEIIKKIKESKTKIDD 677
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1061-1915 |
7.81e-12 |
|
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: 71.24 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1061 QRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSS--------IQSRLEDEQSLVAKLQRQIKELLARIQELEEEL 1132
Cdd:TIGR01612 516 KPDEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKnwkkliheIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEI 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1133 daernsrskaeKARNEMQMELEELGDRLDEAGGATQAQIELNKKREA------ELAKLR-----QDLEDAAINSETSMAA 1201
Cdd:TIGR01612 596 -----------IYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENnnayidELAKISpyqvpEHLKNKDKIYSTIKSE 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1202 LRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKqreVDELQQSADVEAKQRQNCErmAKQLEAQLTDMTLKSDEQARLIQ 1281
Cdd:TIGR01612 665 LSKIYEDDIDALYNELSSIVKENAIDNTEDKAK---LDDLKSKIDKEYDKIQNME--TATVELHLSNIENKKNELLDIIV 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1282 ELtmgKNKVHNE-NQDLNRQLED---AEAQLCALNRIKQQQHSQLEELKRTLdQETRERQSLHSQVSNYQLE-CEQFRES 1356
Cdd:TIGR01612 740 EI---KKHIHGEiNKDLNKILEDfknKEKELSNKINDYAKEKDELNKYKSKI-SEIKNHYNDQINIDNIKDEdAKQNYDK 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1357 LEEEQDAKTDVQRQLSKANSEIQQWRAKFegegVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTlEKNKQRLAhDLE 1436
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKIINEMKFMKDDF----LNKVDKFINFENNCKEKIDSEHEQFAELTNKIKA-EISDDKLN-DYE 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1437 DAQVDADR-ANSIASSLEKKQKGFD--KVLDEWRRKCEALVAEVEQSQREtraaatetfrlRNQLEESGEQTEAVKRENK 1513
Cdd:TIGR01612 890 KKFNDSKSlINEINKSIEEEYQNINtlKKVDEYIKICENTKESIEKFHNK-----------QNILKEILNKNIDTIKESN 958
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1514 ALAQELKD-----IADQLGEGGKSVHDLQkmRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEvsqirsEIEKRLQE 1588
Cdd:TIGR01612 959 LIEKSYKDkfdntLIDKINELDKAFKDAS--LNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD------EKEKATND 1030
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1589 KEEEFENTRKNHSR-------TIESMQVSLETESRGRAELLKTK--KKLEGDV---NELEIALDHSN------KLNVDGQ 1650
Cdd:TIGR01612 1031 IEQKIEDANKNIPNieiaihtSIYNIIDEIEKEIGKNIELLNKEilEEAEINItnfNEIKEKLKHYNfddfgkEENIKYA 1110
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1651 KSMKKLQDTIRELQYQVEEEQRSLSESRDHAN--LAERRSQVLQQEK-EDLAIIYEQSERTRRQAELELAEVKDSVNELS 1727
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEEIKKKSEnyIDEIKAQINDLEDvADKAISNDDPEEIEKKIENIVTKIDKKKNIYD 1190
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1728 NSNSLLlatkrkvegdlqllqSEIEEAMSDaKTSDEKAKKAIMDASKLADELRSEQ--EHASNLNQSKKTLESQVKDLQM 1805
Cdd:TIGR01612 1191 EIKKLL---------------NEIAEIEKD-KTSLEEVKGINLSYGKNLGKLFLEKidEEKKKSEHMIKAMEAYIEDLDE 1254
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1806 RLDEAEAAGIKGGKRQLAKLDMRI----HELETELEGENRRHAETQKVLRNKDRKC--------------RELQFQVDED 1867
Cdd:TIGR01612 1255 IKEKSPEIENEMGIEMDIKAEMETfnisHDDDKDHHIISKKHDENISDIREKSLKIiedfseesdindikKELQKNLLDA 1334
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 1868 KKSQE----------RMYDL-----IEKLQQKIKTYKRQIEDAESLASGNLAKYRQLQHVVED 1915
Cdd:TIGR01612 1335 QKHNSdinlylneiaNIYNIlklnkIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1232 |
8.28e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 839 WFKLFGRVKPL------IKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERdsSAEGE 912
Cdd:PRK03918 360 RHELYEEAKAKkeelerLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK--KAKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 913 ERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKqakdhQIRSLQDEI 992
Cdd:PRK03918 438 CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-----QLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 993 QSQDevISKLNKEKKHQEEVNRKLLE------DIQAEEDKVNHLNKTKAKLESTLDELedtlerekrgrqdcEKQRRKVE 1066
Cdd:PRK03918 513 KKYN--LEELEKKAEEYEKLKEKLIKlkgeikSLKKELEKLEELKKKLAELEKKLDEL--------------EEELAELL 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1067 GEL-KIAQELIEELNRHKHEQEQvIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKA 1145
Cdd:PRK03918 577 KELeELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1146 RNEMQME-LEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINsetsmaalRKKHNDAVAELSDQLDTIQKMR 1224
Cdd:PRK03918 656 YSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--------REKAKKELEKLEKALERVEELR 727
|
....*...
gi 17561652 1225 GKLEREKN 1232
Cdd:PRK03918 728 EKVKKYKA 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1086-1308 |
9.72e-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: 69.02 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1086 QEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGG 1165
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1166 ATQAQIELNKKREAELAKL-RQDLEDAAINSETSMAALRKKH--NDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQ 1242
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1243 QSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTmgknkvhNENQDLNRQLEDAEAQL 1308
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ-------QEAEELEALIARLEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1139 |
2.77e-11 |
|
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: 69.32 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 856 NEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQ 935
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 936 LCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRK 1015
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1016 LLEDIQAEEDKVNHLNKTKAKLESTLDELEDTL-EREKRGRQDCEKQRRKVEGELKIAQELIEELNRhkheqeQVIKKKD 1094
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN------KIKELGP 986
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17561652 1095 IELSSIQ--SRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSR 1139
Cdd:TIGR02168 987 VNLAAIEeyEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
870-1521 |
2.98e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.84 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 870 EEEKTQEERKRKDMEAENARLEAEK-QALLIQLE--QERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNAAL 946
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEElRAQEAVLEetQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 947 TKQKKKIEQDNEGLKKTvSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLnkekkhqeevnRKLLEDIQAEEDK 1026
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-----------HTLQQQKTTLTQK 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1027 VNHLnktkAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLED 1106
Cdd:TIGR00618 395 LQSL----CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1107 EQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRldeagGATQAQIELNKKREAELAKLRQ 1186
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP-----GPLTRRMQRGEQTYAQLETSEE 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1187 DLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQL 1266
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1267 TDMTLKSDEQaRLIQELTMGKNKVHNENQDLNRQLEDAeaqlcALNRIKQQQHSQLEELKRTLDQEtrerQSLHSQVSNY 1346
Cdd:TIGR00618 626 DLQDVRLHLQ-QCSQELALKLTALHALQLTLTQERVRE-----HALSIRVLPKELLASRQLALQKM----QSEKEQLTYW 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1347 QLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEK 1426
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1427 NKQRLAHDLEDAQVD----ADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESG 1502
Cdd:TIGR00618 776 TGAELSHLAAEIQFFnrlrEEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
650 660
....*....|....*....|..
gi 17561652 1503 E---QTEAVKRENKALAQELKD 1521
Cdd:TIGR00618 856 EcskQLAQLTQEQAKIIQLSDK 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
853-1269 |
3.27e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAEnarleaekqalliqLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESE--------------LEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQA-------KDHQIRSLQDEIQSQDEVISKLNKE 1005
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1006 ----KKHQEEVNRKL--LEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEEL 1079
Cdd:PRK02224 484 ledlEEEVEEVEERLerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1080 NRHKHEQEQVIKKKDIELSSIQSRLEdeqSLvaklqRQIKELLARIQELEEELDaERNSRSKAEKARNEMQME-LEELGD 1158
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIE---SL-----ERIRTLLAAIADAEDEIE-RLREKREALAELNDERRErLAEKRE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1159 RLDEAGGatqaqiELNKKREAELAKLRQDLEDAAINSETSMAALRKKHND---AVAELSDQLDTIQKMRGKLEREKNDKQ 1235
Cdd:PRK02224 635 RKRELEA------EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaEIGAVENELEELEELRERREALENRVE 708
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 17561652 1236 R------EVDELQQS-ADVEAKQRQnceRMAKQLEAQLTDM 1269
Cdd:PRK02224 709 AlealydEAEELESMyGDLRAELRQ---RNVETLERMLNET 746
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
939-1383 |
3.53e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 939 EEEKNAALTKQKKKIEQDNEGLKKTVSDLEttikkqesEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLE 1018
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK--------EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1019 DIQAEED--KVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEgelKIAQELIEELNRHKHEQEQVIKKKDIE 1096
Cdd:COG4717 124 LLQLLPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1097 LSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEK--------ARNEMQMELEELGDRLDEAGGATQ 1168
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1169 AQIELNKKREAELAKLRQDLEdAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVE 1248
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1249 AKQRQnCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRI--KQQQHSQLEELK 1326
Cdd:COG4717 360 EEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1327 RTLDQETRERQSLHSQVSNYQLECEQFRESlEEEQDAKTDVQRQLSKANSEIQQWRA 1383
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAA 494
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
855-1432 |
4.70e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.46 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 855 KNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLI--QLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 N------DQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDhQIRSLQDEIQSQDEVISKLNKEK 1006
Cdd:TIGR00618 348 QtlhsqeIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1007 KH---QEEVNRKLLEDIQAEEDKVNHLNKTK-AKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQEL------I 1076
Cdd:TIGR00618 427 AHakkQQELQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpL 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1077 EELNRHKHEQEQVIKKKDIELSSIQsRLEDE----QSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQME 1152
Cdd:TIGR00618 507 CGSCIHPNPARQDIDNPGPLTRRMQ-RGEQTyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1153 LEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELS-----------DQLDTIQ 1221
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlhalqltltqeRVREHAL 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1222 KMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTdmtlKSDEQARLIQELtmgKNKVHNENQDLNRQl 1301
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELET----HIEEYDREFNEI---ENASSSLGSDLAAR- 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1302 EDAEAQLcaLNRIKQQQHSQLEElkRTLDQETRERQSLHSQVSNYQLecEQFRESLEEEQDAKTDVQRQLSKANSEIQQW 1381
Cdd:TIGR00618 738 EDALNQS--LKELMHQARTVLKA--RTEAHFNNNEEVTAALQTGAEL--SHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1382 RAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLA 1432
Cdd:TIGR00618 812 IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
854-1150 |
4.98e-11 |
|
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: 67.84 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 854 KKNEEFEALEK-KFKVLEEEKTQE-ERKRKDMEAENARLEAEKQALLIQLEQERdsSAEGEERSAKLLAQKADLEKQMAN 931
Cdd:pfam17380 288 QQQEKFEKMEQeRLRQEKEEKAREvERRRKLEEAEKARQAEMDRQAAIYAEQER--MAMERERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 932 MNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVsDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEviSKLNKEKKHQEE 1011
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKVEMEQIRAEQE--EARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1012 VNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKV-EGELKI-AQELIEELNRHKH-EQEQ 1088
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEErKQAMIEEERKRKLlEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1089 VIKKKDIELSSIQSRLEDEQSLVAKLQ--RQIKELLARIQELEEELDAERNSRS------KAEKARNEMQ 1150
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMEerRRIQEQMRKATEERSRLEAMEREREmmrqivESEKARAEYE 592
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
875-1598 |
5.35e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 875 QEERKRKDMEAENARLEAekQALLIQLEQERdsSAEGEERSAKLLAQKADLEKQMANMNDQLcDEEEKNAALTKQKK--- 951
Cdd:PRK04863 349 KIERYQADLEELEERLEE--QNEVVEEADEQ--QEENEARAEAAEEEVDELKSQLADYQQAL-DVQQTRAIQYQQAVqal 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 952 -KIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQ------DEIQSQDEVISKLNK------EKKHQEEVNRKLLE 1018
Cdd:PRK04863 424 eRAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEqklsvaQAAHSQFEQAYQLVRkiagevSRSEAWDVARELLR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1019 diQAEEDKvnHLNKTKAKLESTLDELEdtleREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELS 1098
Cdd:PRK04863 504 --RLREQR--HLAEQLQQLRMRLSELE----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1099 SIQSRLEDEQSLVAKLQRQIKEL-------------LARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGG 1165
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLaarapawlaaqdaLARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQ 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1166 ATQAQIE-LNKKREAELAKLRQ-----------------DLEDAAinsETSMAALRKKHNDAVAELSD---QLDTIQKMR 1224
Cdd:PRK04863 656 ALDEEIErLSQPGGSEDPRLNAlaerfggvllseiyddvSLEDAP---YFSALYGPARHAIVVPDLSDaaeQLAGLEDCP 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1225 GKLEREKNDKQR------EVDELQQSADVEAKQRQ---------------NCERMAKQLEAQLTDMTLKSDEQARLIQEL 1283
Cdd:PRK04863 733 EDLYLIEGDPDSfddsvfSVEELEKAVVVKIADRQwrysrfpevplfgraAREKRIEQLRAEREELAERYATLSFDVQKL 812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1284 TMGKNKVHN----------------ENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETR-ERQSLHSQVSNY 1346
Cdd:PRK04863 813 QRLHQAFSRfigshlavafeadpeaELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRlLPRLNLLADETL 892
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1347 QLECEQFRESLEEEQDAKTDVQRQlSKANSEIQQWRAKFEgegvSRAEELEEtrrkLTHKVQEMQEQLENANQKIGTLEK 1426
Cdd:PRK04863 893 ADRVEEIREQLDEAEEAKRFVQQH-GNALAQLEPIVSVLQ----SDPEQFEQ----LKQDYQQAQQTQRDAKQQAFALTE 963
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1427 NKQRLAH-DLEDAQVDADRANSIASSLEKKQKgfdkvldewrrkcealvaEVEQSQRETRAAATET---FRLRNQLEESG 1502
Cdd:PRK04863 964 VVQRRAHfSYEDAAEMLAKNSDLNEKLRQRLE------------------QAEQERTRAREQLRQAqaqLAQYNQVLASL 1025
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1503 EQTEAVKREN-KALAQELKDIADQLGEGgksvhdlqkMRRRLEIEKEELQQALDEAECAleaeeakvmRAQIEVSQIRSE 1581
Cdd:PRK04863 1026 KSSYDAKRQMlQELKQELQDLGVPADSG---------AEERARARRDELHARLSANRSR---------RNQLEKQLTFCE 1087
|
810 820
....*....|....*....|..
gi 17561652 1582 IE-----KRLQEKEEEFENTRK 1598
Cdd:PRK04863 1088 AEmdnltKKLRKLERDYHEMRE 1109
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
865-1898 |
9.15e-11 |
|
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: 67.77 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 865 KFKVLEEEKTQEERKRKDMEAENARL-----EAEKQALL-IQLEQERDSSAEGEERSAKLLAQKADLEKQMANmndQLCD 938
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLdIIVEIKKHIHGEINKDLNKILEDFKNKEKELSN---KIND 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 939 EEEKNAALTKQKKKIEQ--DNEGLKKTVSDLETTIKKQESEKQ--------AKDHQIRSLQDEIQS-QDEVISKLNK--- 1004
Cdd:TIGR01612 774 YAKEKDELNKYKSKISEikNHYNDQINIDNIKDEDAKQNYDKSkeyiktisIKEDEIFKIINEMKFmKDDFLNKVDKfin 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1005 -EKKHQEEVNR------KLLEDIQAE--EDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCekqrRKVEGELKIAQEL 1075
Cdd:TIGR01612 854 fENNCKEKIDSeheqfaELTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL----KKVDEYIKICENT 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1076 IEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQrqiKELLARIQELEEELdaERNSRSKAEKARNEMQMELEE 1155
Cdd:TIGR01612 930 KESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFD---NTLIDKINELDKAF--KDASLNDYEAKNNELIKYFND 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1156 LGDRLDEAGGATQAQiELNKKREAElaklrQDLEDAAINSETSMAALRKKHNDAVAELSDQldtIQKMRGKLEREKNDKQ 1235
Cdd:TIGR01612 1005 LKANLGKNKENMLYH-QFDEKEKAT-----NDIEQKIEDANKNIPNIEIAIHTSIYNIIDE---IEKEIGKNIELLNKEI 1075
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1236 REVDELQQSadveakqrqNCERMAKQLEAQLTDMTLKsDEQARLIQELTMGKNKVHNENQDLNRQLEdaeaqlcALNRIK 1315
Cdd:TIGR01612 1076 LEEAEINIT---------NFNEIKEKLKHYNFDDFGK-EENIKYADEINKIKDDIKNLDQKIDHHIK-------ALEEIK 1138
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1316 QQQHSQLEELKRtldQETRERQSLHSQVSNYQLE-CEQFRESLEEEQDAKTDVQRQLSKANSEI------QQWRAKFEGE 1388
Cdd:TIGR01612 1139 KKSENYIDEIKA---QINDLEDVADKAISNDDPEeIEKKIENIVTKIDKKKNIYDEIKKLLNEIaeiekdKTSLEEVKGI 1215
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 GVSRA--------EELEETRRKLTHKVQEMQEQLEN-----------ANQKIGTLEKNKQ----RLAHD-LEDAQVDADR 1444
Cdd:TIGR01612 1216 NLSYGknlgklflEKIDEEKKKSEHMIKAMEAYIEDldeikekspeiENEMGIEMDIKAEmetfNISHDdDKDHHIISKK 1295
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1445 ANSIASSLEKKQ----KGFDKV--LDEWRRKCEALVAEVEQSQRETRAAATETFRLRN--QLEESGEQTEAVKRENKALA 1516
Cdd:TIGR01612 1296 HDENISDIREKSlkiiEDFSEEsdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIE 1375
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1517 QELKDIADQLGEGGKSVHDLqKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQirSEIEKRLQEKEEEFENT 1596
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKLIKKI-KDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEE--SNIDTYFKNADENNENV 1452
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1597 RKNHSrtiesmqvSLETESRGRAELLKTKKK-----LEGDVNELEIALDHSNKLNVDGQKSMKKLQDTiRELQYQVEEEQ 1671
Cdd:TIGR01612 1453 LLLFK--------NIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDV 1523
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1672 RSLSESRDHANLAERrsqvLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSnslllatkrkvegdlqllQSEI 1751
Cdd:TIGR01612 1524 TELLNKYSALAIKNK----FAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE------------------KFRI 1581
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1752 EeamsDAKTSDEKAKKAIMDASKLADELRSEQEHASNLnqsKKTLESQVKDLQMRLDEAEAAGIKGGKRQLAKLDMRIHE 1831
Cdd:TIGR01612 1582 E----DDAAKNDKSNKAAIDIQLSLENFENKFLKISDI---KKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNS 1654
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1832 LETELEG--ENRRHAETQKV-LRNKDRKCRELQFQVDEDKKSQErmYDLIEKLQQKIKTYKRQIEDAESL 1898
Cdd:TIGR01612 1655 LQEFLESlkDQKKNIEDKKKeLDELDSEIEKIEIDVDQHKKNYE--IGIIEKIKEIAIANKEEIESIKEL 1722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1296-1812 |
2.09e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1296 DLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDqETRERQSlhsqvsnyqlECEQFRESLEEEQDAKTDVQRQLSKAN 1375
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLE-EHEERRE----------ELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1376 SEIQQWRAkfegegvsRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKK 1455
Cdd:PRK02224 279 EEVRDLRE--------RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1456 QKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHD 1535
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1536 LQKMRRRLEIEKEELQQALDEAECALEAEeakvmraQIEVSQIRSEIEKRlQEKEEEFENTRKnhsrTIESMQVSLETes 1615
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKCPECGQ-------PVEGSPHVETIEED-RERVEELEAELE----DLEEEVEEVEE-- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1616 rgRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQE- 1694
Cdd:PRK02224 497 --RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEv 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1695 ---KEDLAIIYEQSERTRRQAEL------------ELAEVKDSVNELSNSNSLLLATKRKVEGDlqlLQSEIEEA-MSDA 1758
Cdd:PRK02224 575 aelNSKLAELKERIESLERIRTLlaaiadaedeieRLREKREALAELNDERRERLAEKRERKRE---LEAEFDEArIEEA 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1759 KTSDEKAKKAIMDASKLADELR--------------SEQEHASNLNQSKKTLESQVKDLQMRLDEAEA 1812
Cdd:PRK02224 652 REDKERAEEYLEQVEEKLDELReerddlqaeigaveNELEELEELRERREALENRVEALEALYDEAEE 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1041-1356 |
4.76e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1041 LDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDI--ELSSIQ---SRLEDEQSLVAKLQ 1115
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAerEIAELEaelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1116 RQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQielnkkREAELAKLRQDledaains 1195
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE------LRALLEERFAA-------- 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1196 etsmAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREV----DELQQSADVEAKQRQNCERMAKQLEAQltDMTL 1271
Cdd:COG4913 758 ----ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDRLEED--GLPE 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1272 KSDEQARLIQELTmgKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQ------HSQLeELKRTLDQETRE-RQSLHSQVS 1344
Cdd:COG4913 832 YEERFKELLNENS--IEFVADLLSKLRRAIREIKERIDPLNDSLKRIpfgpgrYLRL-EARPRPDPEVREfRQELRAVTS 908
|
330
....*....|..
gi 17561652 1345 NYQLECEQFRES 1356
Cdd:COG4913 909 GASLFDEELSEA 920
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
853-1552 |
5.39e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKrkdMEAENARLEAEKQALL-IQLEQERDSSAEGEErsaklLAQKADLEKQmAN 931
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENK---LQENRKIIEAQRKAIQeLQFENEKVSLKLEEE-----IQENKDLIKE-NN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 932 MNDQLCDEEEKNAALTKQK-KKIEQDNEGLKKTVSDLETTIKK-----QESEKQAKDHQIRsLQDEIQSQDEVISKLnkE 1005
Cdd:pfam05483 152 ATRHLCNLLKETCARSAEKtKKYEYEREETRQVYMDLNNNIEKmilafEELRVQAENARLE-MHFKLKEDHEKIQHL--E 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1006 KKHQEEVNRKllediqaeEDKVNHLNKTKAKLESTLDELEDTLEREKrgrqdceKQRRKVEGELKIAQELIEELNRHKHE 1085
Cdd:pfam05483 229 EEYKKEINDK--------EKQVSLLLIQITEKENKMKDLTFLLEESR-------DKANQLEEKTKLQDENLKELIEKKDH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1086 QEQvikkkdiELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGG 1165
Cdd:pfam05483 294 LTK-------ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1166 ATQAQIELNkkrEAELAKLRQDLEDAAinseTSMAALRKKHNDAVAELsDQLDTIQKMRGKLEREKNDKQREVDELQQSA 1245
Cdd:pfam05483 367 TEQQRLEKN---EDQLKIITMELQKKS----SELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1246 DVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQ--------------ELTMGKNKVHNENQDLNRQLEDAEAQLCA- 1310
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEdlktelekeklkniELTAHCDKLLLENKELTQEASDMTLELKKh 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1311 ---LNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEG 1387
Cdd:pfam05483 519 qedIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1388 -----EGVSR-AEELEETRRKLTHK--------------VQEMQEQLENANQKIGTLEKNKQRlahDLEDAQV------- 1440
Cdd:pfam05483 599 lkkqiENKNKnIEELHQENKALKKKgsaenkqlnayeikVNKLELELASAKQKFEEIIDNYQK---EIEDKKIseeklle 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1441 DADRANSIASSLEKKQKGFDKvldewrrKCEALVAEVEQSQRETRAAATETFRLRNQ---LEESGEQTEAVKRenKALAQ 1517
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDK-------RCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAK--AALEI 746
|
730 740 750
....*....|....*....|....*....|....*
gi 17561652 1518 ELKDIADQLgeggksvhdlQKMRRRLEIEKEELQQ 1552
Cdd:pfam05483 747 ELSNIKAEL----------LSLKKQLEIEKEEKEK 771
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
979-1590 |
6.83e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.54 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 979 QAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDC 1058
Cdd:PRK01156 179 RAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1059 EKQRRKVEGELKIAQELIEELNRHKH-EQEQVIKKKD--IELSSIQSRLEDEQSLVAKLQRQIKELLARIQELeEELDAE 1135
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKiINDPVYKNRNyiNDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL-SVLQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1136 RNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAElaklrqdledaainsetsmaalRKKHNDAVAELSD 1215
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY----------------------SKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1216 QL-------DTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQ----LTDMTLKSDEQARLIqelt 1284
Cdd:PRK01156 396 ILkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHII---- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1285 mgkNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRtldQETRERQSLHSQVSNYQLECEQFRESLEEEQDAK 1364
Cdd:PRK01156 472 ---NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES---EEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1365 TdvqrqlsKANSEIQQWRAKfegegvsraeELEETRRKLTHKVQEMQEQlenANQKIGTLEKNKQRLAHDLEDAQvdaDR 1444
Cdd:PRK01156 546 D-------KYEEIKNRYKSL----------KLEDLDSKRTSWLNALAVI---SLIDIETNRSRSNEIKKQLNDLE---SR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1445 ANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQeLKDIAD 1524
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSR-INDIED 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1525 QLGEGGKSVHDLQKMRRRLEIEKEELQQALDeaecaleaeeakvmraqiEVSQIRSEIEKRLQEKE 1590
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRIN------------------ELSDRINDINETLESMK 729
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1015-1188 |
9.43e-10 |
|
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: 61.09 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1015 KLLEDIQAEEDKVNHLNKTK-------AKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEelnRHKHEQE 1087
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1088 QVIKKKdiELSSIQSRLEdeqslvaKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGAT 1167
Cdd:COG1579 84 NVRNNK--EYEALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|..
gi 17561652 1168 QAQIE-LNKKREAELAKLRQDL 1188
Cdd:COG1579 155 EAELEeLEAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
854-1424 |
9.76e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 854 KKNEEFEALEKKFKVLEEEKT-----QEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADlekq 928
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG---- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 929 maNMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEvisKLNKEKKH 1008
Cdd:COG4913 335 --NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE---ALEEALAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1009 QEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRG--------------RQDCEKQRRKVEGEL----- 1069
Cdd:COG4913 410 AEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLdeaelpfvgelievRPEEERWRGAIERVLggfal 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1070 ------KIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKL-------QRQIKELLARIQEL-----EEE 1131
Cdd:COG4913 490 tllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLdfkphpfRAWLEAELGRRFDYvcvdsPEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1132 LDAER----------NSRSKAEKARNemqmeleelgDRLDEA---GGATQAQIELNKKREAELAKLRQDLEDAAINSETS 1198
Cdd:COG4913 570 LRRHPraitragqvkGNGTRHEKDDR----------RRIRSRyvlGFDNRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1199 MAALRKKHnDAVAELSDQLDTIQKMRGkLEREKNDKQREVDELQQ-SADVEAKQRQncermAKQLEAQLTDMTlksDEQA 1277
Cdd:COG4913 640 LDALQERR-EALQRLAEYSWDEIDVAS-AEREIAELEAELERLDAsSDDLAALEEQ-----LEELEAELEELE---EELD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1278 RLIQELTmgknKVHNENQDLNRQLEDAEAQLCAL-NRIKQQQHSQLEELKRTLDQETRE---RQSLHSQVSNYQLECEQF 1353
Cdd:COG4913 710 ELKGEIG----RLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAVErelRENLEERIDALRARLNRA 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1354 RESLEEEQ--------DAKTDVQRQLSkANSEIQQWRAKFEGEGVSRAEE------LEETRRKLTHKVQEMQEQLENANQ 1419
Cdd:COG4913 786 EEELERAMrafnrewpAETADLDADLE-SLPEYLALLDRLEEDGLPEYEErfkellNENSIEFVADLLSKLRRAIREIKE 864
|
....*
gi 17561652 1420 KIGTL 1424
Cdd:COG4913 865 RIDPL 869
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
883-1268 |
1.55e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.20 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 883 MEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLE--KQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGL 960
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 961 ----KKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQD----EVISKLNK----EKKHQEEVNRKLLEDIQAEEDkvn 1028
Cdd:pfam05483 445 lqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlkniELTAHCDKllleNKELTQEASDMTLELKKHQED--- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1029 hLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQ 1108
Cdd:pfam05483 522 -IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1109 SLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAEL------- 1181
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLleeveka 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1182 -------AKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDT-----------IQKMRGKLEREKNDKQREVDELQQ 1243
Cdd:pfam05483 681 kaiadeaVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelglyknkeqeQSSAKAALEIELSNIKAELLSLKK 760
|
410 420
....*....|....*....|....*
gi 17561652 1244 SADVEAKQRQNCERMAKQLEAQLTD 1268
Cdd:pfam05483 761 QLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
979-1205 |
1.72e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 979 QAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDC 1058
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1059 EKQRRKVEGELKiaqELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKEL---LARIQELEEELDAE 1135
Cdd:COG4942 96 RAELEAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELradLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1136 RNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKK 1205
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1811 |
2.65e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 62.68 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1041 LDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQ----------SRLEDEQSL 1110
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALqqtqqshaylTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1111 VAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEelgdrldeaggaTQAQIELNKKREAELAKLRQdled 1190
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH------------IKAVTQIEQQAQRIHTELQS---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1191 aainSETSMAALRKKHNDAVAELSDqLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMaKQLEAQLTDMT 1270
Cdd:TIGR00618 319 ----KMRSRAKLLMKRAAHVKQQSS-IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-HTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1271 LKSDEQARLIQELTMGKNKV---HNENQDLNRQLEDAEAQLcalnrikqqqhsqleelkrTLDQETRERQSLHSQVsnyQ 1347
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIdtrTSAFRDLQGQLAHAKKQQ-------------------ELQQRYAELCAAAITC---T 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1348 LECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLthkvQEMQEQLENANQKIGTLEKN 1427
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL----CGSCIHPNPARQDIDNPGPL 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1428 KQRLAHDLEDaqvdadransiASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEA 1507
Cdd:TIGR00618 527 TRRMQRGEQT-----------YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1508 VKRENKALAQELKDIA----DQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIE 1583
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLAceqhALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1584 KRLQEKEEEFENTRKNHSRTIESMQVSLETESrgraELLKTKKKLEGDVNELEIALdHSNKLNVDGQKSMkkLQDTIREL 1663
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR----ELETHIEEYDREFNEIENAS-SSLGSDLAAREDA--LNQSLKEL 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1664 QYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSL-LLATKRKVEG 1742
Cdd:TIGR00618 749 MHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDiLNLQCETLVQ 828
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1743 DLQLLQSEIEEamsdaktsdekakkaimdASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAE 1811
Cdd:TIGR00618 829 EEEQFLSRLEE------------------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
875-1432 |
2.84e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 875 QEERKRKDMEAENARLEAEKQAlliqLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKN---AALTKQKK 951
Cdd:PRK01156 208 DDEKSHSITLKEIERLSIEYNN----AMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyyKELEERHM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 952 KIEQDNEGLKKT-VSDLETTIKKQESEKQAkdhqIRSLQDEIQSQDEVISKlnkekkhqeevnrklLEDIQAEEDKVNHL 1030
Cdd:PRK01156 284 KIINDPVYKNRNyINDYFKYKNDIENKKQI----LSNIDAEINKYHAIIKK---------------LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1031 NKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSL 1110
Cdd:PRK01156 345 KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1111 VAKLQRQIKELLARIQELEEELdAERNSRSK--------AEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAELA 1182
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNM-EMLNGQSVcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1183 KLRQDLEDAAINsetSMAALRKKHNDAVAELSDQLDTIQKMrgkleREKNDKQREVDELQQSADVEAKQRQNCERMAKQL 1262
Cdd:PRK01156 504 KRKEYLESEEIN---KSINEYNKIESARADLEDIKIKINEL-----KDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1263 EAQLTDmtlksdeqarlIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQ 1342
Cdd:PRK01156 576 VISLID-----------IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKIL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1343 VSNYQLECEQFRE---SLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAeELEETRRKLTHKVQEMQEQLENANQ 1419
Cdd:PRK01156 645 IEKLRGKIDNYKKqiaEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA-RLESTIEILRTRINELSDRINDINE 723
|
570
....*....|...
gi 17561652 1420 KIGTLEKNKQRLA 1432
Cdd:PRK01156 724 TLESMKKIKKAIG 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1584-1943 |
4.86e-09 |
|
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: 61.61 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1584 KRLQEKEEEFENTRKNHSRT------IESMQVSLETESRgRAELLKTKKKlegDVNELEIAL------DHSNKLNvDGQK 1651
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLedilneLERQLKSLERQAE-KAERYKELKA---ELRELELALlvlrleELREELE-ELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1652 SMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNS 1731
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1732 LLLATKRKVEGDLQLLQSEIEEamsdaktsdekakkaimdaskLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAE 1811
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEE---------------------LKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1812 AAgIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKC-----RELQFQVDEDKKSQERMYDLIEKLQQKIK 1886
Cdd:TIGR02168 386 SK-VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1887 TYKRQIEDAESL---ASGNLAKYRQLQHVVEDAQERADAAENALQKLRLKGRSTSGVFGP 1943
Cdd:TIGR02168 465 ELREELEEAEQAldaAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
880-1520 |
4.89e-09 |
|
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: 61.38 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 880 RKDMEAENARLEAEKQAL---------LIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQK 950
Cdd:pfam10174 136 RKTLEEMELRIETQKQTLgardesikkLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 951 KKIEQDNEGLKKTvSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEviSKLNKEKKHQEEVnrKLLEDIQAEED----K 1026
Cdd:pfam10174 216 HRRNQLQPDPAKT-KALQTVIEMKDTKISSLERNIRDLEDEVQMLKT--NGLLHTEDREEEI--KQMEVYKSHSKfmknK 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1027 VNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQrrkvegelkiaqelIEELNRHKHEQEQVIKKKDIELSSIQSRLED 1106
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTKLETLTNQNSDCKQH--------------IEVLKESLTAKEQRAAILQTEVDALRLRLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1107 EQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLdeaggatqaqielnKKREAELAKLR- 1185
Cdd:pfam10174 357 KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQL--------------RDKDKQLAGLKe 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1186 --QDLEDAAINSETSMAALRKKhndavaeLSDQLDTIQKMRGKLEREKNDKQREVDELQqsadveaKQRQNCERMAKQLE 1263
Cdd:pfam10174 423 rvKSLQTDSSNTDTALTTLEEA-------LSEKERIIERLKEQREREDRERLEELESLK-------KENKDLKEKVSALQ 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1264 AQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHsQLEELKRTLDQETRERQSLHSQV 1343
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEV 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1344 SNY-------QLECEQFRESLEEEQDAKTD-----------VQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTH 1405
Cdd:pfam10174 568 ARYkeesgkaQAEVERLLGILREVENEKNDkdkkiaeleslTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDN 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1406 KVQEMQE-QLEnanQKIGTLEKNKQRLahdledaQVDADRANSIASSLEKKQKGFDKVLDEWRR--------KCEALVAE 1476
Cdd:pfam10174 648 LADNSQQlQLE---ELMGALEKTRQEL-------DATKARLSSTQQSLAEKDGHLTNLRAERRKqleeilemKQEALLAA 717
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 17561652 1477 VeqSQRETRAAATETFRLRNQleESGEQTEAVKRENKALAQELK 1520
Cdd:pfam10174 718 I--SEKDANIALLELSSSKKK--KTQEEVMALKREKDRLVHQLK 757
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1085-1678 |
5.31e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1085 EQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEeldAERNSrSKAEKARNEMQMELEELGDRLDEAG 1164
Cdd:PRK01156 118 EKNILGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEILEINS---LERNY-DKLKDVIDMLRAEISNIDYLEEKLK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1165 GATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKH--NDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQ 1242
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1243 QSADVEakqrqncERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRqLEDAEAQLCALnrikQQQHSQL 1322
Cdd:PRK01156 274 YYKELE-------ERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK-YHAIIKKLSVL----QKDYNDY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1323 EELKRTLDQETRERQSLHSQVSNYQleceqfreSLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRK 1402
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYN--------SYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1403 LTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLE-----------DAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCE 1471
Cdd:PRK01156 414 INVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1472 ALVAE-VEQSQRETRAAATETFRL---RNQLEESGEQTEAVKRENKALAqELKDIADQLGEGGKSVH--DLQK------- 1538
Cdd:PRK01156 494 DIDEKiVDLKKRKEYLESEEINKSineYNKIESARADLEDIKIKINELK-DKHDKYEEIKNRYKSLKleDLDSkrtswln 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1539 -MRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRkNHSRTIESMQVSLET---- 1613
Cdd:PRK01156 573 aLAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN-NKYNEIQENKILIEKlrgk 651
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1614 ------ESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESR 1678
Cdd:PRK01156 652 idnykkQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
849-1253 |
6.51e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 849 LIKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQA--LLIQLEQERDSSAEGEERSAKLLAQKADLE 926
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 927 KQMANMNDQLCDEEEKNAALTKQKkkiEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEK 1006
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1007 KHQEEVNRKLLEDIQAEedkvnhLNKTKAKLESTLDELEDTLEREK-----------RGRQDCEKQRRKVEGELKIAQEL 1075
Cdd:COG4717 237 EAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAgvlflvlgllaLLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1076 IEELNRHKHEQEQVIKKKDIELSSIQSRLEDeqslVAKLQRQIKELLARIQELEEELDAERNsrskaekaRNEMQMELEE 1155
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQELLREAEELEEELQLEEL--------EQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1156 LGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKH-NDAVAELSDQLDTIQKMRGKLEREKNDK 1234
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410
....*....|....*....
gi 17561652 1235 QREVDELQQSADVEAKQRQ 1253
Cdd:COG4717 459 EAELEQLEEDGELAELLQE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1163-1384 |
7.31e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1163 AGGATQAQIELNKKREAELAKLRQDLE------DAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQR 1236
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAelekelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1237 EVDELQQSadvEAKQRQNCERMAKQL----EAQLTDMTLKSDEQARLIQELTMgknkVHNENQDLNRQLEDAEAQLCALN 1312
Cdd:COG4942 91 EIAELRAE---LEAQKEELAELLRALyrlgRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1313 RIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAK 1384
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1191-1833 |
7.65e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1191 AAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMT 1270
Cdd:pfam12128 187 AMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1271 LKSDE-------------QARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCAlnriKQQQHSQLEELKRTLDQETRERQ 1337
Cdd:pfam12128 267 YKSDEtliasrqeerqetSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAK----DRSELEALEDQHGAFLDADIETA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1338 SLH-SQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEI-QQWRAKFEGEGvSRAEELEETRRKLTHKVQEMQEQLE 1415
Cdd:pfam12128 343 AADqEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIK-DKLAKIREARDRQLAVAEDDLQALE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1416 NA-----NQKIGTLEKNKQRLAHDLEDAQVDADRAnSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAA--- 1487
Cdd:pfam12128 422 SElreqlEAGKLEFNEEEYRLKSRLGELKLRLNQA-TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQArkr 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1488 ---ATETFRLRNQ-LEESGEQTEAVK---------------------REN--KALAQEL-------KDIADQLGEGGKSV 1533
Cdd:pfam12128 501 rdqASEALRQASRrLEERQSALDELElqlfpqagtllhflrkeapdwEQSigKVISPELlhrtdldPEVWDGSVGGELNL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1534 HDLQKMRRRLEIEK-----EELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKrLQEKEEEFENTRKNHSRTIESMQ 1608
Cdd:pfam12128 581 YGVKLDLKRIDVPEwaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK-ASREETFARTALKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1609 VSLETESRGRAELLKTKKKLegdVNELEIALDHSNKLNVDGQKSMKK-LQDTIRELQYQVEEEQRSLSESRDhanlaerr 1687
Cdd:pfam12128 660 DEKQSEKDKKNKALAERKDS---ANERLNSLEAQLKQLDKKHQAWLEeQKEQKREARTEKQAYWQVVEGALD-------- 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1688 sqvLQQEKEDLAIIYEQSERTRRQAELElaevKDSVNELSnsnslllatKRKVEGD-LQLLQSEIeeamsdaKTSDEKAK 1766
Cdd:pfam12128 729 ---AQLALLKAAIAARRSGAKAELKALE----TWYKRDLA---------SLGVDPDvIAKLKREI-------RTLERKIE 785
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1767 KAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKGGKRQLAKLDMRIHELE 1833
Cdd:pfam12128 786 RIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE 852
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
924-1521 |
8.17e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 924 DLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDneglKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSqdevISKLN 1003
Cdd:PRK01156 177 MLRAEISNIDYLEEKLKSSNLELENIKKQIADD----EKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE----LSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1004 KEKKHQEEVNRKLLEDIQAEEDKVNHLnktkAKLESTLDELEDTLEREKRGR-QDCEKQRRKVEGELKIAQELIEELNRH 1082
Cdd:PRK01156 249 DMKNRYESEIKTAESDLSMELEKNNYY----KELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1083 kheqeQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELlariQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDE 1162
Cdd:PRK01156 325 -----HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILEL----EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1163 AGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRkKHNDAVAELSDQL---------------DTIQKMRGKL 1227
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALR-ENLDELSRNMEMLngqsvcpvcgttlgeEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1228 EREKNDKQREVDELQqsadVEAKQRQNCERMAKQLEAQltdmtLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQ 1307
Cdd:PRK01156 475 NEKKSRLEEKIREIE----IEVKDIDEKIVDLKKRKEY-----LESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1308 LCALNRIKQQQHSQLEElkrtLDQETRERQSLHSQVSNYQLECEQFResleeeqdaKTDVQRQLSKANSEIQQWRAKFEG 1387
Cdd:PRK01156 546 DKYEEIKNRYKSLKLED----LDSKRTSWLNALAVISLIDIETNRSR---------SNEIKKQLNDLESRLQEIEIGFPD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1388 EGV---SRAEELEETRRKLTHKVQEMQE---QLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDK 1461
Cdd:PRK01156 613 DKSyidKSIREIENEANNLNNKYNEIQEnkiLIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDD 692
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1462 V---LDEWRRKCEALVAEVE-------------QSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKD 1521
Cdd:PRK01156 693 AkanRARLESTIEILRTRINelsdrindinetlESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRK 768
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1119-1553 |
8.41e-09 |
|
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: 61.12 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1119 KELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIE-LNKKREA-----ELAKLRQDLEDAA 1192
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhLNLVQTAlrqqeKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1193 INSEtsmaalrkKHNDAVAELSDQLDTiqkmrgkLEREKNDKQREVDELQ-QSADVEakqrqncermaKQLEAQltdmtl 1271
Cdd:COG3096 361 ERLE--------EQEEVVEEAAEQLAE-------AEARLEAAEEEVDSLKsQLADYQ-----------QALDVQ------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1272 ksdeQARLIQEltmgknkvhneNQDLNRqLEDAEaQLCALNRIKQQQHSQ-LEELKRTLDQETRERQSLHSQVSNYQLEC 1350
Cdd:COG3096 409 ----QTRAIQY-----------QQAVQA-LEKAR-ALCGLPDLTPENAEDyLAAFRAKEQQATEEVLELEQKLSVADAAR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1351 EQFRESLEEEQDAKTDVQRQ--LSKANSEIQQWRakfegEGVSRAEELEETRRKLthkvQEMQEQLENANQKIGTLEKNK 1428
Cdd:COG3096 472 RQFEKAYELVCKIAGEVERSqaWQTARELLRRYR-----SQQALAQRLQQLRAQL----AELEQRLRQQQNAERLLEEFC 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1429 QRLAHDLEDAQVdadransiasslekkqkgfdkvLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAV 1508
Cdd:COG3096 543 QRIGQQLDAAEE----------------------LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1509 KRENKALAQELKDIADQLGEGGKSVHDLQKMR-------RRLEIEKEELQQA 1553
Cdd:COG3096 601 APAWLAAQDALERLREQSGEALADSQEVTAAMqqllereREATVERDELAAR 652
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
957-1870 |
1.03e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 957 NEGLKKTVSDLETTIKKQESEKQAKDHQiRSLQDEIQsqdEVISK-----LNKEKKHQEEVNRKLLEDIQAEEDK---VN 1028
Cdd:PRK04863 225 NSGVRKAFQDMEAALRENRMTLEAIRVT-QSDRDLFK---HLITEstnyvAADYMRHANERRVHLEEALELRRELytsRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1029 HLNKTKAKLESTLDELEDTLEREKRGRQDCEKQR---------RKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSS 1099
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1100 IQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKAR---NEMQMELEELGDRLDEAggatQAQielnkk 1176
Cdd:PRK04863 381 NEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKqlcGLPDLTADNAEDWLEEF----QAK------ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1177 rEAELAKLRQDLEdaainSETSMAALRKKHNDAVAELsdqldtIQKMRGKLEREK-NDKQREVDELQQSADVEAKQRQnc 1255
Cdd:PRK04863 451 -EQEATEELLSLE-----QKLSVAQAAHSQFEQAYQL------VRKIAGEVSRSEaWDVARELLRRLREQRHLAEQLQ-- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1256 ermakQLEAQLTDMTLKSDEQA---RLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQE 1332
Cdd:PRK04863 517 -----QLRMRLSELEQRLRQQQraeRLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1333 TRERQSLHSQVS---NYQ--LE--CEQFRESLEEEQDAKTDVQRQLskanseiqqwrakfegegvSRAEELEETRRKLTH 1405
Cdd:PRK04863 592 QARIQRLAARAPawlAAQdaLArlREQSGEEFEDSQDVTEYMQQLL-------------------ERERELTVERDELAA 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1406 KVQEMQEQLENANQKIGTLEKNKQRLAHDL---------EDAQVD-----------------ADRANSIASSLEKKQKGF 1459
Cdd:PRK04863 653 RKQALDEEIERLSQPGGSEDPRLNALAERFggvllseiyDDVSLEdapyfsalygparhaivVPDLSDAAEQLAGLEDCP 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1460 DKVLdewrrkceaLVAEVEQSQRETRAAATETFR------LRNQLEESGEQTEAV----KREN--KALAQELKDIADQLg 1527
Cdd:PRK04863 733 EDLY---------LIEGDPDSFDDSVFSVEELEKavvvkiADRQWRYSRFPEVPLfgraAREKriEQLRAEREELAERY- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1528 egGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQievsqiRSEIEKRLQEKEEEfentrknhsrtiesm 1607
Cdd:PRK04863 803 --ATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLNRR------RVELERALADHESQ--------------- 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1608 qvsletESRGRAELLKTKKKLEGdVNELeiaLDHSNKLNVDGqksmkkLQDTIRELQYQV---EEEQRSLSESRDHANLA 1684
Cdd:PRK04863 860 ------EQQQRSQLEQAKEGLSA-LNRL---LPRLNLLADET------LADRVEEIREQLdeaEEAKRFVQQHGNALAQL 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1685 ERRSQVLQQEKEDLAII---YEQSERTRRQAELE---LAEVKDSVNELSNSNSLLLATKrkvEGDLQ-LLQSEIEEAMSD 1757
Cdd:PRK04863 924 EPIVSVLQSDPEQFEQLkqdYQQAQQTQRDAKQQafaLTEVVQRRAHFSYEDAAEMLAK---NSDLNeKLRQRLEQAEQE 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1758 AKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKGGKRQLAKL----DMRIHELE 1833
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHARlsanRSRRNQLE 1080
|
970 980 990
....*....|....*....|....*....|....*..
gi 17561652 1834 TELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKS 1870
Cdd:PRK04863 1081 KQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAG 1117
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1208-1891 |
1.05e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1208 DAVAELSDQLDTIQKMRGKLEREKndKQRE----VDELQQSADVEAKQRQNCERMAKQLEAQltDMTLKSDEQARLIQEL 1283
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAR--EQIEllepIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1284 TMGKNKVHNENQDLNRQLEDAEAQLCAL-NRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQD 1362
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1363 AKTDVQRQLSKANSEIQQWRakfegegvsraEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDa 1442
Cdd:COG4913 381 EFAALRAEAAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1443 dransIASSLEKKQkgfdkvlDEWRRKCEALvaEVEQSQRETRAAAtE----TFRLRNQLEEsgeqteavKRENKALAqe 1518
Cdd:COG4913 449 -----LAEALGLDE-------AELPFVGELI--EVRPEEERWRGAI-ErvlgGFALTLLVPP--------EHYAAALR-- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1519 lkdIADQLgeggksvhdlqKMRRRLEIEK-EELQQALDEAECALEAEEAKVmraQIEVSQIRSEIEKRLQ--------EK 1589
Cdd:COG4913 504 ---WVNRL-----------HLRGRLVYERvRTGLPDPERPRLDPDSLAGKL---DFKPHPFRAWLEAELGrrfdyvcvDS 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1590 EEEFENTRKnhSRTIESMqvsleTESRGRAELLKTKKKLEGDvneleialdhsnklNVDGQKSMKKLQdtirELQYQVEE 1669
Cdd:COG4913 567 PEELRRHPR--AITRAGQ-----VKGNGTRHEKDDRRRIRSR--------------YVLGFDNRAKLA----ALEAELAE 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1670 EQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTR--RQAELELAEVKDSVNELSNSNSlllatkrkvegDLQLL 1747
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSD-----------DLAAL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1748 QSEIEEAMSDAKTSDEKAKKAIMDASKLADELrseqehasnlnqskKTLESQVKDLQMRLDEAEAAGikggkrqlakldm 1827
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKEL--------------EQAEEELDELQDRLEAAEDLA------------- 743
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1828 rihELETELEGENRRHAETQKVLRNKDRkcRELQFQVDEDKKSQERmydLIEKLQQKIKTYKRQ 1891
Cdd:COG4913 744 ---RLELRALLEERFAAALGDAVERELR--ENLEERIDALRARLNR---AEEELERAMRAFNRE 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
860-1331 |
1.52e-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: 60.06 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 860 EALEKKFKVLEEEKTQEERKRKDMEAENARLEAekqaLLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDE 939
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ----FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDK 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 940 EEKNAALTKQKKKIEQD----NEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQE--EVN 1013
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcLTD 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1014 RKLLEDIQAE-EDKVNHLNKTKAKLESTldELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNrhkhEQEQVIKK 1092
Cdd:TIGR00606 791 VTIMERFQMElKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ----EQIQHLKS 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 KDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIE 1172
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 LNKKREAELAKLRQDL--------EDAAINSETSMAAL----------RKKHNDAVAELSDQLDTIQKMRGKLE-----R 1229
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIenkiqdgkDDYLKQKETELNTVnaqleecekhQEKINEDMRLMRQDIDTQKIQERWLQdnltlR 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1230 EKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEA--- 1306
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEkyr 1104
|
490 500
....*....|....*....|....*
gi 17561652 1307 QLCALNRIKQQQHSQLEELKRTLDQ 1331
Cdd:TIGR00606 1105 EMMIVMRTTELVNKDLDIYYKTLDQ 1129
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1312-1918 |
1.70e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1312 NRIKQQQhSQLEELKRTLDQETRERQSLHSQVSNYQ---LECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEgE 1388
Cdd:PRK03918 193 ELIKEKE-KELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-E 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 GVSRAEELEETRRKLTH------KVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKV 1462
Cdd:PRK03918 271 LKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1463 ------LDEWRRKCEALVAEVEQSQR-ETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHD 1535
Cdd:PRK03918 351 ekrleeLEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1536 LQKMRRRLEIEKEELQQaldeaecalEAEEAKVMRAQIEVSQIRSEIeKRLQEKEEEFENTRKNhsrtiesmqvsLETES 1615
Cdd:PRK03918 431 LKKAKGKCPVCGRELTE---------EHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRE-----------LEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1616 RGRAELLKTKKKLEgdvnELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEK 1695
Cdd:PRK03918 490 KKESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1696 EDLaiiyeqsertrrqaELELAEVKDSVNELSNSnslllaTKRKVEGDLQLLQSEIEE--AMSDAKTSDEKAKKAImdaS 1773
Cdd:PRK03918 566 DEL--------------EEELAELLKELEELGFE------SVEELEERLKELEPFYNEylELKDAEKELEREEKEL---K 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1774 KLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKggkRQLAKLDMRIHELETELEGENRRHAETQKVLRNK 1853
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR---EEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1854 DR---KCRELQFQVDEDKKSQERMYDLIEklqqKIKTYKrqiedaeslasgNLAKYRQLQHVVEDAQE 1918
Cdd:PRK03918 700 KEeleEREKAKKELEKLEKALERVEELRE----KVKKYK------------ALLKERALSKVGEIASE 751
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
975-1522 |
2.57e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.98 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 975 ESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRG 1054
Cdd:pfam05557 33 EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1055 RQDCEKQRRKVEGELKIAQELIEELNrhkhEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEelDA 1134
Cdd:pfam05557 113 LSELRRQIQRAELELQSTNSELEELQ----ERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ--DS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1135 ERNSRSKAEKAR-NEMQMELEelgdRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETsMAALRKKHNDAVAEL 1213
Cdd:pfam05557 187 EIVKNSKSELARiPELEKELE----RLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1214 SDQLDTIQKMRGKLeREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNE 1293
Cdd:pfam05557 262 QSWVKLAQDTGLNL-RSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1294 NQDLNRQLEDAEAQLCALNRIKQQQHSQLEElKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSK 1373
Cdd:pfam05557 341 VRRLQRRVLLLTKERDGYRAILESYDKELTM-SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1374 ANSEIQQWRAKFEGEGVSRA-EELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSL 1452
Cdd:pfam05557 420 LERELQALRQQESLADPSYSkEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAY 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1453 EKKQKGFDKVLDE---WRRKCEALVAEVEQSQRETRAAATETFR----LRNQLEESGEQTEAVKRENKALAQELKDI 1522
Cdd:pfam05557 500 QQRKNQLEKLQAEierLKRLLKKLEDDLEQVLRLPETTSTMNFKevldLRKELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1236-1897 |
2.68e-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: 58.96 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1236 REVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVH-------NENQDLNRQlEDAEAQL 1308
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSlkleeeiQENKDLIKE-NNATRHL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1309 CalNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGE 1388
Cdd:pfam05483 157 C--NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 GVSRAEELEETRRKLTHKVQEMQEQ---LENANQKIGTLEKN--------------KQRLAHDLEDAQVDADRANSIASS 1451
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKtklqdenlkeliekKDHLTKELEDIKMSLQRSMSTQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1452 LEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESgEQTEAVKRENKAlaQELKDIADQLGEGGK 1531
Cdd:pfam05483 315 LEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL-LRTEQQRLEKNE--DQLKIITMELQKKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1532 SVHDLQKMRRRLEIEKEELQQALdeaecaleAEEAKVMRAQIEVSQIRSEiekrLQEKEEEFENTRKNHSRTIESMQVSL 1611
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKIL--------AEDEKLLDEKKQFEKIAEE----LKGKEQELIFLLQAREKEIHDLEIQL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1612 ETESRGRAELLKTKKKLEGDVNELEIA----LDHSNKLNVDGQKSMKKLQDTIRELQYQVEeeqrslsesrDHANLAERR 1687
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKnielTAHCDKLLLENKELTQEASDMTLELKKHQE----------DIINCKKQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1688 SQVLQQekedlaiiYEQSERTRRQAELELAEVKDSvnelsnsnslllatkrkvegdlqlLQSEIEEAMSDAKTSDEKAKK 1767
Cdd:pfam05483 530 ERMLKQ--------IENLEEKEMNLRDELESVREE------------------------FIQKGDEVKCKLDKSEENARS 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1768 AIMDASKLADELRSEQEHASNLnqsKKTLESQVKDLQMRLDEAEAAGIKGG--KRQLAKLDMRIHELETELEGENRRHAE 1845
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNL---KKQIENKNKNIEELHQENKALKKKGSaeNKQLNAYEIKVNKLELELASAKQKFEE 654
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1846 TQKVLRN--KDRKCRE-----------------LQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDAES 1897
Cdd:pfam05483 655 IIDNYQKeiEDKKISEeklleevekakaiadeaVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDS 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1685-1940 |
2.81e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1685 ERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSLLLATK-RKVEGDLQLLQSEIEEAMSDAKTSDE 1763
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1764 KAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLD------EAEAAGIKGGKRQLAKLDMRIHELETELE 1837
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraelEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1838 GENRRHAETQKVLRNKDRKCRELQFQV----DEDKKSQERMYDL---IEKLQQKIKTYKRQIEDAESLASGNLAKYRQLQ 1910
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIagieAKINELEEEKEDKaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
250 260 270
....*....|....*....|....*....|
gi 17561652 1911 HVVEDAQERADAAENALQKLRLKGRSTSGV 1940
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
857-1517 |
2.86e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 857 EEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQL 936
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 937 cdeeeknAALTKQKKKIEQDNEGLKKTVSDLETTIKKQ-ESEKQAKDHQIRSLQDEIQSQDEVISKLnkekKHQEEVNRK 1015
Cdd:COG4913 312 -------ERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAAL----GLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1016 LLEDIQAEedkvnhLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELK--------IAQELIEelNRHKHEQE 1087
Cdd:COG4913 381 EFAALRAE------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrksnIPARLLA--LRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1088 QVIKKKDI----ELssIQSRLEDEQ-----------------------SLVAKLQRQIKeLLARIQ------ELEEELDA 1134
Cdd:COG4913 453 LGLDEAELpfvgEL--IEVRPEEERwrgaiervlggfaltllvppehyAAALRWVNRLH-LRGRLVyervrtGLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1135 ERNSRSKAEK---ARNEMQMELE-ELGDRLDEAGGATQAQielnkkreaelakLRQdlEDAAINSE--TSMAALRKKHND 1208
Cdd:COG4913 530 RLDPDSLAGKldfKPHPFRAWLEaELGRRFDYVCVDSPEE-------------LRR--HPRAITRAgqVKGNGTRHEKDD 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1209 AVAELS---------DQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLtDMTLKSDEQARL 1279
Cdd:COG4913 595 RRRIRSryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1280 IQELtmgknkvhnenqdlnRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEE 1359
Cdd:COG4913 674 EAEL---------------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1360 EQDAKTDVQRQLskanseiqqWRAKFEGEGVSRAEelEETRRKLTHKVQEMQEQLENANQKIgtlekNKQRLAHDLEDAQ 1439
Cdd:COG4913 739 AEDLARLELRAL---------LEERFAAALGDAVE--RELRENLEERIDALRARLNRAEEEL-----ERAMRAFNREWPA 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1440 VDADRANSIASslekkqkgfdkvLDEWRRKCEALVA----EVEQSQRETRAAATETFR--LRNQLEESGEQ-TEAVKREN 1512
Cdd:COG4913 803 ETADLDADLES------------LPEYLALLDRLEEdglpEYEERFKELLNENSIEFVadLLSKLRRAIREiKERIDPLN 870
|
....*
gi 17561652 1513 KALAQ 1517
Cdd:COG4913 871 DSLKR 875
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
863-1143 |
2.90e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 863 EKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEK 942
Cdd:pfam07888 58 EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 943 NAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQA 1022
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1023 EEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVikkkDIELSSIQS 1102
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL----TLQLADASL 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1103 RLEDEQSLVAK----LQR-------QIKELLARIQELEEELDAERNSRSKAE 1143
Cdd:pfam07888 294 ALREGRARWAQeretLQQsaeadkdRIEKLSAELQRLEERLQEERMEREKLE 345
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
863-1231 |
4.05e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 863 EKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLE--QERDSSAEGEERSAKLLAQKADLEKQMANMndqlcdeE 940
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERL-------D 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 941 EKNAALTKQKKKIEQdnegLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEevnRKLLEDI 1020
Cdd:COG4913 682 ASSDDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL---RALLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1021 QAEEDKVNHLNKTKAKLESTLDELEDTLEREkrgrqdcekqrrkvegelkiAQELIEELNRHKHEQeqvikkkDIELSSI 1100
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRA--------------------EEELERAMRAFNREW-------PAETADL 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1101 QSRLEDEQSLVAKLQRQIKELLAriqELEEELDAERNSRSKAEKAR--NEMQMELEELGDRLDEA---------GGATQA 1169
Cdd:COG4913 808 DADLESLPEYLALLDRLEEDGLP---EYEERFKELLNENSIEFVADllSKLRRAIREIKERIDPLndslkripfGPGRYL 884
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1170 QIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREK 1231
Cdd:COG4913 885 RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
990-1455 |
9.58e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.61 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 990 DEIQSQdevISKLNKEKKHQEEVNR---------KLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEK 1060
Cdd:PRK11281 39 ADVQAQ---LDALNKQKLLEAEDKLvqqdleqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1061 QRRkveGELKIAQeLIEELNRHKHEQEQVIKkkdiELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAER-NSR 1139
Cdd:PRK11281 116 ETL---STLSLRQ-LESRLAQTLDQLQNAQN----DLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKvGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1140 SKAEKARNEMQMELEELgdrldeaggatQAQIELNKKrEAELAKLRQDLedaainsetsmaaLRKKHNdavaELSDQLDT 1219
Cdd:PRK11281 188 ALRPSQRVLLQAEQALL-----------NAQNDLQRK-SLEGNTQLQDL-------------LQKQRD----YLTARIQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1220 IQKMRGKLEREKNDKQREVDELQ----QSADVEAKQRQNcERMAKQLEA--QLTDMTLKSDEQA-RLIQELTMGKNKVHN 1292
Cdd:PRK11281 239 LEHQLQLLQEAINSKRLTLSEKTvqeaQSQDEAARIQAN-PLVAQELEInlQLSQRLLKATEKLnTLTQQNLRVKNWLDR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1293 ENQDlNRQLEDaeaQLCA------LNRIKQQQhsqleelKRTLDQETrERQSLHSQVSN---YQLECEQFREsleeeqda 1363
Cdd:PRK11281 318 LTQS-ERNIKE---QISVlkgsllLSRILYQQ-------QQALPSAD-LIEGLADRIADlrlEQFEINQQRD-------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1364 ktdvqrQLSKANSEIQQWRAKfegegvSRAEELEETRRKLTHKVQEMQEQLENANQKIG-------TLEKNKQRLahdle 1436
Cdd:PRK11281 378 ------ALFQPDAYIDKLEAG------HKSEVTDEVRDALLQLLDERRELLDQLNKQLNnqlnlaiNLQLNQQQL----- 440
|
490
....*....|....*....
gi 17561652 1437 daqvdadraNSIASSLEKK 1455
Cdd:PRK11281 441 ---------LSVSDSLQST 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1295-1908 |
1.13e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1295 QDLNR---QLEDAEAQLCALNRIKQ---------QQHSQLEELKRTLDQETRERQslhsqVSNYQLECEQFRESLEEEQD 1362
Cdd:COG4913 235 DDLERaheALEDAREQIELLEPIRElaeryaaarERLAELEYLRAALRLWFAQRR-----LELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1363 AKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEknkQRLAHDLEDAQVDA 1442
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1443 DRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQREtraaatetfrlRNQLEESG----EQTEAVKrenKALAQE 1518
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE-----------IASLERRKsnipARLLALR---DALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1519 LKDIADQL---GE-------------------GG----------------KSVHDLqKMRRRLEIEK-EELQQALDEAEC 1559
Cdd:COG4913 453 LGLDEAELpfvGElievrpeeerwrgaiervlGGfaltllvppehyaaalRWVNRL-HLRGRLVYERvRTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1560 ALEAEEAKVmraQIEVSQIRSEIEKRLQ--------EKEEEFENTRKnhSRTIESMqvsleTESRGRAELLKTKKKLEGD 1631
Cdd:COG4913 532 DPDSLAGKL---DFKPHPFRAWLEAELGrrfdyvcvDSPEELRRHPR--AITRAGQ-----VKGNGTRHEKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1632 vneleialdhsnklNVDGQKSMKKLQdtirELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTR-- 1709
Cdd:COG4913 602 --------------YVLGFDNRAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdv 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1710 RQAELELAEVKDSVNELSNSNSlllatkrkvegDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELrseqehasnl 1789
Cdd:COG4913 664 ASAEREIAELEAELERLDASSD-----------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL---------- 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1790 nqskKTLESQVKDLQMRLDEAEAAGikggkrqlakldmrihELETELEGENRRHAETQkvlrnkdrkcrelqfqvdedkk 1869
Cdd:COG4913 723 ----EQAEEELDELQDRLEAAEDLA----------------RLELRALLEERFAAALG---------------------- 760
|
650 660 670
....*....|....*....|....*....|....*....
gi 17561652 1870 sQERMYDLIEKLQQKIKTYKRQIEDAESLASGNLAKYRQ 1908
Cdd:COG4913 761 -DAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1474-1920 |
1.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1474 VAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLgeggkSVHDLQKMRRRLEIEKEELQQA 1553
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1554 LDEAECALEAEEakvmRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVN 1633
Cdd:COG4717 148 LEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1634 ELEIALDhsnklNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQV-----------------LQQEKE 1696
Cdd:COG4717 224 ELEEELE-----QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgllallfllLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1697 DLAIIYEQSERTRRQAELELAEVKDSVNEL----SNSNSLLLATKRKVEgDLQLLQSEIEEAMSDAKTSD-EKAKKAIMD 1771
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIE-ELQELLREAEELEEELQLEElEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1772 ASKLADElrSEQEHASNLNQSKKTLESQVKDLQMRLDE-AEAAGIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVL 1850
Cdd:COG4717 378 EAGVEDE--EELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1851 rnkdrkcRELQFQVDEDKKSQErmydlIEKLQQKIKTYKRQIEDAESLAsgnlAKYRQLQHVVEDAQERA 1920
Cdd:COG4717 456 -------AELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEW----AALKLALELLEEAREEY 509
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
984-1231 |
1.21e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.56 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 984 QIRSLQDEIQSQD----EVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLErekrgrqDCE 1059
Cdd:PHA02562 175 KIRELNQQIQTLDmkidHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELL-------NLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1060 KQRRKVEGEL-KIAQELIEELNRHKHEQ-EQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAErn 1137
Cdd:PHA02562 248 MDIEDPSAALnKLNTAAAKIKSKIEQFQkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1138 srSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAELAKLRQDledaainsetsmaalRKKHNDAVAELSDQL 1217
Cdd:PHA02562 326 --EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE---------------FVDNAEELAKLQDEL 388
|
250
....*....|....
gi 17561652 1218 DTIQKMRGKLEREK 1231
Cdd:PHA02562 389 DKIVKTKSELVKEK 402
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
947-1802 |
1.95e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.60 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 947 TKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKhqeEVNRKLLEDIqaeeDK 1026
Cdd:TIGR01612 522 SKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIK---DLFDKYLEID----DE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1027 VNHLNKTKAKLESTLDELEDTLEREKRGRQdcekQRRKVEGElkiaQELIEELNR-HKHEQEQVIKKKDIELSSIQSRL- 1104
Cdd:TIGR01612 595 IIYINKLKLELKEKIKNISDKNEYIKKAID----LKKIIENN----NAYIDELAKiSPYQVPEHLKNKDKIYSTIKSELs 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1105 ----EDEQSLVAKLQRQIKELLARIQELEEELDaerNSRSKAEKARNEMQ-MELEELGDRL----DEAGGATQAQIELNK 1175
Cdd:TIGR01612 667 kiyeDDIDALYNELSSIVKENAIDNTEDKAKLD---DLKSKIDKEYDKIQnMETATVELHLsnieNKKNELLDIIVEIKK 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1176 KREAELAK-LRQDLEDAainsETSMAALRKKHNDaVAELSDQLDTIQKMRGKLEREKNDkQREVDELQqsaDVEAKQRQN 1254
Cdd:TIGR01612 744 HIHGEINKdLNKILEDF----KNKEKELSNKIND-YAKEKDELNKYKSKISEIKNHYND-QINIDNIK---DEDAKQNYD 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1255 cermakQLEAQLTDMTLKSDEQARLIQELTMGK-------NKVHNENQDLNRQLEDAEAQLCAL-NRIKQQ--------- 1317
Cdd:TIGR01612 815 ------KSKEYIKTISIKEDEIFKIINEMKFMKddflnkvDKFINFENNCKEKIDSEHEQFAELtNKIKAEisddklndy 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1318 ------QHSQLEELKRTLDQETRERQSLhSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSK-------ANSEIQQWRAK 1384
Cdd:TIGR01612 889 ekkfndSKSLINEINKSIEEEYQNINTL-KKVDEYIKICENTKESIEKFHNKQNILKEILNKnidtikeSNLIEKSYKDK 967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1385 FEGEGVSRAEELEETRRKLT-----HKVQEMQEQLENANQKIGTLEKN--------KQRLAHDLEDAQVDADRANS---- 1447
Cdd:TIGR01612 968 FDNTLIDKINELDKAFKDASlndyeAKNNELIKYFNDLKANLGKNKENmlyhqfdeKEKATNDIEQKIEDANKNIPniei 1047
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1448 -IASSLEKKqkgFDKVLDEWRRKCEALVAEVeqsQRETRAAATETFRLRNQLEESgEQTEAVKRENKALAQELKDIADQL 1526
Cdd:TIGR01612 1048 aIHTSIYNI---IDEIEKEIGKNIELLNKEI---LEEAEINITNFNEIKEKLKHY-NFDDFGKEENIKYADEINKIKDDI 1120
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1527 G----EGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQirSEIEKRLQEKEEEFENTRK--NH 1600
Cdd:TIGR01612 1121 KnldqKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKI--ENIVTKIDKKKNIYDEIKKllNE 1198
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1601 SRTIESMQVSLE-----TESRGRA-------ELLKTKKKLEGDVNELEIALDHSNKLNvdgQKSMKKLQDTIRELQYQVE 1668
Cdd:TIGR01612 1199 IAEIEKDKTSLEevkgiNLSYGKNlgklfleKIDEEKKKSEHMIKAMEAYIEDLDEIK---EKSPEIENEMGIEMDIKAE 1275
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1669 EEQRSLSESRD----------HANLAERRSQVLQ-----QEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSN-SNSL 1732
Cdd:TIGR01612 1276 METFNISHDDDkdhhiiskkhDENISDIREKSLKiiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiYNIL 1355
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1733 LLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAImdaSKLADElrseqehaSNLNQSKKTLESQVKD 1802
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI---KKIKDD--------INLEECKSKIESTLDD 1414
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1001-1270 |
2.39e-07 |
|
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: 55.80 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1001 KLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEdtlEREKRGRQDCEKQRRKVEGELKIAQE---LIE 1077
Cdd:pfam05667 241 RKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFS---GSSTTDTGLTKGSRFTHTEKLQFTNEapaATS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1078 ELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELG 1157
Cdd:pfam05667 318 SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1158 DrLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINsetSMAALRKKHNDAVAELSDQLDTIQKMRgklerekndkqre 1237
Cdd:pfam05667 398 D-AEENIAKLQALVDASAQRLVELAGQWEKHRVPLIE---EYRALKEAKSNKEDESQRKLEEIKELR------------- 460
|
250 260 270
....*....|....*....|....*....|...
gi 17561652 1238 vDELQQSADvEAKQRqncERMAKQLEAQLTDMT 1270
Cdd:pfam05667 461 -EKIKEVAE-EAKQK---EELYKQLVAEYERLP 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1260-1715 |
2.63e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1260 KQLEAQLTDMTLKSDEQARLIQELtmgknkvhnenQDLNRQLEDAEAQLCALnrikQQQHSQLEELKRTLDQEtRERQSL 1339
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEEL-----------EELEEELEELEAELEEL----REELEKLEKLLQLLPLY-QELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1340 HSQVSNYQLECEQFRESLEEEQDAktdvQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQ 1419
Cdd:COG4717 138 EAELAELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1420 KIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQK-----------GFDKVLDEWRRKCEALVAEVEQSqreTRAAA 1488
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallGLGGSLLSLILTIAGVLFLVLGL---LALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1489 TETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLG-EGGKSVHDLQKMRRRLEIEKEELQQALDeaecaleaeeak 1567
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEE------------ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1568 vMRAQIEVSQIRSEIEKRLQ----EKEEEFE------NTRKNHSRTIESMQVSLETESRGRAELLK--TKKKLEGDVNEL 1635
Cdd:COG4717 359 -LEEELQLEELEQEIAALLAeagvEDEEELRaaleqaEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1636 EIALDhsnklnvDGQKSMKKLQDTIRELQYQVE--EEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAE 1713
Cdd:COG4717 438 EEELE-------ELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
..
gi 17561652 1714 LE 1715
Cdd:COG4717 511 EE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1205-1500 |
2.81e-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: 55.90 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1205 KHNDAVAELSDQlDTIQKM-RGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEaqltdmtlksdEQARLIQEl 1283
Cdd:pfam17380 279 QHQKAVSERQQQ-EKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYA-----------EQERMAME- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1284 tmgknkvhnENQDLNR-QLEDAEAQLcalNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNyQLECEQFRESLEEEQd 1362
Cdd:pfam17380 346 ---------RERELERiRQEERKREL---ERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKILEEER- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1363 aktdvQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKV----QEMQEQLENANQKigtlEKNKQRLAHDLEDA 1438
Cdd:pfam17380 412 -----QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVrleeQERQQQVERLRQQ----EEERKRKKLELEKE 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1439 QVDADRANSIASS-LEKKQKGFDKVLDEWRRKCEALVAEVEQSQR-----ETRAAATETFRLRNQLEE 1500
Cdd:pfam17380 483 KRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEMEERQKaiyeeERRREAEEERRKQQEMEE 550
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
957-1873 |
2.89e-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: 56.11 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 957 NEGLKKTVSDLETTIKKQESEKQAkdhqIRslqdEIQSQDEVISKLNKEK---------KHQEEVNRKLLEDIQAEED-- 1025
Cdd:COG3096 224 NSGVRKAFQDMEAALRENRMTLEA----IR----VTQSDRDLFKHLITEAtnyvaadymRHANERRELSERALELRRElf 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1026 -KVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQR---RKVEGELKiAQELIEelnrhkHEQEqvikkkdiELSSIQ 1101
Cdd:COG3096 296 gARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASdhlNLVQTALR-QQEKIE------RYQE--------DLEELT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1102 SRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQ---MELEELGDRLDEAGGATQAQIELNKKRE 1178
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQtraIQYQQAVQALEKARALCGLPDLTPENAE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1179 AELAKLRQDLEDAainsETSMAALRKKHND---AVAELSDQLDTIQKMRGKLEREK-NDKQREVdeLQQSADVEAKQRQn 1254
Cdd:COG3096 441 DYLAAFRAKEQQA----TEEVLELEQKLSVadaARRQFEKAYELVCKIAGEVERSQaWQTAREL--LRRYRSQQALAQR- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1255 cermAKQLEAQLTDMTLKSDEQA---RLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQ 1331
Cdd:COG3096 514 ----LQQLRAQLAELEQRLRQQQnaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1332 ETRERQSLHSQ-----VSNYQLE--CEQFRESLEEEQDAKTDVQRQLSkanseiqqwrakfegegvsRAEELEETRRKLT 1404
Cdd:COG3096 590 LRARIKELAARapawlAAQDALErlREQSGEALADSQEVTAAMQQLLE-------------------REREATVERDELA 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1405 HKVQEMQEQLENANQKIGTLEKNKQRLAHDL---------EDAQVD-----------------ADRANSIASSLEKKQKG 1458
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALAERLggvllseiyDDVTLEdapyfsalygparhaivVPDLSAVKEQLAGLEDC 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1459 FDKVL---------DEWRRKCE----ALVAEVEQSQ-RETR--------AAATEtfrlrnqleesgEQTEAVKRENKALA 1516
Cdd:COG3096 731 PEDLYliegdpdsfDDSVFDAEeledAVVVKLSDRQwRYSRfpevplfgRAARE------------KRLEELRAERDELA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1517 QELKDIAdqlgeggksvHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQievsqiRSEIEKRLQEKEEEfent 1596
Cdd:COG3096 799 EQYAKAS----------FDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQR------RSELERELAQHRAQ---- 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1597 rknhsrtiESMQVSLETESRGRAELLktkKKLEGDVNELEIAlDHSNKLnvdgqksmkklqDTIRELQYQVEEEQRSLSE 1676
Cdd:COG3096 859 --------EQQLRQQLDQLKEQLQLL---NKLLPQANLLADE-TLADRL------------EELREELDAAQEAQAFIQQ 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1677 SRDHANLAERRSQVLQ---QEKEDLAIIYEQSERTRRQAE---LELAEV---------KDSVNELSNSNSLLLATKRKVE 1741
Cdd:COG3096 915 HGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKqqiFALSEVvqrrphfsyEDAVGLLGENSDLNEKLRARLE 994
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1742 gdlqllqsEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHAsnlNQSKKTLESQVKDLQMRLDEAEAAGIKGGKR- 1820
Cdd:COG3096 995 --------QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAK---QQTLQELEQELEELGVQADAEAEERARIRRDe 1063
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1821 ---QLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQER 1873
Cdd:COG3096 1064 lheELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCA 1119
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1014-1717 |
3.17e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1014 RKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQrrkvegelkiAQELIEELNRHKHEQEQvIKKK 1093
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQ----------AAEAVEQRSELRQQLEQ-LRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1094 DIELSSIQSRLEDEQSLVAKLQRQIKELLARIQEL----EEELDAERN---SRSKAEKARNEMQMELEelgdRLDEAGGA 1166
Cdd:COG3096 594 IKELAARAPAWLAAQDALERLREQSGEALADSQEVtaamQQLLEREREatvERDELAARKQALESQIE----RLSQPGGA 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1167 tqAQIELNKKREAELAKLRQDL-EDAAINSETSMAALR--KKHNDAVAELS---DQLDTIQKMRGKL---EREKN---DK 1234
Cdd:COG3096 670 --EDPRLLALAERLGGVLLSEIyDDVTLEDAPYFSALYgpARHAIVVPDLSavkEQLAGLEDCPEDLyliEGDPDsfdDS 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1235 QREVDELQQSADVEAKQRQ----------NCERMAKqlEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQD-------- 1296
Cdd:COG3096 748 VFDAEELEDAVVVKLSDRQwrysrfpevpLFGRAAR--EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfsqfvggh 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1297 ---------------LNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRerqsLHSQVS-----NYQLECEQFRES 1356
Cdd:COG3096 826 lavafapdpeaelaaLRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNK----LLPQANlladeTLADRLEELREE 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1357 LEEEQDAKTDVQRQlskanseiqqwrakfeGEGVSRAEELEETRRK-------LTHKVQEMQEQLENANQKIGTLEKNKQ 1429
Cdd:COG3096 902 LDAAQEAQAFIQQH----------------GKALAQLEPLVAVLQSdpeqfeqLQADYLQAKEQQRRLKQQIFALSEVVQ 965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1430 RLAH-DLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQREtRAAATETFRLRNQleesgeqteav 1508
Cdd:COG3096 966 RRPHfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQV-LASLKSSRDAKQQ----------- 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1509 krENKALAQELKDIAdqlgeggksVHDLQKMRRRLEIEKEELQQALdeaecaleaeeaKVMRAQievsqiRSEIEKRLQE 1588
Cdd:COG3096 1034 --TLQELEQELEELG---------VQADAEAEERARIRRDELHEEL------------SQNRSR------RSQLEKQLTR 1084
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1589 KEEEFENTRKNHSRtiesmqvsLETESRGRAELLKTKKKLEGDVneLEIALDHsnklnvDGQKSMKKlqdtiRELQYQVE 1668
Cdd:COG3096 1085 CEAEMDSLQKRLRK--------AERDYKQEREQVVQAKAGWCAV--LRLARDN------DVERRLHR-----RELAYLSA 1143
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 17561652 1669 EEQRSLSesrDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELA 1717
Cdd:COG3096 1144 DELRSMS---DKALGALRLAVADNEHLRDALRLSEDPRRPERKVQFYIA 1189
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
853-1339 |
3.85e-07 |
|
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: 55.14 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKrkdMEAENARLEAEKQAlliqleqERDSSAEGEERSAKLlAQKADLEKQMANM 932
Cdd:pfam07111 69 SRQLQELRRLEEEVRLLRETSLQQKMR---LEAQAMELDALAVA-------EKAGQAEAEGLRAAL-AGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQLCDE-----EEKNAALTKQKKK----IEQDNEGLKKTVSDLET-------TIKKQESEKQAKDHQIRSLQDEIQSQD 996
Cdd:pfam07111 138 SQRELEEiqrlhQEQLSSLTQAHEEalssLTSKAEGLEKSLNSLETkrageakQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 997 EVISKLNKEKKHQ--EEVNRKLLEDIQAEE-DKVNHLNKTKAKLESTLDEL--------------EDTLEREKRGRQDCE 1059
Cdd:pfam07111 218 TLVESLRKYVGEQvpPEVHSQTWELERQELlDTMQHLQEDRADLQATVELLqvrvqslthmlalqEEELTRKIQPSDSLE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1060 KQ-RRKVEGELKIAQE----LIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQ-------E 1127
Cdd:pfam07111 298 PEfPKKCRSLLNRWREkvfaLMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEvermsakG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1128 LEEELDAERNSRSKAEK--------------ARNEMQMELEELGDRLDEAGGATQA-------------QIELNKKREAE 1180
Cdd:pfam07111 378 LQMELSRAQEARRRQQQqtasaeeqlkfvvnAMSSTQIWLETTMTRVEQAVARIPSlsnrlsyavrkvhTIKGLMARKVA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1181 LAKLRQD---LEDAAINSETSMAA----LRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQ 1253
Cdd:pfam07111 458 LAQLRQEscpPPPPAPPVDADLSLeleqLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQ 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1254 -NCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKN--------KVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEE 1324
Cdd:pfam07111 538 eSLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqeKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQ 617
|
570
....*....|....*
gi 17561652 1325 LKRTLDQETRERQSL 1339
Cdd:pfam07111 618 IQHRATQEKERNQEL 632
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1155 |
4.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 850 IKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAekqalLIQLEQERDSSAEGEERSAKLLAQKAdlekqm 929
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-----LVEAEDRIERLEERREDLEELIAERR------ 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 930 anmnDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSdlettikKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEkkhq 1009
Cdd:PRK02224 530 ----ETIEEKRERAEELRERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAELKERIESLERI---- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1010 eevnRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLErekrgrqdcEKQRRKVEGELKIAQELIEELNRHKHEQEQV 1089
Cdd:PRK02224 595 ----RTLLAAIADAEDEIERLREKREALAELNDERRERLA---------EKRERKRELEAEFDEARIEEAREDKERAEEY 661
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1090 IKKKDIELSSIQSRLEDEQSLVAKLQRQIKELlariQELEEELDAERNSRSKAEKARNEMQmELEE 1155
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREALENRVEALEALYDEAE-ELES 722
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1070-1378 |
5.90e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1070 KIAQELIEELNRHKHEQEQVIKKKDIeLSSIQSRLEDEQ---------SLVAKLQRQIKELLARIQELEEELDAERNsRS 1140
Cdd:COG3206 94 PVLERVVDKLNLDEDPLGEEASREAA-IERLRKNLTVEPvkgsnvieiSYTSPDPELAAAVANALAEAYLEQNLELR-RE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1141 KAEKARNEMQMELEELGDRLDEAggatqaqielnkkrEAELAKLRQ-----DLEDAAINSETSMAALRKKHNDAVAELSD 1215
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEA--------------EAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1216 QLDTIQKMRGKLEREKNdkqrEVDELQQSADVEAKQRQncermAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNE-N 1294
Cdd:COG3206 238 AEARLAALRAQLGSGPD----ALPELLQSPVIQQLRAQ-----LAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1295 QDLNRQLEDAEAQLCALNRIKQQQHSQLEELK---RTLDQETRERQSLHSQVSNYQLECEQFRESLEEeqdakTDVQRQL 1371
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEarlAELPELEAELRRLEREVEVARELYESLLQRLEE-----ARLAEAL 383
|
....*..
gi 17561652 1372 SKANSEI 1378
Cdd:COG3206 384 TVGNVRV 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1142-1363 |
5.91e-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: 54.00 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1142 AEKARNEMQMELEELGDRLDEaggaTQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQ 1221
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1222 KMRGKLEREKNDKQREVDELQQSADVE--------------AKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTmgk 1287
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1288 nkvhNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDA 1363
Cdd:COG4942 171 ----AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
853-1036 |
5.96e-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: 54.00 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAE--------GEERSAKLLAQKAD 924
Cdd:COG4942 51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlGRQPPLALLLSPED 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 925 LEkQMANMNDQLcdeEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNK 1004
Cdd:COG4942 131 FL-DAVRRLQYL---KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|..
gi 17561652 1005 EKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAK 1036
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1033-1358 |
6.04e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.91 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1033 TKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQsrLEDEQSLVA 1112
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQ--LEDLVGMIQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1113 KLQRQIKEL-LARIQELEEeLDAERNSRSKAEKARNEMQMELEELGDRLDEAGgATQAQIELNkkrEAELAKLRQDLEDA 1191
Cdd:PLN02939 139 NAEKNILLLnQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAA-QEKIHVEIL---EEQLEKLRNELLIR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1192 AINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLErekndkqrEVDELQQSADVEAKQRQNCERMAKQLEAQL----T 1267
Cdd:PLN02939 214 GATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELI--------EVAETEERVFKLEKERSLLDASLRELESKFivaqE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1268 DM----TLKSD---EQARLIQE-LTMGKNKVHN------ENQDLNRQLEDAEAQLCALNRIK---------QQQHSQLEE 1324
Cdd:PLN02939 286 DVsklsPLQYDcwwEKVENLQDlLDRATNQVEKaalvldQNQDLRDKVDKLEASLKEANVSKfssykvellQQKLKLLEE 365
|
330 340 350
....*....|....*....|....*....|....
gi 17561652 1325 LKRTLDQETrerqslHSQVSNYQLECEQFRESLE 1358
Cdd:PLN02939 366 RLQASDHEI------HSYIQLYQESIKEFQDTLS 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1094-1346 |
6.18e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1094 DIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDaernsrsKAEKARNEMQMELEELGDRLDEAggatQAQIEl 1173
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIAEA----EAEIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1174 nkKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADveaKQRQ 1253
Cdd:COG3883 83 --ERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE---AKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1254 NCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQET 1333
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|...
gi 17561652 1334 RERQSLHSQVSNY 1346
Cdd:COG3883 238 AAAAAAASAAGAG 250
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1319-1896 |
6.77e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1319 HSQLEELKRTLDQET----RERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQqwrakfegEGVSRAE 1394
Cdd:pfam05557 8 KARLSQLQNEKKQMElehkRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR--------EQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1395 ELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDAdransiaSSLEKKQKGFDKVLDEWRRKC---E 1471
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL-------QSTNSELEELQERLDLLKAKAseaE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1472 ALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQ--ELKDIADQLGEGGKSVHDLQKMRRRLEIEKEE 1549
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1550 LQQALDEAECaleaeeakvMRAQIEVSQIRSEiekRLQEKEEEFENTRKNHSRTIesmqVSLETESRGRAELLKTKKKLE 1629
Cdd:pfam05557 233 LKRKLEREEK---------YREEAATLELEKE---KLEQELQSWVKLAQDTGLNL----RSPEDLSRRIEQLQQREIVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1630 GDVNELEIALDHSnklnvdgQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSErtr 1709
Cdd:pfam05557 297 EENSSLTSSARQL-------EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYD--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1710 rqaelelaevkdsvNELSNSNSLLLATKRKVEG-----DLQLLQSEIEEAMSDAKTSDEKAKKAimdASKLADELRSEQE 1784
Cdd:pfam05557 367 --------------KELTMSNYSPQLLERIEEAedmtqKMQAHNEEMEAQLSVAEEELGGYKQQ---AQTLERELQALRQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1785 HASNLNQSKKTLEsqVKDLQMRLDEAEAagikggkrQLAKLDMRIHELETELEGENRRHAETQKvlrnkdrKCRELQFQV 1864
Cdd:pfam05557 430 QESLADPSYSKEE--VDSLRRKLETLEL--------ERQRLREQKNELEMELERRCLQGDYDPK-------KTKVLHLSM 492
|
570 580 590
....*....|....*....|....*....|..
gi 17561652 1865 DEDKKSQERMYDLIEKLQQKIKTYKRQIEDAE 1896
Cdd:pfam05557 493 NPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE 524
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1057-1269 |
7.48e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 54.31 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1057 DCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDI------ELSSIQSRLEDEQSLVAKLQR--QIKELLARIQEL 1128
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLlrfqleELEAAALQPGEEEELEEERRRlsNAEKLREALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1129 EEEL-DAERNSRSKAEKARNEMQmELEELGDRLDEAGGA-TQAQIELNkkrEA--ELAKLRQDLED-----AAInsETSM 1199
Cdd:COG0497 232 LEALsGGEGGALDLLGQALRALE-RLAEYDPSLAELAERlESALIELE---EAasELRRYLDSLEFdperlEEV--EERL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1200 AALR---KKHNDAVAELsdqLDTIQKMRGKLEREKNDKQR------EVDELQQSADVEAKQ-----RQNCERMAKQLEAQ 1265
Cdd:COG0497 306 ALLRrlaRKYGVTVEEL---LAYAEELRAELAELENSDERleeleaELAEAEAELLEAAEKlsaarKKAAKKLEKAVTAE 382
|
....
gi 17561652 1266 LTDM 1269
Cdd:COG0497 383 LADL 386
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1293-1555 |
8.89e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 53.00 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1293 ENQDLNRQLEDAEAQLCAL-NRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQL 1371
Cdd:pfam00038 26 QNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1372 SKANSEIQQ---WRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQkigTLEKNKQRlahdledaQVDADRA-NS 1447
Cdd:pfam00038 106 VGLRKDLDEatlARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV---NVEMDAAR--------KLDLTSAlAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1448 IASSLEKKQKGFDKVLDEW-RRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQL 1526
Cdd:pfam00038 175 IRAQYEEIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERY 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 17561652 1527 GEGGKSVHD--------LQKMRRRLEIEKEELQQALD 1555
Cdd:pfam00038 255 ELQLADYQEliseleaeLQETRQEMARQLREYQELLN 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
986-1203 |
1.04e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 986 RSLQDEIQSQDEVISKLNKE-KKHQEEVNR--KLLEDIQAEEDKVNhLNKTKAKLESTLDELEDTLEREKRGRQDCEKQR 1062
Cdd:COG3206 164 QNLELRREEARKALEFLEEQlPELRKELEEaeAALEEFRQKNGLVD-LSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1063 RKVEGELKIAQELIEELNRHKHEQE--QVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARI-QELEEELDAERNSR 1139
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1140 SKAEKARNEMQMELEELGDRLDEAGGATQAQIELNkkREAELAK-----LRQDLEDAAINSETSMAALR 1203
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLE--REVEVARelyesLLQRLEEARLAEALTVGNVR 389
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1256-1896 |
1.14e-06 |
|
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: 53.87 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1256 ERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNenqdLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRE 1335
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINN----SNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1336 RQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEgEGVSRAEELEETRRKLTHKVQEMQEQLE 1415
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1416 NANQKIGTLEKnkqrLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLR 1495
Cdd:TIGR04523 191 KIKNKLLKLEL----LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1496 NQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKsvhdlQKMRRRLEIEKEELQQaldeAECALEAEEAKVMRAQIEV 1575
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN-----QKEQDWNKELKSELKN----QEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1576 SQIRSEIEKRLQEKEEEfENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKK 1655
Cdd:TIGR04523 338 SQLNEQISQLKKELTNS-ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1656 LQDTIRELqyqvEEEQRSLSESRDHANLAERRsqvLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNelsnsnsllla 1735
Cdd:TIGR04523 417 LQQEKELL----EKEIERLKETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN----------- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1736 tkrKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAeaagi 1815
Cdd:TIGR04523 479 ---KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD----- 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1816 kggkrqlaKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDA 1895
Cdd:TIGR04523 551 --------DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
.
gi 17561652 1896 E 1896
Cdd:TIGR04523 623 K 623
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1361-1596 |
1.34e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1361 QDAKTDVQRQLSKANSEIQQWRAKFEgEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQv 1440
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1441 dadransiaSSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELK 1520
Cdd:COG4942 97 ---------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1521 DIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENT 1596
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
841-1143 |
1.53e-06 |
|
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: 53.04 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 841 KLFGRVKPLIKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENA----RLEAEKQALLIQLEQERDSSAEGEER-S 915
Cdd:COG5185 227 EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAesskRLNENANNLIKQFENTKEKIAEYTKSiD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 916 AKLLAQKADLEKQMANMNDQLCD-EEEKNAALTKQKKKIEQDNEGLKKTVsdleTTIKKQESEKQAkdhqirslqdeIQS 994
Cdd:COG5185 307 IKKATESLEEQLAAAEAEQELEEsKRETETGIQNLTAEIEQGQESLTENL----EAIKEEIENIVG-----------EVE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 995 QDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTkakLESTLDELEDTLEREKRgrqDCEKQRRKVEGELKIAQE 1074
Cdd:COG5185 372 LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---LEDTLKAADRQIEELQR---QIEQATSSNEEVSKLLNE 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1075 LIEELNRHKHE-----QEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAE 1143
Cdd:COG5185 446 LISELNKVMREadeesQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
853-1762 |
1.56e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAE--NARLEAEKQALLIQLEqerDSSAEGEERSAKLLAQKADLEKQMA 930
Cdd:TIGR01612 938 NKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTliDKINELDKAFKDASLN---DYEAKNNELIKYFNDLKANLGKNKE 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 931 NMNDQLCDEEEKNAaltkqkKKIEQDNEGLKKTVSDLETTIKKQesekqakdhqIRSLQDEIQsqdevisklNKEKKHQE 1010
Cdd:TIGR01612 1015 NMLYHQFDEKEKAT------NDIEQKIEDANKNIPNIEIAIHTS----------IYNIIDEIE---------KEIGKNIE 1069
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1011 EVNRKLLEDIqaeEDKVNHLNKTKAKLEstLDELEDTLEREKRGRQDcekQRRKVEGELKiaqELIEELNRHKHEQEQVI 1090
Cdd:TIGR01612 1070 LLNKEILEEA---EINITNFNEIKEKLK--HYNFDDFGKEENIKYAD---EINKIKDDIK---NLDQKIDHHIKALEEIK 1138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1091 KKKDIELSSIQSRLEDEQSLVAKL--QRQIKELLARIQELEEELDAERNSRSKAEKARNEMQmELEELGDRLDEAGGatq 1168
Cdd:TIGR01612 1139 KKSENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA-EIEKDKTSLEEVKG--- 1214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1169 aqieLNKKREAELAKL-RQDLEDAAINSETSMAALRKKHNDavaelsdqLDTIQKMRGKLERE---KNDKQREVDELQQS 1244
Cdd:TIGR01612 1215 ----INLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIED--------LDEIKEKSPEIENEmgiEMDIKAEMETFNIS 1282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1245 ADVEAKQRQncerMAKQLEAQLTDMTLKSdeqARLIQELTMgKNKVHNENQDLNRQLEDAEAQLCALNrikqQQHSQLEE 1324
Cdd:TIGR01612 1283 HDDDKDHHI----ISKKHDENISDIREKS---LKIIEDFSE-ESDINDIKKELQKNLLDAQKHNSDIN----LYLNEIAN 1350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1325 LKRTLdqETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLsKANSEIQQWRAKFEGegVSRAEELEETRRKLT 1404
Cdd:TIGR01612 1351 IYNIL--KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKI-KDDINLEECKSKIES--TLDDKDIDECIKKIK 1425
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1405 HKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVdadrANSIASSLEKKQKgfdkvlDEWRRKCEALVAEVEQSQRET 1484
Cdd:TIGR01612 1426 ELKNHILSEESNIDTYFKNADENNENVLLLFKNIEM----ADNKSQHILKIKK------DNATNDHDFNINELKEHIDKS 1495
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1485 RAAATETFRLRNQLEESGEQTEAVKRE-----NKALAQELKDIADQL-GEGGKSVHDLQKMRRRLEIEKEELQQALDeae 1558
Cdd:TIGR01612 1496 KGCKDEADKNAKAIEKNKELFEQYKKDvtellNKYSALAIKNKFAKTkKDSEIIIKEIKDAHKKFILEAEKSEQKIK--- 1572
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1559 caleaeeakvmraQIEVSQIRSEiekrlqekEEEFENTRKNhsRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIA 1638
Cdd:TIGR01612 1573 -------------EIKKEKFRIE--------DDAAKNDKSN--KAAIDIQLSLENFENKFLKISDIKKKINDCLKETESI 1629
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1639 LDHSNKLNVDGQKS-MKKLQDTIRELQYQVEeeqrSLSESRDhaNLAERRSQvLQQEKEDLAIIYEQSERTRRQAELELA 1717
Cdd:TIGR01612 1630 EKKISSFSIDSQDTeLKENGDNLNSLQEFLE----SLKDQKK--NIEDKKKE-LDELDSEIEKIEIDVDQHKKNYEIGII 1702
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 17561652 1718 EvkdSVNELSNSNslllatKRKVEGDLQLLQSEIEEAMSDAKTSD 1762
Cdd:TIGR01612 1703 E---KIKEIAIAN------KEEIESIKELIEPTIENLISSFNTND 1738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
853-1065 |
1.68e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 NDQlcdEEEKNAALTKQKKKIEQDNEGLkKTVSDLETTI---KKQESEKQAKDHQIRSLQDEIQSQDEVISKLnkekkhq 1009
Cdd:TIGR02169 902 ERK---IEELEAQIEKKRKRLSELKAKL-EALEEELSEIedpKGEDEEIPEEELSLEDVQAELQRVEEEIRAL------- 970
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1010 EEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLErekrgrqDCEKQRRKV 1065
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE-------EYEKKKREV 1019
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1084-1673 |
1.72e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1084 HEQEQViKKKDIE----LSSIQSRLEDEQSLVAKLQRQIKellARIQELEEELDAERNSRSKAEKARNEMQMELEELGDR 1159
Cdd:pfam05483 60 HYQEGL-KDSDFEnsegLSRLYSKLYKEAEKIKKWKVSIE---AELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1160 LDEAGGATQAQIELN---------------------KKREAELAKLRQDLEDAAINSETSMAA---LRKKHNDAVAE--- 1212
Cdd:pfam05483 136 LEEEIQENKDLIKENnatrhlcnllketcarsaektKKYEYEREETRQVYMDLNNNIEKMILAfeeLRVQAENARLEmhf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1213 -LSDQLDTIQKMRGKLEREKNDKQREVDELQ-QSADVEAKQR------QNCERMAKQLEAQ-------LTDMTLKSDEQA 1277
Cdd:pfam05483 216 kLKEDHEKIQHLEEEYKKEINDKEKQVSLLLiQITEKENKMKdltfllEESRDKANQLEEKtklqdenLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1278 RLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNrikQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESL 1357
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT---EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1358 EEEQDAKTDVQRQLSKANSEIQQwRAKFEGEGVSRAEEL------EETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRL 1431
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEE-MTKFKNNKEVELEELkkilaeDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1432 AHDLEdAQVDADRANSiaSSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRE 1511
Cdd:pfam05483 452 IHDLE-IQLTAIKTSE--EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1512 NKALAQELKDIADQLgeggksvhdlQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIeKRLQEKEE 1591
Cdd:pfam05483 529 EERMLKQIENLEEKE----------MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM-KILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1592 EFENTRKNHSRTIESMQvsletesrgrAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQ 1671
Cdd:pfam05483 598 NLKKQIENKNKNIEELH----------QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
..
gi 17561652 1672 RS 1673
Cdd:pfam05483 668 IS 669
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
867-1305 |
1.79e-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: 52.93 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 867 KVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMN-----DQLCDEEE 941
Cdd:pfam06160 107 EELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELTESGDylearEVLEKLEE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 942 KNAALTKQKKKIEQDNEGLKKT----VSDLETTIKKQESEKQAKDH-----QIRSLQDEIQSQDEVISKLNkekkhQEEV 1012
Cdd:pfam06160 187 ETDALEELMEDIPPLYEELKTElpdqLEELKEGYREMEEEGYALEHlnvdkEIQQLEEQLEENLALLENLE-----LDEA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 nRKLLEDIQAEedkvnhlnktkaklestLDELEDTLEREKRGRQDCEKQRRKVEGELkiaQELIEELNRHKHEQEQVikK 1092
Cdd:pfam06160 262 -EEALEEIEER-----------------IDQLYDLLEKEVDAKKYVEKNLPEIEDYL---EHAEEQNKELKEELERV--Q 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 KDIELSsiqsrlEDEQSLVAKLQRQIKELLARIQELEEELDAErnsrskaEKARNEMQMELEELGDRLDEAGgatQAQIE 1172
Cdd:pfam06160 319 QSYTLN------ENELERVRGLEKQLEELEKRYDEIVERLEEK-------EVAYSELQEELEEILEQLEEIE---EEQEE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 LNKKreaeLAKLRQDLEDA---AINSETSMAALR---KKHN--DAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQs 1244
Cdd:pfam06160 383 FKES----LQSLRKDELEArekLDEFKLELREIKrlvEKSNlpGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNR- 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1245 adveakQRQNCERMAKQLEAQLTDMTlksdEQARLIQELTMGKNKVHNENQDLNRQLEDAE 1305
Cdd:pfam06160 458 ------LLDEAQDDVDTLYEKTEELI----DNATLAEQLIQYANRYRSSNPEVAEALTEAE 508
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
874-1100 |
1.84e-06 |
|
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: 52.93 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 874 TQEERKRKD----MEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEE--KNAALT 947
Cdd:pfam09726 429 TSLERSLKSelgqLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEAtaARAVAL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 948 KQKKKIEQdNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSqdevISKLNKEKKHQEevnrKLLEDIQAEEDKV 1027
Cdd:pfam09726 509 AAASRGEC-TESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQE----LRKYKESEKDTE----VLMSALSAMQDKN 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1028 NHlnktkaklestldeLEDTLEREKRGRQDCEKQRRKVEGELKIAQELIeelnrHKHEQEQV-IKKKDIELSSI 1100
Cdd:pfam09726 580 QH--------------LENSLSAETRIKLDLFSALGDAKRQLEIAQGQI-----YQKDQEIKdLKQKIAEVMAV 634
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1286-1726 |
2.08e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1286 GKNKVHNENQ--DLNRQLEDAEAQLCALNRIKQQQHS---QLEELKRTLDQETRERQSLHSQVSNYQLEceQFRESLEEE 1360
Cdd:COG4717 63 GRKPELNLKElkELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLEKLLQLLPLY--QELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1361 QDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQV 1440
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1441 DADRANSIASSLEKKQKGFDKvldewrrkcEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELK 1520
Cdd:COG4717 221 ELEELEEELEQLENELEAAAL---------EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1521 DIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEE-EFENTRKN 1599
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1600 HSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDhsNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSEsrD 1679
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE--ELLGELEELLEALDEEELEEELEELEEELEELEE--E 447
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 17561652 1680 HANLAERRSQvLQQEKEDLAiiyeqSERTRRQAELELAEVKDSVNEL 1726
Cdd:COG4717 448 LEELREELAE-LEAELEQLE-----EDGELAELLQELEELKAELREL 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1463-1931 |
2.09e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1463 LDEWR-RKCEALVAeVEQSQRETRAAATEtfrLRNQLEESgEQTEAVKRENkALAQELKDIADQLgeggksvhdlqkmrR 1541
Cdd:PRK02224 164 LEEYReRASDARLG-VERVLSDQRGSLDQ---LKAQIEEK-EEKDLHERLN-GLESELAELDEEI--------------E 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1542 RLEIEKEELQQALDEAECALEAEEAKvmraQIEVSQIRSEIEKrLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAEL 1621
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEER----REELETLEAEIED-LRETIAETEREREELAEEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1622 LKtkkklEGDVNELEIaldhsnklnvdgqksmKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAii 1701
Cdd:PRK02224 299 LA-----EAGLDDADA----------------EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE-- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1702 yEQSERTRRQAELELAEVKDSVNELsnsnslllatkRKVEGDLQLLQSEIEEAMsdaktsdEKAKKAIMDASKLADELRS 1781
Cdd:PRK02224 356 -ERAEELREEAAELESELEEAREAV-----------EDRREEIEELEEEIEELR-------ERFGDAPVDLGNAEDFLEE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1782 EQEHASNLNQSKKTLESQVKDLQMRLDEAE---AAG--------IKGGKR--QLAKLDMRIHELETELEgenrrhaetqk 1848
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEallEAGkcpecgqpVEGSPHveTIEEDRERVEELEAELE----------- 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1849 vlrnkdrkcrELQFQVDEDKKSQERMYDL------IEKLQQKIKTYKRQIEDAESLASGNLAKYRQLQHVVEDAQERADA 1922
Cdd:PRK02224 486 ----------DLEEEVEEVEERLERAEDLveaedrIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE 555
|
....*....
gi 17561652 1923 AENALQKLR 1931
Cdd:PRK02224 556 KREAAAEAE 564
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1409-1931 |
2.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1409 EMQEQLENANQKIGTLEKNKQrLAHDLEDAQVDADRANSIASSL-----EKKQKGFDKVLDEWRRKCEALVAEVEQSQRE 1483
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRE-LAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1484 TRAAATETFRLRNQLEES-GEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALE 1562
Cdd:COG4913 318 LDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1563 AEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHS---RTIESMQVSLETESRGR-------AELLKTKKKLEGDV 1632
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipARLLALRDALAEALGLDeaelpfvGELIEVRPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1633 NELEIALdHSNKLN--------------VDGQKSMKKLQ----DTIRELQYQVEEEQRSLS---ESRDHA------NLAE 1685
Cdd:COG4913 478 GAIERVL-GGFALTllvppehyaaalrwVNRLHLRGRLVyervRTGLPDPERPRLDPDSLAgklDFKPHPfrawleAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1686 RRSQVL------QQEKEDLAI-----IYeqSERTRRQAELELAEVKDSVneLSNSNSLLLATKRKvegDLQLLQSEIEEA 1754
Cdd:COG4913 557 RRFDYVcvdspeELRRHPRAItragqVK--GNGTRHEKDDRRRIRSRYV--LGFDNRAKLAALEA---ELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1755 msdaktsdekaKKAIMDASKLADELRSEQEHASNLNQSKKTlESQVKDLQMRLDEAEAAgikggKRQLAKLDMRIHELET 1834
Cdd:COG4913 630 -----------EERLEALEAELDALQERREALQRLAEYSWD-EIDVASAEREIAELEAE-----LERLDASSDDLAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1835 ELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIED---AESLASGNLAKYR-QLQ 1910
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfAAALGDAVERELReNLE 772
|
570 580
....*....|....*....|.
gi 17561652 1911 HVVEDAQERADAAENALQKLR 1931
Cdd:COG4913 773 ERIDALRARLNRAEEELERAM 793
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
955-1345 |
2.29e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 955 QDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQ------SQDEVISKLNKEKKHQEEVNRKLLEDiQAEEDKVN 1028
Cdd:pfam17380 221 KEVQGMPHTLAPYEKMERRKESFNLAEDVTTMTPEYTVRyngqtmTENEFLNQLLHIVQHQKAVSERQQQE-KFEKMEQE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1029 HLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQeqviKKKDIELSSiQSRLEDEQ 1108
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEE----RKRELERIR-QEEIAMEI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1109 SLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIE-LNKKREAELAKLRQD 1187
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrLEEERAREMERVRLE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1188 ledaAINSETSMAALRKKHNDavaelsdqldtiqKMRGKLEREKNDKQREVDELQQSADVEakqrqncermaKQLEAQLT 1267
Cdd:pfam17380 455 ----EQERQQQVERLRQQEEE-------------RKRKKLELEKEKRDRKRAEEQRRKILE-----------KELEERKQ 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1268 DMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSN 1345
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVES 584
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
869-1145 |
2.51e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.99 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 869 LEEEKTQEERKRKDMEAENARLEAEKQAL---LIQLEQERdssAEGEERSAKLLAQKADLEKQMANMNDQLcdeeeknAA 945
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAekaLQRAEGEL---ATARERLALLEQENRRLQALSEEQAAEL-------AE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 946 LTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQI----RSLQDEIQSQDEVISKLNKEKKHQEEVN-------R 1014
Cdd:pfam19220 193 LTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLeeavEAHRAERASLRMKLEALTARAAATEQLLaearnqlR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1015 KLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKvegelkiAQELIEELNRHKHEQEQVIKKKD 1094
Cdd:pfam19220 273 DRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAE-------LEERAEMLTKALAAKDAALERAE 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1095 IELSSIQSRLEdeqSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKA 1145
Cdd:pfam19220 346 ERIASLSDRIA---ELTKRFEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
940-1598 |
2.64e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 940 EEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDevISKLNKEKKHqeEVNRKLLEd 1019
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKG--LPKKSGEEDW--ERTRRIAE- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1020 iqaEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRR-KVEGELKIAQELIEELNRHKHEQEQVIKKKDIELS 1098
Cdd:pfam10174 190 ---AEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKAlQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLH 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1099 SIQSRLEDEQSLVAK----------------LQRQIKELLARIQELE----------EELDAERNSRSKAEKARNEMQME 1152
Cdd:pfam10174 267 TEDREEEIKQMEVYKshskfmknkidqlkqeLSKKESELLALQTKLEtltnqnsdckQHIEVLKESLTAKEQRAAILQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1153 LEELGDRLDEaggatqaqielnkkREAELAKLRQDLEDAAINSETSMAALRkkhndavaELSDQLDTiqkmrgkLEREKN 1232
Cdd:pfam10174 347 VDALRLRLEE--------------KESFLNKKTKQLQDLTEEKSTLAGEIR--------DLKDMLDV-------KERKIN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1233 DKQREVDELQQSADVEAKQRQNCERMAKQLEAQL--TDMTLKSDEQA-----RLIQELTMGKNKVH----NENQDLNRQL 1301
Cdd:pfam10174 398 VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsnTDTALTTLEEAlsekeRIIERLKEQREREDrerlEELESLKKEN 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1302 EDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRE--SLEEEQDAKTDVQRQLSKANSEIQ 1379
Cdd:pfam10174 478 KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecSKLENQLKKAHNAEEAVRTNPEIN 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1380 QWRAKFEGEGVSRAEELEETR---RKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLedaqvdADRANSIASSLEKKQ 1456
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQaevERLLGILREVENEKNDKDKKIAELESLTLRQMKEQ------NKKVANIKHGQQEMK 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1457 KGFDKVLDEWRRKCEALVAEVEQSqretraaatetfrlrnQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDL 1536
Cdd:pfam10174 632 KKGAQLLEEARRREDNLADNSQQL----------------QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNL 695
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1537 QKMRRR-LEIEKEELQQAL-------DEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRK 1598
Cdd:pfam10174 696 RAERRKqLEEILEMKQEALlaaisekDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNRMK 765
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1353-1861 |
2.78e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1353 FRESLEEEQDAKTDVQRQLSKAN-SEIQQWRAKFEgegvsRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRL 1431
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELK-----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1432 AHDLEDAQVDADRAnsiasSLEKKQKGFDKVLDEWRRKcealVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRE 1511
Cdd:COG4717 122 EKLLQLLPLYQELE-----ALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1512 nkalaqELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDeaecaleaeeakvmraQIEVSQIRSEIEKRLQEKEE 1591
Cdd:COG4717 193 ------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE----------------QLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1592 EF-------------ENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEiALDHSNKLnvdgqkSMKKLQD 1658
Cdd:COG4717 251 LLliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ-ALPALEEL------EEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1659 TIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIiyeQSERTRRQAELELAEVkDSVNELsNSNSLLLATKR 1738
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL---EELEQEIAALLAEAGV-EDEEEL-RAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1739 KVEGDLQLLQSEIEEAmsdakTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGikgg 1818
Cdd:COG4717 399 ELKEELEELEEQLEEL-----LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG---- 469
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17561652 1819 krQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQ 1861
Cdd:COG4717 470 --ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1287-1530 |
2.89e-06 |
|
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: 52.91 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1287 KNKVHNENQDLNRQLEDAEAQLCALN----------RIKQQQHSQLEELKRTldQETRERQSLHSQVSNYQLEceqfRES 1356
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALAdkeraeadrqRLEQEKQQQLAAISGS--QSQLESTDQNALETNGQAQ----RDA 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1357 LEEEQDAKT----DVQRQLSKANSEI-------QQWRAKFEGEGVSRAEE-LEETRRKLTHKVQEMQEQLENANQKI--- 1421
Cdd:NF012221 1611 ILEESRAVTkeltTLAQGLDALDSQAtyagesgDQWRNPFAGGLLDRVQEqLDDAKKISGKQLADAKQRHVDNQQKVkda 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1422 ------GTL--EKNKQRLAHDLEDAQVDADransiasslekkqkgfdkvldewRRKCEALVAEVEQSQRETRA-AATETF 1492
Cdd:NF012221 1691 vakseaGVAqgEQNQANAEQDIDDAKADAE-----------------------KRKDDALAKQNEAQQAESDAnAAANDA 1747
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 17561652 1493 RLRNQLEES--GEQTEAVKRENKALAQELKDIADQLGEGG 1530
Cdd:NF012221 1748 QSRGEQDASaaENKANQAQADAKGAKQDESDKPNRQGAAG 1787
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1092-1251 |
3.04e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1092 KKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGG-----A 1166
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyeA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1167 TQAQIELNKKReaelaklRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSAD 1246
Cdd:COG1579 94 LQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 17561652 1247 VEAKQ 1251
Cdd:COG1579 167 ELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1709-1931 |
3.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1709 RRQAELELAEVKDSVNELSNSNSLLLATKRKVE--GDLQLLQSEIEEAMSDAKTSDE-----KAKKAIMDASKLADELRS 1781
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1782 EQEHASNLNQSKKTLESQVKDLQMRLDEAEAA--GIKGGkrqlakldmRIHELETELEGENRRHAETQKVLRNKDRKCRE 1859
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQirGNGGD---------RLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1860 LQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIEDAESLASGNLakyrqlqhvvEDAQERADAAENALQKLR 1931
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL----------RDLRRELRELEAEIASLE 432
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
892-1069 |
4.51e-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: 49.92 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 892 AEKQALLIQLeQERDSS-AEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETT 970
Cdd:COG1579 3 PEDLRALLDL-QELDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 971 IKKQESEKQAKDhqirsLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLER 1050
Cdd:COG1579 82 LGNVRNNKEYEA-----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*....
gi 17561652 1051 EkrgRQDCEKQRRKVEGEL 1069
Cdd:COG1579 157 E---LEELEAEREELAAKI 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
868-1347 |
4.72e-06 |
|
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: 51.50 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 868 VLEEEKTQEERKRKDMEAENARL---EAEKQALLIQLeQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNA 944
Cdd:COG5185 73 QNDVKKSESSVKARKFLKEKKLDtkiLQEYVNSLIKL-PNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 945 ALTKQKKKIEQD---------NEGLKKTVSDLETTIKKQESEKQAKDH--QIRSLQDEIQSQDEVISKLNKEKKHQEEVN 1013
Cdd:COG5185 152 SYGEVETGIIKDifgkltqelNQNLKKLEIFGLTLGLLKGISELKKAEpsGTVNSIKESETGNLGSESTLLEKAKEIINI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1014 RKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTleREKRGRQDCEKQRRKVEgelkIAQELIEELNRHKHEQEQVIKKK 1093
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDL--RLEKLGENAESSKRLNE----NANNLIKQFENTKEKIAEYTKSI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1094 DIELSSIQSRLEDEQS-LVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRldeaggatqaqie 1172
Cdd:COG5185 306 DIKKATESLEEQLAAAeAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL------------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1173 lnKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQR 1252
Cdd:COG5185 373 --SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISEL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1253 QNCERMAkqleaqltdmtlKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCAL-----------NRIKQQQHSQ 1321
Cdd:COG5185 451 NKVMREA------------DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLkatleklraklERQLEGVRSK 518
|
490 500
....*....|....*....|....*.
gi 17561652 1322 LEELKRTLDQETRERQSLHSQVSNYQ 1347
Cdd:COG5185 519 LDQVAESLKDFMRARGYAHILALENL 544
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1059-1265 |
5.05e-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: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1059 EKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNS 1138
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1139 RSKAEKARNEMQM-----ELEELGDR---LDEAGGATQAQIELNKKREAELAKLRQDLEDA---AINSETSMAALRKKHN 1207
Cdd:COG3883 95 LYRSGGSVSYLDVllgseSFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKlaeLEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1208 DAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQ 1265
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
925-1333 |
8.28e-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: 50.99 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 925 LEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQdeviskLNK 1004
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKA------LAE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1005 EKKHQEEVNRKLlediqAEEDKVNhLNKTKAKLESTLDE-LEDTLEREKRgrqdcekqRRKVEGELK-----IAQELIEE 1078
Cdd:pfam12128 676 RKDSANERLNSL-----EAQLKQL-DKKHQAWLEEQKEQkREARTEKQAY--------WQVVEGALDaqlalLKAAIAAR 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1079 LNRHKHEQEQVIKKKDIELSsiqSRLEDEQSlVAKLQRQIKELLARIQELE----EELDAERNSRSKAEKARNEMQMELE 1154
Cdd:pfam12128 742 RSGAKAELKALETWYKRDLA---SLGVDPDV-IAKLKREIRTLERKIERIAvrrqEVLRYFDWYQETWLQRRPRLATQLS 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1155 ELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALR------------KKHNDAVAELSDQLDTIQK 1222
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemsklatlkedANSEQAQGSIGERLAQLED 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1223 MRGKLEREKNDKQREVDELQqsaDVEAKQR-----QNCERMAKQlEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDL 1297
Cdd:pfam12128 898 LKLKRDYLSESVKKYVEHFK---NVIADHSgsglaETWESLREE-DHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMV 973
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 17561652 1298 NRQL-----EDAEAQLCALNRIKQQQHSQLEELKRTLDQET 1333
Cdd:pfam12128 974 LREQvsilgVDLTEFYDVLADFDRRIASFSRELQREVGEEA 1014
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
898-1283 |
8.52e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 898 LIQLEQERDSSAEGEER-----SAKLLaqKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIK 972
Cdd:pfam07888 6 LVTLEEESHGEEGGTDMllvvpRAELL--QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 973 KQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREK 1052
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1053 RGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELeeel 1132
Cdd:pfam07888 164 AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL---- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1133 daernsRSKAEKArNEMQMELEELGDRLDEAGGA-TQAQIELNKKReAELAKLRQDLEDAAI----------NSETSMAA 1201
Cdd:pfam07888 240 ------RSLQERL-NASERKVEGLGEELSSMAAQrDRTQAELHQAR-LQAAQLTLQLADASLalregrarwaQERETLQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1202 LRKKHNDAVAELSDQldtIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTdMTLKSDEQARL-I 1280
Cdd:pfam07888 312 SAEADKDRIEKLSAE---LQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR-VAQKEKEQLQAeK 387
|
...
gi 17561652 1281 QEL 1283
Cdd:pfam07888 388 QEL 390
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1498-1813 |
9.39e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1498 LEESGEQTEAVKRENKALAQELKDIADQLgeggksvhdlqKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQ 1577
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREV-----------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1578 IRSEIEKRLQEKEEEFE-NTRKNHSRTIESMQVSLETES-RGRAELLKTKKklegdVNELEIALDHSNKLNVDGQKSMKK 1655
Cdd:pfam17380 353 IRQEERKRELERIRQEEiAMEISRMRELERLQMERQQKNeRVRQELEAARK-----VKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1656 LQDTIRELQYQVEEEQRSLSESRDHANLAERRSQV---LQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSL 1732
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVerlRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1733 LLATKRK---VEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASK-LADELRSEQEHASNLNQSKKTLE--SQVKDLQMR 1806
Cdd:pfam17380 508 MIEEERKrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRrIQEQMRKATEERSRLEAMEREREmmRQIVESEKA 587
|
....*..
gi 17561652 1807 LDEAEAA 1813
Cdd:pfam17380 588 RAEYEAT 594
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
903-1178 |
9.76e-06 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 50.67 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 903 QERDSSAEGEERSAKLLAQKADLEKQMANMN-DQLCDEEEKNAA-----LTKQKKKIEQDNEGLKK-------------- 962
Cdd:pfam15964 327 QQRESSAYEQVKQAVQMTEEANFEKTKALIQcEQLKSELERQKErlekeLASQQEKRAQEKEALRKemkkereelgatml 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 963 ----TVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQeeVNRKLLEDIQAEEDKVNHLNKTKAKLE 1038
Cdd:pfam15964 407 alsqNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQ--LNQTKMKKDEAEKEHREYRTKTGRQLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1039 STLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDielSSIQSRLEDEQSLVAKLQRQI 1118
Cdd:pfam15964 485 IKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKE---SIQQSFSNEAKAQALQAQQRE 561
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1119 KELLARIQELEEELDAERNSRSKAEKARNEMQMELEE----LGDRLDEAGGATQAQIE-LNKKRE 1178
Cdd:pfam15964 562 QELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctLAKKLEEITQKSRSEVEqLSQEKE 626
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1095-1551 |
1.00e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1095 IELSSIQSRLEDEqslvakLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELN 1174
Cdd:pfam05557 5 IESKARLSQLQNE------KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1175 KKREAELAKLRQDLEDAAinsetsmaALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQN 1254
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKE--------SQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1255 CERMAKQLEAQLTDMTLKSDEQARLIQELTM---GKNKVHNENQDLNR---------QLEDAEAQLCALNRIKQQQHSQL 1322
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSqeqDSEIVKNSKSELARipelekeleRLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1323 EELKRTLDQETRERQSLHS-QVSNYQLECE-QFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEG---VSRAEELE 1397
Cdd:pfam05557 231 EDLKRKLEREEKYREEAATlELEKEKLEQElQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENsslTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1398 ETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKK--QKGFDKVLDEWRRKCEALVA 1475
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKEltMSNYSPQLLERIEEAEDMTQ 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1476 EVEQSQRETRA---AATETFRLRNQLEESGEQTEAVKRENKALAqELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQ 1551
Cdd:pfam05557 391 KMQAHNEEMEAqlsVAEEELGGYKQQAQTLERELQALRQQESLA-DPSYSKEEVDSLRRKLETLELERQRLREQKNELE 468
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1035-1190 |
1.25e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.58 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1035 AKLESTLDELEDTLEREKRGRQDCEKQ-------RRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDE 1107
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQDSvanlrasLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1108 QSLVAKLQRQIKELLARIQELEEELDAernsrskAEKARNEMQMELEELGDRLDEAgGATQAQiELNKKREAELAKLRQD 1187
Cdd:PRK09039 136 LAQVELLNQQIAALRRQLAALEAALDA-------SEKRDRESQAKIADLGRRLNVA-LAQRVQ-ELNRYRSEFFGRLREI 206
|
...
gi 17561652 1188 LED 1190
Cdd:PRK09039 207 LGD 209
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1415 |
1.38e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.44 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 850 IKGSKKNEEfEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALL-------IQLEQER-----DSSAEGEERSAK 917
Cdd:TIGR01612 1116 IKDDIKNLD-QKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAIsnddpeeIEKKIENivtkiDKKKNIYDEIKK 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 918 LLAQKADLEKqmanmnDQLCDEEEKNAALT--------------KQKKKIEQDNEGLKKTVSDLETtIKKQESEKQAKDH 983
Cdd:TIGR01612 1195 LLNEIAEIEK------DKTSLEEVKGINLSygknlgklflekidEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 984 QIRSLQDEIQSQDevISKlNKEKKHQ--EEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEK- 1060
Cdd:TIGR01612 1268 IEMDIKAEMETFN--ISH-DDDKDHHiiSKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLy 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1061 --------------QRRKVEGELKIAQELIEELNRHKHEQ----EQVIK--KKDIELSSIQSRLEDEQSlvaklQRQIKE 1120
Cdd:TIGR01612 1345 lneianiynilklnKIKKIIDEVKEYTKEIEENNKNIKDEldksEKLIKkiKDDINLEECKSKIESTLD-----DKDIDE 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1121 LLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNK--------------KREAELAKLRQ 1186
Cdd:TIGR01612 1420 CIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKdnatndhdfninelKEHIDKSKGCK 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1187 DLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQkMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEaql 1266
Cdd:TIGR01612 1500 DEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIK--- 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1267 tdmtlksDEQARlIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKR------TLDQETRERQSlh 1340
Cdd:TIGR01612 1576 -------KEKFR-IEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESiekkisSFSIDSQDTEL-- 1645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1341 SQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQ-------QWRAKFEgegVSRAEELEETRRKLTHKVQEMQEQ 1413
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEkieidvdQHKKNYE---IGIIEKIKEIAIANKEEIESIKEL 1722
|
..
gi 17561652 1414 LE 1415
Cdd:TIGR01612 1723 IE 1724
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1056-1249 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1056 QDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQE-------L 1128
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvsyL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1129 EEELDAE--------RNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAELAKLRQDLEdaainsetsma 1200
Cdd:COG3883 106 DVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE----------- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17561652 1201 ALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEA 1249
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
870-1449 |
1.49e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 870 EEEKTQEERKRKDMEAENArLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQ 949
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDD-LQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 950 KKKIEQDNEGLKKTVSDLETTikkqeseKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEdiqaeedkvnH 1029
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQA-------RKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH----------F 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1030 LNKTKAKLESTLDELedtLEREKRGRQDC--EKQRRKVEGEL-----KIAQELIEELNRHKHEQEQvikkkDIELSSIQS 1102
Cdd:pfam12128 540 LRKEAPDWEQSIGKV---ISPELLHRTDLdpEVWDGSVGGELnlygvKLDLKRIDVPEWAASEEEL-----RERLDKAEE 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1103 RLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIE-----LNKKR 1177
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANerlnsLEAQL 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1178 EAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKmrGKLEREKNDKqREVDELQQSADVEAKQRQNCER 1257
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKA--AIAARRSGAK-AELKALETWYKRDLASLGVDPD 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1258 MAKQLEAQLTDMTLKSDEQARLIQELT----MGKNKVHNENQDLNRQLEDAEAqlcALNRIKQQQHSQLEELKRTLDQET 1333
Cdd:pfam12128 769 VIAKLKREIRTLERKIERIAVRRQEVLryfdWYQETWLQRRPRLATQLSNIER---AISELQQQLARLIADTKLRRAKLE 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1334 RERQSLHSQV-----SNYQLECEQFR-ESLEEEQDAKtDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLT-HK 1406
Cdd:pfam12128 846 MERKASEKQQvrlseNLRGLRCEMSKlATLKEDANSE-QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAdHS 924
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17561652 1407 VQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIA 1449
Cdd:pfam12128 925 GSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRV 967
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
984-1653 |
1.59e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 984 QIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRgrqdcekqrr 1063
Cdd:pfam10174 61 QYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAK---------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1064 kvegELKIAQELIEELNRHKHEQEQVIKKKDielSSIQSRLEDEQS--LVAKLQRQIKELLARIQELEEELDAERNSRSK 1141
Cdd:pfam10174 131 ----ELFLLRKTLEEMELRIETQKQTLGARD---ESIKKLLEMLQSkgLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1142 AEKarnEMQMELEELGDRLDEAGG-----ATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQ 1216
Cdd:pfam10174 204 KEK---ENIHLREELHRRNQLQPDpaktkALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1217 LDTIQKMRGKLEREKND---KQREVDELQQSADVEAKQRQNCERMAKQLEAQLtdmTLKSDEQARLIQELTMGKNKVHNE 1293
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQElskKESELLALQTKLETLTNQNSDCKQHIEVLKESL---TAKEQRAAILQTEVDALRLRLEEK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1294 NQDLNRQLEdaeaQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQlecEQFRES---LEEEQDAKTDVQRQ 1370
Cdd:pfam10174 358 ESFLNKKTK----QLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ---EQLRDKdkqLAGLKERVKSLQTD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1371 LSKANSEIQQWR-AKFEGEGVSRA--EELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQvdaDRANS 1447
Cdd:pfam10174 431 SSNTDTALTTLEeALSEKERIIERlkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK---EHASS 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1448 IASSLEKKQKgfdkvldewrrKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKREnKALAQELKDIADQLG 1527
Cdd:pfam10174 508 LASSGLKKDS-----------KLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARYKEESG 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1528 EGGKSVHDLQKMRRRLEIEK-------EELQQALDEAECALEAEEAKV-MRAQIEVSQIRSEIEKRLQEKEEEfenTRKN 1599
Cdd:pfam10174 576 KAQAEVERLLGILREVENEKndkdkkiAELESLTLRQMKEQNKKVANIkHGQQEMKKKGAQLLEEARRREDNL---ADNS 652
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1600 HSRTIESMQVSLEtesRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSM 1653
Cdd:pfam10174 653 QQLQLEELMGALE---KTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1189-1400 |
1.77e-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: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1189 EDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLER---EKNDKQREVDELQQS-ADVEAKQRQNCERMAKQLEA 1264
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAEiAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1265 Q--------LTDMTLKSDEQARLIQELTMGK------NKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLD 1330
Cdd:COG3883 95 LyrsggsvsYLDVLLGSESFSDFLDRLSALSkiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1331 QETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETR 1400
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
892-1238 |
1.79e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 892 AEKQALLIQLEQERDSSAegeERSAKLLAQKADLE------KQMANMNDQLCDEEEKNAALTKQKKKIEQdneglkktvs 965
Cdd:PRK04863 782 AAREKRIEQLRAEREELA---ERYATLSFDVQKLQrlhqafSRFIGSHLAVAFEADPEAELRQLNRRRVE---------- 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 966 dLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVI--SKLNKEKKHQEEVNRKLLEDIQAEEDK--VNHLNKTKAKLE--- 1038
Cdd:PRK04863 849 -LERALADHESQEQQQRSQLEQAKEGLSALNRLLprLNLLADETLADRVEEIREQLDEAEEAKrfVQQHGNALAQLEpiv 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1039 STLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELS-SIQSRLEDEQSLVAKLQRQ 1117
Cdd:PRK04863 928 SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNeKLRQRLEQAEQERTRAREQ 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1118 IKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAggatqaqielnkkrEAELAKLRQD-LEDAAINSE 1196
Cdd:PRK04863 1008 LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSG--------------AEERARARRDeLHARLSANR 1073
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17561652 1197 TSMAALRKKhndaVAELSDQLDTIQKMRGKLEREKNDKQREV 1238
Cdd:PRK04863 1074 SRRNQLEKQ----LTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1148 |
1.80e-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: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 934 DQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQsqdevisKLNKEKKHQEEVN 1013
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1014 RKLLEDIQAEEDKVNHLNktkAKLESTldELEDTLEREKRGRQDCEKQRRKVEgELKIAQELIE----ELNRHKHEQEQV 1089
Cdd:COG3883 89 GERARALYRSGGSVSYLD---VLLGSE--SFSDFLDRLSALSKIADADADLLE-ELKADKAELEakkaELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1090 IKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNE 1148
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
659-683 |
1.89e-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: 46.95 E-value: 1.89e-05
10 20
....*....|....*....|....*
gi 17561652 659 YRESLNKLMHMLHQTHPHFIRCIIP 683
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
853-1053 |
1.90e-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: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 853 SKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLeqeRDSSAEGEERSAKLLAQKADLEKQMANM 932
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 933 ndQLCDEEEKNAALTKQK---------KKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLN 1003
Cdd:COG4942 114 --YRLGRQPPLALLLSPEdfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17561652 1004 KEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKR 1053
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1128-1594 |
1.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1128 LEEELDAERNSRSKAEKARNEMQM-ELEELGDRLDEAggatQAQIELNKKREAELAKLRQDLEDAainsETSMAALRKKH 1206
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEA----EEKEEEYAELQEELEELEEELEEL----EAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1207 nDAVAELSDQLDTIQKMRgKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEaqltdmtlksDEQARLIQELTMG 1286
Cdd:COG4717 119 -EKLEKLLQLLPLYQELE-ALEAELAELPERLEELEERLEELRELEEELEELEAELA----------ELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1287 KNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTD 1366
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1367 VQRQLSKANSEIQ-----------QWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDL 1435
Cdd:COG4717 267 SLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1436 EDAQVDADRANSIASSLEkkqkgfdkvLDEWRRKCEALVAEVEQSQRETRAAATETFR----LRNQLEESGEQTEAVKRE 1511
Cdd:COG4717 347 EELQELLREAEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRAALEQAEeyqeLKEELEELEEQLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1512 NKALAQ--ELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALdeaecaleaeeaKVMRAQIEVSQIRSEIEKRLQEK 1589
Cdd:COG4717 418 LEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAEL------------EQLEEDGELAELLQELEELKAEL 485
|
....*
gi 17561652 1590 EEEFE 1594
Cdd:COG4717 486 RELAE 490
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1572-1894 |
2.21e-05 |
|
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: 49.35 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1572 QIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQK 1651
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1652 SMKKLQDTIRELQYQVEEEQRSLSESRDhaNLAERRSQVLQQEKEDLAIIYEQSERTRRQAELE--LAEVKDSVNELSNS 1729
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISCLKN--ELSELRRQIQRAELELQSTNSELEELQERLDLLKakASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1730 NSLLLATKRKVegdlQLLQSEIEEAMSDAK-TSDEKAKKA-IMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRL 1807
Cdd:pfam05557 162 QSSLAEAEQRI----KELEFEIQSQEQDSEiVKNSKSELArIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1808 DEAEaagikGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDL---------- 1877
Cdd:pfam05557 238 EREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLtssarqleka 312
|
330
....*....|....*..
gi 17561652 1878 IEKLQQKIKTYKRQIED 1894
Cdd:pfam05557 313 RRELEQELAQYLKKIED 329
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1059-1267 |
2.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1059 EKQRRKVEGELKIAQElieELNRHKheQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERN- 1137
Cdd:COG3206 181 EEQLPELRKELEEAEA---ALEEFR--QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDa 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1138 -SRSKAEKARNEMQMELEELGDRLDEAGGATQAQ----IELNKKREAELAKLRQDLEDAAINSETSMAALRKKhndaVAE 1212
Cdd:COG3206 256 lPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR----EAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1213 LSDQLDTIQKMRGKLerekNDKQREVDELQQsaDVEAKQRQNCERMAKQLEAQLT 1267
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLER--EVEVARELYESLLQRLEEARLA 380
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
940-1169 |
2.37e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 940 EEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLED 1019
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1020 IQAEEDKVNHLN-----KTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKD 1094
Cdd:COG3883 95 LYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1095 IELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQA 1169
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
944-1209 |
2.42e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 944 AALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQ----DEVISKLNKEKKHQEEVNRKL--- 1016
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrDELNEKVKELKEERDELNEKLnel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1017 ---LEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRqdcEKQRRKVEgelkiaqeLIEELNRHKHEQEQVIKKK 1093
Cdd:COG1340 91 reeLDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSP---EEEKELVE--------KIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1094 DiELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGA-TQAQIE 1172
Cdd:COG1340 160 E-KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEiIELQKE 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 17561652 1173 LNKKREaELAKLRQDLEDAAinSETSMAALRKKHNDA 1209
Cdd:COG1340 239 LRELRK-ELKKLRKKQRALK--REKEKEELEEKAEEI 272
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1078-1296 |
3.04e-05 |
|
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: 49.45 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1078 ELNRHKHEQEqvikkKDIELSSI---QSRLE--DEQSLVAKLQRQikellariqeleeeldaernsRSKAEKARNEMQME 1152
Cdd:NF012221 1568 EADRQRLEQE-----KQQQLAAIsgsQSQLEstDQNALETNGQAQ---------------------RDAILEESRAVTKE 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1153 LEELGDRLDEAGGATQAQIEL-----NKKREAELAKLRQDLEDAAINSETSMAALRKKHndaVAELSDQLDTIQKMRGKL 1227
Cdd:NF012221 1622 LTTLAQGLDALDSQATYAGESgdqwrNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRH---VDNQQKVKDAVAKSEAGV 1698
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 1228 ER-EKNdkQREVDELQQSADVEAKQRQNcERMAKQLEAQLTDM---TLKSDEQARLIQELTMGKNKVHNENQD 1296
Cdd:NF012221 1699 AQgEQN--QANAEQDIDDAKADAEKRKD-DALAKQNEAQQAESdanAAANDAQSRGEQDASAAENKANQAQAD 1768
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1019-1251 |
4.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1019 DIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKK------ 1092
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1093 -KDIELSSIQSRLE--------DEQSLVAKLQRQIKELLARIQELEEELDAERnsrSKAEKARNEMQMELEELGDRLDEA 1163
Cdd:COG3883 97 rSGGSVSYLDVLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1164 GGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQ 1243
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAG 253
|
....*...
gi 17561652 1244 SADVEAKQ 1251
Cdd:COG3883 254 AAGAAAGS 261
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1648-1894 |
4.54e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1648 DGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAE------LELAEVKD 1721
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEklekevKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1722 SVNELSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAK------KAIMDASKLADELRSEQEHASNLNQSKKT 1795
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1796 LESQVKDLQMRLDEAEAAgikggKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQERMY 1875
Cdd:PRK03918 319 LEEEINGIEERIKELEEK-----EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
250
....*....|....*....
gi 17561652 1876 DLIEKLQQKIKTYKRQIED 1894
Cdd:PRK03918 394 EELEKAKEEIEEEISKITA 412
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
993-1121 |
4.66e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 993 QSQDEVISKLnkEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIA 1072
Cdd:COG2433 376 LSIEEALEEL--IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17561652 1073 QELIEElnrhKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKEL 1121
Cdd:COG2433 454 RSEERR----EIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
863-1015 |
4.83e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 863 EKKFKVLEEEKTQ---EERKRKDMEAENARLEAEKQALLIQLEQERDSsaegEERSAKLLAQKADLEKQMANMNDQLCDE 939
Cdd:PRK12704 30 EAKIKEAEEEAKRileEAKKEAEAIKKEALLEAKEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 940 EEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQE---------SEKQAKDHQIRSLQDEIQSQDEVISKlNKEKKHQE 1010
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisglTAEEAKEILLEKVEEEARHEAAVLIK-EIEEEAKE 184
|
....*
gi 17561652 1011 EVNRK 1015
Cdd:PRK12704 185 EADKK 189
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1620-1883 |
5.18e-05 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 48.52 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1620 ELLKTKKKLEGDVNELEIALDH--SNKLNVDGQKSMKklqDTIRElQYQVEEEQRSLSESRDHANLAERRSQvLQQEKEd 1697
Cdd:pfam05911 591 DVLSGKADLEDFVLELSHILDWisNHCFSLLDVSSME---DEIKK-HDCIDKVTLSENKVAQVDNGCSEIDN-LSSDPE- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1698 laiIYEQSERTRRQAELELAEVKDSVNELSNsnslLLATKRKVEGDLQLLQSEIEEAMSDAKTSDekakkaimdasKLAD 1777
Cdd:pfam05911 665 ---IPSDGPLVSGSNDLKTEENKRLKEEFEQ----LKSEKENLEVELASCTENLESTKSQLQESE-----------QLIA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1778 ELRSEQEhasNLNQSKKTLESQVK-------DLQMRLDEAEAagikggkrQLAKLDMRIHELETELEGENRRHAETqkvl 1850
Cdd:pfam05911 727 ELRSELA---SLKESNSLAETQLKcmaesyeDLETRLTELEA--------ELNELRQKFEALEVELEEEKNCHEEL---- 791
|
250 260 270
....*....|....*....|....*....|....*.
gi 17561652 1851 rnkDRKCRELQFQVDEDKKSQERMYDLIE---KLQQ 1883
Cdd:pfam05911 792 ---EAKCLELQEQLERNEKKESSNCDADQedkKLQQ 824
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1336-1517 |
5.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1336 RQSLHSQVSNYQLECEQFREslEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLE 1415
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1416 NANQKIGTLEKNKQRLAHDLEDaqvdadransiassLEKKQKGFDKVLDEWRRKCE---ALVAE------VEQSQRETRA 1486
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQE--------------LEKKEEELEELIEEQLQELErisGLTAEeakeilLEKVEEEARH 169
|
170 180 190
....*....|....*....|....*....|.
gi 17561652 1487 AATETFRlrnQLEESGEQtEAVKRENKALAQ 1517
Cdd:PRK12704 170 EAAVLIK---EIEEEAKE-EADKKAKEILAQ 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1355-1579 |
6.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1355 ESLEEEQDAKTDVQRQLSKANSEIQQWRAKfEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHD 1434
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1435 LED------AQVDADRANSIASSLE-----KKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGE 1503
Cdd:COG4942 99 LEAqkeelaELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1504 QTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIR 1579
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
898-1316 |
7.13e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 898 LIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKnaaltkqKKKIEQDNEGLKKTVSDLETTIKKQESE 977
Cdd:PRK01156 331 LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESL-------KKKIEEYSKNIERMSAFISEILKIQEID 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 978 KQAKdhqirslqdeiqsqdevisklnkeKKHQEEVNRKLLEdiqaEEDKVNHLNKTKAKLESTLDELEDTLEREKrGRQD 1057
Cdd:PRK01156 404 PDAI------------------------KKELNEINVKLQD----ISSKVSSLNQRIRALRENLDELSRNMEMLN-GQSV 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1058 CEKQRRKVeGELKIaQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQ-----------RQIKELLARIQ 1126
Cdd:PRK01156 455 CPVCGTTL-GEEKS-NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeinksineyNKIESARADLE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1127 ELEEELDAERNSRSKAEKARNEMQ-MELEELGDRLDEAGGA----TQAQIELNKKREAELAKLRQDLEDAAINSETSMAA 1201
Cdd:PRK01156 533 DIKIKINELKDKHDKYEEIKNRYKsLKLEDLDSKRTSWLNAlaviSLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1202 LRKKHNDAVAELSDQLDT--------------IQKMRGKLEREKnDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLT 1267
Cdd:PRK01156 613 DKSYIDKSIREIENEANNlnnkyneiqenkilIEKLRGKIDNYK-KQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD 691
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 17561652 1268 DMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQ 1316
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
989-1130 |
7.55e-05 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 46.86 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 989 QDEIQSQdEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQdceKQRRKVEGE 1068
Cdd:pfam14362 105 EKEIDRE-LLEIQQEEADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQAEARCELDGTP---GTGTGVPGD 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1069 LKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQS----LVAKLQRQIKE---LLARIQELEE 1130
Cdd:pfam14362 181 GPVAKTKQAQLDAAQAELAALQAQNDARLAALRAELARLTAeraaARARSQAAIDGddgLLARLEALNR 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1473-1699 |
7.56e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1473 LVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQ 1552
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1553 ---ALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLE 1629
Cdd:COG4942 91 eiaELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1630 GDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLA 1699
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1318-1573 |
8.46e-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: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1318 QHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAkfegegvsraeELE 1397
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-----------ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1398 ETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEkkqkgfdKVLDEWRRKCEALVAEV 1477
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-------YLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1478 EQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEA 1557
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|....*.
gi 17561652 1558 ECALEAEEAKVMRAQI 1573
Cdd:COG4942 240 AERTPAAGFAALKGKL 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1744-1939 |
9.50e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1744 LQLLQSEIEEAmsDAKTSDEKAKKAIMDaskLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKGGK---- 1819
Cdd:COG3206 184 LPELRKELEEA--EAALEEFRQKNGLVD---LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDalpe 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1820 ----RQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVD-EDKKSQERMYDLIEKLQQKIKTYKRQIED 1894
Cdd:COG3206 259 llqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQ 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17561652 1895 AESLASG---NLAKYRQLQHVVEDAQERADAAENALQKLRLKGRSTSG 1939
Cdd:COG3206 339 LEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVG 386
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1030-1155 |
1.01e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1030 LNKTKAKLESTLDELEDTLEREKR-----GRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRL 1104
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17561652 1105 EDEQSLVAKLQRQIKELLARIQELEEELDA--ERNSRSKAEKARNEMQMELEE 1155
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEEAKEILLEKVEE 165
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1172-1415 |
1.02e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.98 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1172 ELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDA------VAELSDQLDTIQKMRGKLEREKN---DKQREVDELQ 1242
Cdd:pfam15742 55 EENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIreleleVLKQAQSIKSQNSLQEKLAQEKSrvaDAEEKILELQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1243 QSADVEAKQR--QNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQ---LEDAEAQLCALN----- 1312
Cdd:pfam15742 135 QKLEHAHKVCltDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQvrsLQDKEAQLEMTNsqqql 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1313 RIKQQ--QHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFReslEEEQDAKTDVQRQLSKANSEIQQWRAKF---EG 1387
Cdd:pfam15742 215 RIQQQeaQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALQ---EELQQVLKQLDVHVRKYNEKHHHHKAKLrraKD 291
|
250 260
....*....|....*....|....*...
gi 17561652 1388 EGVSRAEELEETRRKLTHKVQEMQEQLE 1415
Cdd:pfam15742 292 RLVHEVEQRDERIKQLENEIGILQQQSE 319
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1247-1457 |
1.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1247 VEAKQRQNcERMAKQLEAQLTDMTLKSDEQARLIQELtMGKNKVHN---ENQDLNRQLEDAEAQLCALNRIKQQQHSQLE 1323
Cdd:COG3206 166 LELRREEA-RKALEFLEEQLPELRKELEEAEAALEEF-RQKNGLVDlseEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1324 ELKRTLDQETRERQSL--HSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRR 1401
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1402 KLTHKVQEMQEQLENANQKIGTLEKNKQRLAhDLEDaqvDADRANSIASSLEKKQK 1457
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR-RLER---EVEVARELYESLLQRLE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1394-1931 |
1.23e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1394 EELEETRRKLTHKVQEMQEQLENANQkigTLEKNKQRLAHDLEDAQvdadransiaSSLEKKQKGFDKVLDEWRRKceal 1473
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNE---LHEKQKFYLRQSVIDLQ----------TKLQEMQMERDAMADIRRRE---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1474 vaevEQSQREtraaatetfrLRNQLEESGEQTEAvkrenkalAQELKDiaDQLGEGGKSVHDLQKMRRRLEIEKEELQQA 1553
Cdd:pfam15921 137 ----SQSQED----------LRNQLQNTVHELEA--------AKCLKE--DMLEDSNTQIEQLRKMMLSHEGVLQEIRSI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1554 L-DEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEEFeNTRKNHSRTIESMQVSLETESRGRAELLktkkklegdv 1632
Cdd:pfam15921 193 LvDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEI-SYLKGRIFPVEDQLEALKSESQNKIELL---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1633 neleialdhsnklnvdgqksMKKLQDTIRELQYQVEEEQRSLSESrdhANLAERRSQVLQQEKEdlaIIYEQSErtrrqa 1712
Cdd:pfam15921 262 --------------------LQQHQDRIEQLISEHEVEITGLTEK---ASSARSQANSIQSQLE---IIQEQAR------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1713 elelaevkdsvnelsNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASnlnQS 1792
Cdd:pfam15921 310 ---------------NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS---QE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1793 KKTLESQVKDLQMRLD--EAEAAGIKGGKRQLAKLDM----RIHELETELEGENRRHAETQKVLRNKDRKCR---ELQFQ 1863
Cdd:pfam15921 372 SGNLDDQLQKLLADLHkrEKELSLEKEQNKRLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmERQMA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1864 VDEDK-KSQERMYDLIEKLQQKIKTYKRQIEDAESLASGNLAKYRQLQHVVEDAQ--ERADAAENA-LQKLR 1931
Cdd:pfam15921 452 AIQGKnESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQekERAIEATNAeITKLR 523
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1006-1221 |
1.76e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1006 KKHQEEVN-----RKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQ-DCEKQRRKVEGELKIAQELIEEL 1079
Cdd:TIGR01612 1974 KKEQDTLNiifenQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKlSCDSQNYDTILELSKQDKIKEKI 2053
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1080 NRHKHEQEQVIKkkDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDR 1159
Cdd:TIGR01612 2054 DNYEKEKEKFGI--DFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDK 2131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1160 LDEAGGATQAQIELNKK-REAELAKLRQDLEDAAIN-SE--TSMAALRKKH----NDAVAELSDQLDTIQ 1221
Cdd:TIGR01612 2132 IIEKNDLIDKLIEMRKEcLLFSYATLVETLKSKVINhSEfiTSAAKFSKDFfefiEDISDSLNDDIDALQ 2201
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1322-1436 |
1.87e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1322 LEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKtdVQRQLSKANSEIQQwrAKFEGEGVSRaeELEETRR 1401
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL--LEEAEKEAQQAIKE--AKKEADEIIK--ELRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17561652 1402 KLT-----HKVQEMQEQLENANQKIGTLEKNKQRLAHDLE 1436
Cdd:PRK00409 599 GGYasvkaHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1602-1938 |
2.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1602 RTIESMQVSLETESRGRAELLKTKKKLEGDvneLEIALDHSNKLN--VDGQKSMKKLQDTIRELQYQVEEEQRSLSESRD 1679
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQD---YQAASDHLNLVQtaLRQQEKIERYQADLEELEERLEEQNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1680 HANLAERRSQVLQQEKEDLA---IIYEQS---ERTR----RQAELELAEVKD--SVNELSNSN-SLLLATKRKVEGDLQL 1746
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKsqlADYQQAldvQQTRaiqyQQAVQALERAKQlcGLPDLTADNaEDWLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1747 LQSEIEEAMSDAKTSDEKAKKAIMDASKLADE----------------LRSEQEHASNLNQskktLESQVKDLQMRLDEA 1810
Cdd:PRK04863 457 ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEvsrseawdvarellrrLREQRHLAEQLQQ----LRMRLSELEQRLRQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1811 EAAgikggKRQLAKLDMRIH---ELETELEGENRRHAETQKvlrnkdrkcrELQFQVDEDKKSQERMYDLIEKLQQKIKT 1887
Cdd:PRK04863 533 QRA-----ERLLAEFCKRLGknlDDEDELEQLQEELEARLE----------SLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1888 YKRQ----IEDAESLAsgnlakyrQLQHVVEDAQERADAAENALQKLRLKGRSTS 1938
Cdd:PRK04863 598 LAARapawLAAQDALA--------RLREQSGEEFEDSQDVTEYMQQLLERERELT 644
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1351-1929 |
2.41e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1351 EQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEqLENANQKIGT-----LE 1425
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQE-LQFENEKVSLkleeeIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1426 KNKQRLAHDLEDAQVDADRANSIASSLEKKQKgFDKVLDEWRRKCEALVAEVEQsqretraAATETFRLRNQLEESGEQT 1505
Cdd:pfam05483 142 ENKDLIKENNATRHLCNLLKETCARSAEKTKK-YEYEREETRQVYMDLNNNIEK-------MILAFEELRVQAENARLEM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1506 EAVKRENKALAQELKDiadqlgEGGKSVHDLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQiEVSQIRSEIEKR 1585
Cdd:pfam05483 214 HFKLKEDHEKIQHLEE------EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE-EKTKLQDENLKE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1586 LQEKEEEFENTRKNHSRtieSMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQY 1665
Cdd:pfam05483 287 LIEKKDHLTKELEDIKM---SLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1666 QVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSL---LLATKRKVEG 1742
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIaeeLKGKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1743 DLQLLQSEI---EEAMSDAKTSDE--------------------------------KAKKAIMDASKLADELRSEQEHAS 1787
Cdd:pfam05483 444 LLQAREKEIhdlEIQLTAIKTSEEhylkevedlktelekeklknieltahcdklllENKELTQEASDMTLELKKHQEDII 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1788 NLNQSKKTLESQVKDLQ---MRLDEAEAAGIKGGKRQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQV 1864
Cdd:pfam05483 524 NCKKQEERMLKQIENLEekeMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1865 DEDKKSqermydlIEKLQQKIKTYKRQIEDAESLASGNLAKYRQLQHVVEDAQERADAAENALQK 1929
Cdd:pfam05483 604 ENKNKN-------IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1021-1386 |
2.59e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1021 QAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQdcekQRRKVEGELKIAQELIEELNRHKHeqeqviKKKDIELSSI 1100
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQ----YQQVIDNFPKLSAELRQQLNNERD------EPRSVPPNMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1101 QSRLEDE----QSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGA--TQAQIELN 1174
Cdd:PRK10929 104 TDALEQEilqvSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAqlTALQAESA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1175 KKR----EAELAKL----RQDLedAAINSETsmaaLRKKHndavaelsDQLDT-IQKMRGKLereKNDKQREVDELQQSA 1245
Cdd:PRK10929 184 ALKalvdELELAQLsannRQEL--ARLRSEL----AKKRS--------QQLDAyLQALRNQL---NSQRQREAERALEST 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1246 DVEAKQrqnCERMAKQLEAQLT---DMTLKSDEQARLIQELTMGKNKVHNENQDLnRQledaeaqlcALNRIKQQqhSQ- 1321
Cdd:PRK10929 247 ELLAEQ---SGDLPKSIVAQFKinrELSQALNQQAQRMDLIASQQRQAASQTLQV-RQ---------ALNTLREQ--SQw 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1322 ------LEELKRTldQETR-----ERQSLHSQVSNYQLECEQFRESLEEEQ---DAKTDVQRQLSKANSEI--QQWRAKF 1385
Cdd:PRK10929 312 lgvsnaLGEALRA--QVARlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPqlrQIRQADGQPLTAEQNRIldAQLRTQR 389
|
.
gi 17561652 1386 E 1386
Cdd:PRK10929 390 E 390
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
965-1132 |
2.60e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 45.46 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 965 SDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNhlnktkAKLESTLDEL 1044
Cdd:pfam04108 13 NELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAAL------ERLEETLDKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1045 EDTLeREKRGRQDCEKQR--------RKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDeQSLVAKLQR 1116
Cdd:pfam04108 87 RNTP-VEPALPPGEEKQKtlldfideDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELES-LSSPSESIS 164
|
170
....*....|....*.
gi 17561652 1117 QIKELLARIQELEEEL 1132
Cdd:pfam04108 165 LIPTLLKELESLEEEM 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1095-1282 |
2.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1095 IELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAggatQAQIELN 1174
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY----EEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1175 KKREaELAKLRQDLEdaainsetSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQrqn 1254
Cdd:COG1579 86 RNNK-EYEALQKEIE--------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE--- 153
|
170 180
....*....|....*....|....*...
gi 17561652 1255 cermakqLEAQLTDMTLKSDEQARLIQE 1282
Cdd:COG1579 154 -------LEAELEELEAEREELAAKIPP 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1269-1511 |
2.87e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1269 MTLKSDEQARLIQEL-------TMGK-NK-----VHNENQDLNRQLEDAEAQLCA----LNRIKQQQHSQLEELKRTLDQ 1331
Cdd:PHA02562 145 MQLSAPARRKLVEDLldisvlsEMDKlNKdkireLNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1332 ETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWR--AKFEGEG------VSRAEELEETRRKL 1403
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGgvcptcTQQISEGPDRITKI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1404 THKVQEMQEQLENANQKIGTLEKnkqrLAHDLEDAQVdadRANSIASSLEKkqkgFDKVLDEWRRKCEALVAEVEQSQRE 1483
Cdd:PHA02562 305 KDKLKELQHSLEKLDTAIDELEE----IMDEFNEQSK---KLLELKNKIST----NKQSLITLVDKAKKVKAAIEELQAE 373
|
250 260
....*....|....*....|....*...
gi 17561652 1484 TRAAATETFRLRNQLEESGEQTEAVKRE 1511
Cdd:PHA02562 374 FVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
851-1161 |
3.00e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.19 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 851 KGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLiqleQERDSsaegeersakLLAQKADLEKQMA 930
Cdd:pfam15905 67 KNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAV----REKTS----------LSASVASLEKQLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 931 nmndqlcdEEEKNAALTKQKKKieqdNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKlnkekkhqe 1010
Cdd:pfam15905 133 --------ELTRVNELLKAKFS----EDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQK--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1011 evnrkllediqaeedkvnHLNKTKAKLEstldELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHE---QE 1087
Cdd:pfam15905 192 ------------------NLEHSKGKVA----QLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDiaqLE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1088 QVIKKKDIELSSIQSRLEDEqslVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEmqmELEELGDRLD 1161
Cdd:pfam15905 250 ELLKEKNDEIESLKQSLEEK---EQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNA---ELEELKEKLT 317
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1077-1185 |
3.33e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1077 EELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNE---MQMEL 1153
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREisrLDREI 474
|
90 100 110
....*....|....*....|....*....|..
gi 17561652 1154 EELGDRLDEAggatQAQIELNKKREAELAKLR 1185
Cdd:COG2433 475 ERLERELEEE----RERIEELKRKLERLKELW 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1507-1728 |
4.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1507 AVKRENKALAQELKDIADQLGEggksvhdLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEI---E 1583
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaelE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1584 KRLQEKEEEFENTRKNHSRTIESMQVSletESRGRAELLKTKKklegDVNELEIALDHSNKLNVDGQKSMKKLQDTIREL 1663
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRL---GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1664 QYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSN 1728
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
935-1152 |
4.57e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.36 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 935 QLCDEEEKNAALTKQKKKIEQD-NEGLKKTVSDLETTIKKQ-ESEKQAKDHQirslQDEIQSQDEVISKLNKEKKHQEev 1012
Cdd:pfam09787 8 ELADYKQKAARILQSKEKLIASlKEGSGVEGLDSSTALTLElEELRQERDLL----REEIQKLRGQIQQLRTELQELE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1013 NRKLLEDIQAEEDkvnhlnktkaklestLDELEDTLEREKRGRQDCEKQRRKVEGELkiaQELIEELNRHKHEQEQVIKK 1092
Cdd:pfam09787 82 AQQQEEAESSREQ---------------LQELEEQLATERSARREAEAELERLQEEL---RYLEEELRRSKATLQSRIKD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 1093 KDIELSSIQSRL-------EDEQSLVAKLqRQIKELLARIQELEEELDAERNSR----SKAEKARNEMQME 1152
Cdd:pfam09787 144 REAEIEKLRNQLtsksqssSSQSELENRL-HQLTETLIQKQTMLEALSTEKNSLvlqlERMEQQIKELQGE 213
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1010-1417 |
4.76e-04 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 44.99 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1010 EEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRhKHEQEQV 1089
Cdd:COG5281 14 AAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALA-EDAAAAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1090 IKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQA 1169
Cdd:COG5281 93 AAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1170 QIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEA 1249
Cdd:COG5281 173 AAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1250 KQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTL 1329
Cdd:COG5281 253 AAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1330 DQETRERQSLHSQVSNYQlecEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQE 1409
Cdd:COG5281 333 ALAQRALAAAALAAAAQE---AALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATS 409
|
....*...
gi 17561652 1410 MQEQLENA 1417
Cdd:COG5281 410 AFSGLTDA 417
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1102-1430 |
4.87e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1102 SRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDeaggatqaqiELNKKREAEL 1181
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQ----------ELREKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1182 AKLRQdledaainsetsMAALRKKHNDAVAELSDQLDTIQKMRGKLerekNDKQREVDELQqsadveakqrqnceRMAKQ 1261
Cdd:COG1340 71 EKVKE------------LKEERDELNEKLNELREELDELRKELAEL----NKAGGSIDKLR--------------KEIER 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1262 LEAQLTDMTLKSDEQARLIQELtmgknkvhnenQDLNRQLEDAEAQLcalnrikqQQHSQLEELKRTLDQETRERQSLHS 1341
Cdd:COG1340 121 LEWRQQTEVLSPEEEKELVEKI-----------KELEKELEKAKKAL--------EKNEKLKELRAELKELRKEAEEIHK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1342 QVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKfegegvsrAEELEETRRKLTHKVQEMQEQLENANQKI 1421
Cdd:COG1340 182 KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK--------ADELHEEIIELQKELRELRKELKKLRKKQ 253
|
....*....
gi 17561652 1422 GTLEKNKQR 1430
Cdd:COG1340 254 RALKREKEK 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1620 |
5.09e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1389 GVSRAEELEETRRKLthkvQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRR 1468
Cdd:COG4942 15 AAAQADAAAEAEAEL----EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1469 KCEALVAEVEQSQRETRAAATETFRLRNQ-----------LEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQ 1537
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1538 KMRRRLEI---EKEELQQALDeaecaleaeeakvmRAQIEVSQIRSEIEKRLQEKEEEFENTRKNhSRTIESMQVSLETE 1614
Cdd:COG4942 171 AERAELEAllaELEEERAALE--------------ALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAE 235
|
....*.
gi 17561652 1615 SRGRAE 1620
Cdd:COG4942 236 AAAAAE 241
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1183-1465 |
5.16e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1183 KLRQDLEDAAINSEtsMAALRKkhnDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNcermakql 1262
Cdd:PHA02562 154 KLVEDLLDISVLSE--MDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQN-------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1263 eaqltdmtlKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLD--QETRERQSLH 1340
Cdd:PHA02562 221 ---------KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1341 SQVSNYQleceqfrESLEEEQDAKTDVQRQLSKANSEIQQwrakfegegvsrAEELEETRRKLTHKVQEMQEQLENANQK 1420
Cdd:PHA02562 292 QQISEGP-------DRITKIKDKLKELQHSLEKLDTAIDE------------LEEIMDEFNEQSKKLLELKNKISTNKQS 352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17561652 1421 IGTLEKNKQRLAHDLEDAQvdADRANsIASSLEKKQKGFDKVLDE 1465
Cdd:PHA02562 353 LITLVDKAKKVKAAIEELQ--AEFVD-NAEELAKLQDELDKIVKT 394
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1295-1591 |
5.24e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1295 QDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKA 1374
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1375 NSEIQQWRAKFEgEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEK 1454
Cdd:COG4372 121 QKERQDLEQQRK-QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1455 KQKGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVH 1534
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1535 DLQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEE 1591
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1210-1436 |
5.41e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1210 VAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTL-KSDEQAR---LIQELTM 1285
Cdd:pfam00038 56 IEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLaRVDLEAKiesLKEELAF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1286 GKNKVHNENQDLNRQLEDAEAQL-------CALNRIKQQQHSQLEELKRTLDQETRErqSLHSQVSNYQLECEQFRESLE 1358
Cdd:pfam00038 136 LKKNHEEEVRELQAQVSDTQVNVemdaarkLDLTSALAEIRAQYEEIAAKNREEAEE--WYQSKLEELQQAAARNGDALR 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1359 EEQDAKTDVQRQLSKANSEIQQWRakfegegvSRAEELEETRRKLThkvQEMQEQLENANQKIGTLEKNKQRLAHDLE 1436
Cdd:pfam00038 214 SAKEEITELRRTIQSLEIELQSLK--------KQKASLERQLAETE---ERYELQLADYQELISELEAELQETRQEMA 280
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
881-1001 |
5.44e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 881 KDMEAENARLEAEKQALliqleqERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIEQDNEGL 960
Cdd:COG0542 414 DELERRLEQLEIEKEAL------KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17561652 961 KktvsDLETTIKKQESEKQAKDhqiRSLQDEIQSQD--EVISK 1001
Cdd:COG0542 488 P----ELEKELAELEEELAELA---PLLREEVTEEDiaEVVSR 523
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1042-1337 |
5.64e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1042 DELEDTLEREKRGRQDCEKQRRKvEGELKIAQELIEELNRHKHEQEQVIKkkdielSSIQSRLEDEQSLVAKLQRQIKEL 1121
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELK------PSGQGGLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1122 LARIQELEE---ELDAErNSRSKAEKARNEMQMELEELGDRLDEAggatQAQIELNKKREAELAKLRQDLEDAAINSETS 1198
Cdd:pfam02029 76 QKRLQEALErqkEFDPT-IADEKESVAERKENNEEEENSSWEKEE----KRDSRLGRYKEEETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1199 MAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDE-----LQQSADVEAKQRQNCERMAKQLEAQLTDM---- 1269
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYeskvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRRqggl 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1270 ----TLKSDEQARLIQELTMGKNKVHN---ENQDL----NRQLEdAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQ 1337
Cdd:pfam02029 231 sqsqEREEEAEVFLEAEQKLEELRRRRqekESEEFeklrQKQQE-AELELEELKKKREERRKLLEEEEQRRKQEEAERK 308
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1025-1339 |
5.70e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1025 DKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCekqrrkVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRL 1104
Cdd:pfam00038 18 DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSL------YEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1105 EDEQSLVaklqrqikellariQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDeaggatqaqiELNKKREAELAKL 1184
Cdd:pfam00038 92 EDELNLR--------------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELA----------FLKKNHEEEVREL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1185 RQDLEDAAINSETSmAALRKKHNDAVAELSDQLDTIQKmRGKLEREKNDKQReVDELQQSADVEAKQRQNCERMAKQLEa 1264
Cdd:pfam00038 148 QAQVSDTQVNVEMD-AARKLDLTSALAEIRAQYEEIAA-KNREEAEEWYQSK-LEELQQAAARNGDALRSAKEEITELR- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17561652 1265 qltdmtlksdeqaRLIQELTMGKNKVHNENQDLNRQLEDAEAQLCA----LNRIKQQQHSQLEELKRTLDQETRERQSL 1339
Cdd:pfam00038 224 -------------RTIQSLEIELQSLKKQKASLERQLAETEERYELqladYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
972-1144 |
6.38e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 972 KKQESEKQAKdhqirSLQDEIQSQDEVISKlNKEKKHQEEvNRKLLEDIQAE-EDKVNHLNKtkakLESTLDELEDTLER 1050
Cdd:PRK12704 32 KIKEAEEEAK-----RILEEAKKEAEAIKK-EALLEAKEE-IHKLRNEFEKElRERRNELQK----LEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1051 EKrgrQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDE--QSLVAKLQRQIK-ELLARIQE 1127
Cdd:PRK12704 101 KL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEakEILLEKVEEEARhEAAVLIKE 177
|
170
....*....|....*..
gi 17561652 1128 LEEEldAERNSRSKAEK 1144
Cdd:PRK12704 178 IEEE--AKEEADKKAKE 192
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1668-1819 |
6.49e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1668 EEEQRSLSESRDHANLAERRSQV-----------LQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSNSNSLLLAT 1736
Cdd:pfam05262 188 EDNEKGVNFRRDMTDLKERESQEdakraqqlkeeLDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1737 KRKVEGDLQLLQS-EIEEAMSDAKTSDEKAKKAI-MDASKLADELRSEQEHASNLN-QSKKTLESQVKDLQMRLDEAEAA 1813
Cdd:pfam05262 268 SPKEDKQVAENQKrEIEKAQIEIKKNDEEALKAKdHKAFDLKQESKASEKEAEDKElEAQKKREPVAEDLQKTKPQVEAQ 347
|
....*.
gi 17561652 1814 GIKGGK 1819
Cdd:pfam05262 348 PTSLNE 353
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
884-1019 |
7.40e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 884 EAENARLEAEKQALLIQLEQ-----ERDSSAEGEERSAKLLAQKADLEK----------QMANMNDQLCDEEEKnaaLTK 948
Cdd:pfam08614 20 EAENAKLQSEPESVLPSTSSsklskASPQSASIQSLEQLLAQLREELAElyrsrgelaqRLVDLNEELQELEKK---LRE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17561652 949 QKKKIEQdnegLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSqdeviskLNKEKKHQEEVNRKLLED 1019
Cdd:pfam08614 97 DERRLAA----LEAERAQLEEKLKDREEELREKRKLNQDLQDELVA-------LQLQLNMAEEKLRKLEKE 156
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1315-1530 |
8.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1315 KQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFE-------- 1386
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1387 -GEGVSRAEELEE--------TRRKLTHKVQE-MQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQ 1456
Cdd:COG3883 98 sGGSVSYLDVLLGsesfsdflDRLSALSKIADaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17561652 1457 KGFDKVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGG 1530
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1569-1837 |
8.72e-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: 44.12 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1569 MRAQIEVSQIRSEIEKRLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVD 1648
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1649 GQKSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNELSN 1728
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1729 SNSLLLATKRKVEGDL---QLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRS---------EQEHASNLNQSKKTL 1796
Cdd:pfam07888 207 QVLQLQDTITTLTQKLttaHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqAELHQARLQAAQLTL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17561652 1797 ESQVKDLQMRLDEAEAAGIKGGKRQLAKLDM-RIHELETELE 1837
Cdd:pfam07888 287 QLADASLALREGRARWAQERETLQQSAEADKdRIEKLSAELQ 328
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
870-1185 |
8.87e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 870 EEEKTQEERKRKDMEAENARLEAEKQalliQLEQERDSSAEGEERSAKLLAQKADLEKqmANMNDQLCDEEEKNAALTKQ 949
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQ----QLRQQLDQLKEQLQLLNKLLPQANLLAD--ETLADRLEELREELDAAQEA 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 950 KKKIEQDNeglkKTVSDLETtikkqesekqakdhQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKL--LEDIQAeedKV 1027
Cdd:COG3096 909 QAFIQQHG----KALAQLEP--------------LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfaLSEVVQ---RR 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1028 NHLNKTKAklESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRhkheqeqvikkkdiELSSIQSRLEDE 1107
Cdd:COG3096 968 PHFSYEDA--VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--------------VLASLKSSRDAK 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1108 QSLVAKLQRQIKEL------------LARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQielnk 1175
Cdd:COG3096 1032 QQTLQELEQELEELgvqadaeaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE----- 1106
|
330
....*....|
gi 17561652 1176 KREAELAKLR 1185
Cdd:COG3096 1107 REQVVQAKAG 1116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
882-1043 |
9.31e-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: 42.99 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 882 DMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKI--EQDNEG 959
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 960 LKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKvnhLNKTKAKLES 1039
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---LEAEREELAA 170
|
....
gi 17561652 1040 TLDE 1043
Cdd:COG1579 171 KIPP 174
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
921-1248 |
1.03e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 921 QKADLEKQMANMNDQLCDEEEknaaLTKQKKKIEQDNEGLKKTVSD-LETTIKKQESEKqakDHQIRS------LQDEIQ 993
Cdd:PLN03229 417 RKVNMKKREAVKTPVRELEGE----VEKLKEQILKAKESSSKPSELaLNEMIEKLKKEI---DLEYTEaviamgLQERLE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 994 SQDEVISKLNKEkkhQEEVNRKLLEDIQAEEDKVNHlNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQ 1073
Cdd:PLN03229 490 NLREEFSKANSQ---DQLMHPVLMEKIEKLKDEFNK-RLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINK 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1074 ELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAE-----------------R 1136
Cdd:PLN03229 566 KFKEVMDRPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEvigvtkknkdtaeqtppP 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1137 NSRSKAEKARNEMQMELEELGD-----------RLDEAGGATQAQIELNKKREAELAKLRQDLEdAAINSetsmAALRKK 1205
Cdd:PLN03229 646 NLQEKIESLNEEINKKIERVIRssdlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIA-EALNS----SELKEK 720
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17561652 1206 HNDAVAELSDQLDTIQKMRGKLereKNDKQREVDELQQSADVE 1248
Cdd:PLN03229 721 FEELEAELAAARETAAESNGSL---KNDDDKEEDSKEDGSRVE 760
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1585-1896 |
1.04e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1585 RLQEKEEEFENTRKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALDHSNKLNVDGQKSMKKLQDTIRELQ 1664
Cdd:pfam02029 11 RRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1665 YQVEEEQRSLSESRDHANLAERRSQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNElsnSNSLLLATKRKV-EGD 1743
Cdd:pfam02029 91 PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQ---AEEEGEEEEDKSeEAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1744 LQLLQSEIEEAMSDAKTSDEKAK----KAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAGIKGGK 1819
Cdd:pfam02029 168 EVPTENFAKEEVKDEKIKKEKKVkyesKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1820 RQLAKLDMRIHELETElEGENRRHA--------ETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQ 1891
Cdd:pfam02029 248 QKLEELRRRRQEKESE-EFEKLRQKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRR 326
|
....*
gi 17561652 1892 IEDAE 1896
Cdd:pfam02029 327 AEAAE 331
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
878-1026 |
1.04e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 878 RKRKDMEAENARLEAEKQAlliqleQERDSSAEGEERSAKLLAQKADLEKQMANMNDqLCDEEEKNAALTKQKKKIEQDN 957
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEA------EEKLEAALLEAKELLLRERNQQRQEARREREE-LQREEERLVQKEEQLDARAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 958 EGLKKTVSDLETTIKKQESEKQAKDHQIR------SLQDEIQSQDEVISKLNKEKKHQEEVN-RKLLEDIQAEEDK 1026
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDnelyrvAGLTPEQARKLLLKLLDAELEEEKAQRvKKIEEEADLEAER 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
856-1093 |
1.14e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 856 NEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLI-----------QLEQERDSSAEGEERSAKllAQKAD 924
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneynkiesaraDLEDIKIKINELKDKHDK--YEEIK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 925 LEKQMANMNDQLCDEEEKNAALTkQKKKIEQDN-----EGLKKTVSDLETTIKKQESE----KQAKDHQIRSLQDEIQSQ 995
Cdd:PRK01156 553 NRYKSLKLEDLDSKRTSWLNALA-VISLIDIETnrsrsNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNL 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 996 DEVISKLnKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQEL 1075
Cdd:PRK01156 632 NNKYNEI-QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
250
....*....|....*...
gi 17561652 1076 IEELNRHKHEQEQVIKKK 1093
Cdd:PRK01156 711 INELSDRINDINETLESM 728
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1580-1933 |
1.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1580 SEIEKRLQEKEEEFENTrKNHSRTIESMQVSLETESRGRAELLKTKKKLEGDVNELEialdhsnKLNVDGQKSMKKLQDT 1659
Cdd:PRK03918 189 ENIEELIKEKEKELEEV-LREINEISSELPELREELEKLEKEVKELEELKEEIEELE-------KELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1660 IRELQYQVEEEQRSLSESRD----------HANLAERRSQVLQQEKEDLAIIYEQSERTRRQAEL------ELAEVKDSV 1723
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEkvkelkelkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieerikELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1724 NELSNSNSLLLATKRKVEGDLQLLQS--EIEEAMSDAKT-----SDEKAKKAIMDASKLADELRSEQEhasNLNQSKKTL 1796
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEakAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEIS---KITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1797 ESQVKDLQMRLDEAEAAGIKGG--KRQLAKLDMR--IHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKK--S 1870
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPvcGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliK 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1871 QERMYDLIEKLQQKIKTY-----KRQIEDAESLaSGNLAKYRQLQHVVEDAQERADAAENALQKLRLK 1933
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYnleelEKKAEEYEKL-KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1322-1898 |
1.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1322 LEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFE--GEGVSRAEELEET 1399
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1400 RRKLTHKVQEMQEQLENANQKIGTLEKNKQRLaHDLEDAQVDADRANSIASSLEKKQkgfdkvLDEWRRKCEALVAEVeQ 1479
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKND------IENKKQILSNIDAEI-N 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1480 SQRETRAAATETFRLRNQLEESGEQTEAVKREnkalAQELKDIADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAEC 1559
Cdd:PRK01156 323 KYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ----ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1560 ALEAEEAkvmraqiEVSQIRSEIEKRLQEKEEEfentrknhsrtIESMQVSLETESRGRAELLKTKKKLEGD----VNEL 1635
Cdd:PRK01156 399 IQEIDPD-------AIKKELNEINVKLQDISSK-----------VSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGT 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1636 EIALDHSNKLNVDGQKSMKKLQDTIRELqyqvEEEQRSLSESRDHanLAERRSQVLQQEKEDlaiiYEQSERTRRQAELE 1715
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKKSRLEEKIREI----EIEVKDIDEKIVD--LKKRKEYLESEEINK----SINEYNKIESARAD 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1716 LAEVKDSVNELSnsnslllatkrkvegdlqllqseieeamsDAKTSDEKAKKAImDASKLADeLRSEQEHASNLNQSKKT 1795
Cdd:PRK01156 531 LEDIKIKINELK-----------------------------DKHDKYEEIKNRY-KSLKLED-LDSKRTSWLNALAVISL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1796 LEsqVKDLQMRLDEAeaagikggKRQLAKLDMRIHELETELEGENrrhAETQKVLRNKDRKCRELQFQVDE--DKKSQer 1873
Cdd:PRK01156 580 ID--IETNRSRSNEI--------KKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEiqENKIL-- 644
|
570 580
....*....|....*....|....*
gi 17561652 1874 mydlIEKLQQKIKTYKRQIEDAESL 1898
Cdd:PRK01156 645 ----IEKLRGKIDNYKKQIAEIDSI 665
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1061-1195 |
1.30e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1061 QRRKVEGELKIAQELIEELNRHKHEQEqvikkkdiELSSIQSRLEDEQSLVAKLQRQikelLARIQEL-------EEELD 1133
Cdd:COG1566 84 ALAQAEAQLAAAEAQLARLEAELGAEA--------EIAAAEAQLAAAQAQLDLAQRE----LERYQALykkgavsQQELD 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17561652 1134 AERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELnKKREAELAKLRQDLEDAAINS 1195
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQV-AQAEAALAQAELNLARTTIRA 212
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
874-1860 |
1.48e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 874 TQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAegeersAKLLAQKA-DLEKQMANMNDQLCDEEEKNAALTKQ--K 950
Cdd:NF041483 191 AEEARQRLGSEAESARAEAEAILRRARKDAERLLNA------ASTQAQEAtDHAEQLRSSTAAESDQARRQAAELSRaaE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 951 KKIEQDNEGLK-------KTVSDLETTIKKQESEKQAKDHQ-IRSLQDEIQsqdEVISKLNKEKKHQEEVNRKLLEDIQA 1022
Cdd:NF041483 265 QRMQEAEEALRearaeaeKVVAEAKEAAAKQLASAESANEQrTRTAKEEIA---RLVGEATKEAEALKAEAEQALADARA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1023 EEDKVNHLNKTKAKlestldeledTLEREKRGRQdCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKkdiELSSIQS 1102
Cdd:NF041483 342 EAEKLVAEAAEKAR----------TVAAEDTAAQ-LAKAARTAEEVLTKASEDAKATTRAAAEEAERIRR---EAEAEAD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1103 RLEDE-----QSLVAKLQRQIKELLARIQELEEEldaERNSRSKAEKARNEMQMELEELgdRLDEAGGATQAQIELNKKR 1177
Cdd:NF041483 408 RLRGEaadqaEQLKGAAKDDTKEYRAKTVELQEE---ARRLRGEAEQLRAEAVAEGERI--RGEARREAVQQIEEAARTA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1178 EAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLD-TIQKMRGKLEREKNDKQREVDELQQSADVEAKQ-RQNC 1255
Cdd:NF041483 483 EELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEeTLERTRAEAERLRAEAEEQAEEVRAAAERAARElREET 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1256 ER--MAKQLEAQLTDMTLKSDEQARLI---QELTMGKNKVHNENQDLNRQLEDAEAQlcALNRIKQQQHSQLEELKRTLD 1330
Cdd:NF041483 563 ERaiAARQAEAAEELTRLHTEAEERLTaaeEALADARAEAERIRREAAEETERLRTE--AAERIRTLQAQAEQEAERLRT 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1331 QETRERQSLHSQVSNYQLECEQfrESLEEEQDAKTDVQRQLSKANSEIQqwrAKFEGEGVSRAEELEETRRKLTHKVQEM 1410
Cdd:NF041483 641 EAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQESADRVRAEAA---AAAERVGTEAAEALAAAQEEAARRRREA 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1411 QEQLENANQKIgtlEKNKQRLAHDLEDAQVDADRansiasSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETR----- 1485
Cdd:NF041483 716 EETLGSARAEA---DQERERAREQSEELLASARK------RVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRdsvag 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1486 ---AAATETFRLRNQLEESGEQTeavkrenKALAQELKD--IADQLGEGGKSVHDLQKMRRRLEIEKEELQQALDEAECA 1560
Cdd:NF041483 787 lqeQAEEEIAGLRSAAEHAAERT-------RTEAQEEADrvRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1561 LEAEEAKVMRAQIEVSQ-IRSEIEKRLQEKEEEFENTRK------NHSRTIESMQV-SLETESRGRAELLKTKKKLEGDV 1632
Cdd:NF041483 860 AIAEAERLRSDASEYAQrVRTEASDTLASAEQDAARTRAdaredaNRIRSDAAAQAdRLIGEATSEAERLTAEARAEAER 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1633 NELEIALDHSNKLNVDGQKSMKKLQDTIRELQYQVEEEQRSLSESRDHanlAERRSQVLQQEKEDLAiiyEQSERTRRQA 1712
Cdd:NF041483 940 LRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQH---AERIRTEAERVKAEAA---AEAERLRTEA 1013
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1713 ELELAEVKDSVNELSNSNSLLLAtkRKVEGDLQLLQSEIEEAMSDAKtsdEKAKKAIMDASKLADEL----RSEQEHASn 1788
Cdd:NF041483 1014 REEADRTLDEARKDANKRRSEAA--EQADTLITEAAAEADQLTAKAQ---EEALRTTTEAEAQADTMvgaaRKEAERIV- 1087
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1789 lnqSKKTLESQVKDLQMRLDEAEAagIKGGKRQLAKLDMRIHELETELEGE-----NRRHAETQKVLRNKDRKCREL 1860
Cdd:NF041483 1088 ---AEATVEGNSLVEKARTDADEL--LVGARRDATAIRERAEELRDRITGEieelhERARRESAEQMKSAGERCDAL 1159
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
876-1074 |
1.55e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 876 EERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGE-ERSAKLLAQKADLEKQMANMNDQLCDEEEKNAALTKQ--KKK 952
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREElELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQaaQER 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 953 IEQDNEGLKKTVSDLETTIKKQESEKQAKdhqirslqdEIQSQDEVISKLNKEKKHQEEVnrkllediqAEEDKVNHLNK 1032
Cdd:pfam15709 421 ARQQQEEFRRKLQELQRKKQQEEAERAEA---------EKQRQKELEMQLAEEQKRLMEM---------AEEERLEYQRQ 482
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17561652 1033 TKaklestldeledtlEREKRGRQDCEKQRRKVEGELKIAQE 1074
Cdd:pfam15709 483 KQ--------------EAEEKARLEAEERRQKEEEAARLALE 510
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
893-1308 |
1.62e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 893 EKQALLIQLEQERdssaegeersAKLLAQKADLEKQMANMNDQLCDEEEK-NAALTKQKKKIEQDNEGLKKTVSDLETTI 971
Cdd:pfam15964 350 EKTKALIQCEQLK----------SELERQKERLEKELASQQEKRAQEKEAlRKEMKKEREELGATMLALSQNVAQLEAQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 972 KKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQeevnrkllediqaeedkvnhLNKTKAKlestldelEDTLERE 1051
Cdd:pfam15964 420 EKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQ--------------------LNQTKMK--------KDEAEKE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1052 KRgrqdcekqrrkvegelkiaqELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEE 1131
Cdd:pfam15964 472 HR--------------------EYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1132 LDAERNSRSKAEKARNEmqmeleelgdrlDEAGGATQAQielnkKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVA 1211
Cdd:pfam15964 532 LHLTRLEKESIQQSFSN------------EAKAQALQAQ-----QREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIA 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1212 ELSDQLDTIQKmrgKLEREKNDKQREVDELQQSAD-----VEAKQRQNCE---------RMAKQLEAQLTDMTLKSDEQA 1277
Cdd:pfam15964 595 KLKEECCTLAK---KLEEITQKSRSEVEQLSQEKEylqdrLEKLQKRNEEleeqcvqhgRMHERMKQRLRQLDKHCQATA 671
|
410 420 430
....*....|....*....|....*....|.
gi 17561652 1278 RLIQELTMGKNKVHNENQDLNRQLEDAEAQL 1308
Cdd:pfam15964 672 QQLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
996-1282 |
1.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 996 DEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQEL 1075
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1076 IEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEE 1155
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1156 LGDRLDEAGgaTQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQ 1235
Cdd:COG4372 162 LQEELAALE--QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17561652 1236 REVDELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQE 1282
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
968-1133 |
1.88e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.11 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 968 ETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKL---LEDIQAEEDKVnhLNKTKAKLESTLDEL 1044
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLaekYEEIKDKQEKL--MRRCKKVLQRLNSQL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1045 EDTLEREKrgrqDCEKQRRKVEGELKIAQELIEELNRHKHEQE-QVIKKKDIELSSiqsrledEQSLVAKLQRQIKELLa 1123
Cdd:pfam10168 624 PVLSDAER----EMKKELETINEQLKHLANAIKQAKKKMNYQRyQIAKSQSIRKKS-------SLSLSEKQRKTIKEIL- 691
|
170
....*....|
gi 17561652 1124 riQELEEELD 1133
Cdd:pfam10168 692 --KQLGSEID 699
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
856-1043 |
1.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 856 NEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQE-RDSSAEGEERS--AKLLAQK--ADLEKQMA 930
Cdd:COG3883 43 QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaRALYRSGGSVSylDVLLGSEsfSDFLDRLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 931 NMNDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAkdhqirsLQDEIQSQDEVISKLNKEKKHQE 1010
Cdd:COG3883 123 ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE-------LEAQQAEQEALLAQLSAEEAAAE 195
|
170 180 190
....*....|....*....|....*....|...
gi 17561652 1011 EVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDE 1043
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
857-995 |
2.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 857 EEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLeqERDSSAEGEERSAK----LLAQKADLEKQMANM 932
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--KKYEEQLGNVRNNKeyeaLQKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17561652 933 NDQLCDEEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQ 995
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
947-1143 |
2.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 947 TKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQ------SQDEVISKLnKEKKHQE----EVNRKL 1016
Cdd:PRK05771 78 KVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIErlepwgNFDLDLSLL-LGFKYVSvfvgTVPEDK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1017 LEDIQAEEDKVNHLNKTKAKLES-----TLDELEDtlerekrgrqdcekqrrKVEGELKIAQELIEELNRHKHEQEqvik 1091
Cdd:PRK05771 157 LEELKLESDVENVEYISTDKGYVyvvvvVLKELSD-----------------EVEEELKKLGFERLELEEEGTPSE---- 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17561652 1092 kkdiELSSIQSRLEDEQSLVAKLQRQIKELLAR----IQELEEELDAERNsrsKAE 1143
Cdd:PRK05771 216 ----LIREIKEELEEIEKERESLLEELKELAKKyleeLLALYEYLEIELE---RAE 264
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
859-1198 |
2.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 859 FEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLCD 938
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 939 EEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLnkEKKHQEEVNRKLLE 1018
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1019 DIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDIELS 1098
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1099 SIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKRE 1178
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
330 340
....*....|....*....|
gi 17561652 1179 AELAKLRQDLEDAAINSETS 1198
Cdd:COG4372 344 QLLLVGLLDNDVLELLSKGA 363
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
870-1189 |
2.37e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 870 EEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQmanmndQLCDEEEKNAALTKQ 949
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEE------AFLDRTAKREERRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 950 KKKIEQDNEG-LKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDkvn 1028
Cdd:pfam02029 78 RLQEALERQKeFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1029 hlnktkaKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQviKKKDIELSSIQSRLEDEQ 1108
Cdd:pfam02029 155 -------EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV--KSQNGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1109 SLVAKLQRQIKELLARIQeLEEELDAERNSRSKAEKARNEMQ----------MELEELGDRLDEAGGATQAQiELNKKRE 1178
Cdd:pfam02029 226 RQGGLSQSQEREEEAEVF-LEAEQKLEELRRRRQEKESEEFEklrqkqqeaeLELEELKKKREERRKLLEEE-EQRRKQE 303
|
330
....*....|.
gi 17561652 1179 AELAKLRQDLE 1189
Cdd:pfam02029 304 EAERKLREEEE 314
|
|
| Syntaxin-6_N |
pfam09177 |
Syntaxin 6, N-terminal; Members of this family, which are found in the amino terminus of ... |
1363-1430 |
2.44e-03 |
|
Syntaxin 6, N-terminal; Members of this family, which are found in the amino terminus of various SNARE proteins, adopt a structure consisting of an antiparallel three-helix bundle. Their exact function has not been determined, though it is known that they regulate the SNARE motif, as well as mediate various protein-protein interactions involved in membrane-transport.
Pssm-ID: 462706 [Multi-domain] Cd Length: 99 Bit Score: 39.09 E-value: 2.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1363 AKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQR 1430
Cdd:pfam09177 6 VKEEVQESLDKLESLYRSWLRLLSLTSSSSSPELDELRRELRTALESLEWDLEDLEEAVRIVESNPSK 73
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
1031-1258 |
2.49e-03 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 41.84 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1031 NKTKAKLEST---LDELEDTLEREKRGRQDCEKQRRKV--EGELKIAQELIEELNRHKHEQEQVIKKKDIELSSIQSRLE 1105
Cdd:pfam06705 1 NETAVKLSNMnerVSGFHDKMENEIEVKRVDEDTRVKMikEAIAHLEKLIQTESKKRQESFEDIQEEFKKEIDNMQETIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1106 DE-QSLVAKLQRQIKELLARIQELEEELDAERNSRSKA-EKARNEMQMELEELGDRLD-EAGGATQAQIELNKKREAELA 1182
Cdd:pfam06705 81 EEiDDMAANFRKALAELNDTINNVETNLQNEIAIHNDAiEALRKEALKSLNDLETGIAtENAERKKMYDQLNKKVAEGFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1183 KLRQDLEDAAINSETSMAALRKKHNDAVAE---LSDQ-----LDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQN 1254
Cdd:pfam06705 161 RISAAIDTEKNARDSAVSAATTELTNTKLVekcVNEQfenavLSEIAAIKEELDREKAERKAADDKIVQAVNDYTKALQG 240
|
....
gi 17561652 1255 CERM 1258
Cdd:pfam06705 241 GLSL 244
|
|
| CENP-Q |
pfam13094 |
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ... |
1015-1133 |
2.67e-03 |
|
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.
Pssm-ID: 432970 [Multi-domain] Cd Length: 159 Bit Score: 40.35 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1015 KLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLEREKRGRQD----CEKQRRKVEGELKIAQELIEELNRHKH---EQE 1087
Cdd:pfam13094 23 KLLDRNKALEAQLSAELHSLELLEEEIEKEEALLESDEEYLEEleknAKAEARERKEKLKKEHPLLQEDDSGVLslpELS 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1088 QVIKKKDIELSSIQSRLEDE-QSLVAKLQR----------QIKELLARIQELEEELD 1133
Cdd:pfam13094 103 SDLGLGDTDFSLFDPTLDEElLPLLEQLQKhlesmqgnlaQLEGLNEAIERAYAALD 159
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1315-1490 |
3.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1315 KQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEgegvsRAE 1394
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-----KYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1395 ELEETRRKlTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKqkgfdkvLDEWRRKCEALV 1474
Cdd:COG1579 80 EQLGNVRN-NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE-------LEEKKAELDEEL 151
|
170
....*....|....*.
gi 17561652 1475 AEVEQSQRETRAAATE 1490
Cdd:COG1579 152 AELEAELEELEAEREE 167
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
867-1194 |
3.27e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 867 KVLEEEKTQEERKRKDMEAENARLE--------AEKQALLiqLEQERdssAEGEERSAKLLAQKADLEKQMANMNDQLCD 938
Cdd:PLN02939 107 AIAAIDNEQQTNSKDGEQLSDFQLEdlvgmiqnAEKNILL--LNQAR---LQALEDLEKILTEKEALQGKINILEMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 939 EEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEiqsqdevisklNKEKKHQEEVNRKLLE 1018
Cdd:PLN02939 182 TDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE-----------NMLLKDDIQFLKAELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1019 DIQAEEDKVNHLNKTKAKLESTLDELEDTlerekrgrqdcekqrrkvegeLKIAQELIEELNRHKHEqeqVIKKKDIELS 1098
Cdd:PLN02939 251 EVAETEERVFKLEKERSLLDASLRELESK---------------------FIVAQEDVSKLSPLQYD---CWWEKVENLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1099 SIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKArNEMQMELEELGDRLDEAGGATQAQIELNKKRE 1178
Cdd:PLN02939 307 DLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKV-ELLQQKLKLLEERLQASDHEIHSYIQLYQESI 385
|
330 340
....*....|....*....|
gi 17561652 1179 AE----LAKLRQDLEDAAIN 1194
Cdd:PLN02939 386 KEfqdtLSKLKEESKKRSLE 405
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1275-1640 |
3.67e-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: 42.19 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1275 EQARLIQELTMGKNKVHNENQDLNRqledaeaQLCALNRIKQQQHSQLEELKRTLDQETRERQSLHSQvsnyQLECEQFR 1354
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKR-------DREQWERQRRELESRVAELKEELRQSREKHEELEEK----YKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1355 ESLEEEQDAKTDVQrqlskanseiqqwrakfeGEGVSRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHD 1434
Cdd:pfam07888 111 EELSEEKDALLAQR------------------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1435 LEDAQVDADRANSIASSLEKKQKGFDKVLDEWRRKCEALVAEVEQSQRETRAA---ATETFRLRNQLEESGEQTEAVKRE 1511
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1512 NKALAQELKDIADQLGEGGKSVHD------------------LQKMRRRLEIEKEELQQALDEAECALEAEEAKVMRAQI 1573
Cdd:pfam07888 253 VEGLGEELSSMAAQRDRTQAELHQarlqaaqltlqladaslaLREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1574 EVSQIRSEIEKRLQEKEEEFENTRKNHS---RTIESMQVSLETESRGRAELLKTKKKLEGDVNELEIALD 1640
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSesrRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
883-1189 |
3.82e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 883 MEAENARLEAEKQALLIQLEQER---DSSAEGEERSAK-----LLAQKADLEKQMANMNDQLCDEEEKNAALTKQKKKIE 954
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPsrlYSLYEKEIEDLRrqldtLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 955 QDNEGLKKTVSDLetTIKKQESEKQakdhqIRSLQDEIQSQdevisklnkEKKHQEEVnRKLLEDIQAEEDKVNHLNKTK 1034
Cdd:pfam00038 103 NDLVGLRKDLDEA--TLARVDLEAK-----IESLKEELAFL---------KKNHEEEV-RELQAQVSDTQVNVEMDAARK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1035 AKLESTLDELEDTLERE-KRGRQDCEKQ-RRKVEgelkiaqELIEELNRHKHEqeqvikkkdieLSSIQSrledeqslva 1112
Cdd:pfam00038 166 LDLTSALAEIRAQYEEIaAKNREEAEEWyQSKLE-------ELQQAAARNGDA-----------LRSAKE---------- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1113 klqrQIKELLARIQELEEELDAERNSRSKAEKArnemqmeLEELGDRLDEAGGATQAQIElnkKREAELAKLRQDLE 1189
Cdd:pfam00038 218 ----EITELRRTIQSLEIELQSLKKQKASLERQ-------LAETEERYELQLADYQELIS---ELEAELQETRQEMA 280
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
924-1212 |
3.87e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 42.47 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 924 DLEKQMANMNDQLCDEEEKNaaltkqKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDEIQSQdevISKLN 1003
Cdd:PTZ00341 855 DIENTAKNAAEQILSDEGLD------EKKLKKRAESLKKLANAIEKYAGGGKKDKKAKKKDAKDLSGNIAHE---INLIN 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1004 KEKKHQ-EEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLER--EKRGRQDCEKQ-RRKVEGELkiaQELIEEl 1079
Cdd:PTZ00341 926 KELKNQnENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEEnvEENVEENVEENvEENVEENV---EENVEE- 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1080 NRHKHEQEQVikKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEElDAERNSRSKAEKARNEMQMELEE---- 1155
Cdd:PTZ00341 1002 NIEENVEENV--EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEE-NVEENIEENIEEYDEENVEEIEEniee 1078
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1156 -LGDRLDEAGGATQAQIELNKKREAELAKLRQDLEDAAINSETSMAALRKKHNDAVAE 1212
Cdd:PTZ00341 1079 nIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
857-1183 |
3.96e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 857 EEFEALEKKFKVLEEEKtqEERKRKDMEAENARLEAEKQAlliqleqerdssaegEERSAKLLAQKADLEKQMANMNDql 936
Cdd:pfam05701 145 EELESLRKEYASLVSER--DIAIKRAEEAVSASKEIEKTV---------------EELTIELIATKESLESAHAAHLE-- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 937 CDEEEKNAALTKQKKKIEQDNEglkktvsdlettikkqesEKQAKDhQIRSLQDEIQSQDEVISKLnkekkhqeEVNRKL 1016
Cdd:pfam05701 206 AEEHRIGAALAREQDKLNWEKE------------------LKQAEE-ELQRLNQQLLSAKDLKSKL--------ETASAL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1017 LEDIQAEedkvnhlnkTKAKLESTLDEledtlerEKRGRQDCEKQRRKVEGELKIAQELIEE--LNRHKHEQEQVIKKkd 1094
Cdd:pfam05701 259 LLDLKAE---------LAAYMESKLKE-------EADGEGNEKKTSTSIQAALASAKKELEEvkANIEKAKDEVNCLR-- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1095 IELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAG--------GA 1166
Cdd:pfam05701 321 VAAASLRSELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAqeaeeaksLA 400
|
330
....*....|....*...
gi 17561652 1167 TQAQIELNK-KREAELAK 1183
Cdd:pfam05701 401 QAAREELRKaKEEAEQAK 418
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
854-1022 |
4.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 854 KKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAE--GEERSAKLLAQKADLEKQMAN 931
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 932 MNDQLcdeEEKNAALTKQKKKIEQDNEGLKKTVSDLETTIkkqESEKQAKDHQIRSLQDEIQSQDEVISKLN-KEKKHQE 1010
Cdd:COG3206 282 LSARY---TPNHPDVIALRAQIAALRAQLQQEAQRILASL---EAELEALQAREASLQAQLAQLEARLAELPeLEAELRR 355
|
170
....*....|....*..
gi 17561652 1011 -----EVNRKLLEDIQA 1022
Cdd:COG3206 356 lerevEVARELYESLLQ 372
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
971-1125 |
4.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 971 IKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEEDKVNHLNKTKAKLESTLDELEDTLER 1050
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1051 EKRGRQDCEKQR----RKVEGELKIA---------QELIEELNRHKHEQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQ 1117
Cdd:PRK12705 110 REKALSARELELeeleKQLDNELYRVagltpeqarKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRI 189
|
....*...
gi 17561652 1118 IKELLARI 1125
Cdd:PRK12705 190 ASETASDL 197
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1161-1435 |
4.78e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1161 DEAGGATQAQIELNKKREAELAKLR-QDLEDAAINSETSMAALrkkhNDAVAELSDQLDTIQKMRGKLEREKNDKQREVD 1239
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAEKNILLL----NQARLQALEDLEKILTEKEALQGKINILEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1240 ELQQSADVEAKQRQNCERMAKQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNR------ 1313
Cdd:PLN02939 181 ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAEteervf 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1314 IKQQQHSQLEELKRTLDQETRERQSLHSQVSNYQLECeqFRESLEEEQDAKTDVQRQLSKANSEIQQwrakfegegvsra 1393
Cdd:PLN02939 261 KLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQ------------- 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1394 eeleetRRKLTHKVQEMQEQLENAN-------------QKIGTLEKNKQRLAHDL 1435
Cdd:PLN02939 326 ------NQDLRDKVDKLEASLKEANvskfssykvellqQKLKLLEERLQASDHEI 374
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
886-1005 |
4.83e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.28 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 886 ENARLEAEKQALLIQLEQERDSSAEGEERSAK----------LLAQKADLEKQMANMNDQLcdeEEKNAALTKQKKKIEQ 955
Cdd:pfam10186 27 DLARLLSEKDSLKKKVEEALEGKEEGEQLEDNignkklklrlLKSEVAISNERLNEIKDKL---DQLRREIAEKKKKIEK 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 17561652 956 DNEGLKKTVSDLETTikkQESEKQAKDHQIRSLQDEIQSQDEVISKLNKE 1005
Cdd:pfam10186 104 LRSSLKQRRSDLESA---SYQLEERRASQLAKLQNSIKRIKQKWTALHSK 150
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1031-1465 |
5.34e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1031 NKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQELIEELNRHKHEQEQVIKKKDI----------ELSSI 1100
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEgkalmdeiraRLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1101 QSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQMELEELGDRLDEAGGATQAQIELNKKREAE 1180
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1181 LAKLRQDLEDAAINSETSMAALRKKHNDAVAELSDQLDTIQKMRGKLEREKNDKQREVDELQQSADVEAKQRQNCERMAK 1260
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1261 QLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCALNRIKQQQHSQLEELKRTLDQETRERQSLH 1340
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1341 SQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEIQQWRAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQK 1420
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 17561652 1421 IGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDE 1465
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1085-1278 |
5.50e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1085 EQEQVIKKKDIELSSIQSRLEDEQSLVAKLQRQIKELLARIQELEEELDAERNSRSKAEKARNEMQmelEELGDRLDEA- 1163
Cdd:PRK11637 58 AKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQLDAAf 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1164 --GGATQAQI------------------ELNKKREAELAKLRQDLEDAAinseTSMAALRKKHNDAVAELSDQldtiQKM 1223
Cdd:PRK11637 135 rqGEHTGLQLilsgeesqrgerilayfgYLNQARQETIAELKQTREELA----AQKAELEEKQSQQKTLLYEQ----QAQ 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17561652 1224 RGKLEREKNDKQREVDELQQSadVEAKQRQNCErmAKQLEAQLTDMTLKSDEQAR 1278
Cdd:PRK11637 207 QQKLEQARNERKKTLTGLESS--LQKDQQQLSE--LRANESRLRDSIARAEREAK 257
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1260-1552 |
5.67e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.68 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1260 KQLEAQLTDMTLKSDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAqlcalnrikQQQHSQLEELKRTLDQETRERQSL 1339
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKS---------TGNYDEVKKAQKDLEKSLRKREHL 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1340 HSQVSNYQLECEQFRESLEEEQDAKTDVQRQLSKANSEiqqwrAKFEGEGVSRAEELEETRRKLTHKVQEMQEQLENANQ 1419
Cdd:pfam18971 630 EKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKE-----ANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSK 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1420 KIGTLEKNKQRlahdledaqvDADRANSIASSLEKKQKGFDkVLDEWRRKCEALVAEVEQSQRETRAAATETFRLRNQLE 1499
Cdd:pfam18971 705 SFDEFKNGKNK----------DFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLE 773
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1500 ESgeqteavkRENKALAQELKDIADQLGEG---GKSVHDLQKMRRRL----EIEKEELQQ 1552
Cdd:pfam18971 774 NS--------VKDVIINQKVTDKVDNLNQAvsvAKAMGDFSRVEQVLadlkNFSKEQLAQ 825
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
840-1038 |
6.22e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 840 FKLFGRVKPLIKGSKKNEEFEALEKKFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQ-------ERDSSAEGE 912
Cdd:PRK05771 62 LRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfDLDLSLLLG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 913 ERSAKLLAQKADLEKQmanmNDQLCDEEEKNAALTKQKKkieqdNE------GLKKTVSDLETTIKKQESEKQAKDHqIR 986
Cdd:PRK05771 142 FKYVSVFVGTVPEDKL----EELKLESDVENVEYISTDK-----GYvyvvvvVLKELSDEVEEELKKLGFERLELEE-EG 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 987 SLQDEIQSQDEVISKLNKE----KKHQEEVNRKLLEDIQAEEDKV-NHLNKTKAKLE 1038
Cdd:PRK05771 212 TPSELIREIKEELEEIEKEreslLEELKELAKKYLEELLALYEYLeIELERAEALSK 268
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1635-1815 |
6.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1635 LEIA-LDHSNKLNVD---GQKSMKKLQD-TIRELQYQVEEEQRSLSESR--DHANLAERRSQVLQQEKEDLAIIYEQSER 1707
Cdd:PHA02562 160 LDISvLSEMDKLNKDkirELNQQIQTLDmKIDHIQQQIKTYNKNIEEQRkkNGENIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1708 TRRQAELELaEVKDSVNELSNSNSLLLATKRKVE---GDLQLLQ-------------------SEIEEAMSDAKTSDEKA 1765
Cdd:PHA02562 240 TDELLNLVM-DIEDPSAALNKLNTAAAKIKSKIEqfqKVIKMYEkggvcptctqqisegpdriTKIKDKLKELQHSLEKL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17561652 1766 KKAIMDASKLADELRSEQEHA-------SNLNQSKKTLESQVKDLQMRLDEAEAAGI 1815
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLlelknkiSTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1473-1935 |
6.92e-03 |
|
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: 41.49 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1473 LVAEVEQSQRETRAA----ATETFRLRNQLEESGEQTEAVKRENKALA-----QELKDIADQLGEGGKSVHDLQKMRRRL 1543
Cdd:TIGR00618 196 AELLTLRSQLLTLCTpcmpDTYHERKQVLEKELKHLREALQQTQQSHAyltqkREAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1544 EIEKEELQQALDEAECALEAEEAKvmRAQIEVSQIRSEIEKRLQEKEEEFENTRKnHSRTIESMQVSLETESRGRAELLK 1623
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQRIHTELQSKMRSRAKLLM-KRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1624 TKKKLEGDVNELEIALDHSNKLNVDGQ----------------KSMKKLQDTIRELQYQVEEEQRSLSESRDHANLAERR 1687
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttltqklQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1688 SQVLQQEKEDLAIIYEQSERTRRQAELELAEVKDSVNE----LSNSNSLLLATKRKVEGDLQLLQSEIEEAMSDAKTSDE 1763
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEreqqLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1764 KAKKAImdaskLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAeaagIKGGKRQLAKLDMRIHELETELEGENRRH 1843
Cdd:TIGR00618 513 PNPARQ-----DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE----RKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1844 AETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTYKRQIED---AESLASGNLAKYRQLQHVVEDAQERA 1920
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLqqcSQELALKLTALHALQLTLTQERVREH 663
|
490
....*....|....*
gi 17561652 1921 DAAENALQKLRLKGR 1935
Cdd:TIGR00618 664 ALSIRVLPKELLASR 678
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
862-1015 |
6.93e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 862 LEKKFKVLEEEKTQEERKRKDMEA--ENARLEAEKQALLIQLEQERDSSAEGEE--RSAKLLAQKA-DLEKQ---MANMN 933
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEklEAALLEAKELLLRERNQQRQEARREREElqREEERLVQKEeQLDARaekLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 934 DQLCDEEEKnaaLTKQKKKIEQDNEGLkktvsDLETTIKKQESEKQAKDHQIRSLQDEIQSQDEVISKLNKEKKHqEEVN 1013
Cdd:PRK12705 105 NQLEEREKA---LSARELELEELEKQL-----DNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEAD-LEAE 175
|
..
gi 17561652 1014 RK 1015
Cdd:PRK12705 176 RK 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1735-1931 |
7.64e-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: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1735 ATKRKVEGDLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEAAg 1814
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1815 IKGGKRQLAKL------DMRIHELETELEGENrrHAETQKVLRNKDRKCRELQFQVDEDKKSQERMYDLIEKLQQKIKTY 1888
Cdd:COG4942 99 LEAQKEELAELlralyrLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17561652 1889 KRQIEDAESLASGNLAKYRQLQHVVEDAQERADAAENALQKLR 1931
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1171-1326 |
7.82e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 41.08 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1171 IELNKKREAELAKLRQDLEDAAINSETSMAALRKKHND--AVAELSDQLDTIQKMRGKLErekndkqREVDELQqsadVE 1248
Cdd:PRK10787 142 IKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADkqSVLEMSDVNERLEYLMAMME-------SEIDLLQ----VE 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561652 1249 AKQRQnceRMAKQLEAQLTDMTLksDEQARLIQELTMGKNKVHNENQDLNRQLEDAEAQLCAlnriKQQQHSQLEELK 1326
Cdd:PRK10787 211 KRIRN---RVKKQMEKSQREYYL--NEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEA----KEKAEAELQKLK 279
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
868-1034 |
8.79e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 40.73 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 868 VLEEEKTQEERKRKDMEAEnarleAEKQALLIQLEQerDSSAEGEERSAKLLAqkaDLEKQMANMNDQLCDEEEknAALT 947
Cdd:pfam17060 105 ELKEDVKSSPRSEADSLGT-----PIKVDLLRNLKP--QESPETPRRINRKYK---SLELRVESMKDELEFKDE--TIME 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 948 KQKKKIEqdnegLKKTVSDLETTIKKQESE----KQAKDHQIRSLQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAE 1023
Cdd:pfam17060 173 KDRELTE-----LTSTISKLKDKYDFLSREfefyKQHHEHGGNNSIKTATKHEFIISELKRKLQEQNRLIRILQEQIQFD 247
|
170
....*....|.
gi 17561652 1024 EDKVnHLNKTK 1034
Cdd:pfam17060 248 PGAL-HDNGPK 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
870-1074 |
8.94e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 870 EEEKTQEERKRKDMEAENARLEAEKQALLIQLEQERDSSAEGEERSAKLLAQKADLEKQMANMNDQLcdeEEKNAALTKQ 949
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 950 KKKIEQDNEGLKK-----TVSDLETTIKKQESEKQAKDHQirslQDEIQSQDEVISKLNKEKKHQEEVNRKLLEDIQAEE 1024
Cdd:COG3883 92 ARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17561652 1025 DKVNHLNKTKAKLESTLDELEDTLEREKRGRQDCEKQRRKVEGELKIAQE 1074
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1592 |
9.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1391 SRAEELEETRRKLTHKVQEMQEQLENANQKIGTLEKNKQRLAHDLEDAQVDADRANSIASSLEKKQKGFDKVLDEWRR-- 1468
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARal 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1469 -KCEALVAEVEQ--SQRETRAAATETFRLRNQLEESGEQTEAVKRENKALAQELKDIADQLGEGGKSVHDLQKMRRRLEI 1545
Cdd:COG3883 96 yRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17561652 1546 EKEELQQALDEAECALEAEEAKVMRAQIEVSQIRSEIEKRLQEKEEE 1592
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1743-1909 |
9.29e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1743 DLQLLQSEIEEAMSDAKTSDEKAKKAIMDASKLADELRSEQEHASNLNQSKKTLESQVKDLQMRLDEAEA--AGIKGGK- 1819
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1820 -----RQLAKLDMRIHELETELEGENRRHAETQKVLRNKDRKCRELQFQVDEDKKSQErmyDLIEKLQQKIKTYKRQIED 1894
Cdd:COG1579 91 yealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167
|
170
....*....|....*.
gi 17561652 1895 -AESLASGNLAKYRQL 1909
Cdd:COG1579 168 lAAKIPPELLALYERI 183
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
865-1103 |
9.67e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 865 KFKVLEEEKTQEERKRKDMEAENARLEAEKQALLIQLEQErdsSAEGEERSAKLLAQKADLEKQMANMNDQLCDEEEKNA 944
Cdd:pfam15742 120 KSRVADAEEKILELQQKLEHAHKVCLTDTCILEKKQLEER---IKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 945 ALTKQKKKIEQDNEGLKKTVSDLETTIKKQESEKQAKDHQIRSLQDeiqsQDEVISKLNKEKKHQEEVNRKLLEDIQAEE 1024
Cdd:pfam15742 197 SLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKLSSLQQEKEALQEELQQVLKQLDVHV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561652 1025 DKVNH-LNKTKAKLESTLDELEDTLE-REKRGRQ---DCEKQRRKVEGELKIAQELIEE-----LNRHK-----HEQEQV 1089
Cdd:pfam15742 273 RKYNEkHHHHKAKLRRAKDRLVHEVEqRDERIKQlenEIGILQQQSEKEKAFQKQVTAQneillLEKRKlleqlTEQEEL 352
|
250
....*....|....
gi 17561652 1090 IKKKDIELSSIQSR 1103
Cdd:pfam15742 353 IKNNKRTISSVQNR 366
|
|
| |
