|
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, ... |
95-782 |
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: 1261.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQetfgakkaaTEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK---------KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEW 414
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 415 VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKgISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 494
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 NHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKP-LGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFekpKP 573
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNF---KK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 574 PKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDYttqeeaaaaAAKGTAGAKKKGK 653
Cdd:cd01377 468 PKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDP-LVASLFKDY---------EESGGGGGKKKKK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 654 SGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQ 733
Cdd:cd01377 538 GGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQ 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150292 734 RYALLAADESIIGKTDAKKGSALMLarlvKEKKLEEENFRVGLTKVFFK 782
Cdd:cd01377 618 RYSILAPNAIPKGFDDGKAACEKIL----KALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-782 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1070.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 83 TEDMSNLTFLNDASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNML 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 163 QNHENQSMLITGESGAGKTENTKKVISYFAAVGAAQQETfgakkaateedknkKKVTLEDQIVQTNPVLEAFGNAKTVRN 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG--------------NVGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 243 NNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQ-AE 321
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNP-KDYHYLSQsGC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 322 LIIDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLK 401
Cdd:pfam00063 226 YTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 402 ALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQL 481
Cdd:pfam00063 306 ALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 482 WINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLIDQ 560
Cdd:pfam00063 386 CINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYST 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 561 HlGKHPNFEKPKPpkgkQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYTTQEEaaAA 640
Cdd:pfam00063 465 F-SKHPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSS-DPLLAELFPDYETAES--AA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 641 AAKGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRK 720
Cdd:pfam00063 537 ANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRA 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 721 GFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLVkekkLEEENFRVGLTKVFFK 782
Cdd:pfam00063 617 GFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLN----LDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-794 |
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: 1004.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 76 NPPKFEKTEDMSNLTFLNDASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 156 EAYRNMLQNHENQSMLITGESGAGKTENTKKVISYFAAVGAaqqetfgakkaateedKNKKKVTLEDQIVQTNPVLEAFG 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG----------------SNTEVGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 236 NAKTVRNNNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYW 315
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL-KSPEDYR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 316 FIAQA-ELIIDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQA-EPDGTDDAERAAKCFG 393
Cdd:smart00242 224 YLNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 394 IDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIF 473
Cdd:smart00242 304 VDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKD-GSTYFIGVLDIYGFEIF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 474 DFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVPKATDLT 552
Cdd:smart00242 383 EVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 553 LAQKLiDQHLGKHPNFEKPKppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYT 632
Cdd:smart00242 462 FLEKL-NQHHKKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSK-NPLIASLFPSGV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 633 TQEEaaaaaakgtagakkkgKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVL 712
Cdd:smart00242 536 SNAG----------------SKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVL 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 713 EGIRICRKGFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFKAGIVAHLEDL 792
Cdd:smart00242 600 ENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSL----GLDEDEYQLGKTKVFLRPGQLAELEEL 675
|
..
gi 25150292 793 RD 794
Cdd:smart00242 676 RE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-782 |
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: 952.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQEtfgakkaateEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT----------DEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEW 414
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 415 VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 494
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQ-KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 NHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPP 574
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 575 KGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEeaaaaAAKGTAGAKKKGKS 654
Cdd:cd14909 470 KPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKS-QNKLLIEIFADHAGQS-----GGGEQAKGGRGKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 655 GSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 734
Cdd:cd14909 544 GGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 735 YALLAADEsIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14909 624 YKILNPAG-IQGEEDPKKAAEIILESI----ALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-782 |
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: 903.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVgAAQQETFGAKkaaTEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIV-AALGDGPGKK---AQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEW 414
Cdd:cd14927 237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 415 VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKgISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 494
Cdd:cd14927 317 VTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTK-LPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 NHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPP 574
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 575 KGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEeaaAAAAKGTAGAKKKGKS 654
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKS-QNKLLATLYENYVGSD---STEDPKSGVKEKRKKA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 655 GSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 734
Cdd:cd14927 552 ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQR 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 25150292 735 YALLAA----DESIIgktDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14927 632 YRILNPsaipDDKFV---DSRKATEKLLGSL----DIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-782 |
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: 869.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAavgaaqqeTFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14913 82 SGAGKTVNTKRVIQYFA--------TIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKgISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14913 314 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTK-LPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14913 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEeaaaaaAKGTAGAKKKGKSG 655
Cdd:cd14913 473 GR-AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKS-SNRLLAHLYATFATAD------ADSGKKKVAKKKGS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14913 545 SFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14913 625 RVLNASAIPEGQfIDSKKACEKLLASI----DIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-782 |
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: 862.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQETFGAKKaateedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGKG------------SLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEW 414
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 415 VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKgISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 494
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTK-MQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 NHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPP 574
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 575 KGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKasKEHALIVEVWQdyttQEEaaaaaaKGTAGAKKKGKS 654
Cdd:cd14934 468 KGKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQ--KSSLGLLALLF----KEE------EAPAGSKKQKRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 655 GSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 734
Cdd:cd14934 536 SSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 735 YALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14934 616 YQVLNPNVIPQGFVDNKKASELLLGSI----DLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-782 |
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: 815.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVgaaqqetfgakkAATEEDKnKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATI------------AAMIESK-KKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYlPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGK-KELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEW 414
Cdd:cd14929 227 ATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 415 VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKgISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 494
Cdd:cd14929 307 VTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAK-LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 NHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPP 574
Cdd:cd14929 386 NQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 575 KgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEeaaaaaAKGTAGAKKKGKS 654
Cdd:cd14929 466 K-KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKS-SNRLLASLFENYISTD------SAIQFGEKKRKKG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 655 GSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQR 734
Cdd:cd14929 538 ASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 735 YALLaaDESIIGKTD---AKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14929 618 YCIL--NPRTFPKSKfvsSRKAAEELLGSL----EIDHTQYRFGITKVFFK 662
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
27-1478 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 809.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 27 YDSKKNVWIPDSEDGYIEGVITKTAgDNVTVSIGQGAEK-----TVKKDVVQ--EMNPPKFEKTEDMSNLTFLNDASVLY 99
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKEA-FNKGKVTEEGKKEdgesvSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 100 NLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGESGAG 179
Cdd:COG5022 85 NLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 180 KTENTKKVISYFAAVGAAQQETFGAkkaateedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFSKQ 259
Cdd:COG5022 165 KTENAKRIMQYLASVTSSSTVEISS---------------IEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDEN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 260 GRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDyLPNLKKDLLLNKPVKDYWFIAQAEL-IIDGINDKEEHQLTDE 338
Cdd:COG5022 230 GEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAG-DPEELKKLLLLQNPKDYIYLSQGGCdKIDGIDDAKEFKITLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 339 AFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRpREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKG 418
Cdd:COG5022 309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKED-RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 419 QNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHM 498
Cdd:COG5022 388 LNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSA-AASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHM 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 499 FVLEQEEYAREGIQWTFIDFgLDLQACIELIEK--PLGIIAMLDEECIVPKATDLTLAQKLIDQ-HLGKHPNFEKPkppk 575
Cdd:COG5022 467 FKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKS---- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 gKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHAL--IVEVWQDYTTQeeaaaaaakgtagakkkgk 653
Cdd:COG5022 542 -RFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVstLFDDEENIESK------------------- 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 654 sGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQ 733
Cdd:COG5022 602 -GRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQ 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 734 RYALLAADESIIG----KTDAKKGSALMLarlvKEKKLEEENFRVGLTKVFFKAGIVAHLEDLRDQSLAQLITGLQAQIR 809
Cdd:COG5022 681 RYRILSPSKSWTGeytwKEDTKNAVKSIL----EELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIR 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 810 WYYQTIERKRRVEKITALKIIQRNIRSWAELRTWVWFKLYGKVKPLVNSGKIEAQYEKLQETVATLKDTvvqeEEKKRQL 889
Cdd:COG5022 757 GRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKT----IKREKKL 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 890 QEGAERLNKETADLLAQleaSKGSTREVEERMTAMNEQKVALEGK--LADASKKLEVEEARAVEINKQKKLVEAECADLK 967
Cdd:COG5022 833 RETEEVEFSLKAEVLIQ---KFGRSLKAKKRFSLLKKETIYLQSAqrVELAERQLQELKIDVKSISSLKLVNLELESEII 909
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 968 KNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQE--EQNKKLTEdlqAAEEQNLAANKLKAKLMQ 1045
Cdd:COG5022 910 ELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKlhEVESKLKE---TSEEYEDLLKKSTILVRE 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1046 SLeDSEQTMEREKRNRADMDKNKrkaeGELKIAQETLEELNKSKSDAENALRRKETELHTLGmKLEDEQAAVAKLQKGIQ 1125
Cdd:COG5022 987 GN-KANSELKNFKKELAELSKQY----GALQESTKQLKELPVEVAELQSASKIISSESTELS-ILKPLQKLKGLLLLENN 1060
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1126 QDEARVKDLhdqladekdARQRADRSRADQQAEYDELTEQLEDqaRATAAQIELGKKKDAELTKLRRDLEESGLKFGeql 1205
Cdd:COG5022 1061 QLQARYKAL---------KLRRENSLLDDKQLYQLESTENLLK--TINVKDLEVTNRNLVKPANVLQFIVAQMIKLN--- 1126
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1206 tvLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESS-------AALDQEAKLRADQ-ERIAKGYEVRLLELRL 1277
Cdd:COG5022 1127 --LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEAlpspppfAALSEKRLYQSALyDEKSKLSSSEVNDLKN 1204
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1278 KADEQSRQ------LQDFV---SSKGRLNSENSDL---ARQVEELEAKIQAANRLKL-QFSNELDHA----KRQAEEESR 1340
Cdd:COG5022 1205 ELIALFSKifsgwpRGDKLkklISEGWVPTEYSTSlkgFNNLNKKFDTPASMSNEKLlSLLNSIDNLlssyKLEEEVLPA 1284
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1341 E-RQNLSNLSKNLARELeqlkesIEDEVAGKNEASRQLSKASVELDQW-------RTKFETEGLIGADEFDEVKKRQNQK 1412
Cdd:COG5022 1285 TiNSLLQYINVGLFNAL------RTKASSLRWKSATEVNYNSEELDDWcrefeisDVDEELEELIQAVKVLQLLKDDLNK 1358
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1413 TSEIQDALDACN-AKIVALENARSRLTAEadaNRLEAEHHAQAVSSLEK-KQKAFDKVIDEWKKKVDD 1478
Cdd:COG5022 1359 LDELLDACYSLNpAEIQNLKSRYDPADKE---NNLPKEILKKIEALLIKqELQLSLEGKDETEVHLSE 1423
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-782 |
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: 802.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAQQETfgakkaatEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRS--------KKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14917 154 FGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14917 234 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14917 314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14917 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEeaaaaaAKGTAGAKKKGKSG 655
Cdd:cd14917 473 GK-PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKS-SLKLLSNLFANYAGAD------APIEKGKGKAKKGS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14917 545 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14917 625 RILNPAAIPEGQfIDSRKGAEKLLSSL----DIDHNQYKFGHTKVFFK 668
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-782 |
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: 799.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRT-EMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVGAAQqetfgakkaatEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSG-----------SSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWF----IAQAELIIDGIND 329
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 330 KEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREE--QAEPDGTDDAERAAKCFGIDSEEFLKALTRPR 407
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 408 VKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRD-HFIGVLDIAGFEIFDFNSFEQLWINFV 486
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 487 NEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLIDQHlGKH 565
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH-GSH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 566 PNFEKPKppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKehalivevwqdyttqeeaaaaaakgt 645
Cdd:cd00124 468 PRFFSKK----RKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS-------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 646 agakkkgksgsfmtvsmLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNR 725
Cdd:cd00124 518 -----------------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVR 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 25150292 726 TLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd00124 581 LPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLL----KLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-782 |
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: 793.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAQQEtfgakkaATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDR-------SKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14916 155 FGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14916 315 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14916 394 HHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKQaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYTTQEeaaaaAAKGTAGAKKKGKSG 655
Cdd:cd14916 474 GKQ-EAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSS-LKLMATLFSTYASAD-----TGDSGKGKGGKKKGS 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14916 547 SFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14916 627 RILNPAAIPEGQfIDSRKGAEKLLGSL----DIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-782 |
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: 790.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 97 VLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 177 GAGKTENTKKVISYFAAVGAAqqetfGAKKaatEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHF 256
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVT-----GEKK---KEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 257 SKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQLT 336
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 337 DEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWVN 416
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 417 KGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNH 496
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 497 HMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPKG 576
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 577 KqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALiVEVWQDYTTQEeaaaaaAKGTAGAKKKGKSGS 656
Cdd:cd14918 474 K-AEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTL-ASLFSTYASAE------ADSGAKKGAKKKGSS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 657 FMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA 736
Cdd:cd14918 546 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150292 737 LLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14918 626 VLNASAIPEGQfIDSKKASEKLLASI----DIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-782 |
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: 787.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAqqetfGAKKaaTEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVT-----GDKK--KEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14923 315 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14923 394 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEeaaaAAAKGTAGAKKKGKSG 655
Cdd:cd14923 474 GK-AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS-SLKLLSFLFSNYAGAE----AGDSGGSKKGGKKKGS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14923 548 SFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14923 628 RILNASAIPEGQfIDSKNASEKLLNSI----DVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-782 |
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: 779.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAqqetfgAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVT------GEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIvevwQDYTTQEEAAAAAAKGTAGAKKKGKSG 655
Cdd:cd14912 475 GK-AEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLA----YLFSGAQTAEGASAGGGAKKGGKKKGS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14912 630 KVLNASAIPEGQfIDSKKASEKLLASI----DIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-782 |
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: 774.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAqqetfgAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVT------GEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALiVEVWQDYTTQEeaaaaAAKGTAGAKKKGKSG 655
Cdd:cd14910 475 GK-VEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTL-ALLFSGAAAAE-----AEEGGGKKGGKKKGS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14910 548 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14910 628 KVLNASAIPEGQfIDSKKASEKLLGSI----DIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-782 |
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: 772.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAqqetfgAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVT------GEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWV 415
Cdd:cd14915 236 TDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 416 NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFN 495
Cdd:cd14915 316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 496 HHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPK 575
Cdd:cd14915 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 576 GKqAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIVEVWQDYTTQEEaaaaaaKGTAGAKKKGKSG 655
Cdd:cd14915 475 GK-AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAE------GGGGKKGGKKKGS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 656 SFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14915 548 SFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150292 736 ALLAADESIIGK-TDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14915 628 KVLNASAIPEGQfIDSKKASEKLLGSI----DIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-782 |
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: 746.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQETFGAKkAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAV-PHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV-KSYAFLSNGSLPVPGVDDYAEFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd14911 239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 493
Cdd:cd14911 318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 494 FNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHlGKHPNFEKPKp 573
Cdd:cd14911 398 FNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTD- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 574 pkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWQDytTQEEAAAAAAKGTAGAKKKGK 653
Cdd:cd14911 476 ---FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQD-PFVVNIWKD--AEIVGMAQQALTDTQFGARTR 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 654 SGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQ 733
Cdd:cd14911 550 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150292 734 RYALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14911 630 RYELLTPNVIPKGFMDGKKACEKMIQAL----ELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-782 |
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: 744.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQetfGAKKAATEEDknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHK---GRKDHNIPGE-------LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd14920 230 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENTV-AQKLCHLLGMNVMEFTRAILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 493
Cdd:cd14920 309 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 494 FNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL---GIIAMLDEECIVPKATDLTLAQKLIdQHLGKHPNFEK 570
Cdd:cd14920 389 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 571 PKPPKGkqaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQ--DYTTQEEAAAAAAKGTAGA 648
Cdd:cd14920 468 PRQLKD---KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDR-FVAELWKdvDRIVGLDQVTGMTETAFGS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 649 KKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLH 728
Cdd:cd14920 544 AYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 25150292 729 PDFVQRYALLAADESIIGKTDAKKGSALMLARLVKEKKLeeenFRVGLTKVFFK 782
Cdd:cd14920 624 QEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNL----YRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-782 |
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: 677.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAM-LIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQETfgakkaateedknkkkVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGE----------------TQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAE-LIIDGINDKEEH 333
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSA-EDFFYTNQGGsPVIDGVDDAAEF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd01380 225 EETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDH-FIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQ 492
Cdd:cd01380 305 VIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 493 FFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGK-HPNFEKP 571
Cdd:cd01380 385 QFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 572 KPPKGKqaeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHalivevwqdyttqeeaaaaaakgtagakkk 651
Cdd:cd01380 464 RFSNTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR------------------------------ 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 652 gksgsFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDF 731
Cdd:cd01380 509 -----KKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEF 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 732 VQRYALLaADESIIGKTDAKKGSALMLARLVKekklEEENFRVGLTKVFFK 782
Cdd:cd01380 584 FSRYRVL-LPSKEWLRDDKKKTCENILENLIL----DPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-782 |
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: 672.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKnkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGE------LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKdYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSK-YRFLSNGNVTIPGQQDKELFA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd14932 234 ETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDTA-AQKVCHLLGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 493
Cdd:cd14932 313 YVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 494 FNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL---GIIAMLDEECIVPKATDLTLAQKLIdQHLGKHPNFEK 570
Cdd:cd14932 393 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 571 PKPPKGkqaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWQDYT-TQEEAAAAAAKGTAGAK 649
Cdd:cd14932 472 PKKLKD---DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTD-KFVSELWKDVDrIVGLDKVAGMGESLHGA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 650 KKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHP 729
Cdd:cd14932 548 FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 25150292 730 DFVQRYALLAADESIIGKTDAKKGSALMlarlVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14932 628 EFRQRYEILTPNAIPKGFMDGKQACVLM----VKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-782 |
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: 652.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQetfGAKKAATEEDknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHK---GKKDTSITGE-------LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd14921 230 ETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 493
Cdd:cd14921 309 VVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 494 FNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL---GIIAMLDEECIVPKATDLTLAQKLIdQHLGKHPNFEK 570
Cdd:cd14921 389 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 571 PKPPKGKqaeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDY--TTQEEAAAAAAKGTAGA 648
Cdd:cd14921 468 PKQLKDK---TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDK-FVADLWKDVdrIVGLDQMAKMTESSLPS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 649 KKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLH 728
Cdd:cd14921 544 ASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVF 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 25150292 729 PDFVQRYALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14921 624 QEFRQRYEILAANAIPKGFMDGKQACILMIKAL----ELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-782 |
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: 649.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVgaaqqetfgakkaATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHV-------------ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd14919 227 ETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 493
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 494 FNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL---GIIAMLDEECIVPKATDLTLAQKLIdQHLGKHPNFEK 570
Cdd:cd14919 386 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 571 PKPPKGKqaeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWQDY--TTQEEAAAAAAKGTAGA 648
Cdd:cd14919 465 PKQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD-KFVSELWKDVdrIIGLDQVAGMSETALPG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 649 KKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLH 728
Cdd:cd14919 541 AFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVF 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 25150292 729 PDFVQRYALLAADESIIGKTDAKKGSALMlarlVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14919 621 QEFRQRYEILTPNSIPKGFMDGKQACVLM----IKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-782 |
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: 643.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQetfgakkaaTEEDKNKKKVT---LEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKF 251
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHK---------TKKDQNSLALShgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 252 IRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKpVKDYWFIAQAELIIDGINDKE 331
Cdd:cd15896 152 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLEN-YNNYRFLSNGNVTIPGQQDKD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 332 EHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKV 410
Cdd:cd15896 231 LFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNTA-AQKVCHLMGMNVTDFTRAILSPRIKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 411 GNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKL 490
Cdd:cd15896 310 GRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 491 QQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL---GIIAMLDEECIVPKATDLTLAQKLIdQHLGKHPN 567
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 568 FEKPKPPKGkqaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDYTTQEEAAAAAAKGTAG 647
Cdd:cd15896 469 FFKPKKLKD---EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDK-FVSELWKDVDRIVGLDKVSGMSEMP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 648 AKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTL 727
Cdd:cd15896 545 GAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 728 HPDFVQRYALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd15896 625 FQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSL----ELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-782 |
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: 630.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQetfGAKKAATEEDknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPK---GRKEPGVPGE-------LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGiNDKEEHQ 334
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDdAERAAKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd14930 229 ETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 WVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQF 493
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 494 FNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL---GIIAMLDEECIVPKATDLTLAQKlIDQHLGKHPNFEK 570
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEK-VAQEQGGHPKFQR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 571 pkpPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDYTTQEEAAAAAAKGTAGAKK 650
Cdd:cd14930 467 ---PRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR-LTAEIWKDVEGIVGLEQVSSLGDGPPGG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 651 KGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPD 730
Cdd:cd14930 543 RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 25150292 731 FVQRYALLAADESIIGKTDAKKGSALMLARLvkekKLEEENFRVGLTKVFFK 782
Cdd:cd14930 623 FRQRYEILTPNAIPKGFMDGKQACEKMIQAL----ELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-782 |
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: 605.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAaqqetfgakkaateedknkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG-------------------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAELII-DGINDKEEH 333
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDA-SDYYYLTQGNCLTcEGRDDAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPRE--EQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVG 411
Cdd:cd01381 221 ADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 412 NEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLdQKGISRDHF---IGVLDIAGFEIFDFNSFEQLWINFVNE 488
Cdd:cd01381 301 GETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAI-YKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 489 KLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELI-EKPLGIIAMLDEECIVPKATDLTLAQKLIDQHlGKHPN 567
Cdd:cd01381 380 NLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 568 FEKPKppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDYttqeeaaaaaakgtaG 647
Cdd:cd01381 458 YLKPK----SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNK-FLKQLFNED---------------I 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 648 AKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTL 727
Cdd:cd01381 518 SMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHT 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 728 HPDFVQRYALLAADESIIGKTDAKKGSALMLARLVkekkLEEENFRVGLTKVFFK 782
Cdd:cd01381 598 FEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVL----GGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-782 |
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: 598.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFmGKRRTEmPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGaaqqetfGAKKAateedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALG-------GGSSG------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAE-LIIDGINDKEEHQ 334
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNcLTIDGVDDAKKFH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEW 414
Cdd:cd01383 220 ELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 415 VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFF 494
Cdd:cd01383 300 IVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 NHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLiDQHLGKHPNFekpkp 573
Cdd:cd01383 380 NRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF----- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 574 pKGKQAEAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHalivevwqdyTTQEEAAAAAAKGTAGAKKKGK 653
Cdd:cd01383 453 -KGERGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ----------LPQLFASKMLDASRKALPLTKA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 654 SGS-FM--TVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPD 730
Cdd:cd01383 521 SGSdSQkqSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQE 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 25150292 731 FVQRYALLaadesiIGKTDAKKGSALMLARLVKEK-KLEEENFRVGLTKVFFK 782
Cdd:cd01383 601 FARRYGFL------LPEDVSASQDPLSTSVAILQQfNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-782 |
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: 597.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAQQEtfgakkaateedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHSW-------------------VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLK-KDLLLNKPVKDYWFIAQAELI-IDGINDKEEH 333
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHSKElKEKLKLGEPEDYHYLNQSGCIrIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE-PDGTDDAERAAKCFGIDSEEFLKALTRPRVKVgn 412
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINV-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 413 ewvnKGQNIE---QVNWAV---GAMAKGLYSRIFNWLVKKCNQTLDqKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFV 486
Cdd:cd14883 301 ----RGNVTEiplKVQEARdnrDAMAKALYSRTFAWLVNHINSCTN-PGQKNSRFIGVLDIFGFENFKVNSFEQLCINYT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 487 NEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIEK-PLGIIAMLDEECIVPKATDLTLAQKLIDQHlGKH 565
Cdd:cd14883 376 NEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKH 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 566 PNFEKPKPPKGKQAeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWqDYTTQEEAAAAAAKGT 645
Cdd:cd14883 454 PYYEKPDRRRWKTE---FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKN-KFVKELF-TYPDLLALTGLSISLG 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 646 AGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNR 725
Cdd:cd14883 529 GDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIH 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 25150292 726 TLHPDFVQRYALLAADEsiiGKTDAKKGSALMLArLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14883 609 LTFKEFVDRYLCLDPRA---RSADHKETCGAVRA-LMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-782 |
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: 595.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAQQETFGAKKaateedknkkkvtleDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERVK---------------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQL 335
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 336 TDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQrprEEQAEPDGTDDAERA--AKCFGIDSEEFLKALTRPRVKVGNE 413
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAISDTSVLDfvAYLLGVDPDQLEKALTHRTIETGGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 414 W---VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKL 490
Cdd:cd01378 304 GrsvYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 491 QQFFNHhmFVL--EQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGIIAMLDEECI-VPKATDLTLAQKLiDQHLGKHP 566
Cdd:cd01378 384 QQIFIE--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 567 NFEKPKPPKGkQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYTTQEEAAAAAakgta 646
Cdd:cd01378 460 HFECPSGHFE-LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSS-NPFLRSLFPEGVDLDSKKRPP----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 647 gakkkgksgsfmTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRT 726
Cdd:cd01378 533 ------------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQ 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 727 LHPDFVQRYALLAADESIIGKTDAKKGSalmlARLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd01378 601 TYEKFLERYKLLSPKTWPAWDGTWQGGV----ESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-782 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 564.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVGaaqqetfgaKKAATEEDknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG---------GRAVTEGR------SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELI-IDGINDKEE 332
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKCFeLDGVDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 HQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPdgTDDAER-----AAKCFGIDSEEFLKALTRPR 407
Cdd:cd01384 225 YRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVP--KDEKSEfhlkaAAELLMCDEKALEDALCKRV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 408 VKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRdHFIGVLDIAGFEIFDFNSFEQLWINFVN 487
Cdd:cd01384 303 IVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSK-RLIGVLDIYGFESFKTNSFEQFCINLAN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 488 EKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLIDQhLGKHP 566
Cdd:cd01384 382 EKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 567 NFEKPKPPKGKqaeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWqdyttqeeaaaaaakGTA 646
Cdd:cd01384 460 RFSKPKLSRTD-----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASK-CPFVAGLF---------------PPL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 647 GAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRT 726
Cdd:cd01384 519 PREGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRK 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 727 LHPDFVQRYALLAAdESIIGKTDAKKGSALMLArlvkekKLEEENFRVGLTKVFFK 782
Cdd:cd01384 599 PFEEFLDRFGLLAP-EVLKGSDDEKAACKKILE------KAGLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-782 |
6.85e-166 |
|
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: 522.19 E-value: 6.85e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAavgaaqqETFGAKKAateedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLT-------ESWGSGAG-----------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnkpvkdywfiaqaeliIDGINDKEEH 333
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK----------------DPLLDDVGDF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREE----QAEPDGTDDAERAAKCFGIDSEEFLKALTRpRVK 409
Cdd:cd01382 207 IRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 410 VGNEWVNKGQNI------EQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKgiSRDHFIGVLDIAGFEIFDFNSFEQLWI 483
Cdd:cd01382 286 QTTRGGAKGTVIkvplkvEEANNARDALAKAIYSKLFDHIVNRINQCIPFE--TSSYFIGVLDIAGFEYFEVNSFEQFCI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 484 NFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLIDQHL 562
Cdd:cd01382 364 NYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 563 gKHPNFEKPKPPKGKQ------AEAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYTTQEE 636
Cdd:cd01382 443 -NHFRLSIPRKSKLKIhrnlrdDEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESK-DKFIRSLFESSTNNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 637 AAAAAAKGtagakkkgksGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIR 716
Cdd:cd01382 520 DSKQKAGK----------LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLD 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 717 ICRKGFPNRTLHPDFVQRYALLAADEsiIGKTDAKkgsaLMLARLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd01382 590 LMQGGFPSRTSFHDLYNMYKKYLPPK--LARLDPR----LFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-780 |
1.33e-163 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 516.26 E-value: 1.33e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFM--GKRR----TEMPPHLFAVSDEAYRNMLQNHE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYehGERRaageRKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 167 --NQSMLITGESGAGKTENTKKVISYFAAVGAAQqetfgakkaaTEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNN 244
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSAT----------THGQNATERENVRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 245 SSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNkPVKDYWFIAQAELII 324
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLT-HVEEYKYLNSSQCYD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 325 --DGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKC-FGIDSEEFLK 401
Cdd:cd14901 230 rrDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACDlLGLDMDVLEK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 402 ALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGIS-RDHFIGVLDIAGFEIFDFNSFEQ 480
Cdd:cd14901 310 TLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTgASRFIGIVDIFGFEIFATNSLEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 481 LWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLID 559
Cdd:cd14901 390 LCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 560 QhLGKHPNFEKPKPpkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkehalivevwqdyttqeeaaa 639
Cdd:cd14901 469 L-LAKHASFSVSKL---QQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTS--------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 640 aaakgtagakkkgkSGSFM--TVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRI 717
Cdd:cd14901 524 --------------SNAFLssTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 718 CRKGFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLVKEKKLEE-ENFRVGLTKVF 780
Cdd:cd14901 590 SRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHlPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-782 |
3.50e-163 |
|
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: 515.08 E-value: 3.50e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEM---PPHLFAVSDEAYRNML-----QNHe 166
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKgvgkgQGT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 167 NQSMLITGESGAGKTENTKKVISYFAAVGAAqqetfgAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSS 246
Cdd:cd14892 80 PQSIVVSGESGAGKTEASKYIMKYLATASKL------AKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 247 RFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDyLPNLKKDLLLNKPVKDYWFIAQAELI-ID 325
Cdd:cd14892 154 RFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAG-LDANENAALELTPAESFLFLNQGNCVeVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 326 GINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQR--PREEQAEPDGTDDAERAAKCFGIDSEEFLKAL 403
Cdd:cd14892 233 GVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 404 TRpRVKVGnewvNKGQNIE------QVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGI---------SRDHFIGVLDIA 468
Cdd:cd14892 313 VT-QTTST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINACHKQQTSgvtggaaspTFSPFIGILDIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 469 GFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIEK-PLGIIAMLDEECIVP- 546
Cdd:cd14892 388 GFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKr 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 547 KATDLTLAQKLIDQHLGKHPNFEKPkppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhalive 626
Cdd:cd14892 467 KTTDKQLLTIYHQTHLDKHPHYAKP-----RFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 627 vwqdyttqeeaaaaaakgtagakkkgksgsfmtvsmlYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQL 706
Cdd:cd14892 536 -------------------------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 707 TCNGVLEGIRICRKGFPNRTLHPDFVQRYALLaADESIIGKTDAKKGSALMLARLVKE---KKLEEENFRVGLTKVFFK 782
Cdd:cd14892 579 IYSGVLEVVRIRREGFPIRRQFEEFYEKFWPL-ARNKAGVAASPDACDATTARKKCEEivaRALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-782 |
1.75e-159 |
|
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: 504.69 E-value: 1.75e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQEtfgakkaateedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDylPNLKKDLLLNKPvKDYWFIAQAELI-IDGINDKEEH 333
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLAS--PDPASRGGWGSS-AAYGYLSLSGCIeVEGVDDVADF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKqrprEEQAEPDGT-------DDAERAAKCFGIDSEEFLKALTRP 406
Cdd:cd14872 219 EEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFA----SGGGKSLVSgstvanrDVLKEVATLLGVDAATLEEALTSR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 407 RVKVgnewvnKGQNI-------EQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFE 479
Cdd:cd14872 295 LMEI------KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 480 QLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIEK-PLGIIAMLDEECIVPKATDLTLAQKlI 558
Cdd:cd14872 369 QLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIA-A 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 559 DQHLGKHPNFEkpkPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWQDYTTQEeaa 638
Cdd:cd14872 447 NQTHAAKSTFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKN-KLIAVLFPPSEGDQ--- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 639 aaaakgtagakkkgkSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRIC 718
Cdd:cd14872 520 ---------------KTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIR 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 719 RKGFPNRTLHPDFVQRYALLAADESI-IGKTDAKKGSALMlarlvKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14872 585 KTGYPFRYSHERFLKRYRFLVKTIAKrVGPDDRQRCDLLL-----KSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-782 |
2.67e-159 |
|
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: 504.70 E-value: 2.67e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVgaaqqetfgakkAATEEDKNKKKvtledqIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATI------------AGGLNDSTIKK------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDylPNLKKDLLLNKPvKDYWFIAQAELI-IDGINDKEE 332
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLAS--PDVEERLFLDSA-NECAYTGANKTIkIEGMSDRKH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 HQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAE--PDGTDDAERAAKCFGIDSEEFLKALTRPRVKV 410
Cdd:cd14903 220 FARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 411 GNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHfIGVLDIAGFEIFDFNSFEQLWINFVNEKL 490
Cdd:cd14903 300 AGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANH-IGVLDIFGFEHFKHNSFEQFCINYANEKL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 491 QQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEK 570
Cdd:cd14903 379 QQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 571 PKPPKgkqaeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWqDYTTQEEAAAAAAKGTAGAKK 650
Cdd:cd14903 458 PRTSR-----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSK-PFLRMLF-KEKVESPAAASTSLARGARRR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 651 KGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPD 730
Cdd:cd14903 531 RGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEE 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 25150292 731 FVQRYALLaadesIIGKTDAKKGSALMLARLVKEKKLEE-ENFRVGLTKVFFK 782
Cdd:cd14903 611 FLDKFWLF-----LPEGRNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-782 |
4.84e-158 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 500.86 E-value: 4.84e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATeedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC----------VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAELIID-GINDKEE 332
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTP-ENYHYLNQSGCVEDkTISDQES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 HQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQrprEEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGN 412
Cdd:cd14873 230 FREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 413 EWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLdqKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQ 492
Cdd:cd14873 307 EEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 493 FFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHlGKHPNFEKPk 572
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 573 ppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDYTTQEEAAAAAAKGTAGAKkkg 652
Cdd:cd14873 462 ----RVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFD-FIYDLFEHVSSRNNQDTLKCGSKHRRP--- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 653 ksgsfmTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFV 732
Cdd:cd14873 534 ------TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFY 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 25150292 733 QRYALLAadESIIGKTDAKKGSALMLARLVKEKKleeeNFRVGLTKVFFK 782
Cdd:cd14873 608 KRYKVLM--RNLALPEDVRGKCTSLLQLYDASNS----EWQLGKTKVFLR 651
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-782 |
5.80e-158 |
|
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: 501.23 E-value: 5.80e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNH----ENQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 170 MLITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 249
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 250 KFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVkDYWFIAQAELIIDGIND 329
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPV-EYFYLRGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 330 KEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKqrprEEQAEPDGTDDAER-----AAKCFGIDSEEFLKALT 404
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFE----SENDTTVLEDATTLqslklAAELLGVNEDALEKALL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 405 RPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWIN 484
Cdd:cd14890 316 TRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPD-DKWGFIGVLDIYGFEKFEWNTFEQLCIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 485 FVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-----KPlGIIAMLDeECIVPKATDltlAQKLID 559
Cdd:cd14890 395 YANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLD-DCWRFKGEE---ANKKFV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 560 QHL-----------------GKHPNFEKPKPPKGKQaeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHa 622
Cdd:cd14890 469 SQLhasfgrksgsggtrrgsSQHPHFVHPKFDADKQ----FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRS- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 623 lIVEVwqdyttqeeaaaaaakgtagakkkgksgsfmTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLV 702
Cdd:cd14890 544 -IREV-------------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDC 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 703 LNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADESIIGKtdakkgsalMLARLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14890 592 LRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENIEQ---------LVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-782 |
7.69e-157 |
|
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: 498.06 E-value: 7.69e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEmPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISK-SPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVGAaqqetfgakkaateEDKnKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGS--------------EDI-KKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSK---------QGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQ-----------VFSDYLPNLKKDLLLN-KPVK 312
Cdd:cd14888 145 LQFSKlkskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQlcaaareakntGLSYEENDEKLAKGADaKPIS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 313 --DYWFIAQAELI---------IDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFK-QRPREEQA--E 378
Cdd:cd14888 225 idMSSFEPHLKFRyltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAvvS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 379 PDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISR 458
Cdd:cd14888 305 ASCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 459 DHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELI-EKPLGIIA 537
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 538 MLDEECIVPKATDLTLAQKLIDQHLGkHPNFekpKPPKGKQAEahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKA 617
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKG-HKRF---DVVKTDPNS--FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 618 SKE---HALIVEVWQDYTTQEEAAAAaakgtagakkkgksgsFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKAS 694
Cdd:cd14888 538 SKNpfiSNLFSAYLRRGTDGNTKKKK----------------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 695 GVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLaadesiigktdakkgsalmlarLVKEKKLEEENFRV 774
Cdd:cd14888 602 DLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL----------------------LNGEGKKQLSIWAV 659
|
....*...
gi 25150292 775 GLTKVFFK 782
Cdd:cd14888 660 GKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-782 |
3.79e-156 |
|
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: 494.87 E-value: 3.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGaaqqetfgakKAATEedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG----------KANNR--------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLK-KDLLLNKPVKDYWFIAQAELIIDGIND---KE 331
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNsgnRE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 332 EHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQ----AEPDGTDDAERAAKCFGIDSEEFLKALTRPR 407
Cdd:cd01379 224 KFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 408 VKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTL--DQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINF 485
Cdd:cd01379 304 VVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 486 VNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFG-----LDLqacieLIEKPLGIIAMLDEECIVPKATDLTLAQKLidQ 560
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF--H 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 561 HLGKHPNFEKPkppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVevwqdyttqeeaaaa 640
Cdd:cd01379 457 NNIKSKYYWRP-----KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS-ENPLVR--------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 641 aakgtagakkkgksgsfMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRK 720
Cdd:cd01379 516 -----------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQ 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 721 GFPNRTLHPDFVQRYALLA--ADESIIGKTDAkkgSALMLARLvkekKLeeENFRVGLTKVFFK 782
Cdd:cd01379 579 GFSHRILFADFLKRYYFLAfkWNEEVVANREN---CRLILERL----KL--DNWALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-782 |
1.36e-155 |
|
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: 495.74 E-value: 1.36e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVgaaQQETFGAkkaateedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL---SQKGYGS--------------GVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAE-LIIDGINDKEEH 333
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNQSDcYTLEGEDEKYEF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRP--REEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVG 411
Cdd:cd01385 223 ERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 412 NEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTL---DQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNE 488
Cdd:cd01385 303 GETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 489 KLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLiDQHLGKHPN 567
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKF-KQQHKDNKY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 568 FEKPkppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEV-------------------- 627
Cdd:cd01385 461 YEKP-----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSS-SAFVRELigidpvavfrwavlraffra 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 628 ----------WQDYTTQEEAAAAAAKGTAGAKKKGKSGSfMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVI 697
Cdd:cd01385 535 maafreagrrRAQRTAGHSLTLHDRTTKSLLHLHKKKKP-PSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRF 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 698 DAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMlarlvkekKLEEENFRVGLT 777
Cdd:cd01385 614 DDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL--------NLDRDNYQIGKT 685
|
....*
gi 25150292 778 KVFFK 782
Cdd:cd01385 686 KVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-782 |
4.98e-153 |
|
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: 487.34 E-value: 4.98e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVgaaqqetfgakkaateedkNKKKVTL-EDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV-------------------NQRRNNLvTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFsKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEH 333
Cdd:cd01387 142 VFF-EGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQR-PREEQAEPDGTDDAE--RAAKCFGIDSEEFLKALTRPRVKV 410
Cdd:cd01387 221 RRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRqLRHGQEGVSVGSDAEiqWVAHLLQISPEGLQKALTFKVTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 411 GNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLdQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKL 490
Cdd:cd01387 301 RRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIV-YSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 491 QQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELI-EKPLGIIAMLDEECIVPKATDLTLAQKLIDQHlGKHPNFE 569
Cdd:cd01387 380 QYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 570 KPKPPkgkqaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhALIVEVWQDYTTQEEaaaaaakgtaGAK 649
Cdd:cd01387 458 KPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRT-RVVAHLFSSHRAQTD----------KAP 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 650 KKGKSGSFMTvsMLYR---------ESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRK 720
Cdd:cd01387 522 PRLGKGRFVT--MKPRtptvaarfqDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKE 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 721 GFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSalMLARLvkEKKLEEENFRVGLTKVFFK 782
Cdd:cd01387 600 GYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVS--LLSRL--CTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-782 |
3.20e-146 |
|
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: 467.63 E-value: 3.20e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKR-RTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVGAAQQETfgakkaateedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD------------------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvkDYWFIAQAELIIDGI-NDKEE 332
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDP--DCHRILRDDNRNRPVfNDSEE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 ----HQLTDEAFDILK---FTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTR 405
Cdd:cd14897 221 leyyRQMFHDLTNIMKligFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 406 PRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTL----DQKGISRDHFIGVLDIAGFEIFDFNSFEQL 481
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 482 WINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELI-EKPLGIIAMLDEECIVPKATDLTLAQKLIDq 560
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 561 HLGKHPNFekpKPPKGKQAEahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYttqeeaaaa 640
Cdd:cd14897 459 YCGESPRY---VASPGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNS-NNEFISDLFTSY--------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 641 aakgtagakkkgksgsfmtvsmlYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRK 720
Cdd:cd14897 524 -----------------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRD 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 721 GFPNRTLHPDFVQRYAllaadesIIGKTDAKKGSALMLARLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14897 581 GYPIRIKYEDFVKRYK-------EICDFSNKVRSDDLGKCQKILKTAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-738 |
4.40e-138 |
|
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: 446.40 E-value: 4.40e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGK--------RRTEMPPHLFAVSDEAYRNMLQNH 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 166 ENQSMLITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEED-KNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNN 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRaTSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 245 SSRFGKFIRIHFSKQ-GRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDL-LLNKPVKD-YWFIAQAE 321
Cdd:cd14907 161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 322 LI-IDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQR--PREEQAEPDGTDDAERAAKCFGIDSEE 398
Cdd:cd14907 241 CYeVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 399 FLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHF-------IGVLDIAGFE 471
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQLfqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 472 IFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTF--IDFgLDLQACIELIEK-PLGIIAMLDEECIVPKA 548
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 549 TDLTLAQKLIDQhlgkHPNFEKPKPPKGKQAEAhFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVW 628
Cdd:cd14907 480 TDEKLLNKIKKQ----HKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNR-IISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 629 QDYTTQEeaaaaaakGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTC 708
Cdd:cd14907 554 SGEDGSQ--------QQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|
gi 25150292 709 NGVLEGIRICRKGFPNRTLHPDFVQRYALL 738
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-743 |
2.29e-137 |
|
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: 442.82 E-value: 2.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP------------IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNM-- 161
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmakylLSFEARSSSTRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 162 --LQNHENQSMLITGESGAGKTENTKKVISYFAAVGAAQqetfgakkAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKT 239
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNN--------LAASVSMGKSTSGIAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 240 VRNNNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKdywfiaq 319
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYRRVMD------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 320 aeliidgindkeehqltdeAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDA-------ERAAKCF 392
Cdd:cd14900 227 -------------------AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 393 GIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDH----FIGVLDIA 468
Cdd:cd14900 288 SVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHgglhFIGILDIF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 469 GFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELI-EKPLGIIAMLDEECIVPK 547
Cdd:cd14900 368 GFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 548 ATDLTLAQKLIdQHLGKHPNFEKPKPPKGKqaeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTvmkaskehaLIVEV 627
Cdd:cd14900 447 GSDTTLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVD---------LFVYG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 628 WQdyttqeeaaaaaakgtagakkkgksgsfmtvsmlYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLT 707
Cdd:cd14900 514 LQ----------------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLR 559
|
650 660 670
....*....|....*....|....*....|....*.
gi 25150292 708 CNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADES 743
Cdd:cd14900 560 CNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKN 595
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-782 |
5.45e-131 |
|
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: 425.61 E-value: 5.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAA--MLIYTYSGLFCVVINPYKRLPiytDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHE---NQS 169
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 170 MLITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 249
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 250 KFIRIHFSKQG-RVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAELII-DGI 327
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSP-EDFIYLNQSGCVSdDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 328 NDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREE----QAEPDGTDDAERAAKCFGIDSEEFLKAL 403
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 404 TRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDqKGISRDHFIGVLDIAGFEIFD-FNSFEQLW 482
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG-HDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 483 INFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELI-EKPLGIIAMLDEECIVPKATDLTLAQKLIDQH 561
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 562 lGKHPNFEKPKPpkgKQAEAHFAMRHYAGTVRYNCLNWLEKNkdplNDTVVTVMkaskehalivevwqdyttqeeaaaaa 641
Cdd:cd14891 475 -KRHPCFPRPHP---KDMREMFIVKHYAGTVSYTIGSFIDKN----NDIIPEDF-------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 642 akgtagakkkgksGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKG 721
Cdd:cd14891 521 -------------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVG 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150292 722 FPNRTLHPDFVQRYALLAADE--SIIGKTDAKKGSALMLARLVkekklEEENFRVGLTKVFFK 782
Cdd:cd14891 588 LPTRVTYAELVDVYKPVLPPSvtRLFAENDRTLTQAILWAFRV-----PSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
101-782 |
8.46e-131 |
|
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: 427.45 E-value: 8.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 101 LKARYAAMLIYTYSGLFCVVINPYKRLPIYTDsvarmfMGKRRTEMP------PHLFAVSDEAYRNM-LQNHE------N 167
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYD------LHKYREEMPgwtalpPHVFSIAEGAYRSLrRRLHEpgaskkN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 168 QSMLITGESGAGKTENTKKVISYFAAVgaaqqetfgAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSR 247
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAES---------SKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 248 FGKFIRIHFSKQG-----RVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLN-KPVKDYWFIAQAE 321
Cdd:cd14895 152 FGKFVRMFFEGHEldtslRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLElLSAQEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 322 LII--DGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDA-------------- 385
Cdd:cd14895 232 CYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 386 ----ERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQ-------- 453
Cdd:cd14895 312 qqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 454 KGISRD--HFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDlQACIELIE- 530
Cdd:cd14895 392 KAANKDttPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEq 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 531 KPLGIIAMLDEECIVPKATDLTLAQKLIdQHLGKHPNFEKPKPpkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDT 610
Cdd:cd14895 471 RPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASRT---DQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 611 VVTVMKASKEhALIVEVWQDYTTQEEAAAAAAKGTAGAKKKGKSGsfMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNE 690
Cdd:cd14895 547 LFSVLGKTSD-AHLRELFEFFKASESAELSLGQPKLRRRSSVLSS--VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 691 KKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAAdesiigktdAKKGSALMLARLVkeKKLEEE 770
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA---------AKNASDATASALI--ETLKVD 692
|
730
....*....|..
gi 25150292 771 NFRVGLTKVFFK 782
Cdd:cd14895 693 HAELGKTRVFLR 704
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-782 |
2.21e-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: 416.23 E-value: 2.21e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 97 VLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNML----QNHENQSMLI 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 173 TGESGAGKTENTKKVISYFAAVGAAQQEtfgakkaateedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNSQ-------------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 253 RIHFsKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLL--------------NKPVKDYWFIA 318
Cdd:cd14889 144 QLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLldpgkyrylnngagCKREVQYWKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 319 QAELIidgindkeehqltdEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREE-QAEPDGTDDAERAAKCFGIDSE 397
Cdd:cd14889 223 YDEVC--------------NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 398 EFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHF--IGVLDIAGFEIFDF 475
Cdd:cd14889 289 DLLKTLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVELreIGILDIFGFENFAV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 476 NSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIEL-IEKPLGIIAMLDEECIVPKATDLTLA 554
Cdd:cd14889 369 NRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 555 QKLiDQHLGKHPNFEKP--KPPKgkqaeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIVeVWQDYT 632
Cdd:cd14889 448 DKL-NIHFKGNSYYGKSrsKSPK-------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSV-LFTATR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 633 TQEEAAAAAAKGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVL 712
Cdd:cd14889 519 SRTGTLMPRAKLPQAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLL 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 713 EGIRICRKGFPNRTLHPDFVQRYALLAADESIIGktdaKKGSALmlaRLVKEKKLeeENFRVGLTKVFFK 782
Cdd:cd14889 599 ETIRIRREGFSWRPSFAEFAERYKILLCEPALPG----TKQSCL---RILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-782 |
4.41e-123 |
|
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: 403.55 E-value: 4.41e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVgaaqqetfgakkAATEEDKNKKKVtledqiVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASV------------AGGRKDKTIAKV------IDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNkPVKDYWFI--AQAELIIDGINDKE 331
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLD-PNCQYQYLgdSLAQMQIPGLDDAK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 332 EHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGtDDAERAAKCFGIDSEEFLKALTRPRVKVG 411
Cdd:cd14904 222 LFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 412 NEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQ 491
Cdd:cd14904 301 NESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 492 QFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNfEKP 571
Cdd:cd14904 381 QKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDN-ESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 572 KPPKGKQAEahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEEAAAAAAKGTAGAKKK 651
Cdd:cd14904 459 DFPKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLS-SLDLLTELFGSSEAPSETKEGKSGKGTKAPKS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 652 GKSGsfmtvsmlYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDF 731
Cdd:cd14904 536 LGSQ--------FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKEL 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 732 VQRYALLAAdESIIGKTDAKKGSALMLArLVKEKKLEeenFRVGLTKVFFK 782
Cdd:cd14904 608 ATRYAIMFP-PSMHSKDVRRTCSVFMTA-IGRKSPLE---YQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-782 |
3.31e-121 |
|
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: 399.28 E-value: 3.31e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMF--MGKRRTE-------MPPHLFAVSDEAYRNMLQN- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqEGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 165 HENQSMLITGESGAGKTENTKKVISYFAAVGAAQQEtfgakkaATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNN 244
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEG-------APNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 245 SSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVF--------SDYLPNLKKDLLLNKPvKDYWF 316
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeehEKYEFHDGITGGLQLP-NEFHY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 317 IAQAELI-IDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAE---RAAKCF 392
Cdd:cd14908 233 TGQGGAPdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 393 GIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLdqkGISRDHFI----GVLDIA 468
Cdd:cd14908 313 GVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSI---NWENDKDIrssvGVLDIF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 469 GFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVP- 546
Cdd:cd14908 390 GFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGi 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 547 KATDLTLAQKLIDQHLGK----HPNFEKPKPPKGKQAEAHFAMRHYAGTVRYNC-LNWLEKNKDPLNDTVVTVMKASKEh 621
Cdd:cd14908 469 RGSDANYASRLYETYLPEknqtHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 622 alivevwqdyttqeeaaaaaakgtagakkkgksgsfmtvsmlYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGL 701
Cdd:cd14908 548 ------------------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 702 VLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADESIIGKT---DAKKGSALMLARLVKE-------------K 765
Cdd:cd14908 586 VTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLIPEVVLSwsmERLDPQKLCVKKMCKDlvkgvlspamvsmK 665
|
730
....*....|....*..
gi 25150292 766 KLEEENFRVGLTKVFFK 782
Cdd:cd14908 666 NIPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-782 |
8.44e-121 |
|
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: 396.84 E-value: 8.44e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQQETFGAkkaateedknkkkvtledQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLR------------------QPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFsKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPvKDYWFIAQAELI-IDGINDKEEH 333
Cdd:cd14896 143 HL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGP-ETYYYLNQGGACrLQGKEDAQDF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAE--RAAKCFGIDSEEFLKALTRPRVKVG 411
Cdd:cd14896 221 EGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPPERLEGAVTHRVTETP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 412 NEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISR-DHFIGVLDIAGFEIFDFNSFEQLWINFVNEKL 490
Cdd:cd14896 301 YGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAEsDATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 491 QQFFNHHMFVLEQEEYAREGIQWTFIDfGLDLQACIELI-EKPLGIIAMLDEECIVPKATDLTLAQKlIDQHLGKHPNFE 569
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQK-CHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 570 KPKPPKgkqaeAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYTTQEEAAAAAAkgtagak 649
Cdd:cd14896 459 KPQLPL-----PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQ-LQLVGSLFQEAEPQYGLGQGKP------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 650 kkgksgsfmTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHP 729
Cdd:cd14896 526 ---------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQ 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 25150292 730 DFVQRYALLAAdESIIGKTDAKKGSALMLARLVKEKKLeeenFRVGLTKVFFK 782
Cdd:cd14896 597 AFLARFGALGS-ERQEALSDRERCGAILSQVLGAESPL----YHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-738 |
1.58e-117 |
|
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: 390.02 E-value: 1.58e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP---------IYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNH 165
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLKPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 166 E-NQSMLITGESGAGKTENTKKVISYFAAVGAAQQETfgakkaateEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNN 244
Cdd:cd14902 81 RrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSST---------EQEGSDAVEIGKRILQTNPILESFGNAQTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 245 SSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVK----DYWFIAQA 320
Cdd:cd14902 152 SSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyellNSYGPSFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 321 ELIIDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKC---FGIDSE 397
Cdd:cd14902 232 RKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLAKCaelMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 398 EFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLD----QKGISRDH----FIGVLDIAG 469
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsAVSISDEDeelaTIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 470 FEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVPKA 548
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 549 TDLTLAQKLIDQHLGkhpnfekpkppkgkqaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhalivEVW 628
Cdd:cd14902 471 SNQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN-----EVV 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 629 QDYTTQEEAAAAAAKGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTC 708
Cdd:cd14902 530 VAIGADENRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRS 609
|
650 660 670
....*....|....*....|....*....|
gi 25150292 709 NGVLEGIRICRKGFPNRTLHPDFVQRYALL 738
Cdd:cd14902 610 VGVLEAVRIARHGYSVRLAHASFIELFSGF 639
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-782 |
1.43e-116 |
|
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: 385.11 E-value: 1.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMG-KRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAvgaaqqetfgAKKAATEedknkkkVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS----------AKSGNMD-------LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGINDKEEH 333
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHL-LGLKEYKFLNPKCLDVPGIDDVADF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 334 QLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFkqrpreEQAEPDGTDDA-----------ERAAKCFGIDSEEFLKA 402
Cdd:cd14876 223 EEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKI------TGKTEQGVDDAaaisneslevfKEACSLLFLDPEALKRE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 403 LTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLW 482
Cdd:cd14876 297 LTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPG-GFKNFMGMLDIFGFEVFKNNSLEQLF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 483 INFVNEKLQQFFNHHMFVLEQEEYAREGI-----QWTfidfglDLQACIE-LIEKPLGIIAMLDEECIVPKATDltlaQK 556
Cdd:cd14876 376 INITNEMLQKNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSD----EK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 557 LIDQHLGKHPNFEKPKPPKGKQaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQee 636
Cdd:cd14876 446 FVSACVSKLKSNGKFKPAKVDS-NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQAS-TNPVVKALFEGVVVE-- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 637 aaaaaakgtagakkKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIR 716
Cdd:cd14876 522 --------------KGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQ 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 717 ICRKGFPNRTLHPDFVQRYAL--LAADESiigKTDAKKGSALmlaRLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14876 588 LRQLGYSYRRPFEEFLYQFKFldLGIAND---KSLDPKVAAL---KLLESSGLSEDEYAIGKTMVFLK 649
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
85-835 |
3.94e-115 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 386.69 E-value: 3.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 85 DMSNLTFLNDASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFM-GKRRTEMPPHLFAVSDEAYRNMLQ 163
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 164 NHENQSMLITGESGAGKTENTKKVISYFAAvgaaqqetfgakkaATEEDKNKKkvtLEDQIVQTNPVLEAFGNAKTVRNN 243
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFAS--------------SKSGNMDLK---IQNAIMAANPVLEAFGNAKTIRNN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 244 NSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELI 323
Cdd:PTZ00014 243 NSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 324 IDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKqrPREEQAEPDG---TDDAE----RAAKCFGIDS 396
Cdd:PTZ00014 322 VPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDAaaiSDESLevfnEACELLFLDY 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 397 EEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFN 476
Cdd:PTZ00014 400 ESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPG-GFKVFIGMLDIFGFEVFKNN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 477 SFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQK 556
Cdd:PTZ00014 479 SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSS 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 557 LIDQhLGKHPNFEKPKppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKeHALIVEVWQDYTTQEe 636
Cdd:PTZ00014 559 CNTN-LKNNPKYKPAK----VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASP-NPLVRDLFEGVEVEK- 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 637 aaaaaakgtagakkkgksgSFMTVSML----YRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVL 712
Cdd:PTZ00014 632 -------------------GKLAKGQLigsqFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSIL 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 713 EGIRICRKGFPNRTLHPDFVQRYALL----AADESIIGKTDAKKgsalmlarLVKEKKLEEENFRVGLTKVFFKAGIVAH 788
Cdd:PTZ00014 693 EALQLRQLGFSYRRTFAEFLSQFKYLdlavSNDSSLDPKEKAEK--------LLERSGLPKDSYAIGKTMVFLKKDAAKE 764
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 789 LEDLRDQSLAQ---LITGLQAQIRwyyqTIERKRRVEK-ITALKIIQRNIR 835
Cdd:PTZ00014 765 LTQIQREKLAAwepLVSVLEALIL----KIKKKRKVRKnIKSLVRIQAHLR 811
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
862-1939 |
2.82e-113 |
|
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: 388.38 E-value: 2.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 862 EAQYEKLQETVATLKDTVVQEEEKKRQLQEgaerlnkETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKK 941
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCE-------EKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 942 LEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKK 1021
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1022 LTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKET 1101
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1102 ELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGK 1181
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1182 KKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQ 1261
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1262 ERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRE 1341
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1342 RQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIgADEFDEVKKRQNQKTSEIQDALD 1421
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1422 ACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLR 1501
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1502 GQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEV 1581
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1582 SQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRR 1661
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1662 YLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAA 1741
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1742 AKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVM 1821
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1822 KGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEA 1901
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 25150292 1902 EEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSR 1939
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-739 |
3.33e-113 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 375.73 E-value: 3.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTE-MPPHLFAVSDEAYRNMLQNHE--NQSM 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 171 LITGESGAGKTENTKKVISYFAAVGAAqqetfgakkaATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGK 250
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 251 FIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDylPNLKKDLLLNKPVK-DYWFIAQAELIIDgind 329
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKG--ASADERLQWHLPEGaAFSWLPNPERNLE---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 330 KEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEP--DGTDDAER-AAKCFGIDSEEFLKALTRP 406
Cdd:cd14880 225 EDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQpmDDTKESVRtSALLLKLPEDHLLETLQIR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 407 RVKVGNEWV--NKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWIN 484
Cdd:cd14880 305 TIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 485 FVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVPKATDLTLAQKLIDQHLG 563
Cdd:cd14880 385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 564 KHPNFEKPKPPKgkqaEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIV--EVWQDYTTQEEAAAAA 641
Cdd:cd14880 464 GNPCLGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKlfPANPEEKTQEEPSGQS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 642 AKGTagakkkgksgsfMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKG 721
Cdd:cd14880 540 RAPV------------LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAG 607
|
650
....*....|....*...
gi 25150292 722 FPNRTLHPDFVQRYALLA 739
Cdd:cd14880 608 FPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-735 |
1.86e-103 |
|
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: 349.39 E-value: 1.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVAR--------MFMGKRRTEMP--PHLFAVSDEAYRNMLQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRgyaydhnsQFGDRVTSTDPrePHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 164 NHENQSMLITGESGAGKTENTKKVISYFAaVGAAQQETFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNN 243
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 244 NSSRFGKFIRIHFSKQGR-VASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKD----LLLNKPVKDYWFIA 318
Cdd:cd14899 160 NSSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEqkqvLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 319 QA--ELIIDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRP--REEQAEPDGT----------DD 384
Cdd:cd14899 240 QSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEArvmssttgafDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 385 AERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGIS------- 457
Cdd:cd14899 320 FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASApwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 458 -------RDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE 530
Cdd:cd14899 400 dvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 531 -KPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGK--HPNFekpKPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPL 607
Cdd:cd14899 479 hRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKnsHPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 608 NDTVVTVMkASKEHALIVEVWQDYTTQEEAAAAAAKGTAGAKKKGKSGSFMTVSM--LYRESLNKLMTMLHSTHPHFIRC 685
Cdd:cd14899 556 CESAAQLL-AGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVgtQFKIQLNELLSTVRATTPRYVRC 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 25150292 686 IIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRY 735
Cdd:cd14899 635 IKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-782 |
9.53e-103 |
|
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: 345.64 E-value: 9.53e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAM-LIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEM-PPHLFAVSDEAYRNM-LQNHENQSML 171
Cdd:cd14875 1 ATLLHCIKERFEKLhQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 172 ITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKNKKkvtledqivQTNPVLEAFGNAKTVRNNNSSRFGKF 251
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDENLK---------WSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 252 IRIHF-SKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDY-------WFIAQAeli 323
Cdd:cd14875 152 IKLYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 324 IDG--INDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFkqrpreeqaEPDGTDDAE--------RAAKCFG 393
Cdd:cd14875 229 VDGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF---------ESDQNDKAQiadetpflTACRLLQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 394 IDSEEFLKALTrprVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKG-ISRDHFIGVLDIAGFEI 472
Cdd:cd14875 300 LDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdCSGCKYIGLLDIFGFEN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 473 FDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIE-KPLGIIAMLDEECIVPKATDL 551
Cdd:cd14875 377 FTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 552 TLAQKLIDQHLGKHPNFEKPKPPKGKQaeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEhalivEVWQDY 631
Cdd:cd14875 456 RFTTNLWDQWANKSPYFVLPKSTIPNQ----FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTD-----EFIRTL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 632 TTQEEAAAAAAKgtagakkkgksgsfmTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGV 711
Cdd:cd14875 527 LSTEKGLARRKQ---------------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 712 LEGIRICRKGFPNRTLHPDFVqRYALLAADESIIGKTDAKKGSAL---MLARLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14875 592 LQTIALKRQGYPVRRPIEQFC-RYFYLIMPRSTASLFKQEKYSEAakdFLAYYQRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-738 |
2.99e-101 |
|
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: 343.11 E-value: 2.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRR-TEMPPHLFAVSDEAYRNMLQNHENQSMLI 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 173 TGESGAGKTENTKKVISYFAAVGAAQQETfgakkaatEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 252
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQ--------NNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 253 RIHF-SKQGRVASCDIEHYLLEKSRVI-RQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIID----- 325
Cdd:cd14906 153 KIEFrSSDGKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISsfksq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 326 ------GINDKEEhqlTDEAFDILKFT----PTEKMEC---YRLVAAMMHMGNMKFKQ---RPREEQAEPDGTDDAERAA 389
Cdd:cd14906 233 ssnknsNHNNKTE---SIESFQLLKQSmesmSINKEQCdaiFLSLAAILHLGNIEFEEdsdFSKYAYQKDKVTASLESVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 390 KCFGIDSEEFLKALTRPRVKVGNEW--VNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDH------- 460
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAGGRGsvYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLaggsnkk 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 461 ---FIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIE-KPLGII 536
Cdd:cd14906 390 nnlFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGIL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 537 AMLDEECIVPKATDLTLAQKLIDQHlgkhpnFEKPKPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMK 616
Cdd:cd14906 469 SLLDDECIMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLL 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 617 ASKEHALivevwQDYTTQEEaaaaaakGTAGAKKKGKSGSfMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGV 696
Cdd:cd14906 543 ASSNFLK-----KSLFQQQI-------TSTTNTTKKQTQS-NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNN 609
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 25150292 697 IDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALL 738
Cdd:cd14906 610 FNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCI 651
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-782 |
4.24e-101 |
|
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: 340.33 E-value: 4.24e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRT-----EMPPHLFAVSDEAYRNMLQNHENQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 169 SMLITGESGAGKTENTKKVISYFAavgaaqqetFGAKKAATEedknkkkvtLEDQIVQTNPVLEAFGNAKTVRNNNSSRF 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFA---------YGHSTSSTD---------VQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 249 GKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELI-IDGI 327
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGF-KSLESYNFLNASKCYdAPGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 328 NDKEEHQLTDEAFDILkFTPTEKMECYRLVAAMMHMGNMKFKQRPR---EEQAEPDGTDDAERAAKCFGIDSEEFLKALT 404
Cdd:cd14886 222 DDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAII 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 405 RPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDhFIGVLDIAGFEIFDFNSFEQLWIN 484
Cdd:cd14886 301 TKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARP-WIGILDIYGFEFFERNTYEQLLIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 485 FVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGlDLQACIELIEKP-LGIIAMLDEECIVPkatdlTLAQKLIDQHLG 563
Cdd:cd14886 380 YANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQ-----TGSSEKFTSSCK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 564 KHPNFEKPKPPKGKQAEahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHaLIVEVWQDYTTQEeaaaaaak 643
Cdd:cd14886 454 SKIKNNSFIPGKGSQCN--FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNP-IVNKAFSDIPNED-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 644 gtagakkKGKSGSFmtVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFP 723
Cdd:cd14886 523 -------GNMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFA 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150292 724 NRTLHPDFVQRYALLAADESiigkTDAKKGSALMLA--RLVKEKKLEEENFRVGLTKVFFK 782
Cdd:cd14886 594 YNDTFEEFFHRNKILISHNS----SSQNAGEDLVEAvkSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-782 |
4.49e-92 |
|
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: 314.45 E-value: 4.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFM---GKRRTEMPPHLFAVSDEAYRNMLQNHENQSML 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 172 ITGESGAGKTENTKKVISYFAAVGAAqqetfgakkaateedknkKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKF 251
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS------------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 252 IRIHF-SKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFY---------QVFSDYLPNLKKDLLLNKPVKDYWFIAQAE 321
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYllmdglsaeEKYGLHLNNLCAHRYLNQTMREDVSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 322 LiidginDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLK 401
Cdd:cd14878 223 L------NREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 402 ALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCN---QTLDQKGISRDHFIGVLDIAGFEIFDFNSF 478
Cdd:cd14878 297 ALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclQSQDEQKSMQTLDIGILDIFGFEEFQKNEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 479 EQLWINFVNEKLQQFFNHHMFVLEQEEYAREGI----------QWTFIDFgldlqacieLIEKPLGIIAMLDEECIVPKA 548
Cdd:cd14878 377 EQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVtmetayspgnQTGVLDF---------FFQKPSGFLSLLDEESQMIWS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 549 TDLTLAQKLIDQHLGKHPN--FEKPKPPKG----KQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHA 622
Cdd:cd14878 448 VEPNLPKKLQSLLESSNTNavYSPMKDGNGnvalKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTS-ENV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 623 LIVEVWQdyttqeeaaaaaakgtagakkkgksGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLV 702
Cdd:cd14878 527 VINHLFQ-------------------------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYV 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 703 LNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAadESIIGktDAKKGSALMLARLV-KEKKLeeENFRVGLTKVFF 781
Cdd:cd14878 582 SAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA--DTLLG--EKKKQSAEERCRLVlQQCKL--QGWQMGVRKVFL 655
|
.
gi 25150292 782 K 782
Cdd:cd14878 656 K 656
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-782 |
4.24e-91 |
|
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: 312.32 E-value: 4.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAVGAAQqetfgakkaateedknKKKVTLEdQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSV----------------GGVLSVE-KLNAALTVLEAFGNVRTALNGNATRFSQLFSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLN-KPVKDYWFIAqaelIIDGINDKEE- 332
Cdd:cd01386 144 DFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqLAESNSFGIV----PLQKPEDKQKa 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 ----HQLTdEAFDILKFTPTEKMECYRLVAAMMHMGN---MKFKQRPREEQAEPDGtddAERAAKCFGIDSEEFLKALTR 405
Cdd:cd01386 220 aaafSKLQ-AAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARPEW---AQRAAYLLGCTLEELSSAIFK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 406 PRVKVGNEWVNKGQNIEQVNW------------AVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRdHFIGVLDIAGFEIF 473
Cdd:cd01386 296 HHLSGGPQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHST-SSITIVDTPGFQNP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 474 DFN------SFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPL-------------- 533
Cdd:cd01386 375 AHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedr 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 534 -GIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPKGKQAEaHFAMRHYAGT--VRYNCLNWLEKNK-DPLND 609
Cdd:cd01386 455 rGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEGPL-QFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 610 TVVTVMKAS-KEHALIVevwqdyttqeeaaaaaakgtagakkkgKSGSFMTVSMlyreSLNKLMTMLHSTHPHFIRCIIP 688
Cdd:cd01386 534 NATQLLQESqKETAAVK---------------------------RKSPCLQIKF----QVDALIDTLRRTGLHFVHCLLP 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 689 --NEKKASG----------VIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADESiigKTDAKKGSAL 756
Cdd:cd01386 583 qhNAGKDERstsspaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLT---KKLGLNSEVA 659
|
730 740 750
....*....|....*....|....*....|
gi 25150292 757 MLARLVKE----KKLEEENFRVGLTKVFFK 782
Cdd:cd01386 660 DERKAVEElleeLDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-782 |
2.78e-85 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 293.84 E-value: 2.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLpiytDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFAAvgaaqqetfGAKKaateedKNKKKVTLEDqivqTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd14937 77 ESGSGKTEASKLVIKYYLS---------GVKE------DNEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 255 HFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGINDKEEHQ 334
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKI-RSENEYKYIVNKNVVIPEIDDAKDFG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTeKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDD-----AERAAKCFGIDSEEFLKALTRPRVK 409
Cdd:cd14937 217 NLMISFDKMNMHDM-KDDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKnnlelVNEISNLLGINYENLKDCLVFTEKT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 410 VGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGiSRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEK 489
Cdd:cd14937 296 IANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 490 LQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDlQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQhLGKHPNFE 569
Cdd:cd14937 375 IHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNK-FSKHEKYA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 570 KPKppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkEHALIVEVWQDYTTQEEAaaaaakgtagak 649
Cdd:cd14937 453 STK----KDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVS-NNKLVRSLYEDVEVSESL------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 650 kkgksGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRIcRKGFPNRTLHP 729
Cdd:cd14937 516 -----GRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFD 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 25150292 730 DFVQRYALLAADESIIGKTDAKKGSALMLarlvkEKKLEEENFRVGLTKVFFK 782
Cdd:cd14937 590 VFLSYFEYLDYSTSKDSSLTDKEKVSMIL-----QNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-791 |
8.69e-83 |
|
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: 286.75 E-value: 8.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 92 LNDASVLYNLKARYAAMLIYTY---SGLfcVVINPYKRLPIYTDSVARMF-------MGKRRTEMPPHLFAVSDEAYRNM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 162 LQNHENQSMLITGESGAGKTEN----TKKVISYFAAvgaaqqetfgakkaateedkNKKKVTLEDQIVQTNPVLEAFGNA 237
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESrrllLRQLLRLSSH--------------------SKKGTKLSSQISAAEFVLDSFGNA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 238 KTVRNNNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVkDYWFI 317
Cdd:cd14879 139 KTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPS-DYALL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 318 AQAELI----IDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQrpreeqaEPDGTDDA-------- 385
Cdd:cd14879 218 ASYGCHplplGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdv 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 386 -ERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNieqvnwAVGAM------AKGLYSRIFNWLVKKCNQTLDQKGISR 458
Cdd:cd14879 291 lDIVAAFLGVSPEDLETSLTYKTKLVRKELCTVFLD------PEGAAaqrdelARTLYSLLFAWVVETINQKLCAPEDDF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 459 DHFIGVLDIAGFEIFD---FNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELI-EKPLG 534
Cdd:cd14879 365 ATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 535 IIAMLDEEC-IVPKATDLTLAQKLiDQHLGKHPNFEKPKPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVT 613
Cdd:cd14879 444 LLGILDDQTrRMPKKTDEQMLEAL-RKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVN 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 614 VMKAskehalivevwqdyTTQEeaaaaaakgtagakkkgksgsfmtvsmlyRESLNKLMTMLHSTHPHFIRCIIPNEKKA 693
Cdd:cd14879 523 LLRG--------------ATQL-----------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQL 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 694 SGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYA-LLAADESIIGKTDAKkgsalmlarlvKEKKLEEENF 772
Cdd:cd14879 560 PNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKsTLRGSAAERIRQCAR-----------ANGWWEGRDY 628
|
730
....*....|....*....
gi 25150292 773 RVGLTKVFFKAGIVAHLED 791
Cdd:cd14879 629 VLGNTKVFLSYAAWRMLED 647
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-738 |
9.38e-83 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 284.48 E-value: 9.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTdsvARMFMGKRRTEMPPHLFAVSDEAYRNMLQnHENQSMLITGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAG---AMKAYLKNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAavgaaqqetfgakkaateeDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-------------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FskQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLlnkpvkDY-WFIAQAELIIdgiNDKEEHQ 334
Cdd:cd14898 139 F--DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI------DTsSTAGNKESIV---QLSEKYK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 335 LTDEAFDILKFTPTEKMEcyRLVAAMMHMGNMKFKQrpreeqaepDGTDDAERAaKCF-------GIDSEEFLKALTRPR 407
Cdd:cd14898 208 MTCSAMKSLGIANFKSIE--DCLLGILYLGSIQFVN---------DGILKLQRN-ESFtefcklhNIQEEDFEESLVKFS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 408 VKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLdqkGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVN 487
Cdd:cd14898 276 IQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCL---EGSGERSISVLDIFGFEIFESNGLDQLCINWTN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 488 EKLQQFFNHHMFVLEQEEYAREGIQWTFIDFgLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKlIDQHLGKHPN 567
Cdd:cd14898 353 EKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVK-IKKYLNGFIN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 568 fekpkppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNdtvvtvMKASKEHALIVEvwqdyttqeeaaaaaakgtag 647
Cdd:cd14898 431 ---------TKARDKIKVSHYAGDVEYDLRDFLDKNREKGQ------LLIFKNLLINDE--------------------- 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 648 akkkgksGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTL 727
Cdd:cd14898 475 -------GSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIP 547
|
650
....*....|.
gi 25150292 728 HPDFVQRYALL 738
Cdd:cd14898 548 KDRFEERYRIL 558
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-727 |
8.01e-79 |
|
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: 276.40 E-value: 8.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFMGKRRTE-------MPPHLFAVSDEAYRNMLQNHE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 167 NQSMLITGESGAGKTENTKKVISYFAAVGAAQQETfgakkaateedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSS 246
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMT-----------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 247 RFGKFIRIHFSK---------QGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVF---SD---YLPNLKKDL----LL 307
Cdd:cd14884 144 RCGRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrglSDedlARRNLVRNCgvygLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 308 NKPVKDYWFIAQAELIIDGIN---DKEEHQLTDEAFDIL-------KFTPTEKMECYRLVAAMMHMGNMKFKQrpreeqa 377
Cdd:cd14884 224 NPDESHQKRSVKGTLRLGSDSldpSEEEKAKDEKNFVALlhglhyiKYDERQINEFFDIIAGILHLGNRAYKA------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 378 epdgtddaerAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTL----DQ 453
Cdd:cd14884 297 ----------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 454 KGISRDH-------FIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDF--GLDLQA 524
Cdd:cd14884 367 DESDNEDiysineaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 525 CIELIEKPLGIIAMLdEECIVPKA-----TDLTLAQKLIdQHLGKH------PNFEKPKPPKGKQAEAHFAMRHYAGTVR 593
Cdd:cd14884 447 FIAKIFRRLDDITKL-KNQGQKKTddhffRYLLNNERQQ-QLEGKVsygfvlNHDADGTAKKQNIKKNIFFIRHYAGLVT 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 594 YNCLNWLEKNKDPLNDTVVTVMKASKEHALivevwqdyttqeeaaaaaakgtAGAKKKGKSGSFMTVSMLYRESLNKLMT 673
Cdd:cd14884 525 YRINNWIDKNSDKIETSIETLISCSSNRFL----------------------REANNGGNKGNFLSVSKKYIKELDNLFT 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 25150292 674 MLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTL 727
Cdd:cd14884 583 QLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-782 |
4.09e-73 |
|
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: 260.74 E-value: 4.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAML--------IYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHE 166
Cdd:cd14887 1 PNLLENLYQRYNKAYinkenrncIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 167 NQSMLITGESGAGKTENTKKVISYFAAVGAAQQetfGAKKAateedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNNSS 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRH---GADSQ-----------GLEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 247 RFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLlnkPVKDYWFIAQAELIIdg 326
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS---AGEGDPESTDLRRIT-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 327 indkeehqltdEAFDILKFTPTEKMECYRLVAAMMHMGNMKF-----KQRPREEQAEPDGTDDAERAA--------KCF- 392
Cdd:cd14887 222 -----------AAMKTVGIGGGEQADIFKLLAAILHLGNVEFttdqePETSKKRKLTSVSVGCEETAAdrshssevKCLs 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 393 ------------------------GIDSEEFLK-ALTRPRVKVgnewVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKC 447
Cdd:cd14887 291 sglkvteasrkhlktvarllglppGVEGEEMLRlALVSRSVRE----TRSFFDLDGAAAARDAACKNLYSRAFDAVVARI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 448 NQTL-------------DQKGISRDHFIGVLDIAGFEIF---DFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGI 511
Cdd:cd14887 367 NAGLqrsakpsesdsdeDTPSTTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 512 QWTFI--DFGLDLQACIELIEKPLGIIAML------DEECIVPKATDLTLAQKLIDQHLGKHPNFE-------------- 569
Cdd:cd14887 447 FQNQDcsAFPFSFPLASTLTSSPSSTSPFSptpsfrSSSAFATSPSLPSSLSSLSSSLSSSPPVWEgrdnsdlfyeklnk 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 570 --------KPKPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASkehalivevwqDYTTQEeaaaaa 641
Cdd:cd14887 527 niinsakyKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLAC-----------STYTRL------ 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 642 AKGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKG 721
Cdd:cd14887 590 VGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADG 669
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 722 FPNRTLHPDFVQRYallaadESIIGKTDAKKGSALMLARLVKE-KKLEEENFRVGLTKVFFK 782
Cdd:cd14887 670 FPCRLPYVELWRRY------ETKLPMALREALTPKMFCKIVLMfLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-781 |
9.67e-69 |
|
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: 247.96 E-value: 9.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 98 LYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRR----------TEMPPHLFAVSDEAYRNMLQNHEN 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 168 QSMLITGESGAGKTENTKKVISYFAAVG---AAQQETFGAKKAATeedknkkkvTLEDQIVQTNPVLEAFGNAKTVRNNN 244
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGdetEPRPDSEGASGVLH---------PIGQQILHAFTILEAFGNAATRQNRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 245 SSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFS--DYLPNLKKDLLLNKPVKDYWFIAQAEL 322
Cdd:cd14893 155 SSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQADP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 323 IIDGIN-DKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDG-TDDAERAAKCFGIDSEEFL 400
Cdd:cd14893 235 LATNFAlDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnSTTVSDAQSCALKDPAQIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 401 KAL----TRPRV------------KVGNEWVN--KGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTL--------DQK 454
Cdd:cd14893 315 LAAklleVEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryeKSN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 455 GISRDHFIGVLDIAGFEIFD--FNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQW-------TFIDFGLDLQAC 525
Cdd:cd14893 395 IVINSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVenrltvnSNVDITSEQEKC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 526 IELIE-KPLGIIAMLDEECIVPKATDLTLAQKLI--DQHLG--KHPNF------EKPKPPkgKQAEAHFAMRHYAGTVRY 594
Cdd:cd14893 475 LQLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNMgadttnEYLAPS--KDWRLLFIVQHHCGKVTY 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 595 NCLNWLEKNKDPLNDTVVTVMKASKE---HAL--------IVEVWQDYTTQEEAAAAAAKGTAGAKKKGKSGSFMTVSML 663
Cdd:cd14893 553 NGKGLSSKNMLSISSTCAAIMQSSKNavlHAVgaaqmaaaSSEKAAKQTEERGSTSSKFRKSASSARESKNITDSAATDV 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 664 YRESlNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYallaadES 743
Cdd:cd14893 633 YNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KN 705
|
730 740 750
....*....|....*....|....*....|....*....
gi 25150292 744 IIGktdaKKGSALMLAR-LVKEKKLEEENFRVGLTKVFF 781
Cdd:cd14893 706 VCG----HRGTLESLLRsLSAIGVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
94-739 |
1.11e-65 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 236.16 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 94 DAsVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPiytdsVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLIT 173
Cdd:cd14881 1 DA-VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG-----NPLTLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATeedknkkkvtledqivqTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14881 75 GTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAA-----------------AFTVLRSLGSAKTATNSESSRIGHFIE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFSkQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNK-PVKDYWFIAQAELIIDGINDKEE 332
Cdd:cd14881 138 VQVT-DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 HQLTDEAFDIL--KFTptekmECYRLVAAMMHMGNMKFKQrPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKV 410
Cdd:cd14881 217 FQAWKACLGILgiPFL-----DVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 411 GNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNqTLDQKGISR-----DHFIGVLDIAGFEIFDFNSFEQLWINF 485
Cdd:cd14881 291 RGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SLKRLGSTLgthatDGFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 486 VNEKLQQFFNHHMFVLEQEEYAREGIQwTFIDFG-LDLQACIELIEK-PLGIIAMLDEECiVPKATDLTLAQKLIDQHLG 563
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 564 kHPNFEKPKPPKGKQaeahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIVEVWQDYTTQeeaaaaaak 643
Cdd:cd14881 448 -NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFATHTQDFHTR--------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 644 gtagakkkgksgsfmtvsmlyresLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFP 723
Cdd:cd14881 514 ------------------------LDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYP 569
|
650
....*....|....*.
gi 25150292 724 NRTLHPDFVQRYALLA 739
Cdd:cd14881 570 HRMRFKAFNARYRLLA 585
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-782 |
5.82e-61 |
|
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: 222.05 E-value: 5.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 95 ASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFmgkrrtemppHLFAVSDEAYRNMLQNHENQSMLI-T 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 174 GESGAGKTENTKKVISYFAAvgaaqqetfgakkaateedKNKKKVTLEdQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------------QPKSKVTTK-HSSAIESVFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 254 IHFsKQGRVASCDIEHYL-LEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYWFIAQAELIIDGINDKEE 332
Cdd:cd14874 131 LLY-KRNVLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI-KGLQKFFYINQGNSTENIQSDVNH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 333 HQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQR--PREEQAEPDGTDDAER--AAKCFGIDSEEFLKALTrPRV 408
Cdd:cd14874 209 FKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKrnPNVEQDVVEIGNMSEVkwVAFLLEVDFDQLVNFLL-PKS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 409 KVGNEWvnkgqnieQVNWAVG---AMAKGLYSRIFNWLVKKCNQTLdqKGISRDHFIGVLDIAGFEIFDFNSFEQLWINF 485
Cdd:cd14874 288 EDGTTI--------DLNAALDnrdSFAMLIYEELFKWVLNRIGLHL--KCPLHTGVISILDHYGFEKYNNNGVEEFLINS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 486 VNEKLQQFFNHHMFVLEQEEYAREGIQwtfIDF----GLDLQACIELI-EKPLGIIAMLDEECIVPKATDLTLAQKLIDQ 560
Cdd:cd14874 358 VNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLN 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 561 HLGKhPNFEKPKppkgKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEH--ALIVEVWQDYTTQEeaa 638
Cdd:cd14874 435 HTDR-SSYGKAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPiiGLLFESYSSNTSDM--- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 639 aaaakgtagakkkgksgsFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRIC 718
Cdd:cd14874 507 ------------------IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFR 568
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 719 RKGFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLVKekklEEENFRVGLTKVFFK 782
Cdd:cd14874 569 IKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQGQGVK----YENDFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
101-742 |
6.26e-59 |
|
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: 217.27 E-value: 6.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 101 LKARYAAMLIYTYSGLFCVVINPYKRLP-IYTDSVARMFmgKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGESGAG 179
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 180 KTENTKKVISYFAAVgaaqqetfgakkaateeDKNKKKVtLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFSKQ 259
Cdd:cd14905 85 KSENTKIIIQYLLTT-----------------DLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 260 GRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKpVKDYWFIAQAELI-IDGINDKEEHQLTDE 338
Cdd:cd14905 147 GEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGD-INSYHYLNQGGSIsVESIDDNRVFDRLKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 339 AFDILKFtPTEKME-CYRLVAAMMHMGNMKFKQrpREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWVNK 417
Cdd:cd14905 226 SFVFFDF-PSEKIDlIFKTLSFIIILGNVTFFQ--KNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 418 GQnieqvnwavgAMAKGLYSRIFNWLVKKCNQTLdqKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHH 497
Cdd:cd14905 303 RD----------SLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 498 MFVLEQEEYAREGIQW-TFIDFGlDLQACIELIEKplgIIAMLDEECIVPKATDLTLAQKLiDQHLGKHPNFEKpKPPKg 576
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 577 kqaeahFAMRHYAGTVRYNCLNWLEKNKDP-------LNDTVVTVMKASKE-----HALIVEVWQDYTTQEEAAAAAAKG 644
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEilqrtnvLHKNSITKYLFSRDgvfniNATVAELNQMFDAKNTAKKSPLSI 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 645 TAGAKKKGK-------------------------SGSFMTVSMLYrESLNKLMTMLHSTHpHFIRCIIPNEKKASGVIDA 699
Cdd:cd14905 518 VKVLLSCGSnnpnnvnnpnnnsgggggggnsgggSGSGGSTYTTY-SSTNKAINNSNCDF-HFIRCIKPNSKKTHLTFDV 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 25150292 700 GLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADE 742
Cdd:cd14905 596 KSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ 638
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-254 |
2.24e-55 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 190.63 E-value: 2.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 117 FCVVINPYKRLPIYTDS-VARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGESGAGKTENTKKVISYFAAVG 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 196 AAQQEtfgAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRI 254
Cdd:cd01363 81 FNGIN---KGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-782 |
8.83e-54 |
|
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: 201.12 E-value: 8.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 176 SGAGKTENTKKVISYFAAVGAAQQETFGakkaateedknkkkvtledQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIH 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG-------------------RVESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 256 FSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSD----------YLPNLKKDLLLNKPV---KDYWFIAQAel 322
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieaqnrlkeyNLKAGRNYRYLRIPPevpPSKLKYRRD-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 323 iiDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRprEEQAEPDGTDDAERAAKCFGIDSEEFLKA 402
Cdd:cd14882 221 --DPEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQN--GGYAELENTEIASRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 403 LTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLD-QKGISRD-HFIGVLDIAGFEIFDFNSFEQ 480
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfPRAVFGDkYSISIHDMFGFECFHRNRLEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 481 LWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEecivpKATDLTLAQKLIDQ 560
Cdd:cd14882 377 LMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 561 HLGKHPNFEKPkppkgkqAEAH-FAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHAliveVWQDYTTQEeaaa 639
Cdd:cd14882 452 IKEKHSQFVKK-------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDES----VKLMFTNSQ---- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 640 aaakgtaGAKKKGKSGSFMTVSMlyrESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICR 719
Cdd:cd14882 517 -------VRNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQ 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 720 KGFPNRTLHPDFVQRYALLAAD-ESIIGKTdaKKGSALMLARLvkekKLeeENFRVGLTKVFFK 782
Cdd:cd14882 587 KGFSYRIPFQEFLRRYQFLAFDfDETVEMT--KDNCRLLLIRL----KM--EGWAIGKTKVFLK 642
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-741 |
4.76e-49 |
|
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: 188.12 E-value: 4.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 96 SVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTE-MPPHLFAVSDEAYRNMLQNHENQSMLITG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 175 ESGAGKTENTKKVISYFA-AVGAAQQETFGAKKAATEEDKN----KKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFG 249
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyQVKGSRRLPTNLNDQEEDNIHNeentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 250 KFIRIHFSKQgRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLnKPVKDYwFIAQAELIIDGIND 329
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL-KNIENY-SMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 330 KEEHQLT-DEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPRE-----------------------EQAEPDGTDDA 385
Cdd:cd14938 239 YSGKILElLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKksllmgknqcgqninyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 386 ER----AAKCFGIDSEEFLKALTRPRVkVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLD--QKGISRD 459
Cdd:cd14938 319 VKnlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 460 HFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLD-LQACIELIEKPLGIIAM 538
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 539 LDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPKGKQAEahFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKAS 618
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT--FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 619 KEHAL--------------IVEVWQDYTTQeeaaaaaaKGTAGAKKKGKSGSFMTVSMLyRESLNKLMTMLHSTHPHFIR 684
Cdd:cd14938 556 ENEYMrqfcmfynydnsgnIVEEKRRYSIQ--------SALKLFKRRYDTKNQMAVSLL-RNNLTELEKLQETTFCHFIV 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 685 CIIPNEKKAS-GVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAAD 741
Cdd:cd14938 627 CMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNED 684
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1843 |
5.10e-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: 120.55 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 978 RKVEAEKnakehQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTE--DLQAAEEQnlaanKLKAKLMQSLEDSEQTME 1055
Cdd:TIGR02168 173 RRKETER-----KLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRE-----LELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1056 REKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLgmkledeQAAVAKLQKGIQQDEARVKDLH 1135
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1136 DQLADEKDARQRADRSRADQQAEYDELTEQLEDQArataAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKgsda 1215
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELEELEAELEELESRLEELEEQLETLRSK---- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1216 IQELSDQIEQLQKQKGRIEKEKGHMQREFDessaaldqeaklRADQERiakgyevrllelrlKADEQSRQLQDFVSSKGR 1295
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRE------------RLQQEI--------------EELLKKLEEAELKELQAE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1296 LNSENSDLARQVEELEAKIQAANRLKLQFsNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASR 1375
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREEL-EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1376 QLSKASvELDQWRTKFET--EGLIGADEFDEVKKRQNQKTSEIqDALDACNAKIVALENARSRLTAEADANRLEA----E 1449
Cdd:TIGR02168 521 ILGVLS-ELISVDEGYEAaiEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREIlkniE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1450 HHAQAVSSLEKKQKAFDKVIDEWkkkVDDLYL--ELDGAQRDARQLSGEA-------HKLR------GQHDTLADQVEGL 1514
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYL---LGGVLVvdDLDNALELAKKLRPGYrivtldgDLVRpggvitGGSAKTNSSILER 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1515 RRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAE 1594
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1595 KEEEfenhrkvhQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVD 1674
Cdd:TIGR02168 756 LTEL--------EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1675 EEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESsvkEHQEHNNELNSQNVALAAAKSQLDNeialLN 1754
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASLEEALALLRSELEE----LS 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1755 SDIAEAHTELSASEDRGRRAASDAAKLAEDLrheQEQSQQLERFKKQLESAVKDLQERADAAEAAVmkggAKAIQKAEQR 1834
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRL---EGLEVRIDNLQERLSEEYSLTLEEAEALENKI----EDDEEEARRR 973
|
....*....
gi 25150292 1835 LKAFQSDLE 1843
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1065-1685 |
4.16e-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: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1065 DKNKRKAEGELKIAQETLE-------ELNKS----KSDAENALR-------RKETELHTLGMKLEDEQAAVAKLQKGIQQ 1126
Cdd:COG1196 171 KERKEEAERKLEATEENLErledilgELERQleplERQAEKAERyrelkeeLKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1127 DEARVKDLHDQLADEKDARQRAdrsRADQQAEYDELTEQLEDQARATAAQIELGKKKDAElTKLRRDLEESGLKFGEQLT 1206
Cdd:COG1196 251 LEAELEELEAELAELEAELEEL---RLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1207 VLKKKgsdaIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQL 1286
Cdd:COG1196 327 ELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1287 QDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDE 1366
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1367 VAGKNEASRQLS----------------KASVELDQWRTKFETEGLIGADEFDEVK--------KRQNQKTSEIQDALDA 1422
Cdd:COG1196 483 LEELAEAAARLLllleaeadyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaalaaALQNIVVEDDEVAAAA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1423 CN---------AKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQL 1493
Cdd:COG1196 563 IEylkaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1494 SGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRgldeaeaALESEESK 1573
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER-------ELAEAEEE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1574 ALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEA--DINELeiALDHANKA 1651
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgPVNLL--AIEEYEEL 793
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 25150292 1652 NE-----DAQKNIrryLDQ-IRELQQTVDE-EQKRREEFRE 1685
Cdd:COG1196 794 EErydflSEQRED---LEEaRETLEEAIEEiDRETRERFLE 831
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
860-1437 |
4.20e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEE-----EKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGK 934
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAEleeleAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 935 LADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKN 1014
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1015 QEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAEN 1094
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1095 ALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADE----------KDARQRADRSRADQQAEYDELTE 1164
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflegvkaaLLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1165 QLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIE--KEKGHMQR 1242
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASdlREADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1243 EFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSE----NSDLARQVEELEAKIQAAN 1318
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAlleaEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1319 RLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTK-FETEGLI 1397
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERElERLEREI 776
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 25150292 1398 GA---------DEFDEVKKRQNQKTSEIQDaldacnakivaLENARSRL 1437
Cdd:COG1196 777 EAlgpvnllaiEEYEELEERYDFLSEQRED-----------LEEARETL 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
883-1754 |
5.58e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.53 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 883 EEKKRQLQEGAERLNKeTADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADAS-KKLEVEEARAVEINKQKKLVEA 961
Cdd:TIGR02168 175 KETERKLERTRENLDR-LEDILNELERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 962 ECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQnlaanklka 1041
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ--------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1042 klmqsLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETElhtlgmkLEDEQAAVAKLQ 1121
Cdd:TIGR02168 325 -----LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1122 KGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELteqledQARATAAQIELGKKKDAELTKLRRDLEESGLKF 1201
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1202 GEQLTVLKKkgsdAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRL-LELRLKAD 1280
Cdd:TIGR02168 467 REELEEAEQ----ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1281 EQSRqLQDFVsskgrlnSENSDLARQVEELEAKiqaANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLK 1360
Cdd:TIGR02168 543 LGGR-LQAVV-------VENLNAAKKAIAFLKQ---NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1361 ESIE-------------DEVAGKNEASRQLSKAS--VELDQwrTKFETEGLI--GADEFDEV--KKRQN-----QKTSEI 1416
Cdd:TIGR02168 612 PKLRkalsyllggvlvvDDLDNALELAKKLRPGYriVTLDG--DLVRPGGVItgGSAKTNSSilERRREieeleEKIEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1417 QDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGE 1496
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1497 AHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALR 1576
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1577 CQIEVSQIRAEIEKrIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQ 1656
Cdd:TIGR02168 850 LSEDIESLAAEIEE-LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1657 KNIRRYLDQIRELQQTVDEEQKRR-EEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQ 1735
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQ 1008
|
890
....*....|....*....
gi 25150292 1736 NVALAAAKSQLDNEIALLN 1754
Cdd:TIGR02168 1009 KEDLTEAKETLEEAIEEID 1027
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
860-1669 |
6.73e-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: 107.06 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKdtVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADAS 939
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 940 KKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQN 1019
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1020 KKLTEDLQAA--------EEQNLAANKLKAkLMQSLEDSEQTMEREKRNRADMdkNKRKAEGELKIAQETLEELNKSKSD 1091
Cdd:TIGR02168 375 EELEEQLETLrskvaqleLQIASLNNEIER-LEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1092 AENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLaDEKDARQRADRSRADQQAEYDELTEQLEDQAR 1171
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1172 A-----TAAQIELGKKKDAELTKlrrDLEESGLKFGEQ-------LTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGH 1239
Cdd:TIGR02168 531 VdegyeAAIEAALGGRLQAVVVE---NLNAAKKAIAFLkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1240 MQREFDESSA----------------ALDQEAKLRAdQERI--AKGYEVRllelrlkadeqsrqlQDFVSSKGRLNSENS 1301
Cdd:TIGR02168 608 VKFDPKLRKAlsyllggvlvvddldnALELAKKLRP-GYRIvtLDGDLVR---------------PGGVITGGSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1302 DLARQVE--ELEAKIQAanrlklqfsneldhAKRQAEEESRERQnlsnlskNLARELEQLKESIEDEVAGKNEASRQLSK 1379
Cdd:TIGR02168 672 ILERRREieELEEKIEE--------------LEEKIAELEKALA-------ELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1380 ASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTsEIQDALDACNAKIVALEnaRSRLTAEADANRLEAEHhaqavSSLE 1459
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIE-ELEERLEEAEEELAEAE--AEIEELEAQIEQLKEEL-----KALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1460 KKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRAT 1539
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1540 HALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEK---RIAEKEEEFENHRKVHQQTIDSIQAT 1616
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTLEEAEALENK 962
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 1617 LD-SETKAKSELFRVKKKLEA--DINELEIA--------LDHANKANEDAQKNIRRYLDQIREL 1669
Cdd:TIGR02168 963 IEdDEEEARRRLKRLENKIKElgPVNLAAIEeyeelkerYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-719 |
5.71e-22 |
|
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: 103.67 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 101 LKARYAAMLIYTYSGLFCV-VINPYKRL------PIYTDSVARMFMGKRRTE--MPPHLFAVSDEAYRNMLQNHEN---- 167
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLFFDNEHtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 168 ---------------QSMLITGESGAGKTENTKKVISYFAAVG--------------------------------AAQQE 200
Cdd:cd14894 87 pstissnrsmtegrgQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftsstksTIQMR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 201 TFGAKKAATEEDKNKKKVT-----------------------------------------LEDQ---------------- 223
Cdd:cd14894 167 TEEARTIALLEAKGVEKYEivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehLEDEeqlrmyfknphaakkl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 224 --IVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFS-----KQGRVASCDIEHYLLEKSRVIRQA------PGERCYHIF 290
Cdd:cd14894 247 siVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAfglhpWEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHIL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 291 YQVFSD-----YLPNLKKDLLLNK-PVKDYWFIAQAELIIDGINDKEEHQLTD--------EAFDILKFTPTEKMECYRL 356
Cdd:cd14894 327 YAMVAGvnafpFMRLLAKELHLDGiDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 357 VAAMMHMGNMKFKQRPREEQAEPDGT---DDAERAAKCFGIDSEEFLKALTRPR---VKVGNEWVNKGQNIEQVNWAVGA 430
Cdd:cd14894 407 LSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 431 MAKGLYSRIFNWLVKKCNQTLDQKGISRD----------------HFIGVLDIAGFEIFDFNSFEQLWINFVNEKLqqff 494
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEATKMSALSTDgnkhqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL---- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 495 nhhmFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQ-----KLIDQHLGKHPNFE 569
Cdd:cd14894 563 ----YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFVRNIYDRNSSR 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 570 KPKPPKG-KQAEAH---------FAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIVEVwqDYTTQEEAAA 639
Cdd:cd14894 639 LPEPPRVlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML--NESSQLGWSP 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 640 AAAKGTAGAKKKGKSGSFMTVSMlYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICR 719
Cdd:cd14894 717 NTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1097-1936 |
8.98e-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: 103.60 E-value: 8.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1097 RRKETELhtlgmKLEDEQAAVAKLQKGIQQDEARVKDLHDQL-ADEKDARQRADRSRADQQ---AEYDELTEQLEDQARA 1172
Cdd:TIGR02168 173 RRKETER-----KLERTRENLDRLEDILNELERQLKSLERQAeKAERYKELKAELRELELAllvLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1173 TAAQIELGKKKDAELTKLRRDLEESGLKFGE---QLTVLKKKgsdaIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSA 1249
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSEleeEIEELQKE----LYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1250 ALDQEAKlradqeriakgyevRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELD 1329
Cdd:TIGR02168 324 QLEELES--------------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1330 HAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVEldqwRTKFETEGLIGADEfdevkkRQ 1409
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----ELEEELEELQEELE------RL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1410 NQKTSEIQDALDACNAKIVALENARSRLTAEADAnrleaehhaqavsslekkqkafdkvidewkkkVDDLYLELDGAQRD 1489
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDS--------------------------------LERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1490 ARQLSGEAHKLRGQHDTLADQVE-------------GLRRENKSLSDET--RDLTESL--SEGGRAT--------HALSK 1544
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISvdegyeaaieaalGGRLQAVVVENLNaaKKAIAFLkqNELGRVTflpldsikGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1545 NLRRLEMEKEELQRGLDEAEAALESEESKAL-----RCQIeVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDS 1619
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllgGVLV-VDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1620 ETKA-----KSELFRVKKK---LEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAE 1691
Cdd:TIGR02168 667 KTNSsilerRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1692 RKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRG 1771
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1772 RRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEaavmkggaKAIQKAEQRLKAFQSDLETESRRAGE 1851
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE--------SELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1852 ASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQL-EEAEEQANSHLSKYRTVQLSLETAEERADSAE 1930
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....*.
gi 25150292 1931 QCLVRI 1936
Cdd:TIGR02168 979 NKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
981-1804 |
1.81e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 102.45 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 981 EAEKNAKEhqIRALQDEMRQQDEnisKLNKERkNQEEQNKKLTEDLQAAEEQNLAANKlkaklmqsledseQTMEREKRN 1060
Cdd:TIGR02169 181 EVEENIER--LDLIIDEKRQQLE---RLRRER-EKAERYQALLKEKREYEGYELLKEK-------------EALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1061 radMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGmklEDEQAAV----AKLQKGIQQDEARVKDLHD 1136
Cdd:TIGR02169 242 ---IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG---EEEQLRVkekiGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1137 QLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKgSDAI 1216
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY-REKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1217 QELSDQIEQLQKQKGRI--EKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKA-----DEQSRQLQDF 1289
Cdd:TIGR02169 395 EKLKREINELKRELDRLqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1290 VSSKGRLNSENSDLARQVEELEAKIQAANRlklqfsnELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIE----- 1364
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEE-------RVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagn 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1365 ---------DEVAGKNEA---SRQLSKAS-----------VELDQWRTKFETEGLIGADEFDEvkKRQNQKTSEIQDALD 1421
Cdd:TIGR02169 548 rlnnvvvedDAVAKEAIEllkRRKAGRATflplnkmrderRDLSILSEDGVIGFAVDLVEFDP--KYEPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1422 ACNakivaLENARsRLTAEADANRLEAEhhaqavssLEKKQKAfdkvidewkkkvddlyleLDGAQRDARQLSGEAHKLR 1501
Cdd:TIGR02169 626 VED-----IEAAR-RLMGKYRMVTLEGE--------LFEKSGA------------------MTGGSRAPRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1502 GQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEV 1581
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1582 SQIRAEI---EKRIAEKEEEFENHRKvhqqTIDSIQATLDSE-----TKAKSELFRVKKKLEADINELEIALDHANKANE 1653
Cdd:TIGR02169 754 ENVKSELkelEARIEELEEDLHKLEE----ALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1654 DAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELN 1733
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1734 SQnvalaaaKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAeDLRHEQEQSQQLERFKKQLES 1804
Cdd:TIGR02169 910 AQ-------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL-SLEDVQAELQRVEEEIRALEP 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1415-1931 |
1.26e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1415 EIQDALDACNAKIVALEnaRSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLS 1494
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1495 GEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKA 1574
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1575 LRCQIEVSQIRAEIEKRIAEKEEEfenhrkvhQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANED 1654
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1655 AQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELI------------VKLEALERARRVVESSV 1722
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeaeadyegflegVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1723 KEHQEHNNELNSQNVALAAAKSQLDNE---------IALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQ 1793
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVeddevaaaaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1794 QLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSD--LETESRRAGEASKTLARADRKVREFEFQVA 1871
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1872 EDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQ 1931
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1217-1905 |
2.15e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.45 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1217 QELSDQIEQLQKQKGRIEKEKGHMQREFDESSAAldQEAKLRADQERIAKgyEVRLLELRLKADEQSRQLQDFVSSKGRL 1296
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKA--EEAKKKAEDARKAE--EARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1297 NSE--NSDLARQVEELEAKIQAANRLKLQFSNELDHAK--RQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNE 1372
Cdd:PTZ00121 1160 AEDarKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1373 ASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKivalENARSRLTAEADANRLEAEHHA 1452
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1453 QAvSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQhdtlADQVEGLRRENKSLSDETRDLTESL 1532
Cdd:PTZ00121 1316 KA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1533 seggRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDS 1612
Cdd:PTZ00121 1391 ----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1613 IQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKnirryLDQIRELQQTVDEEQKRREEfrEHLLAAER 1692
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK-----ADEAKKAEEAKKADEAKKAE--EAKKADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1693 KLAVAKQEQEELiVKLEALERA--RRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELsasedr 1770
Cdd:PTZ00121 1540 KKAEEKKKADEL-KKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA------ 1612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1771 grRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQS-DLETESRRA 1849
Cdd:PTZ00121 1613 --KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKA 1690
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1850 GEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQA 1905
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1202-1942 |
3.81e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.21 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1202 GEQLTVLKKKGSDAI--QELSDQIEQLQKQ--KGRIEKEKGHMQREFDESSAALDQEAKLRADqeriAKGYEVRLLELRL 1277
Cdd:TIGR02168 199 ERQLKSLERQAEKAEryKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1278 KADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELE 1357
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1358 QLKESIEDEVAGKNEASRQLSKASVELDQWRtkfetegligaDEFDEVKKRQNQKTSEIQDALdacnAKIVALENARSRL 1437
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLR-----------SKVAQLELQIASLNNEIERLE----ARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1438 TAEADANRLEAEHHAQAVSSLEKKQKafDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLA---DQVEGL 1514
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1515 RRENKSLSDETRDLTESLSEGGRATHALSKNLR---RLEMEKEE-LQRGLDEAEAALESEESKALRCQIEVSQIRAEIEK 1590
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLSELISvdeGYEAAIEAaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1591 RIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELfrvKKKLEADINELEIALDHANkANEDAQKNIRRYldqireLQ 1670
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL---RKALSYLLGGVLVVDDLDN-ALELAKKLRPGY------RI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1671 QTVDEEQKRR--------EEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSvkehqehNNELNSQNVALAAA 1742
Cdd:TIGR02168 648 VTLDGDLVRPggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE-------LEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1743 KSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAavmk 1822
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE---- 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1823 ggakAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAE 1902
Cdd:TIGR02168 797 ----ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 25150292 1903 EQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRA 1942
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1557 |
5.92e-19 |
|
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: 94.36 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 856 VNSGKIEAQYEKLQETVATLKDtvvqEEEKKRQLQEGAERLNK-ETADLLAQLEASKGSTREVEERMTAMNEQKVALEGK 934
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRR----EREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 935 LADASKKLEVEEARAVEINKQ-KKLVEAECADLKKNcqdvdlsLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERK 1013
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEK-------IGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1014 NQEEQNKKLTEDLQAAeeqnlaaNKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAE 1093
Cdd:TIGR02169 333 KLLAEIEELEREIEEE-------RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1094 NALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLED-QARA 1172
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRvEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1173 TAAQIELgkkkdAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREF---DESSA 1249
Cdd:TIGR02169 486 SKLQREL-----AEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVvveDDAVA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1250 A------------------LDQEAKLRADQERIAK----GYEVRLLELRLKAD----------------EQSRQLQD--- 1288
Cdd:TIGR02169 561 KeaiellkrrkagratflpLNKMRDERRDLSILSEdgviGFAVDLVEFDPKYEpafkyvfgdtlvvediEAARRLMGkyr 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1289 ------------------FVSSKGRLNSENSDLArQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSK 1350
Cdd:TIGR02169 641 mvtlegelfeksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1351 NLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFET-EGLIGADEFDEVKKRQ-----------------NQK 1412
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElEARIEELEEDLHKLEEalndlearlshsripeiQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1413 TSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQ 1492
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1493 LSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQ 1557
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1547-1885 |
7.65e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1547 RRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAE-IEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKS 1625
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEeLEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1626 ElfrvkkkleadINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELI 1705
Cdd:COG1196 296 E-----------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1706 VKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDL 1785
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1786 RHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVRE 1865
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340
....*....|....*....|
gi 25150292 1866 FEFQVAEDKKNYDKLQELVE 1885
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAAL 544
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1632-1931 |
3.07e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1632 KKLEADINELEIALdhankanedAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEAL 1711
Cdd:COG1196 216 RELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1712 ERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQ 1791
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1792 SQQLERfkkQLESAVKDLQERADAAEAAvmkggAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVA 1871
Cdd:COG1196 367 LLEAEA---ELAEAEEELEELAEELLEA-----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1872 EDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQ 1931
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1537 |
3.50e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 880 VQEEEKKRQLQEGAERLNKETADLLAQLEASKG--STREVEERMTAMNEQKVALEGKLADASKKLEveEARAVEINKQKK 957
Cdd:PTZ00121 1193 LRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE--EARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 958 LVEAEcadLKKNCQDVDLSLRKVEAEKNAKEHQIRALqDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAAN 1037
Cdd:PTZ00121 1271 AIKAE---EARKADELKKAEEKKKADEAKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1038 KLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEgELKIAQETLEELNKSKSDAENAlRRKETELHtlgmKLEDEQAAV 1117
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEED-KKKADELK----KAAAAKKKA 1420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1118 AKLQKgiQQDEARVKDLHDQLADEKDARQRAdRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAEltKLRRDLEES 1197
Cdd:PTZ00121 1421 DEAKK--KAEEKKKADEAKKKAEEAKKADEA-KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEA 1495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1198 GLKFGEqltvLKKKGSDaiQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAAldqEAKLRADQERiaKGYEVRLLELRL 1277
Cdd:PTZ00121 1496 KKKADE----AKKAAEA--KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA---EEKKKADELK--KAEELKKAEEKK 1564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1278 KADEQSRQLQDFVSSKGRlnsenSDLARQVEelEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNlSKNLARELE 1357
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRK-----AEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1358 QLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGAD---EFDEVKKRQNQKTSEIQDALDACNAKIVALENAR 1434
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1435 --SRLTAEADANRLEAEhHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKlrgqhDTLADQVE 1512
Cdd:PTZ00121 1717 kaEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDE 1790
|
650 660
....*....|....*....|....*
gi 25150292 1513 GLRRENKSLSDETRDLTESLSEGGR 1537
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1431 |
1.27e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 862 EAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAmNEQKVALEGKLADASKK 941
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-DELKKAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 942 leVEEARAVEINKQKKLVEAECADLKKNCQDVDlslRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKK 1021
Cdd:PTZ00121 1298 --AEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1022 LTEDLQAAEEQnlaanKLKAKLMQSLEDSEQTMEREKRNRADMDKN---KRKAEgELKIAQETLEELNKSKSDAENAlrR 1098
Cdd:PTZ00121 1373 KEEAKKKADAA-----KKKAEEKKKADEAKKKAEEDKKKADELKKAaaaKKKAD-EAKKKAEEKKKADEAKKKAEEA--K 1444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1099 KETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADE-----KDARQRAD--RSRADQQAEYDELtEQLEDQAR 1171
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaEEAKKKADeaKKAAEAKKKADEA-KKAEEAKK 1523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1172 ATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVL--KKKGSDAIQELSDQIEQLQK-------QKGRIEKEKGHMQR 1242
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeeKKKAEEAKKAEEDKNMALRKaeeakkaEEARIEEVMKLYEE 1603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1243 EFDESSAAL--DQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAAnrl 1320
Cdd:PTZ00121 1604 EKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA--- 1680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1321 klqfsneldhakRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGAD 1400
Cdd:PTZ00121 1681 ------------KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
570 580 590
....*....|....*....|....*....|....
gi 25150292 1401 ---EFDEVKKRQNQKTSEIQDALDACNAKIVALE 1431
Cdd:PTZ00121 1749 akkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1213-1804 |
1.31e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1213 SDAIQELSDQIEQLQKQKGRIEKekghmQREFDESSAALDQEAKLRADQERIAK--GYEVRLLELRLKADEQSRQLQDFV 1290
Cdd:COG1196 192 EDILGELERQLEPLERQAEKAER-----YRELKEELKELEAELLLLKLRELEAEleELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1291 SSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGK 1370
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1371 NEASRQLSKASVELDQWRTKFETEgLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEH 1450
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1451 HAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDEtRDLTE 1530
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1531 SLSEGGRATHALSKNLRRLEMEKEELQRGL---DEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQ 1607
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAayeAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1608 QTIDSIQATLDSETKAKSELFRVKKKLEA---DINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFR 1684
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADAryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1685 EHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELnsqnvALAAAKSQLDNEIALLNSDIAEAHTEL 1764
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA-----EEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 25150292 1765 SASEDRGRRAASDAAKLAEDLRHEqEQSQQLERFKKQLES 1804
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-ELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1062-1811 |
1.82e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 89.36 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1062 ADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHtlgmKLEDEQAAVAKLQkgiqqdEARVKDLHDQLADE 1141
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE----KAERYQALLKEKR------EYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1142 KDARQRADRSRADQQAEYDELTEQLEDQARATAaqiELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGS---DAIQE 1218
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLE---EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAsleRSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1219 LSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADqeriakgyevrlLELRLKADEQSRQlqdfvsskgrlns 1298
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK------------LTEEYAELKEELE------------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1299 ensDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLS 1378
Cdd:TIGR02169 368 ---DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1379 KASVELDQWRTKFET--EGLIGAD--------EFDEVKKRQNQKTSEI--------------------QDALDACNAKIV 1428
Cdd:TIGR02169 445 DKALEIKKQEWKLEQlaADLSKYEqelydlkeEYDRVEKELSKLQRELaeaeaqaraseervrggravEEVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1429 ---------------ALENARS-RLTA-----EADA--------------------NRLEAEHHAQAVSSLE-------- 1459
Cdd:TIGR02169 525 gtvaqlgsvgeryatAIEVAAGnRLNNvvvedDAVAkeaiellkrrkagratflplNKMRDERRDLSILSEDgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1460 ------KKQKAFDKV---------IDEWKKKVDDLYL------------ELDGAQRDARQLSGEAHKLRGQHDTLADQVE 1512
Cdd:TIGR02169 605 lvefdpKYEPAFKYVfgdtlvvedIEAARRLMGKYRMvtlegelfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1513 GLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEI---E 1589
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELkelE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1590 KRIAEKEEEFEN--------HRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRR 1661
Cdd:TIGR02169 765 ARIEELEEDLHKleealndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1662 YLDQIRELQQTVDEEQKRREEFREHL-------LAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNS 1734
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELeeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1735 QNVALAAAKSQLDNEIALLNSD-------------IAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQ 1801
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIpeeelsledvqaeLQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
890
....*....|
gi 25150292 1802 LESAVKDLQE 1811
Cdd:TIGR02169 1005 ILERIEEYEK 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
882-1693 |
5.09e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 882 EEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEeaRAVEINKQKKLVEA 961
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR--KAEELRKAEDARKA 1202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 962 ECADLKKNCQDVDlSLRKVEAEKNAKEhqIRALQdEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNL--AANKL 1039
Cdd:PTZ00121 1203 EAARKAEEERKAE-EARKAEDAKKAEA--VKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikAEEAR 1278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1040 KAKLMQSLEDSEQTME-REKRNRADMDKNKRKAEgELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVA 1118
Cdd:PTZ00121 1279 KADELKKAEEKKKADEaKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1119 KLQKGIQQDEARVKDLHDQLADEKDARQRADRSR----ADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTK---LR 1191
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadeAK 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1192 RDLEESglkfgEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALdQEAKLRADQERiaKGYEVR 1271
Cdd:PTZ00121 1438 KKAEEA-----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA-EEAKKKADEAK--KAAEAK 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1272 LLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKN 1351
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1352 LARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETE---GLIGADEFDEVKKRQNQKTSEIQDALDACNAKIV 1428
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1429 ALENAR----SRLTAEADANRLEA----EHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKL 1500
Cdd:PTZ00121 1670 AEEDKKkaeeAKKAEEDEKKAAEAlkkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1501 RGQHDTlADQVEGLRRENKSLSDETRDLTESLSEGGrathaLSKNLRRLEMEKEELQRGLDEAEAALESEESKA-----L 1575
Cdd:PTZ00121 1750 KKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEE-----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlvinD 1823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1576 RCQIEVSQIRAEIEKRIAEKEE--EFENHrKVHQQTIDSIQATLDSETKAKSELFR--VKKKLEADINEleiALDHANKA 1651
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQLEEadAFEKH-KFNKNNENGEDGNKEADFNKEKDLKEddEEEIEEADEIE---KIDKDDIE 1899
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 25150292 1652 NEDAQKNIRRYLDQIRELQQTVDEEQKRR-EEFREHLLAAERK 1693
Cdd:PTZ00121 1900 REIPNNNMAGKNNDIIDDKLDKDEYIKRDaEETREEIIKISKK 1942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1302-1900 |
8.12e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1302 DLARQVEELEAKIQAANRLKLQfsNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKAS 1381
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELE--AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1382 VELDQwrtkfetegLIGADEFDEVKKRQNQKT-SEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEK 1460
Cdd:COG1196 295 AELAR---------LEQDIARLEERRRELEERlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1461 KQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATH 1540
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1541 ALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLdse 1620
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL--- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1621 TKAKSELFRVKKKLEADI-NELEIALDHANKANEDAQKNIRRYLDQirelqqtvdeEQKRREEFREHLLAAERKLAVAKQ 1699
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALeAALAAALQNIVVEDDEVAAAAIEYLKA----------AKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1700 EQEelivkleALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAA 1779
Cdd:COG1196 593 ARG-------AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1780 KLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVmkggakaiQKAEQRLKAFQSDLETESRRAGEASKTLARA 1859
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE--------RELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 25150292 1860 DRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEE 1900
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1143-1918 |
1.27e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1143 DARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESglkfgeqltvlKKKGSDAIQELSDQ 1222
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR-----------KAEEAKKKAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1223 IEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKgyEVRLLELRLKADEqSRQLQDFVSSKGRLNSENSD 1302
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE--DAKKAEAARKAEE-VRKAEELRKAEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1303 LARQVEELEAKIQAANRLKLQFSNELDHAKRQaEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSkasv 1382
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKD-AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD---- 1281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1383 ELDQWRTKFETEGLIGADE---FDEVKKR--QNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSS 1457
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEkkkADEAKKKaeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1458 LEKKQKAFDKVIDEWKKKVDDLYLELDgAQRDARQLSGEAHKLRGQHDTLADQVEGLRR--ENKSLSDETRDLTESLSEG 1535
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1536 GRATHAlsknlRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQA 1615
Cdd:PTZ00121 1441 EEAKKA-----DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1616 TLDSETKAKSELFRVKKKLEADineleialdHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLlaAERKLA 1695
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKAD---------EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM--ALRKAE 1584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1696 VAKQEQEELIVKLEAL---------ERARRVVESSVKEHQ-----------EHNNELNSQNVALAAAKSQLDNEIALLNS 1755
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLyeeekkmkaEEAKKAEEAKIKAEElkkaeeekkkvEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1756 DIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRL 1835
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1836 KAFQSDL-ETESRRAGEASKTLARADRKVREFEFQVAED--KKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKY 1912
Cdd:PTZ00121 1745 KAEEAKKdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS 1824
|
....*.
gi 25150292 1913 RTVQLS 1918
Cdd:PTZ00121 1825 KEMEDS 1830
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
915-1890 |
2.24e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 915 REVEERMTAMNEQKVALEGKLADaskkLEVEEARAVEINKQKKLVEAEcaDLKKNCQDVDLSLRKVEAEKNAKEHQIRAL 994
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIID----EDIDGNHEGKAEAKAHVGQDE--GLKPSYKDFDFDAKEDNRADEATEEAFGKA 1100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 995 QDEMRQQDENIsklnkERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGE 1074
Cdd:PTZ00121 1101 EEAKKTETGKA-----EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1075 LKI-AQETLEELNKSKS--DAENALRRKETElhtlgmKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARqRADRS 1151
Cdd:PTZ00121 1176 KKAeAARKAEEVRKAEElrKAEDARKAEAAR------KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEE 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1152 RADQQAEYDELTEQLEDQARATAAQIELGKKKDaELTKLRRDLEESGLKFGEQ---LTVLKKKGSDA--IQELSDQIEQl 1226
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADEAKKAEEkkkADEAKKKAEEAkkADEAKKKAEE- 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1227 QKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQ-ERIAKGYEVRLLELRLKADEQSRQLQDfVSSKGRLNSENSDLAR 1305
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1306 QVEELEAKIQAANRlklqfsneLDHAKRQAEEESRERQNLSNLSKnlARELEQLKESIEDevAGKNEASRQLSKASVELD 1385
Cdd:PTZ00121 1406 KADELKKAAAAKKK--------ADEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEE--AKKAEEAKKKAEEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1386 QWRTKFETegligADEFDEVKKRQNQKTSEIQDALDACNAKIVALEnarsrltaeadANRLEAEHHAQAVSSLEKKQKAF 1465
Cdd:PTZ00121 1474 EAKKKAEE-----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-----------AKKAEEAKKADEAKKAEEAKKAD 1537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1466 DKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESlSEGGRATHALSKN 1545
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAE 1616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1546 LRRLEMEK----EELQRGLDEAEAALESEESKA--LRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDS 1619
Cdd:PTZ00121 1617 EAKIKAEElkkaEEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1620 ETKAKSELFRVKKKLEADIneleialdhanKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHllaAERKLAVAKQ 1699
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEK-----------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHL 1762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1700 EQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRgrraasDAA 1779
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK------EVA 1836
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1780 KLAEDLRHEQEQSQQlERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARA 1859
Cdd:PTZ00121 1837 DSKNMQLEEADAFEK-HKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDII 1915
|
970 980 990
....*....|....*....|....*....|.
gi 25150292 1860 DRKVREFEFQvaedKKNYDKLQELVEKLTAK 1890
Cdd:PTZ00121 1916 DDKLDKDEYI----KRDAEETREEIIKISKK 1942
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
861-1347 |
3.73e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 84.84 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEA--------SKGSTR---EVEERMTAMNEQKV 929
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklEKTKNRlqqELDDLLVDLDHQRQ 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 930 --------------------ALEGKLADASKKLEVE----EARAV--------------EINKQKKLVEAECADLKKNCQ 971
Cdd:pfam01576 595 lvsnlekkqkkfdqmlaeekAISARYAEERDRAEAEarekETRALslaraleealeakeELERTNKQLRAEMEDLVSSKD 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 972 DVDLSLRKVEAEKNAKEHQIralqDEMRQQDENIsklnkERKNQEEQNKKL-------------TEDLQAAEEQNlaaNK 1038
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQV----EEMKTQLEEL-----EDELQATEDAKLrlevnmqalkaqfERDLQARDEQG---EE 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1039 LKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVA 1118
Cdd:pfam01576 743 KRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRD 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1119 KLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESG 1198
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQ 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1199 LKF-------------GEQLTVLKKKGSDAIQELSDQIEQLQKQ----KGRIEKEKGHMQREFDESSAAL---------- 1251
Cdd:pfam01576 903 SNTellndrlrkstlqVEQLTTELAAERSTSQKSESARQQLERQnkelKAKLQEMEGTVKSKFKSSIAALeakiaqleeq 982
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1252 -DQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDH 1330
Cdd:pfam01576 983 lEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
570
....*....|....*..
gi 25150292 1331 AKRQAEEESRERQNLSN 1347
Cdd:pfam01576 1063 ATESNESMNREVSTLKS 1079
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
881-1415 |
8.60e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 881 QEEEKKRQLQEGAERlNKETADLLAQLEASKGSTREV----EERMTAMNEQKVALEGKLADASKKlEVEEARAVEiNKQK 956
Cdd:PTZ00121 1388 EEKKKADEAKKKAEE-DKKKADELKKAAAAKKKADEAkkkaEEKKKADEAKKKAEEAKKADEAKK-KAEEAKKAE-EAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 957 KLVEAECAD-LKKNCQDvdlSLRKVEAEKNAKEHQIRAlqDEMRQQDENISKLNKERKNQEEQNK---KLTEDLQAAEEQ 1032
Cdd:PTZ00121 1465 KAEEAKKADeAKKKAEE---AKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAEEAKKAdeaKKAEEAKKADEA 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1033 NLAANKLKA---KLMQSLEDSEQTMEREKRNRADMDKNK--RKAEGELKIAQETLEELNK-----SKSDAENALRRKETE 1102
Cdd:PTZ00121 1540 KKAEEKKKAdelKKAEELKKAEEKKKAEEAKKAEEDKNMalRKAEEAKKAEEARIEEVMKlyeeeKKMKAEEAKKAEEAK 1619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1103 LHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKK 1182
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1183 KDAELTKLRRDLEESGLKfGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQE 1262
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKK-AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1263 RIAK-GYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELE----AKIQAANRLKLQFSNELDHAKRQAEE 1337
Cdd:PTZ00121 1779 AVIEeELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEdsaiKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1338 ESRERQNL-SNLSK---NLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEgligadEFDEVKKRQNQKT 1413
Cdd:PTZ00121 1859 ENGEDGNKeADFNKekdLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKL------DKDEYIKRDAEET 1932
|
..
gi 25150292 1414 SE 1415
Cdd:PTZ00121 1933 RE 1934
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1305-1930 |
2.79e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1305 RQVEELEAKIQAANRLKLQFSNELD-------HAKRQAEEESRERQNLSNLSKnlarELEQLKESIEDEVA----GKNEA 1373
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDidgnhegKAEAKAHVGQDEGLKPSYKDF----DFDAKEDNRADEATeeafGKAEE 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1374 SRQLSKASVEldqwRTKFETEGLIGADEFDEVKK-RQNQKTSEIQDALDACNAKIVAL----ENARSRLTAE--ADANRL 1446
Cdd:PTZ00121 1103 AKKTETGKAE----EARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAEDAKRVEIarkaEDARKAEEARkaEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1447 EAEHHAQAVSSLEKKQKAFD-KVIDEWKKKVDDLYLELDGAQRDARQlsgeAHKLRGQHDTLADQVEGLRRENKSLSDET 1525
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKK----AEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1526 RDLTESLSEGGRATHALSK---NLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENH 1602
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKaeeARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1603 RKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKnirryLDQIRELQQTVDEEQKRREE 1682
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-----KKKADEAKKKAEEDKKKADE 1409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1683 FREHLlAAERKLAVAKQEQEELIVKLEALERA--RRVVESSVKEHQEHNNELNSQNVALAAAKSqldneiallnsDIAEA 1760
Cdd:PTZ00121 1410 LKKAA-AAKKKADEAKKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKA-----------DEAKK 1477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1761 HTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQS 1840
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1841 DLETESRRAGEASKTLARADRKVREFE-FQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEE---AEEQANSHLSKYRTVQ 1916
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQ 1637
|
650
....*....|....
gi 25150292 1917 LSLETAEERADSAE 1930
Cdd:PTZ00121 1638 LKKKEAEEKKKAEE 1651
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1258-1946 |
3.36e-15 |
|
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: 81.76 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1258 RADQERIAKgyEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQV--------EELEAKIQAANRlKLQFSNELD 1329
Cdd:pfam01576 2 RQEEEMQAK--EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaEAEEMRARLAAR-KQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1330 HAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEvagknEASRQ-LSKASVELDQWRTKFETEGLIGADEFDEVKKR 1408
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE-----EAARQkLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1409 QNQKTSEIqdaldacnakivalenarsrltAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQR 1488
Cdd:pfam01576 154 RKLLEERI----------------------SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1489 darQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALE 1568
Cdd:pfam01576 212 ---KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1569 SEESK---------ALRCQIEVS--------QIRAEIEKRIAE----KEEEFENH-------RKVHQQTIDSIQATLDSE 1620
Cdd:pfam01576 289 KAEKQrrdlgeeleALKTELEDTldttaaqqELRSKREQEVTElkkaLEEETRSHeaqlqemRQKHTQALEELTEQLEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1621 TKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQE 1700
Cdd:pfam01576 369 KRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1701 QEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEahtELSASEDRGRRAASDAAK 1780
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQ 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1781 LAEDLRHEQEQSQQLE-------RFKKQLESAVKDLQERADAAEAavmkggakaIQKAEQRLkafQSDLETESRRAGEAS 1853
Cdd:pfam01576 526 LSDMKKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAAAYDK---------LEKTKNRL---QQELDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1854 KTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAklklqkkqleEAEEQanshlskyRTVQLSLETAEERADSAEQCL 1933
Cdd:pfam01576 594 QLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEA----------EAREK--------ETRALSLARALEEALEAKEEL 655
|
730
....*....|...
gi 25150292 1934 VRIRSRTRANAEQ 1946
Cdd:pfam01576 656 ERTNKQLRAEMED 668
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1660-1947 |
4.87e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1660 RRYldqiRELQQtvDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVAL 1739
Cdd:COG1196 213 ERY----RELKE--ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1740 AAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAA 1819
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1820 VMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLE 1899
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25150292 1900 EAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK 1947
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1480 |
1.09e-14 |
|
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: 80.10 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASK 940
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 941 KLEveEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQ----------QDENISKLNK 1010
Cdd:TIGR02168 429 KLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerLQENLEGFSE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1011 ERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQ--TMEREKRNRADMDKNKRKAEGELKIAQETLEELNKS 1088
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1089 KSDAENALRRKETELhTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQR--------------------- 1147
Cdd:TIGR02168 587 QGNDREILKNIEGFL-GVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggs 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1148 --ADRSRADQQAEYDELTEQLED-QARATAAQIELGKKKDA------ELTKLRRDLEESGLKFGEQLTVLKKKGSdAIQE 1218
Cdd:TIGR02168 666 akTNSSILERRREIEELEEKIEElEEKIAELEKALAELRKEleeleeELEQLRKELEELSRQISALRKDLARLEA-EVEQ 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1219 LSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQL-------QDFVS 1291
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRE 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1292 SKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKN 1371
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1372 EASRQLSKASVELDQWRTKFETEGL------------------IGADEFDEVKKRQNQKTSEIQDAldacNAKIVALENA 1433
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELrleglevridnlqerlseEYSLTLEEAEALENKIEDDEEEA----RRRLKRLENK 980
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1434 RSR-----LTAEADANRLE------AEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLY 1480
Cdd:TIGR02168 981 IKElgpvnLAAIEEYEELKerydflTAQKEDLTEAKETLEEAIEEIDREARERFKDTF 1038
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1632-1942 |
4.52e-14 |
|
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: 78.17 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1632 KKLEADINELEIALDHANKANEDAQKnIRRYLDQIRELQQTV-----DEEQKRREEFREHLLAAERKLAVAKQEQEELIV 1706
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAER-YKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1707 KLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLr 1786
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1787 heQEQSQQLERFKKQLESAVKDLQERADAAEAAvmkggAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREF 1866
Cdd:TIGR02168 347 --EELKEELESLEAELEELEAELEELESRLEEL-----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1867 EFQVAEDKKNYDKLQelVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRA 1942
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
866-1415 |
3.24e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 866 EKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLL--AQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLE 943
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 944 VEEARAVEINKQKKLVEAECADLKKNCQDV---DLSLRKVEAEKNAKEHQIRAlqDEMRQQDENISKLNKERKNQE---- 1016
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEakkk 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1017 -EQNKKLTEDLQAAEEQNLAANKLK--AKLMQSLEDSEQTMEREKRNRADMDKNKRKAEgELKIAQET--LEELNKSKSD 1091
Cdd:PTZ00121 1479 aEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-EAKKAEEKkkADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1092 AENALRRKETELHTlgmKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQAR 1171
Cdd:PTZ00121 1558 KKAEEKKKAEEAKK---AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1172 ataaqIELGKKKDAELTK----LRRDLEESGLKFGEqltvLKKKGsdaiQELSDQIEQLQKQKGRIEKEKGHMQREfdes 1247
Cdd:PTZ00121 1635 -----VEQLKKKEAEEKKkaeeLKKAEEENKIKAAE----EAKKA----EEDKKKAEEAKKAEEDEKKAAEALKKE---- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1248 saaldQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNE 1327
Cdd:PTZ00121 1698 -----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1328 LDHAKRQAEEESRERQNlSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKK 1407
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEED-EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
|
....*...
gi 25150292 1408 RQNQKTSE 1415
Cdd:PTZ00121 1852 HKFNKNNE 1859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1295-1946 |
7.59e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1295 RLNSENSDLAR---QVEELEAKIqaaNRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKN 1371
Cdd:TIGR02168 180 KLERTRENLDRledILNELERQL---KSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1372 EASRQLSKASVELDQWRtkfetegligaDEFDEVKKRQNqktsEIQDALDACNAKIVALENarsrltaeadanrlEAEHH 1451
Cdd:TIGR02168 257 ELTAELQELEEKLEELR-----------LEVSELEEEIE----ELQKELYALANEISRLEQ--------------QKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1452 AQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTES 1531
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1532 LSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQI-EVSQIRAEIEKRIAEKEEEFENHRKVHQQTI 1610
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1611 DSIQATLDSETKAKSELFRVKKKLEA--DINELEIALDHANKANEDAQKNIRRYLDQIRELQqTVDEEQKRREE--FREH 1686
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSleRLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVDEGYEAAIEaaLGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1687 LLAAE-RKLAVAKQEQEELivKLEALERARRVVESSVKEHQ---EHNNELNSQNVALAAAKS------QLDNEIALLNSD 1756
Cdd:TIGR02168 547 LQAVVvENLNAAKKAIAFL--KQNELGRVTFLPLDSIKGTEiqgNDREILKNIEGFLGVAKDlvkfdpKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1757 IAEAHTELSASEDRGR-RAASDAAKLAEDL---------RHEQEQSQQLERFK--KQLESAVKDLQERADAAEAAVmkgg 1824
Cdd:TIGR02168 625 VLVVDDLDNALELAKKlRPGYRIVTLDGDLvrpggvitgGSAKTNSSILERRReiEELEEKIEELEEKIAELEKAL---- 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1825 akaiqkaeQRLKAFQSDLETEsrrageasktLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQ 1904
Cdd:TIGR02168 701 --------AELRKELEELEEE----------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 25150292 1905 ANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQ 1946
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1079-1816 |
1.01e-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: 73.52 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1079 QETLEELNKSKSDAENalrrKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDarqradrsradqqaE 1158
Cdd:TIGR04523 36 KQLEKKLKTIKNELKN----KEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKD--------------K 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1159 YDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKgSDAIQELSDQIEQLQKQKGRIEKEKG 1238
Cdd:TIGR04523 98 INKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK-EKELEKLNNKYNDLKKQKEELENELN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1239 HMQREFDESSAALDQeaklrADQERIAKGYEVRLLELRL-KADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAA 1317
Cdd:TIGR04523 177 LLEKEKLNIQKNIDK-----IKNKLLKLELLLSNLKKKIqKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1318 NRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEvagKNEASRQLSKasveldqwrtkfetegli 1397
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL---NNQKEQDWNK------------------ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1398 gaDEFDEVKKRQNQKT------SEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDE 1471
Cdd:TIGR04523 311 --ELKSELKNQEKKLEeiqnqiSQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1472 WKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTE-------SLSEGGRATHALSK 1544
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1545 NLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEI---EKRIAE---KEEEFENHRKVHQQTIDSIQATLD 1618
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdlTKKISSlkeKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1619 S--ETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAV 1696
Cdd:TIGR04523 549 KddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1697 AKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALaaaKSQLDNEIALLNSDIAEAHTELSASEDRGRRAaS 1776
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES---KTKIDDIIELMKDWLKELSLHYKKYITRMIRI-K 704
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 25150292 1777 DAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAA 1816
Cdd:TIGR04523 705 DLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1002-1524 |
1.23e-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: 73.13 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1002 DENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQET 1081
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1082 LEELNKSKSDAENALRRKETELHTLGMKLEDE-----------------QAAVAKLQKGIQQDEARVKDLHDQLADEKDA 1144
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNkslesqiselkkqnnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1145 RQRADRSRADQQAEYDE---LTEQLEDQARATAAQIE-LGKKKDAELTKlrrDLEESGLKFGEQLTVLKKKGSD---AIQ 1217
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdLNNQKEQDWNK---ELKSELKNQEKKLEEIQNQISQnnkIIS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1218 ELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRA---------------------DQERIAKGYEVRLLELR 1276
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqeiknlesqindleskiqNQEKLNQQKDEQIKKLQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1277 LKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEesrERQNLSNLSKNLAREL 1356
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK---IKQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1357 EQLKESiedevagkNEASRQLSKASVELDQWRTKFETEgligADEFDEVKKRQNQKTSEIQDALDACNAkivalENARSR 1436
Cdd:TIGR04523 496 KELKKL--------NEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDF-----ELKKEN 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1437 LTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRR 1516
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
....*...
gi 25150292 1517 ENKSLSDE 1524
Cdd:TIGR04523 639 KKNKLKQE 646
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1214-1822 |
1.41e-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: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1214 DAIQELSDQIEQLQKQKGRIEKEK------GHMQREFDESSAALDQEAKLRADQERiakgyeVRLLELRLKADEQSRQLQ 1287
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAReqiellEPIRELAERYAAARERLAELEYLRAA------LRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1288 DFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFS-NELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDE 1366
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1367 VAGKNEASRQLSKASVELDQWRTKFEtegligaDEFDEVKKRQNQKtseiQDALDACNAKIVALENARSRLTAEADANRL 1446
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALE-------EALAEAEAALRDL----RRELRELEAEIASLERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1447 EAEHHAQA-------------VSSLEKK-QKAFDKVI----------DEWKKKVDDLYleldgaqrdarqlsgEAHKLRG 1502
Cdd:COG4913 448 ALAEALGLdeaelpfvgelieVRPEEERwRGAIERVLggfaltllvpPEHYAAALRWV---------------NRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1503 QHDTlaDQVEGLRRENKSLSDETRDLTESLS-EGGRATHALsknlrrlemeKEELQRGLDeaeaaleseeskaLRCqiev 1581
Cdd:COG4913 513 RLVY--ERVRTGLPDPERPRLDPDSLAGKLDfKPHPFRAWL----------EAELGRRFD-------------YVC---- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1582 sqiraeiekriAEKEEEFENHRKvhqqtidSIQAT-----------LDSETKAKSEL---FRVKKKLEADINELEIALDH 1647
Cdd:COG4913 564 -----------VDSPEELRRHPR-------AITRAgqvkgngtrheKDDRRRIRSRYvlgFDNRAKLAALEAELAELEEE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1648 ANKANEDAQ--KNIRRYLDQIRELQQTVDEEQKRREEfrehLLAAERKLAVAKQEQEELI---VKLEALERARRVVESSV 1722
Cdd:COG4913 626 LAEAEERLEalEAELDALQERREALQRLAEYSWDEID----VASAEREIAELEAELERLDassDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1723 KEHQEHNNELNSQnvalaaaKSQLDNEIALLNSDIAEAHTELsasEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQL 1802
Cdd:COG4913 702 EELEEELDELKGE-------IGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
650 660
....*....|....*....|
gi 25150292 1803 ESAVKDLQERADAAEAAVMK 1822
Cdd:COG4913 772 EERIDALRARLNRAEEELER 791
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1593-1823 |
1.74e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 71.33 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1593 AEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQt 1672
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1673 vdEEQKRREEFREHLLAAER-------KLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQ 1745
Cdd:COG4942 98 --ELEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1746 LDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKG 1823
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
911-1727 |
4.03e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 71.93 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 911 KGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECAD-------LKKNCQDVDLSLRKVEAE 983
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldyLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 984 KNAKEHQIRALQDEMRQQDENISKLNKErkNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRAD 1063
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEE--EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1064 MDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELhtlgmKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKD 1143
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK-----LEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1144 ARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDA--IQELSD 1221
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLkeTQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1222 QIEQLQKQKGRIEKEKGHMQREFDESSAAL------------DQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDF 1289
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLlalikdgvggriISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1290 VSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAG 1369
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1370 KNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEiqdaldacNAKIVALENARSRLTAEADANRLEAE 1449
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE--------LAKEEILRRQLEIKKKEQREKEELKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1450 HHAQAVSSLEKKQKAFDKVI----DEWKKKVDDLYLELDGAQRDARQLsgEAHKLRGQHDTLADQVEGLRRENKSLSDET 1525
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKIneelKLLKQKIDEEEEEEEKSRLKKEEK--EEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1526 RDLTESLSEGGRAthALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKV 1605
Cdd:pfam02463 793 EEKLKAQEEELRA--LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1606 HQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVD---EEQKRREE 1682
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEK 950
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 25150292 1683 FREHLLAAERKLAVAKQEQEEL-IVKLEALERARRVVESSVKEHQE 1727
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELgKVNLMAIEEFEEKEERYNKDELE 996
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
860-1410 |
5.51e-12 |
|
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: 71.25 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADAS 939
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 940 KKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERK------ 1013
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtv 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1014 ----NQEEQNKKLTE--------------DLQAAEEQNLAA------------NKLKAK--------------------- 1042
Cdd:TIGR02169 528 aqlgSVGERYATAIEvaagnrlnnvvvedDAVAKEAIELLKrrkagratflplNKMRDErrdlsilsedgvigfavdlve 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1043 -----------------LMQSLEDSEQTMER-----------EK--------RNRADMDKNKRKAEGELKIAQETLEELN 1086
Cdd:TIGR02169 608 fdpkyepafkyvfgdtlVVEDIEAARRLMGKyrmvtlegelfEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1087 KSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQL 1166
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1167 EDQaRATAAQIElgkkkdAELTKLRRDLEESGLK-FGEQLTVLKKKGSD---AIQELSDQIEQLQKQKGRIEKEKGHMQR 1242
Cdd:TIGR02169 768 EEL-EEDLHKLE------EALNDLEARLSHSRIPeIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1243 EFDEssaALDQEAKLRADQERIakgyEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQaanRLKL 1322
Cdd:TIGR02169 841 QRID---LKEQIKSIEKEIENL----NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE---ELEA 910
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1323 QFSNELDHAKRQAEEESRERQNLSNLSKNLARELEqlkESIEDEVAGKNEASRQlskasvELDQWRTKFETEGLIGADEF 1402
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE---IPEEELSLEDVQAELQ------RVEEEIRALEPVNMLAIQEY 981
|
....*...
gi 25150292 1403 DEVKKRQN 1410
Cdd:TIGR02169 982 EEVLKRLD 989
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1479 |
5.61e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 852 VKPLVNSGKIEAQYEKLQETVAT-------LKDTVVQEEEKKRQLQEGAERLN------KETADLLAQLEASKGSTREVE 918
Cdd:PRK03918 151 VRQILGLDDYENAYKNLGEVIKEikrrierLEKFIKRTENIEELIKEKEKELEevlreiNEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 919 ERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDlslrkvEAEKNAKEHqiRALQDEM 998
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK------ELKEKAEEY--IKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 999 RQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIA 1078
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1079 QETLEELNKSKSDAENALRRKETELHTLGMKledeqaavaklqkgIQQDEARVKDLHDQLADEKDARQRADRSRAdqqae 1158
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITAR--------------IGELKKEIKELKKAIEELKKAKGKCPVCGR----- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1159 ydELTEQ----LEDQARATAAQIELGKKK-DAELTKLRRDLEESGLKFGEQLTVLKKKgsdaiqELSDQIEQLQKQKGRI 1233
Cdd:PRK03918 444 --ELTEEhrkeLLEEYTAELKRIEKELKEiEEKERKLRKELRELEKVLKKESELIKLK------ELAEQLKELEEKLKKY 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1234 EKEKghMQREFDESSAALDQEAKLRADQERIAKGYEvRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLA-RQVEELEA 1312
Cdd:PRK03918 516 NLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1313 KIQAANRLKLQFsNELDHAKRQAEEESrerqnlsnlsknlaRELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFE 1392
Cdd:PRK03918 593 RLKELEPFYNEY-LELKDAEKELEREE--------------KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1393 TEgligadEFDEVKKRQNQKTSEiqdaLDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKViDEW 1472
Cdd:PRK03918 658 EE------EYEELREEYLELSRE----LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV-EEL 726
|
....*..
gi 25150292 1473 KKKVDDL 1479
Cdd:PRK03918 727 REKVKKY 733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
861-1361 |
6.26e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKLQETvaTLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASK 940
Cdd:PRK02224 192 LKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 941 KLEVEEARAVEINKQKKLVE---AECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNqee 1017
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEeleEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES--- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1018 qnkkLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAE---N 1094
Cdd:PRK02224 347 ----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELReerD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1095 ALRRKETELHTlgmKLEDEQAAVAKLQK---------------------GIQQDEARVKDLHDQLADEKdarqradrsra 1153
Cdd:PRK02224 423 ELREREAELEA---TLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLE----------- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1154 DQQAEYDELTEQLEDqARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRI 1233
Cdd:PRK02224 489 EEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1234 EK---EKGHMQREFDESSAALDQEAKLRADQERIAKgYEVRLLELRLKAD---EQSRQLQDFVSSKgrlNSENSDLARQV 1307
Cdd:PRK02224 568 EEareEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREalaELNDERRERLAEK---RERKRELEAEF 643
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 25150292 1308 EelEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKE 1361
Cdd:PRK02224 644 D--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
28-72 |
6.45e-12 |
|
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: 61.68 E-value: 6.45e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 25150292 28 DSKKNVWIPDSEDGYIEGVITKTAGDNVTVSIGQGAEKTVKKDVV 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1445-1947 |
1.05e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1445 RLEAEHHAQAVSSLEKKQKAFDKVIDEwKKKVDDLYLELDGAQRDARQL-SGEAHKLRGQHDTLADQVEGLRRENKSLSD 1523
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKE-DNRADEATEEAFGKAEEAKKTeTGKAEEARKAEEAKKKAEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1524 ETRDLTESL-SEGGRATHALSK--NLRRLEM-EKEELQRGLDEAEAALESEESKALRCQIEVSQI----RAEIEKRI--- 1592
Cdd:PTZ00121 1138 DARKAEEARkAEDAKRVEIARKaeDARKAEEaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAeaarKAEEERKAeea 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1593 --AEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIAL--DHANKANEDAQKNIRRYLDQIR- 1667
Cdd:PTZ00121 1218 rkAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaEEARKADELKKAEEKKKADEAKk 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1668 -ELQQTVDEEQKRREEfrehllaaERKLAVAKQEQEELIVKLEAL----ERARRVVESSVKEHQEHNNELNSQNVALAAA 1742
Cdd:PTZ00121 1298 aEEKKKADEAKKKAEE--------AKKADEAKKKAEEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1743 KsqLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAavmK 1822
Cdd:PTZ00121 1370 E--KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA---K 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1823 GGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAE 1902
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 25150292 1903 EQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK 1947
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
989-1674 |
1.41e-11 |
|
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: 70.15 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 989 HQIRALQDEMRQQDE---------NISKLNKERKNQEEQ-NKKLTEDLQAAEEQNlaanklKAKLMQSLEDSEQTMEREK 1058
Cdd:pfam15921 85 HQVKDLQRRLNESNElhekqkfylRQSVIDLQTKLQEMQmERDAMADIRRRESQS------QEDLRNQLQNTVHELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1059 RNRADMDKNKRKAEGELK---IAQE-TLEELNKSKSDAENALRRKETELHTLG-MKLEDEQAAVAKLQKGIQQD----EA 1129
Cdd:pfam15921 159 CLKEDMLEDSNTQIEQLRkmmLSHEgVLQEIRSILVDFEEASGKKIYEHDSMStMHFRSLGSAISKILRELDTEisylKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1130 RVKDLHDQLADEKDARQ------------RADRSRADQQAEYDELTEQL---EDQARATAAQIEL----GKKKDAELTKL 1190
Cdd:pfam15921 239 RIFPVEDQLEALKSESQnkielllqqhqdRIEQLISEHEVEITGLTEKAssaRSQANSIQSQLEIiqeqARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1191 RRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQ--KGRIEKEkghmqrEFDESSAALD-QEAKLRADQERIAKg 1267
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEltEARTERD------QFSQESGNLDdQLQKLLADLHKREK- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1268 yevrllELRLKaDEQSRQLQDFVSSKG----RLNSENSDLARQVEELEAKIQAAnRLKLQFSNELDHAKRQAEEESRERq 1343
Cdd:pfam15921 392 ------ELSLE-KEQNKRLWDRDTGNSitidHLRRELDDRNMEVQRLEALLKAM-KSECQGQMERQMAAIQGKNESLEK- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1344 nLSNLSKNLARELEQLKESIEDEVAGK-----------------NEASRQLSKASVELDQWRTK----------FETEG- 1395
Cdd:pfam15921 463 -VSSLTAQLESTKEMLRKVVEELTAKKmtlessertvsdltaslQEKERAIEATNAEITKLRSRvdlklqelqhLKNEGd 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1396 ---------------LIGADEFDEVKKRQNQKTSEI--QDALDACnakivALENARSRLTAEADANRLEAehhaQAVSSL 1458
Cdd:pfam15921 542 hlrnvqtecealklqMAEKDKVIEILRQQIENMTQLvgQHGRTAG-----AMQVEKAQLEKEINDRRLEL----QEFKIL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1459 EKKQkafDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDE----TRDLTESLSE 1534
Cdd:pfam15921 613 KDKK---DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDyevlKRNFRNKSEE 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1535 GGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEI---EKRI---------AEKEEEF--E 1600
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIdalQSKIqfleeamtnANKEKHFlkE 769
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25150292 1601 NHRKVHQQTidSIQATLDSETKAKSELFRVK-KKLEADINELEIALDHANKANEDAQKNIRRY-LDQIR-ELQQTVD 1674
Cdd:pfam15921 770 EKNKLSQEL--STVATEKNKMAGELEVLRSQeRRLKEKVANMEVALDKASLQFAECQDIIQRQeQESVRlKLQHTLD 844
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1501-1947 |
1.76e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1501 RGQHDTLADQVEGlrRENKSLSDETRDLTESLSEggrathaLSKNLRRLEMEKEELQRGLDEAEAALESEESKalrcQIE 1580
Cdd:PRK02224 186 RGSLDQLKAQIEE--KEEKDLHERLNGLESELAE-------LDEEIERYEEQREQARETRDEADEVLEEHEER----REE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1581 VSQIRAEIEK---RIAEKEEEFENHR-KVHQQT---------IDSIQATLDSETKAKSELFRVKKKLEADINELEIALDH 1647
Cdd:PRK02224 253 LETLEAEIEDlreTIAETEREREELAeEVRDLRerleeleeeRDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1648 ANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQE 1727
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1728 HNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSA-------------------SEDRGRRAASDAAKlaEDLRHE 1788
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAEL--EDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1789 QEQ-SQQLERFK--KQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQ--RLKAFQSDLETESRRAGEASKTLARADRKV 1863
Cdd:PRK02224 491 VEEvEERLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRERaeELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1864 RE----FEFQVAEDKKNYDKLQELVEKLTA---------KLKLQKKQLEEAEEQANSHLS--KYRTVQLS-------LET 1921
Cdd:PRK02224 571 REevaeLNSKLAELKERIESLERIRTLLAAiadaedeieRLREKREALAELNDERRERLAekRERKRELEaefdearIEE 650
|
490 500
....*....|....*....|....*.
gi 25150292 1922 AEERADSAEQCLVRIRSRTRANAEQK 1947
Cdd:PRK02224 651 AREDKERAEEYLEQVEEKLDELREER 676
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
839-1450 |
5.10e-11 |
|
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: 68.22 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 839 ELRTWVWFkLYGKVKPlvnsgkIEAQYEKLQ-ETVATLKDTVVQEEEKKRQLQEGAErlnKETADLLAQLEASKGSTREV 917
Cdd:pfam15921 228 ELDTEISY-LKGRIFP------VEDQLEALKsESQNKIELLLQQHQDRIEQLISEHE---VEITGLTEKASSARSQANSI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 918 EERMTAMNEQKVALEGKLADASKKLE--VEEARAvEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQ 995
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLEstVSQLRS-ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 996 DEMRQQDENISKLNKERKNQEEQNKKLTED-----------LQAAEEQNLAANKLKAKL--------------MQSLEDS 1050
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitidhlRRELDDRNMEVQRLEALLkamksecqgqmerqMAAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1051 EQTMEREKRNRADMDKNK---RKAEGELKIAQETLEELNKSKSDAENALRRKETelhtlgmKLEDEQAAVAKLQKGIQQD 1127
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKER-------AIEATNAEITKLRSRVDLK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1128 EARVKDLHDQLADEKDARQRADRSRAdQQAEYDELTE----QLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGE 1203
Cdd:pfam15921 530 LQELQHLKNEGDHLRNVQTECEALKL-QMAEKDKVIEilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1204 qLTVLKKKGSDAIQELSDQIEQLQKQKGRI---EKEKGHMQREFDESSAALDQEAKL-RADQERIAKGYEVRLLELRLKA 1279
Cdd:pfam15921 609 -FKILKDKKDAKIRELEARVSDLELEKVKLvnaGSERLRAVKDIKQERDQLLNEVKTsRNELNSLSEDYEVLKRNFRNKS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1280 DEQSRQLQDFvssKGRLNSENSDLAR---QVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLAREL 1356
Cdd:pfam15921 688 EEMETTTNKL---KMQLKSAQSELEQtrnTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1357 EQLKESiedevagKNEASRQLSKASVELDQWRTKFETegligadeFDEVKKRQNQKTSEIQDALDACNAKIVALENARSR 1436
Cdd:pfam15921 765 HFLKEE-------KNKLSQELSTVATEKNKMAGELEV--------LRSQERRLKEKVANMEVALDKASLQFAECQDIIQR 829
|
650
....*....|....
gi 25150292 1437 ltAEADANRLEAEH 1450
Cdd:pfam15921 830 --QEQESVRLKLQH 841
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1203-1887 |
6.16e-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: 68.07 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1203 EQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRAD---QERIAKGYEVRLLELRLKA 1279
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREalqQTQQSHAYLTQKREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1280 DEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRL-------KLQFSNELDHAKRQAEEESRE--RQNLSNLSK 1350
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAahikavtQIEQQAQRIHTELQSKMRSRAklLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1351 NLArELEQLKESIEDEVAGKNEASRQLSKASVELDQW-RTKFETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVA 1429
Cdd:TIGR00618 336 QQS-SIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1430 LENARSRLtaEADANRLEAEHHAQAvSSLEKKQKAFDKVIDEWKKKvddlylelDGAQRDARQLSGEAHKLRGQHDTLAD 1509
Cdd:TIGR00618 415 RTSAFRDL--QGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLE--------KIHLQESAQSLKEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1510 QVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIE 1589
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1590 K-------------RIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQ 1656
Cdd:TIGR00618 564 QmqeiqqsfsiltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1657 KNIRRYLDQIRELQQTVDEEQKRREEFREHLLAA-ERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQ 1735
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1736 NVALAAAKSQLDNEIALLNSDI----AEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQE 1811
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLkelmHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKT 803
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1812 -RADAAEAAVMKGGAKAIQ--KAEQRLKAFQSDLETESRRAGEasktLARADRKVREFEFQVAEDKKNYDKLQELVEKL 1887
Cdd:TIGR00618 804 lEAEIGQEIPSDEDILNLQceTLVQEEEQFLSRLEEKSATLGE----ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1542-1818 |
1.22e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1542 LSKNLRRLEMEKE------ELQRGLDEAEAALESEESKALRCQIE-VSQIRAEIEKRIAEKEEEFENHRK-VHQQTIDSI 1613
Cdd:TIGR02169 196 KRQQLERLRREREkaeryqALLKEKREYEGYELLKEKEALERQKEaIERQLASLEEELEKLTEEISELEKrLEEIEQLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1614 QATLDSETKAKSELFRVKKKL---EADINELEIALDHANKANEDAQKN-------IRRYLDQIRELQQTVDEEQKRREEF 1683
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIgelEAEIASLERSIAEKERELEDAEERlakleaeIDKLLAEIEELEREIEEERKRRDKL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1684 REHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTE 1763
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 1764 LSASEDRGRRAASDAAK-------LAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEA 1818
Cdd:TIGR02169 436 INELEEEKEDKALEIKKqewkleqLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1473-1904 |
2.48e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1473 KKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTE-------------SLSEGGRAT 1539
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiklseFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1540 HALSKNLRRLEMEKEELQRGLDEAEAALE-----SEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRK-VHQQTIDSI 1613
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEErleelKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKrLTGLTPEKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1614 QATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELqqTVDEEQKRREEFREHLLAAERK 1693
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL--TEEHRKELLEEYTAELKRIEKE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1694 LAVAKQEQEELIVKLEALERAR------RVVESSVKEHQEHNNELNSQNVALAAAKSQldnEIALLNSDIAEAHTELSAS 1767
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAE---EYEKLKEKLIKLKGEIKSL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1768 EDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLE----SAVKDLQERADAAEAAVMKggAKAIQKAEQRLKAFQSDLE 1843
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNE--YLELKDAEKELEREEKELK 622
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1844 TESRRAGEASKTLARADRKVREFEFQVAEDKKNYD-----KLQELVEKLTAKLKLQKKQLEEAEEQ 1904
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELAGLRAELEELEKR 688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1437 |
3.12e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLqegaerlnketaDLLAQLEASKGSTREVEERMTAMNEQKVALEgkLADAS 939
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQI------------ELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 940 KKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQ-IRALQDEMRQQDENISKLNKERKNQEEQ 1018
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1019 NKKLTEDLqAAEEQNLAANKLKAKlmQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKS-------- 1090
Cdd:COG4913 368 LAALGLPL-PASAEEFAALRAEAA--ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparlla 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1091 ---DAENALRRKETELHTLG----MKLEDE--QAAVAKLQKGI-------QQDEARVKDLHDQLADE--------KDARQ 1146
Cdd:COG4913 445 lrdALAEALGLDEAELPFVGelieVRPEEErwRGAIERVLGGFaltllvpPEHYAAALRWVNRLHLRgrlvyervRTGLP 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1147 RADRSRADQQAEYDELT--------------------------EQLEDQARA-TAA-QI----ELGKKKDaeltklRRDL 1194
Cdd:COG4913 525 DPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdspEELRRHPRAiTRAgQVkgngTRHEKDD------RRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1195 EES---GLKFGEQLTVLKKK---GSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALD------QEAKLRADQE 1262
Cdd:COG4913 599 RSRyvlGFDNRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaerEIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1263 RIAKGY------EVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNE-LDHAKRQA 1335
Cdd:COG4913 679 RLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAA 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1336 EEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELD----------QWRTKFETEGLIGA-DEFDE 1404
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslpeylALLDRLEEDGLPEYeERFKE 838
|
650 660 670
....*....|....*....|....*....|....
gi 25150292 1405 VKKRQN-QKTSEIQDALDAcnakivALENARSRL 1437
Cdd:COG4913 839 LLNENSiEFVADLLSKLRR------AIREIKERI 866
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1068-1812 |
9.60e-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: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1068 KRKAEGELKIAQETLEELNKSKSDAENALRRKETelhtlgmkLEDEQAAVAKLQKgiQQDEARVKDLHDQLADEKDARQR 1147
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEL--------LEPIRELAERYAA--ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1148 ADRSRADQQAEYDELTEQLEDQARATAAQIELgkkkDAELTKLRRDLEESGLkfgeqltvlkkkgsDAIQELSDQIEQLQ 1227
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDAL----REELDELEAQIRGNGG--------------DRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1228 KQKGRIEKEkghmQREFDESSAALDQEAKLRADQeriakgyevrLLELRLKADEQsrqlqdfvssKGRLNSENSDLARQV 1307
Cdd:COG4913 352 RELEERERR----RARLEALLAALGLPLPASAEE----------FAALRAEAAAL----------LEALEEELEALEEAL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1308 EELEAKIQAAnrlklqfsneldhaKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVagkneasrQLSKASV----E 1383
Cdd:COG4913 408 AEAEAALRDL--------------RRELRELEAEIASLERRKSNIPARLLALRDALAEAL--------GLDEAELpfvgE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1384 LDQWRTKFET-----EGLIGadefdevkkrqNQKTSEI--QDALDACNAKIvalenarsrltaeaDANRLEAEHHAQAVS 1456
Cdd:COG4913 466 LIEVRPEEERwrgaiERVLG-----------GFALTLLvpPEHYAAALRWV--------------NRLHLRGRLVYERVR 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1457 SLEKKQKAfdKVIDEwkkkvDDLYLELDGAQRDARqlsGEAHKLRGQHDTLA--DQVEGLRRENKSLS------------ 1522
Cdd:COG4913 521 TGLPDPER--PRLDP-----DSLAGKLDFKPHPFR---AWLEAELGRRFDYVcvDSPEELRRHPRAITragqvkgngtrh 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1523 --DETRDLTESLSEGGRATH---ALSKNLRRLEMEKEELQRgldeaeaaleseESKALRCQIEVSQIRAEIEKRIAEKEE 1597
Cdd:COG4913 591 ekDDRRRIRSRYVLGFDNRAklaALEAELAELEEELAEAEE------------RLEALEAELDALQERREALQRLAEYSW 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1598 EFENHRKVHQQtIDSIQATLDSETKAKSELFRVK---KKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVD 1674
Cdd:COG4913 659 DEIDVASAERE-IAELEAELERLDASSDDLAALEeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1675 EEQKRREEFrEHLLAAERKLAVAKQEQEElivklEALERARRVVESSVKEHQEHNNELNSqnvALAAAKSQLDNEIALLN 1754
Cdd:COG4913 738 AAEDLARLE-LRALLEERFAAALGDAVER-----ELRENLEERIDALRARLNRAEEELER---AMRAFNREWPAETADLD 808
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1755 SDIAEA------HTELSAS-----EDRgrraasdaaklAEDLRHEQEQsQQLERFKKQLESAVKDLQER 1812
Cdd:COG4913 809 ADLESLpeylalLDRLEEDglpeyEER-----------FKELLNENSI-EFVADLLSKLRRAIREIKER 865
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1204-1909 |
1.04e-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: 64.09 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1204 QLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKlRADQERIAKGYEVRLLELRLKADEQS 1283
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELS-AADAAVAKDRSELEALEDQHGAFLDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1284 RqLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKlqfsneldhAKRQAEEESRERQNLSNLSKNlARELEQLKESI 1363
Cdd:pfam12128 338 D-IETAAADQEQLPSWQSELENLEERLKALTGKHQDVT---------AKYNRRRSKIKEQNNRDIAGI-KDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1364 EDEVAGKNEASRQL-SKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEiQDALDACNAKIVALENARSRLTAeAD 1442
Cdd:pfam12128 407 DRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEA-AN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1443 ANRLEAEhhaqavSSLEKKQKAFDKVIDEWK---KKVDDLYLELDGAQRdarQLSGEAHKLrgqHDTLADQVEGLR---- 1515
Cdd:pfam12128 485 AEVERLQ------SELRQARKRRDQASEALRqasRRLEERQSALDELEL---QLFPQAGTL---LHFLRKEAPDWEqsig 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1516 ----RENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEK-----EELQRGLDEAEAALESEESKALRCQIEVSQIRA 1586
Cdd:pfam12128 553 kvisPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1587 EIEKriAEKEEEF-----ENHRKVHQQTIDSIQATLDSETKAkseLFRVKKKLEADINEleiaLDHANKANEdaqknirr 1661
Cdd:pfam12128 633 ELEK--ASREETFartalKNARLDLRRLFDEKQSEKDKKNKA---LAERKDSANERLNS----LEAQLKQLD-------- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1662 yldqiRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHnNELNSQNVAlaa 1741
Cdd:pfam12128 696 -----KKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK-RDLASLGVD--- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1742 aksqlDNEIALLNSDIAEAHTELSasedrgrRAASDAAKLAEDLRHEQEQ-SQQLERFKKQL---ESAVKDLQERAdaae 1817
Cdd:pfam12128 767 -----PDVIAKLKREIRTLERKIE-------RIAVRRQEVLRYFDWYQETwLQRRPRLATQLsniERAISELQQQL---- 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1818 aavmkggAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFqVAEDKKNYDKLQELVEKLTA--KLKLQK 1895
Cdd:pfam12128 831 -------ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT-LKEDANSEQAQGSIGERLAQleDLKLKR 902
|
730
....*....|....
gi 25150292 1896 KQLEEAEEQANSHL 1909
Cdd:pfam12128 903 DYLSESVKKYVEHF 916
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1015-1365 |
1.23e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1015 QEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAEN 1094
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1095 ALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEAR-----VKDLHDQLADEKDARQRADRSRADQQAEYDELT---EQL 1166
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1167 EDQARATAAQIELGKKKDAEltkLRRDLEESGLKFGEQLTVLKKKgSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDE 1246
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKS---IEKEIENLNGKKEELEEELEEL-EAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1247 SSAALDQEaklradqeriakgyEVRLLELRLKADEQSRQLQDFVSSKGRLNSENS------DLARQVEELEAKIQAanrl 1320
Cdd:TIGR02169 908 LEAQIEKK--------------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEeelsleDVQAELQRVEEEIRA---- 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 25150292 1321 kLQFSNELdhAKRQAEEESRERQNLSNLSKNLARELEQLKESIED 1365
Cdd:TIGR02169 970 -LEPVNML--AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1278 |
1.37e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 851 KVKPLVNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLnKETADLLAQLEASKGSTREVEERMTAMNEQKVA 930
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-KELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 931 LEGK-LADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDE-----MRQQDEN 1004
Cdd:PRK03918 381 LTGLtPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1005 ISKLNKERKNQEEQNKKLTEDLQAAE-----EQNLAANKLKAKLMQSLED--SEQTMEREKRNRADMDKNKRKA---EGE 1074
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEkvlkkESELIKLKELAEQLKELEEklKKYNLEELEKKAEEYEKLKEKLiklKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1075 LKIAQETLE---ELNKSKSDAENALRRKETELHTLGMKLEDEQAavaklqKGIQQDEARVKDL---HDQLADEKDARQRA 1148
Cdd:PRK03918 541 IKSLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELGF------ESVEELEERLKELepfYNEYLELKDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1149 DRSRADQQAEYDELTEQLEDQArataaqielgkKKDAELTKLRRDLEESGLKFGEQltvLKKKGSDAIQELSDQIEQLQK 1228
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELA-----------ETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRA 680
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 25150292 1229 QKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEvRLLELRLK 1278
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1163-1811 |
1.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1163 TEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDaIQELSDQIEQLQKQKGRIEKEKGHMQR 1242
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1243 EFDESsaaldqEAKLRADQERIAkgyevRLLELRLKADEQSR---QLQDFVSSKGRLNSENSDLARQVEELEAKIQaanr 1319
Cdd:PRK03918 267 RIEEL------KKEIEELEEKVK-----ELKELKEKAEEYIKlseFYEEYLDELREIEKRLSRLEEEINGIEERIK---- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1320 lklqfsneldhakrQAEEESRERQNLSNLSKNLARELEQLKESIEdevagKNEASRQLSKASVELDQWRTKFETEGLIga 1399
Cdd:PRK03918 332 --------------ELEEKEERLEELKKKLKELEKRLEELEERHE-----LYEEAKAKKEELERLKKRLTGLTPEKLE-- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1400 DEFDEVKKRQnqktSEIQDALDACNAKIVALENARSRLtaEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDL 1479
Cdd:PRK03918 391 KELEELEKAK----EEIEEEISKITARIGELKKEIKEL--KKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1480 YLELDGAQRDARQLSGEAHKLRGqhdTLADQVEGLRreNKSLSDETRDLTESLSEggrathalsKNLRRLEMEKEELQRG 1559
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEK---VLKKESELIK--LKELAEQLKELEEKLKK---------YNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1560 LDeaeaaleseeskalrcqiEVSQIRAEIE--KRIAEKEEEFENHRKVHQQTIDSIQATLDS-ETKAKSELFRVKKKLEA 1636
Cdd:PRK03918 531 KE------------------KLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1637 DINELEIALDHANKAnEDAQKNIRRyldqirelqqtvdeEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERarr 1716
Cdd:PRK03918 593 RLKELEPFYNEYLEL-KDAEKELER--------------EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1717 vvESSVKEHQEHNNELNSQNVALAAAKSQLDneiallnsdiaeahtelsasedRGRRAASDAAKLAEDLRHEQEQSQQLE 1796
Cdd:PRK03918 655 --KYSEEEYEELREEYLELSRELAGLRAELE----------------------ELEKRREEIKKTLEKLKEELEEREKAK 710
|
650
....*....|....*
gi 25150292 1797 RFKKQLESAVKDLQE 1811
Cdd:PRK03918 711 KELEKLEKALERVEE 725
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
846-1268 |
1.99e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 846 FKLYGKvKPLVNSGKIEAQYEKLQETVATLKD--TVVQEEEKKRQLQEGAERLNKETADLLAQLEASKgSTREVEERMTA 923
Cdd:COG4717 59 FKPQGR-KPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 924 MNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDvdLSLRKVEAEKNAKEhQIRALQDEMRQQDE 1003
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAE-ELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1004 NISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLE 1083
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1084 ELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELT 1163
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1164 EQL-------EDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKG--------SDAIQELSDQIEQLQK 1228
Cdd:COG4717 374 ALLaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleeeleelEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 25150292 1229 QKGRIEKEKGHMQREfDESSAALDQEAKLRADQERIAKGY 1268
Cdd:COG4717 454 ELAELEAELEQLEED-GELAELLQELEELKAELRELAEEW 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1280-1926 |
2.24e-09 |
|
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: 62.83 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1280 DEQSRQLQDFvssKGRLNSENS-------DLARQVEELEAKIQaanrlklQFSNELDHAKRQAEEESRERQNLSNLSKNL 1352
Cdd:pfam15921 81 EEYSHQVKDL---QRRLNESNElhekqkfYLRQSVIDLQTKLQ-------EMQMERDAMADIRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1353 ARELEQLKESIEDEVAGKNEASRQLSKASVE----LDQWRT---KFETEGLIGADEFDEVK----KRQNQKTSEIQDALD 1421
Cdd:pfam15921 151 VHELEAAKCLKEDMLEDSNTQIEQLRKMMLShegvLQEIRSilvDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1422 A----CNAKIVALENARSRLTAEADaNRLEAehhaqavsSLEKKQKAFDKVIDEWKkkvddlyLELDGAQRDARQLSGEA 1497
Cdd:pfam15921 231 TeisyLKGRIFPVEDQLEALKSESQ-NKIEL--------LLQQHQDRIEQLISEHE-------VEITGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1498 HKLRGQHDTLADQVeglRREN----KSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESK 1573
Cdd:pfam15921 295 NSIQSQLEIIQEQA---RNQNsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1574 ALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQ------TIDSIQATLDSETKAKSELFRVKKKLEADIN-ELEIALD 1646
Cdd:pfam15921 372 SGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1647 HANKANEDAQK--NIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEA-LERARRVVESSVK 1723
Cdd:pfam15921 452 AIQGKNESLEKvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAeITKLRSRVDLKLQ 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1724 EHQ------EHNNELNSQNVALAAAKSQLDNEIALLNSDIaEAHTELSASEDRGRRAAS-DAAKLAEDLRHEQEQSQQLE 1796
Cdd:pfam15921 532 ELQhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQI-ENMTQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1797 RFKKQLESAVKDLQERADAAEAAVMKggakAIQKAEQRLKAFQsDLETESRRAGEASKTlARADRKVREFEFQVAedKKN 1876
Cdd:pfam15921 611 ILKDKKDAKIRELEARVSDLELEKVK----LVNAGSERLRAVK-DIKQERDQLLNEVKT-SRNELNSLSEDYEVL--KRN 682
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 25150292 1877 YDKLQELVEKLTAKLKLQKKqleeaeeQANSHLSKYRTVQLSLETAEERA 1926
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLK-------SAQSELEQTRNTLKSMEGSDGHA 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1615-1864 |
4.35e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1615 ATLDSETKAKSELFRVKKKLEADINELEIALdhankanEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKL 1694
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKEL-------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1695 AVAKQEQEELIVKLEALER--ARRVVESSVKEHQEHNNEL-NSQNVALAAAKSQLDNEIALLNSDIAEA-HTELSASEDR 1770
Cdd:COG4942 86 AELEKEIAELRAELEAQKEelAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1771 GRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAvmkggAKAIQKAEQRLKAFQSDLETESRRAG 1850
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-----LAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|....
gi 25150292 1851 EASKTLARADRKVR 1864
Cdd:COG4942 241 ERTPAAGFAALKGK 254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
857-1269 |
5.29e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 857 NSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLA 936
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 937 DASKKLEVEEARaveINKQKKLVEA----ECAdlkkncQDVDLSlrkveaeknakEHqiralQDEMRQQDENISKLNKER 1012
Cdd:PRK02224 430 ELEATLRTARER---VEEAEALLEAgkcpECG------QPVEGS-----------PH-----VETIEEDRERVEELEAEL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1013 KNQEEQNKKLTEDLQAAEEQNLAANKLKaKLMQSLEDSEQTMErEKRNRADMDknkrkaegelkiaQETLEELNKSKSDA 1092
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIA-ERRETIEEK-------------RERAEELRERAAEL 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1093 ENALRRKEtelhtlgmkledeqAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADR--SRADQQAEYDELTEQLEDQA 1170
Cdd:PRK02224 550 EAEAEEKR--------------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1171 RATAAQIELGKKKDAELTKLRRDLEES--GLKFgEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESS 1248
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEfdEARI-EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
410 420
....*....|....*....|.
gi 25150292 1249 AALDQEAKLRADQERIAKGYE 1269
Cdd:PRK02224 695 ELRERREALENRVEALEALYD 715
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
857-1394 |
5.42e-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: 61.78 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 857 NSGKIEAQYEKL-QETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGStrEVEERMTAMNEQKVALEGKL 935
Cdd:pfam12128 369 KHQDVTAKYNRRrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELRE--QLEAGKLEFNEEEYRLKSRL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 936 ADAskKLEVEEARAVEinkqkklveaecaDLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQ----QDENISKLNKE 1011
Cdd:pfam12128 447 GEL--KLRLNQATATP-------------ELLLQLENFDERIERAREEQEAANAEVERLQSELRQarkrRDQASEALRQA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1012 RKNQEEQNkklTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTM----EREKRNRADMD--KNKRKAEGELKIAQETL--- 1082
Cdd:pfam12128 512 SRRLEERQ---SALDELELQLFPQAGTLLHFLRKEAPDWEQSIgkviSPELLHRTDLDpeVWDGSVGGELNLYGVKLdlk 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1083 -----------EELNKSKSDAENAL-------RRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDA 1144
Cdd:pfam12128 589 ridvpewaaseEELRERLDKAEEALqsarekqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDK 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1145 RQRAdRSRADQQAEydELTEQLEDQARAtaaqieLGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIE 1224
Cdd:pfam12128 669 KNKA-LAERKDSAN--ERLNSLEAQLKQ------LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIA 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1225 QLQKQ-KGRIEKEKGHMQREFdessaaldqeAKLRADQERIAK-GYEVRLLELRLKADEQSRQ--LQDFVSSKGRLNSEN 1300
Cdd:pfam12128 740 ARRSGaKAELKALETWYKRDL----------ASLGVDPDVIAKlKREIRTLERKIERIAVRRQevLRYFDWYQETWLQRR 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1301 SDLARQVEELEakiQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIE-----DEVAGKNEASR 1375
Cdd:pfam12128 810 PRLATQLSNIE---RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSklatlKEDANSEQAQG 886
|
570
....*....|....*....
gi 25150292 1376 QLSKASVELDQWRTKFETE 1394
Cdd:pfam12128 887 SIGERLAQLEDLKLKRDYL 905
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1337-1889 |
7.11e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1337 EESRERQNLSNLS-KNLARELEQLKESIEDEVAGKNEAsrqlskasvELDQWRTKFETEgligADEFDEVKKRQNQKTSE 1415
Cdd:PRK02224 165 EEYRERASDARLGvERVLSDQRGSLDQLKAQIEEKEEK---------DLHERLNGLESE----LAELDEEIERYEEQREQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1416 IQDALDACNAKIVALENARSRL-TAEADANRLEAehhaqAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLS 1494
Cdd:PRK02224 232 ARETRDEADEVLEEHEERREELeTLEAEIEDLRE-----TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1495 GEAHKLRGQHDTLADQVEGLRREnksLSDETRDLTESLSEGGRAThalsKNLRRLEMEKEELQRGLDEAEAALESEESKA 1574
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDR---LEECRVAAQAHNEEAESLR----EDADDLEERAEELREEAAELESELEEAREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1575 LRCQIEVsqirAEIEKRIAEKEEEFENhrkvHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALD-------- 1646
Cdd:PRK02224 380 EDRREEI----EELEEEIEELRERFGD----APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaeallea 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1647 --------------HANKANEDAQK--NIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEA 1710
Cdd:PRK02224 452 gkcpecgqpvegspHVETIEEDRERveELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1711 LERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDN---EIALLNSDIAEAHTELSASEdRGRRAASDAAKLAEDLRH 1787
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1788 EQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFE 1867
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
570 580
....*....|....*....|..
gi 25150292 1868 FQVAEDKKNYDKLQELVEKLTA 1889
Cdd:PRK02224 691 EELEELRERREALENRVEALEA 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1193 |
8.69e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 859 GKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGaerlnketadllaqLEASKGSTREVEERMTAMNEQKVALEGKLADA 938
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE--------------IENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 939 SKKLEVEEARavEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENIsklnKERKNQEEQ 1018
Cdd:TIGR02169 785 EARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI----KSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1019 NKKLTEDLQAAEEqnlaanKLKAKLMQsLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRR 1098
Cdd:TIGR02169 859 LNGKKEELEEELE------ELEAALRD-LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1099 KETELHTLGMKLEDEQAAVA---KLQKGIQQDEARVKDLhdqladeKDARQRADRSRADQQAEYDELTEQLEDQARATAA 1175
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRAL-------EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
330
....*....|....*...
gi 25150292 1176 QIELgkkkDAELTKLRRD 1193
Cdd:TIGR02169 1005 ILER----IEEYEKKKRE 1018
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
860-1479 |
9.16e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.22 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETaDLLAQLEASKGSTREVEERMTAMNEQKVALEgKLADAS 939
Cdd:TIGR01612 1230 KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDKDHHIISKKHDENIS-DIREKS 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 940 KKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNA-KEHQIRALQDEMRQQDENISKLNKERKNQEEQ 1018
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNIlKLNKIKKIIDEVKEYTKEIEENNKNIKDELDK 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1019 NKKLTEDLQaaeeQNLAANKLKAKLMQSLEDSEqtmerekrnradmdknkrkaegelkiaqetLEELNKSKSDAENALRR 1098
Cdd:TIGR01612 1388 SEKLIKKIK----DDINLEECKSKIESTLDDKD------------------------------IDECIKKIKELKNHILS 1433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1099 KETELHTLGMKLEDEQAAVAKLQKGIQqdearvkdlhdqLADEKDA---RQRADRSRADQQAEYDELTEQLE------DQ 1169
Cdd:TIGR01612 1434 EESNIDTYFKNADENNENVLLLFKNIE------------MADNKSQhilKIKKDNATNDHDFNINELKEHIDkskgckDE 1501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1170 ARATAAQIE----LGKKKDAELTKLRRDLEESGLKfgEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQRE-- 1243
Cdd:TIGR01612 1502 ADKNAKAIEknkeLFEQYKKDVTELLNKYSALAIK--NKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEkf 1579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1244 -FDESSAALDQEAKLRADQERIAKGYEVRLLelrlKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKL 1322
Cdd:TIGR01612 1580 rIEDDAAKNDKSNKAAIDIQLSLENFENKFL----KISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSL 1655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1323 Q-FSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIE-------DEVAGKNEASRQLSKASVE--LDQWRTKFE 1392
Cdd:TIGR01612 1656 QeFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiekiKEIAIANKEEIESIKELIEptIENLISSFN 1735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1393 TEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALEN-ARSRLTAEADAN-RLEAEHHAQAVSSLEKKQKA------ 1464
Cdd:TIGR01612 1736 TNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETvSKEPITYDEIKNtRINAQNEFLKIIEIEKKSKSylddie 1815
|
650
....*....|....*...
gi 25150292 1465 ---FDKVIDEWKKKVDDL 1479
Cdd:TIGR01612 1816 akeFDRIINHFKKKLDHV 1833
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
929-1176 |
1.14e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 929 VALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKL 1008
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1009 NKERKNQEEQNKKLTEDLQAAEEQNlaanklKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGelkiAQETLEELNKS 1088
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1089 KSDAENALRRKETelhtlgmKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLED 1168
Cdd:COG4942 166 RAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....*...
gi 25150292 1169 QARATAAQ 1176
Cdd:COG4942 239 AAERTPAA 246
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
867-1522 |
1.27e-08 |
|
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: 60.24 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 867 KLQETVATLKDTVVQEEEKKRQLQEGAERLNKEtadlLAQLEAskgstrEVEERMTAMNEQKVALEGKLADASKKLEVEE 946
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQL----LRTLDD------QWKEKRDELNGELSAADAAVAKDRSELEALE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 947 ARAVEINKqkklveaecADLKKNCQDVDlSLRKVEAEKNAKEHQIRALQDEMRQQDEnisKLNKERKNQEEQNKKLTEDL 1026
Cdd:pfam12128 329 DQHGAFLD---------ADIETAAADQE-QLPSWQSELENLEERLKALTGKHQDVTA---KYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1027 qaaeEQNLAANK-LKAKLMQSLEDSEQTMEREKRNRADMDKNKRKaEGELKIAqETLEELN------KSKSDAENALRRK 1099
Cdd:pfam12128 396 ----KDKLAKIReARDRQLAVAEDDLQALESELREQLEAGKLEFN-EEEYRLK-SRLGELKlrlnqaTATPELLLQLENF 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1100 ETELHtlgmKLEDEQAAVAKLQKGIQQDEARVKDLHDQladEKDARQRADRSRADQQAEYDELTEQLEDQA-------RA 1172
Cdd:pfam12128 470 DERIE----RAREEQEAANAEVERLQSELRQARKRRDQ---ASEALRQASRRLEERQSALDELELQLFPQAgtllhflRK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1173 TAAQIE--LGKKKDAELTkLRRDLEES--------GLKFG------------------EQLTVLKKKGSDAIQELSDQIE 1224
Cdd:pfam12128 543 EAPDWEqsIGKVISPELL-HRTDLDPEvwdgsvggELNLYgvkldlkridvpewaaseEELRERLDKAEEALQSAREKQA 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1225 QLQKQKGRIEKEKGHMQREFDESSAALDQEaklRADQERIAKGYEvrllELRLKADEQSRQLQDFVsskgrlNSENSDLA 1304
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNA---RLDLRRLFDEKQ----SEKDKKNKALAERKDSA------NERLNSLE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1305 RQVEELEAKIQAA----NRLKLQFSNELDHAKRQAEEE-----SRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASR 1375
Cdd:pfam12128 689 AQLKQLDKKHQAWleeqKEQKREARTEKQAYWQVVEGAldaqlALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1376 QLSKASVELDQWRTKFETEGLIGADE---FDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRleaehha 1452
Cdd:pfam12128 769 VIAKLKREIRTLERKIERIAVRRQEVlryFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR------- 841
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1453 qavSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDArqLSGEAHKLRGQHDTLADQVEGLRRENKSLS 1522
Cdd:pfam12128 842 ---AKLEMERKASEKQQVRLSENLRGLRCEMSKLATLK--EDANSEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
867-1822 |
1.43e-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: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 867 KLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERmtamneqkvalegKLADASKKLEVEE 946
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER-------------ELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 947 ARAVEINKQKK--LVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDE--MRQQDENISKLNKERKNQEEQN--- 1019
Cdd:TIGR00606 333 KERRLLNQEKTelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfSERQIKNFHTLVIERQEDEAKTaaq 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1020 --KKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALR 1097
Cdd:TIGR00606 413 lcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1098 RKETE-LHTLGMKLEDEQAAVAKLQKGIQQDEARV----KDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARA 1172
Cdd:TIGR00606 493 NSLTEtLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1173 TAAQIELGKKKDaELTKLRRDLEESGLKfgeqltvlkkkgsdaIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALD 1252
Cdd:TIGR00606 573 KQLEDWLHSKSK-EINQTRDRLAKLNKE---------------LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1253 QEAKLRADQERIAKGYEVRLLelrlkADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQaanrlklQFSNELDHAK 1332
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAM-----LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ-------EFISDLQSKL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1333 RQAEEESRERQNLsnLSKnlareleqlKESIEDEVAGKNEA-SRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQ 1411
Cdd:TIGR00606 705 RLAPDKLKSTESE--LKK---------KEKRRDEMLGLAPGrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1412 ktseiqdaLDACNAKivaLENARSRLTAEADANRLEAEhhaqavsslekkqkafdkvIDEWKKKVDDLYLELDGA--QRD 1489
Cdd:TIGR00606 774 --------LGTIMPE---EESAKVCLTDVTIMERFQME-------------------LKDVERKIAQQAAKLQGSdlDRT 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1490 ARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQrgldeaeaaleS 1569
Cdd:TIGR00606 824 VQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-----------E 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1570 EESKALRCQIEVSQIRAEIEKRIAEKEeefenhrKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEialDHAN 1649
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQDSPLETFLE-------KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMK---DIEN 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1650 KANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSvKEHQEHN 1729
Cdd:TIGR00606 963 KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE-EELKQHL 1041
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1730 NELNSQNVA-LAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAasdAAKLAE-DLRHEQEQSQQLERFKKQLESAVK 1807
Cdd:TIGR00606 1042 KEMGQMQVLqMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHF---KKELREpQFRDAEEKYREMMIVMRTTELVNK 1118
|
970
....*....|....*
gi 25150292 1808 DLQERADAAEAAVMK 1822
Cdd:TIGR00606 1119 DLDIYYKTLDQAIMK 1133
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1274-1947 |
1.52e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1274 ELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDH------AKRQAEEESRERQNLSN 1347
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHlnlvqtALRQQEKIERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1348 LSKNLARELEQLKESIEdevaGKNEASRQLSKASVELDQWRTKFetegligAD---EFDEVKKRQNQKTSEIQdALDA-- 1422
Cdd:PRK04863 360 LEERLEEQNEVVEEADE----QQEENEARAEAAEEEVDELKSQL-------ADyqqALDVQQTRAIQYQQAVQ-ALERak 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1423 --CNAKIVALENARSRL---TAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLylELDGAQRDARQLSGEA 1497
Cdd:PRK04863 428 qlCGLPDLTADNAEDWLeefQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV--SRSEAWDVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1498 HKLRgqhdTLADQVEGLRRENKSL---SDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKA 1574
Cdd:PRK04863 506 REQR----HLAEQLQQLRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1575 LRCQIEVSQIRAEIEK-------------RIAEKEEEFENHRKVHQQTIDSIQATLDSE---TKAKSELFRVKKKLEADI 1638
Cdd:PRK04863 582 MALRQQLEQLQARIQRlaarapawlaaqdALARLREQSGEEFEDSQDVTEYMQQLLERErelTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1639 NEL----------------------------EIALDHAN-------------------------KANEDAQKNIrrYL-- 1663
Cdd:PRK04863 662 ERLsqpggsedprlnalaerfggvllseiydDVSLEDAPyfsalygparhaivvpdlsdaaeqlAGLEDCPEDL--YLie 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1664 ---DQIRELQQTVDEEQK-----------RREEFREHLL----AAERKLAVAKQEQEELIVKLEALERARRVVESSVkeh 1725
Cdd:PRK04863 740 gdpDSFDDSVFSVEELEKavvvkiadrqwRYSRFPEVPLfgraAREKRIEQLRAEREELAERYATLSFDVQKLQRLH--- 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1726 qEHNNELNSQNVALAAAKSQlDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLaedlrheQEQSQQLERFKKQLES- 1804
Cdd:PRK04863 817 -QAFSRFIGSHLAVAFEADP-EAELRQLNRRRVELERALADHESQEQQQRSQLEQA-------KEGLSALNRLLPRLNLl 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1805 AVKDLQERADAAEA---------AVMKGGAKAIQKAEQRLKAFQSD---LETESRRAGEASKTLARADRKV--------R 1864
Cdd:PRK04863 888 ADETLADRVEEIREqldeaeeakRFVQQHGNALAQLEPIVSVLQSDpeqFEQLKQDYQQAQQTQRDAKQQAfaltevvqR 967
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1865 EFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSH---LSKYRTVQLSL----ETAEERADSAEQCLVRIR 1937
Cdd:PRK04863 968 RAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLkssyDAKRQMLQELKQELQDLG 1047
|
810
....*....|
gi 25150292 1938 SRTRANAEQK 1947
Cdd:PRK04863 1048 VPADSGAEER 1057
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
862-1365 |
2.12e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 862 EAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGstreveERMTAMNEQKVALEGKLADASKK 941
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 942 LEVEEARAVEINKQkklVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKK 1021
Cdd:COG4913 361 RARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1022 LTEDLQA-----AEEQNLAANKLK--AKLMQSLEDSEQ---TMEREKRNRA-DM---DK---------NKRKAEGELKI- 1077
Cdd:COG4913 438 IPARLLAlrdalAEALGLDEAELPfvGELIEVRPEEERwrgAIERVLGGFAlTLlvpPEhyaaalrwvNRLHLRGRLVYe 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1078 -AQETLEELNKSKSDAENALRRKETELHTLGMKLEDE---QAAVAKL--------------------------QKGIQQD 1127
Cdd:COG4913 518 rVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrRFDYVCVdspeelrrhpraitragqvkgngtrhEKDDRRR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1128 -----------EARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLE----------DQARATAAQIELgkkkdAE 1186
Cdd:COG4913 598 irsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswDEIDVASAEREI-----AE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1187 LTKLRRDLEESGLKF---GEQLTVLKKkgsdAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQER 1263
Cdd:COG4913 673 LEAELERLDASSDDLaalEEQLEELEA----ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1264 IakgyevrLLELRLKADEQSRQLQDFVSS-KGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELD------------- 1329
Cdd:COG4913 749 A-------LLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslpeylall 821
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 25150292 1330 --------HAKRQAEEESRERQN---LSNLSKNLARELEQLKESIED 1365
Cdd:COG4913 822 drleedglPEYEERFKELLNENSiefVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1363-1724 |
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 25150292 1363 IEDEVAGKNEASRQLSKASVELDQWRTKFETEGLI----------------GADEFDEVKKR-QNQKTSEIQDALDACNA 1425
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIidekrqqlerlrrereKAERYQALLKEkREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1426 KIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIdewKKKVDDLYLELdgaQRDARQLSGEAHKLRGQHD 1505
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRV---KEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1506 TLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIR 1585
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1586 AEIEKRIAEKEEefenhrkvHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALdhankanEDAQKNIRRYLDQ 1665
Cdd:TIGR02169 392 EKLEKLKREINE--------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-------EDKALEIKKQEWK 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1666 IRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEqeelivkLEALERARRVVESSVKE 1724
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-------LAEAEAQARASEERVRG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1709-1939 |
3.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1709 EALERARRVVEssvkehqeHNNELNSQNVALAAAKSQLD--NEIALLNSDIAEAHTELSASEDRGRRAASDAAK-----L 1781
Cdd:COG4913 222 DTFEAADALVE--------HFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQrrlelL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1782 AEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAkaiqkaeQRLKAFQSDLETESRRAGEASKTLARADR 1861
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1862 KVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANShlskyrtvqlSLETAEERADSAEQCLVRIRSR 1939
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA----------ALRDLRRELRELEAEIASLERR 434
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
992-1817 |
3.52e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 992 RALQDEMRQQDENISKLN---KERKNQEEQNKKLTEDLQAAEEQ-NLAANKLKAKlmqsledseqtmEREKRNRADMDkn 1067
Cdd:COG3096 292 RELFGARRQLAEEQYRLVemaRELEELSARESDLEQDYQAASDHlNLVQTALRQQ------------EKIERYQEDLE-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1068 krKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQ-KGIQQdearvkdlhdqladeKDARQ 1146
Cdd:COG3096 358 --ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQtRAIQY---------------QQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1147 RADrsRADQQAEYDELT-EQLEDQARATAAQIElgkkkdaELTKLRRDLEesglkfgEQLTVlkkkGSDAIQELSDQIEQ 1225
Cdd:COG3096 421 ALE--KARALCGLPDLTpENAEDYLAAFRAKEQ-------QATEEVLELE-------QKLSV----ADAARRQFEKAYEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1226 LQKQKGRIEKEKGHMQ-----REFDESSAALDQEAKLRAdqeriakgyevRLLELRLKADEQS---RQLQDFVSSKGRLN 1297
Cdd:COG3096 481 VCKIAGEVERSQAWQTarellRRYRSQQALAQRLQQLRA-----------QLAELEQRLRQQQnaeRLLEEFCQRIGQQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1298 SENSDLARQVEELEAKIQ-------AANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGK 1370
Cdd:COG3096 550 DAAEELEELLAELEAQLEeleeqaaEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1371 NEASRQLSKasveldqwrtkfETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVAL-ENARSRLTAEA-------D 1442
Cdd:COG3096 630 AAMQQLLER------------EREATVERDELAARKQALESQIERLSQPGGAEDPRLLALaERLGGVLLSEIyddvtleD 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1443 ANRLEA----EHHAQAVSSLEKKQKAFDKVIDewkkKVDDLYLeldgAQRDARQLSGEAHKLRGQHDTLADQVEG--LR- 1515
Cdd:COG3096 698 APYFSAlygpARHAIVVPDLSAVKEQLAGLED----CPEDLYL----IEGDPDSFDDSVFDAEELEDAVVVKLSDrqWRy 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1516 -------------RENK--SLSDETRDLTESLSEggrathaLSKNLRRLEMEKEELQRGLDEAEaaleseeskALRCQIE 1580
Cdd:COG3096 770 srfpevplfgraaREKRleELRAERDELAEQYAK-------ASFDVQKLQRLHQAFSQFVGGHL---------AVAFAPD 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1581 VSQIRAEIEKRIAEKEEEFENHR---KVHQQTIDSIQATLDSETKAKSELFRVKKK-LEADINELEIALDHAnkanEDAQ 1656
Cdd:COG3096 834 PEAELAALRQRRSELERELAQHRaqeQQLRQQLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAA----QEAQ 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1657 KNIRRYLDQIR-----------------ELQQTVDEEQKRREEFREHLLA----AERKLAVAKQEQEELIV--------- 1706
Cdd:COG3096 910 AFIQQHGKALAqleplvavlqsdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevVQRRPHFSYEDAVGLLGensdlnekl 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1707 --KLEALERARRVVESSVKEHQEhnnELNSQNVALAAAKSQLDNEIALLnsdiAEAHTELsasEDRGRRAASDAAKLAED 1784
Cdd:COG3096 990 raRLEQAEEARREAREQLRQAQA---QYSQYNQVLASLKSSRDAKQQTL----QELEQEL---EELGVQADAEAEERARI 1059
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 25150292 1785 LRHE--QEQSQ------QLERFKKQLESAVKDLQERADAAE 1817
Cdd:COG3096 1060 RRDElhEELSQnrsrrsQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
932-1379 |
4.08e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 932 EGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRAlqDEMRQQDENISKLNKE 1011
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL--EELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1012 RKNQEEQNKKLTEDLQAAEEQNLAANKlkaklmQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSD 1091
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATE------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1092 AENALRRKETELHTLG--------------MKLEDEQAAVAKLQKGIQQDEARVKD-LHDQLADEKDARQRADRSRADQQ 1156
Cdd:COG4717 239 AALEERLKEARLLLLIaaallallglggslLSLILTIAGVLFLVLGLLALLFLLLArEKASLGKEAEELQALPALEELEE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1157 AEYDELTEQLE-------DQARATAAQIELGKKKDAELTKLRRDLEESGLKfGEQLTVLKKKGSDAIQELSDQIEQLQKQ 1229
Cdd:COG4717 319 EELEELLAALGlppdlspEELLELLDRIEELQELLREAEELEEELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1230 KgRIEKEKGHMQREFDESSAALDQEAKlRADQERIakgyEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQvEE 1309
Cdd:COG4717 398 Q-ELKEELEELEEQLEELLGELEELLE-ALDEEEL----EEELEELEEELEELEEELEELREELAELEAELEQLEED-GE 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1310 LEAKIQaanrlklqfsnELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVagKNEASRQLSK 1379
Cdd:COG4717 471 LAELLQ-----------ELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPV--LERASEYFSR 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1622-1946 |
5.96e-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: 58.16 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1622 KAKSELFRVKKKLE---ADINELEIALDHANKANEDAQknirRYLDQIRELQQT-VDEEQKRREEFREHLLAAERKLAVA 1697
Cdd:TIGR02169 174 KALEELEEVEENIErldLIIDEKRQQLERLRREREKAE----RYQALLKEKREYeGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1698 KQEQEELIVKLEALERARRVVESSVKEHQEHNNELNS-QNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAAS 1776
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1777 DAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERAD---------AAEAAVMKGGAKAIQKAEQRLKAFQSDLETESR 1847
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1848 RAGEASKTL----ARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAE 1923
Cdd:TIGR02169 410 RLQEELQRLseelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
330 340
....*....|....*....|...
gi 25150292 1924 ERADSAEQCLVRIRSRTRANAEQ 1946
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAV 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1071-1318 |
6.76e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1071 AEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADR 1150
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1151 SRADQQAEYDELTEQLEDQARATAAQIELGKkkdaeltklrrdleESGLKFGEQLTVLKKkgsdAIQELSDQIEQLQKQK 1230
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSP--------------EDFLDAVRRLQYLKY----LAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1231 GRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEEL 1310
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
....*...
gi 25150292 1311 EAKIQAAN 1318
Cdd:COG4942 240 AERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1481-1946 |
6.84e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1481 LELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSE-GGRATHALSKNLRRLEMEKEELQRG 1559
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1560 LDeaeaaleseeskalrcqiEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADIN 1639
Cdd:COG4913 361 RA------------------RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1640 EL--EIAldhankANEDAQKNIRRYLDQIREL--QQT-VDEEQKR--------REEFREHLLAAERKLAVAKQEqeeLIV 1706
Cdd:COG4913 423 ELeaEIA------SLERRKSNIPARLLALRDAlaEALgLDEAELPfvgelievRPEEERWRGAIERVLGGFALT---LLV 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1707 KLEALERARRVVESSVKEHQ---EHNNELNSQNVALAAAKSQLDNEIALLNSDIAE-AHTELSASED-----------RG 1771
Cdd:COG4913 494 PPEHYAAALRWVNRLHLRGRlvyERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwLEAELGRRFDyvcvdspeelrRH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1772 RRAASDAAKLAEDLRHEQEQSQQLERFKKQL----ESAVKDLQERADAAEAAVmKGGAKAIQKAEQRLKAFQSDLETESR 1847
Cdd:COG4913 574 PRAITRAGQVKGNGTRHEKDDRRRIRSRYVLgfdnRAKLAALEAELAELEEEL-AEAEERLEALEAELDALQERREALQR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1848 RAG--EASKTLARADRKVREFEFQVAEDKKNYDKLQELveklTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEER 1925
Cdd:COG4913 653 LAEysWDEIDVASAEREIAELEAELERLDASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
490 500
....*....|....*....|.
gi 25150292 1926 ADSAEQCLVRIRSRTRANAEQ 1946
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRA 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1099 |
7.19e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 862 EAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLAdaskk 941
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 942 lEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKnakeHQIRALQDEMRQQDENISKLNKERKNQEEQNKK 1021
Cdd:COG4942 101 -AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1022 LTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGEL-KIAQETLEELNKSKSDAENALRRK 1099
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIaRLEAEAAAAAERTPAAGFAALKGK 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1607-1906 |
1.21e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1607 QQTIDSIQATLDSETKAKSELFRVK-----KKLEADI-NEL-EIALDHANKANEDAQKNIRRYLD-QIRELQQTVDEEQK 1678
Cdd:COG3206 117 EAAIERLRKNLTVEPVKGSNVIEISytspdPELAAAVaNALaEAYLEQNLELRREEARKALEFLEeQLPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1679 RREEFREhllaaERKLAVAKQEQEELIVKLEALERARrvvessvkehqehnNELNSQNVALAAAKSQLDNEIALLNSDIA 1758
Cdd:COG3206 197 ALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQL--------------AEARAELAEAEARLAALRAQLGSGPDALP 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1759 EAHTELSASEDRGRRAASDaAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVmkggAKAIQKAEQRLKAF 1838
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELE-AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL----EAELEALQAREASL 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1839 QSDLETESRRAGEASKTLARADRKVREFEFQvaedKKNYDKLQElvekltaklKLQKKQLEEAEEQAN 1906
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVA----RELYESLLQ---------RLEEARLAEALTVGN 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
926-1153 |
1.35e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 926 EQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENI 1005
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1006 SKLNkeRKNQEEQNKKLTEDLQAAEEQNLAANKLKAkLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEEL 1085
Cdd:COG4942 107 AELL--RALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1086 NKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRA 1153
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
971-1532 |
1.37e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 971 QDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMqSLEDS 1050
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS-SLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1051 EQTMEREKRnraDMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEAR 1130
Cdd:PRK01156 251 KNRYESEIK---TAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1131 VKDLHDQLADEKDARQRadrsradqQAEYDELTEQL------EDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQ 1204
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKK--------KSRYDDLNNQIlelegyEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1205 LTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDEssaaldqeakLRADQERIAKGYEVRLLELRLKADEQSR 1284
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE----------LSRNMEMLNGQSVCPVCGTTLGEEKSNH 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1285 QLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKlqfsneldhaKRQAEEESRERQNLSNLSKNLARELEQLKES-- 1362
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK----------EYLESEEINKSINEYNKIESARADLEDIKIKin 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1363 -IEDEVAGKNEASRQLSKASVE-LDQWRTKF-ETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTA 1439
Cdd:PRK01156 540 eLKDKHDKYEEIKNRYKSLKLEdLDSKRTSWlNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1440 -----EADANRL-----EAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDD---LYLELDGAQRDARQLSGEAHKLRGQHDT 1506
Cdd:PRK01156 620 sireiENEANNLnnkynEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDlkeITSRINDIEDNLKKSRKALDDAKANRAR 699
|
570 580
....*....|....*....|....*.
gi 25150292 1507 LADQVEGLRRENKSLSDETRDLTESL 1532
Cdd:PRK01156 700 LESTIEILRTRINELSDRINDINETL 725
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
861-1156 |
1.38e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.44 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEgkladasK 940
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-------T 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 941 KLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEknakehqiraLQDEMRQQDENISKLNKERKNQEEQNK 1020
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----------FQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1021 KLTEDLQAAEEQNLAANKLKAkLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALR--- 1097
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRS-LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegr 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1098 -RKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKD-------LHDQLADEKDAR--QRADRSRADQQ 1156
Cdd:pfam07888 300 aRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerekLEVELGREKDCNrvQLSESRRELQE 368
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1042-1514 |
1.48e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1042 KLMQSLEDSEQTMEREKRNRADMDKNKRKAEgELKIAQETLEELNKSKSDAEnaLRRKETELHTLGMKLEDEQAAVAKLQ 1121
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1122 KGIQQDEARVKDLHDQLADEKDARQRADRSRADQ-QAEYDELTEQLEDQAR------ATAAQIELGKKKDAE-LTKLRRD 1193
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERrrarleALLAALGLPLPASAEeFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1194 LEEsglkFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQR-------EFDESSAALDQEAKLRADQERIAK 1266
Cdd:COG4913 389 AAA----LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnipaRLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1267 GY-EVRLLELR----------------LKADEQSRQLQDFVSS---KGRLNSE-----NSDLARQ-------VEELEAKI 1314
Cdd:COG4913 465 ELiEVRPEEERwrgaiervlggfaltlLVPPEHYAAALRWVNRlhlRGRLVYErvrtgLPDPERPrldpdslAGKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1315 -QAANRLKLQFSNELDHAKRQAEEE--------------------------SRERQNL----SNLSK--NLARELEQLKE 1361
Cdd:COG4913 545 hPFRAWLEAELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekddrRRIRSRYvlgfDNRAKlaALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1362 SIedevagkNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKkrqnqktseiqdaLDACNAKIVALENARSRLTAEA 1441
Cdd:COG4913 625 EL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEID-------------VASAEREIAELEAELERLDASS 684
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150292 1442 DAnrleaehhaqaVSSLEKKqkafdkvIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGL 1514
Cdd:COG4913 685 DD-----------LAALEEQ-------LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1076-1291 |
1.57e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1076 KIAQETLEELNKSKSD-AENALRRKETELHTLGMKLEDEQAAVAKLQK--GIQQDEARVKDLHDQLADEKDARQRADRSR 1152
Cdd:COG3206 156 ALAEAYLEQNLELRREeARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1153 ADQQAEYDELTEQLEDQARATAAQIElgkkkDAELTKLRRDLEESGLKFGEQLTVLKKKgSDAIQELSDQIEQLQKQ-KG 1231
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPN-HPDVIALRAQIAALRAQlQQ 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150292 1232 RIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGY---EVRLLELRLKADEQSRQLQDFVS 1291
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQ 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1066-1522 |
1.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1066 KNKRKAEGELKIAQETLEELnkskSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEaRVKDLHDQLADEKDAR 1145
Cdd:COG4717 64 RKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1146 QradrsradQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEEsglkfgeQLTVLKKKGSDAIQELSDQIEQ 1225
Cdd:COG4717 139 A--------ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE-------LLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1226 LQKQKGRIEKEKGHMQREFDESSAALDQ---EAKLRADQERIAKGYEV-----RLLELRLKADEQSRQLQD----FVSSK 1293
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQlenELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTiagvLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1294 GRLNSENSDLARQVEELEAKIQAANRLKLQFSNEldhaKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEA 1373
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1374 SRQLSKASVElDQWRTKFETEGLIGADEFDEVKKRQNQKTsEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHaq 1453
Cdd:COG4717 360 EEELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELE-- 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1454 avsSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDarqlsGEAHKLRGQHDTLADQVEGLRRENKSLS 1522
Cdd:COG4717 436 ---ELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAALK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1172-1386 |
2.17e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1172 ATAAQIELGKKKDAELTKLRRDLEESGLKFgEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAal 1251
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1252 dQEAKLRADQERIAKGYEVRLLEL-------RLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQF 1324
Cdd:COG4942 91 -EIAELRAELEAQKEELAELLRALyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1325 SNELDHAKRQAEEESRERQNLSNL---SKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQ 1386
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALkaeRQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
654-688 |
3.19e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 52.35 E-value: 3.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 25150292 654 SGSFMTV------SMLYRESLNKLMTMLHSTHPHFIRCIIP 688
Cdd:cd01363 130 FGKFIEIlldiagFEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1139-1361 |
3.57e-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: 54.77 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1139 ADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQE 1218
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1219 LSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNS 1298
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150292 1299 ENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKE 1361
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
855-1345 |
3.66e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 855 LVNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREveermtAMNEQKvALEGK 934
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR------SMSTQK-ALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 935 LADASKKL----EVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNK 1010
Cdd:pfam05483 319 LQIATKTIcqltEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1011 ERKNQE--------------------EQNKKLTEDLQAAEEQNLAANKLKAKLMQSLE------------------DSEQ 1052
Cdd:pfam05483 399 FKNNKEveleelkkilaedeklldekKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktseehylkeveDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1053 TMEREKRNRADMDKNKRKAEGELK-IAQETLE---ELNKSKSDAENALRRKETELHtlgmKLEDEQAAVAKLQKGIQQDE 1128
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKeLTQEASDmtlELKKHQEDIINCKKQEERMLK----QIENLEEKEMNLRDELESVR 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1129 ARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTV- 1207
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAy 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1208 ------LKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLradQERIAKGYEVRLLELRLKADE 1281
Cdd:pfam05483 635 eikvnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKL---QKEIDKRCQHKIAEMVALMEK 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1282 QSRQLQDFVSSKgrlnSENSDLARQVEELEAKIQAANRLKL-QFSNELDHAKRQAEEESRERQNL 1345
Cdd:pfam05483 712 HKHQYDKIIEER----DSELGLYKNKEQEQSSAKAALEIELsNIKAELLSLKKQLEIEKEEKEKL 772
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1687-1897 |
4.03e-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: 54.38 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1687 LLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSA 1766
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1767 SEdrgRRAASDAAKLAEDLRH--------------EQEQSQQLERFKKQLESAVKDLQERADA--AEAAVMKGGAKAIQK 1830
Cdd:COG4942 95 LR---AELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1831 AEQRLKAFQSDLETESRR----AGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQ 1897
Cdd:COG4942 172 ERAELEALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1408-1904 |
4.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1408 RQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQkafdkvIDEWKKKVDDLYLELDGAQ 1487
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR------LEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1488 RDARQLSGEAHKLRGQHDTLADQVEGLRRENK----SLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRG---L 1560
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRksnI 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1561 DEAEAALESEESKALrcQIEVSQIR--AE-IEkrIAEKEEEFEN---------------------------------HR- 1603
Cdd:COG4913 439 PARLLALRDALAEAL--GLDEAELPfvGElIE--VRPEEERWRGaiervlggfaltllvppehyaaalrwvnrlhlrGRl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1604 ---KVHQQTIDSIQATLDSET-----KAKSELFR--VKKKLEADIN----ELEIALDHANKA---------NEDA-QKNI 1659
Cdd:COG4913 515 vyeRVRTGLPDPERPRLDPDSlagklDFKPHPFRawLEAELGRRFDyvcvDSPEELRRHPRAitragqvkgNGTRhEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1660 RRYLDQIRELQQTVDEeqkRREEFREHLLAAERKLAVAKQEQEELIVKLEALERaRRVVESSVKEHQEHNNELNSQNVAL 1739
Cdd:COG4913 595 RRRIRSRYVLGFDNRA---KLAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWDEIDVASAEREI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1740 AAAKSQL------DNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLrheQEQSQQLERFKKQLESAVkDLQERA 1813
Cdd:COG4913 671 AELEAELerldasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAE-DLARLE 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1814 DAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRK-VREFEFQVAEDKKNYDKLQELVEKLTaklK 1892
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLD---R 823
|
570
....*....|..
gi 25150292 1893 LQKKQLEEAEEQ 1904
Cdd:COG4913 824 LEEDGLPEYEER 835
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1143-1694 |
5.21e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1143 DARQRADRSRADQQAEYDELTEQLED-QARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLK------KKGSDA 1215
Cdd:PRK02224 173 DARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevleehEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1216 IQELSDQIEQLQKQKGRIEKEKGHMQREF-----------DESSAALDQEAKLRADQERIA----------KGYEVRLLE 1274
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVrdlrerleeleEERDDLLAEAGLDDADAEAVEarreeledrdEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1275 LRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESR-------ERQNLSN 1347
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1348 LSKNLARELEQLKESIEDEvagknEASRQLSKASVEldqwrtkfETEGLIGADEFDEVKkrQNQKTSEIQDALDACNAKI 1427
Cdd:PRK02224 413 FLEELREERDELREREAEL-----EATLRTARERVE--------EAEALLEAGKCPECG--QPVEGSPHVETIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1428 VALENARSRL-----TAEADANRLEAEHHAQA-VSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLR 1501
Cdd:PRK02224 478 EELEAELEDLeeeveEVEERLERAEDLVEAEDrIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1502 GQHDTLADQVEGLRRENKSLSDETRDLTESLseggrathalsKNLRRLEmekeelqrgldeaeaaleseeskalrcqiev 1581
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERI-----------ESLERIR------------------------------- 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1582 sqiraEIEKRIAEKEEEFENHRKVHQQtidsiQATLDSETKAK-SELFRVKKKLEADINELEIALDHANKAN-EDAQKNI 1659
Cdd:PRK02224 596 -----TLLAAIADAEDEIERLREKREA-----LAELNDERRERlAEKRERKRELEAEFDEARIEEAREDKERaEEYLEQV 665
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 25150292 1660 RRYLDQIRE----LQQT---VDEEQKRREEFREHLLAAERKL 1694
Cdd:PRK02224 666 EEKLDELREerddLQAEigaVENELEELEELRERREALENRV 707
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
990-1536 |
6.10e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 990 QIRALQDEMRQQDENISKLNKERKNQE--EQNKKLTEDLQAAEEQNLAANKLKAKLmqSLEDSEQTMEREKRNRADMDKN 1067
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1068 KRKAEGELKIAQETLEELNKSKSDAENALRRKETE-LHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQ 1146
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1147 RADRSRADQQAEYDELTEQLEDQARATAAQielgkkkdaeLTKLRRDLEesglkfgeqltvlkkkgsdaiqELSDQIEQL 1226
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAA----------LRDLRRELR----------------------ELEAEIASL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1227 QKQKGRIEKEKGHMQREFdESSAALDQEA--------KLRADQER-----------------IAKGYEVRLLE----LRL 1277
Cdd:COG4913 432 ERRKSNIPARLLALRDAL-AEALGLDEAElpfvgeliEVRPEEERwrgaiervlggfaltllVPPEHYAAALRwvnrLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1278 KADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAAnrLKLQFSNELDHAKRQAEEE------------------- 1338
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAW--LEAELGRRFDYVCVDSPEElrrhpraitragqvkgngt 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1339 -------SRERQNL----SNLSK--NLARELEQLKESIedevagkNEASRQLSKASVELDQWRTKFETEGLIGADEFDEV 1405
Cdd:COG4913 589 rhekddrRRIRSRYvlgfDNRAKlaALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1406 KKRQNQKT-SEIQDALDACNAKIVALENARSRL-TAEADANRLEAEHHA--QAVSSLEKKQKAFDKVIDEWKKKVDD--- 1478
Cdd:COG4913 662 DVASAEREiAELEAELERLDASSDDLAALEEQLeELEAELEELEEELDElkGEIGRLEKELEQAEEELDELQDRLEAaed 741
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 1479 -----LYLELDG----------AQRDARQLSGEAHKLRGQHDTLADQVEGLRRE-NKSLSDETRDLTESLSEGG 1536
Cdd:COG4913 742 larleLRALLEErfaaalgdavERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1306-1938 |
6.39e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1306 QVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLS-KNLARELEQLKESIEDEVAGKNEASRQLSKASVEL 1384
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1385 DQWRTKFETEgligADEFDEVKKRQNQKTSEIQDALdacNAKIVALENARSRLTAEADANRLEAEhhaqavsSLEKKQKA 1464
Cdd:TIGR02169 261 SELEKRLEEI----EQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKERELE-------DAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1465 FDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSK 1544
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1545 NLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEK--------------------RIAEKEEEFENHRK 1604
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewkleqlaadlskyeqelyDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1605 VHQQTIDSIQATLDSETKAKSELFRVKKKLEADIN------------------ELEIALDHANKA-----NEDAQKNI-- 1659
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryatAIEVAAGNRLNNvvvedDAVAKEAIel 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1660 --------------------RRYLDQIRE------------------------LQQTV---DEEQKRR------------ 1680
Cdd:TIGR02169 567 lkrrkagratflplnkmrdeRRDLSILSEdgvigfavdlvefdpkyepafkyvFGDTLvveDIEAARRlmgkyrmvtleg 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1681 ------------------------------EEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNN 1730
Cdd:TIGR02169 647 elfeksgamtggsraprggilfsrsepaelQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1731 ELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDL-----RHEQEQSQQLERFKKQLESA 1805
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1806 VKDLQERADAAEAAVMKGGA------KAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDK 1879
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLekeyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1880 LQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRS 1938
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1034-1783 |
7.20e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1034 LAANKLKAKLMQSLEDSEQ-----TMEREKRNRADMDKNKRKAEGEL---------KIAQETLEELNKSKSDAENALRRK 1099
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQytqlaLMEFAKKKSLHGKAELLTLRSQLltlctpcmpDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1100 ETELHTLGMKLEDEQAAvAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSR-ADQQAEYDELTEQLEDQARATAAQIe 1178
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERINRARkAAPLAAHIKAVTQIEQQAQRIHTEL- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1179 lgKKKDAELTKLRRdleesglkfgEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREfdESSAALDQEAKLR 1258
Cdd:TIGR00618 317 --QSKMRSRAKLLM----------KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE--ISCQQHTLTQHIH 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1259 ADQERIakgyevrllelrlKADEQSRQLqdfvsskgrLNSENSDLARQVEELEAKIQAANRLKLQfsneLDHAKRQAEEE 1338
Cdd:TIGR00618 383 TLQQQK-------------TTLTQKLQS---------LCKELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1339 SRERQNLSNLSKNLARELEQlkesiedEVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEfDEVKKRQNQKTSEIQD 1418
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKL-------EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV-LARLLELQEEPCPLCG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1419 ALDACNAKIVALENARSrLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAH 1498
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1499 KLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEggrATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQ 1578
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP---EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1579 IEVSQIRAEIEKRIAEKEEEFENHRkvhqQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHA----NKANED 1654
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQKMQSEK----EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLgsdlAAREDA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1655 AQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHN-NELN 1733
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDeDILN 820
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 25150292 1734 SQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAE 1783
Cdd:TIGR00618 821 LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1456-1907 |
8.18e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1456 SSLEKKQKAFDKVIDEWKKKVDDLYLELdgaqRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEG 1535
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKL----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1536 GRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVH----QQTID 1611
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSElknqEKKLE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1612 SIQATLDSETKAKSELfrvkkklEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAE 1691
Cdd:TIGR04523 325 EIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1692 RKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRG 1771
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1772 RRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKaEQRLKAFQSDLET--ESRRA 1849
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK-ESKISDLEDELNKddFELKK 556
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1850 GEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANS 1907
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
860-1168 |
8.30e-07 |
|
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: 54.19 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEE----KKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNE--------Q 927
Cdd:COG5185 240 DPESELEDLAQTSDKLEKLVEQNTDlrleKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAtesleeqlA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 928 KVALEGKLADASKKLEVEEARAV-EINKQKKLVEAECADLKKNCQDVDLS--LRKVEAEKNAKEHQIRAL--------QD 996
Cdd:COG5185 320 AAEAEQELEESKRETETGIQNLTaEIEQGQESLTENLEAIKEEIENIVGEveLSKSSEELDSFKDTIESTkesldeipQN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 997 EMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGelk 1076
Cdd:COG5185 400 QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSV--- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1077 iaQETLEELNKSKSDAENALRRKETELHTLGMKLEdeqAAVAKLQKGIQQDEARVKDLHDQLADE-KDARQRADRSRADQ 1155
Cdd:COG5185 477 --RSKKEDLNEELTQIESRVSTLKATLEKLRAKLE---RQLEGVRSKLDQVAESLKDFMRARGYAhILALENLIPASELI 551
|
330
....*....|...
gi 25150292 1156 QAEYDELTEQLED 1168
Cdd:COG5185 552 QASNAKTDGQAAN 564
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
980-1642 |
1.06e-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: 53.96 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 980 VEAEKNAKEHQIRALQDEMRQQDENISKLNKErknQEEQNKKLTEDLQAAEE---QNLAA----NKLKAKLMQSLEDSEQ 1052
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEIQENKDlikENNATrhlcNLLKETCARSAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1053 -TMEREKRNRADMDKNKR-----KAEGELKIAQET--LEELNKSKSDAENaLRRKETELHTlgmKLEDEQAAVAKLQKGI 1124
Cdd:pfam05483 174 yEYEREETRQVYMDLNNNiekmiLAFEELRVQAENarLEMHFKLKEDHEK-IQHLEEEYKK---EINDKEKQVSLLLIQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1125 QQDEARVKDLHDQLadeKDARQRADRSRADQQAEYDELTEQLEDQARATAaqielgKKKDAELTKLRRDLEESGLKfgEQ 1204
Cdd:pfam05483 250 TEKENKMKDLTFLL---EESRDKANQLEEKTKLQDENLKELIEKKDHLTK------ELEDIKMSLQRSMSTQKALE--ED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1205 LTVLKKKGSDAIQELSDQIEQLQKQKGriekEKGHMQREFDESSAALdqEAKLRADQERIAKGyEVRLLELRLKADEQSR 1284
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKA----AHSFVVTEFEATTCSL--EELLRTEQQRLEKN-EDQLKIITMELQKKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1285 QLQDFVSSKGRlnsensdlaRQVEELEAKIQAANRLKLQFSNEldHAKRQAEEESRERQNLSNLSKNLARELEQLKESIE 1364
Cdd:pfam05483 392 ELEEMTKFKNN---------KEVELEELKKILAEDEKLLDEKK--QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1365 DEVAGKNEASRQLSKASVELDQWRTKfETEGLIGADEFDEVKKRQNQKTSEIqdaldacnakIVALENARSrltaEADAN 1444
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLK-NIELTAHCDKLLLENKELTQEASDM----------TLELKKHQE----DIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1445 RLEAEHHAQAVSSLEKKQ----KAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRR--EN 1518
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEmnlrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKqiEN 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1519 KS-----LSDETRDLTESLSEGGRATHALSKNLRRLEMEKE-----------------------------ELQRGLDEAE 1564
Cdd:pfam05483 606 KNknieeLHQENKALKKKGSAENKQLNAYEIKVNKLELELAsakqkfeeiidnyqkeiedkkiseeklleEVEKAKAIAD 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1565 AALESEESKALRCQIEVSQIRAEIEK------RIAEKEEEFENHRKVHQQTIDSIQATLDSE-TKAKSELFRVKKKLEAD 1637
Cdd:pfam05483 686 EAVKLQKEIDKRCQHKIAEMVALMEKhkhqydKIIEERDSELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIE 765
|
....*
gi 25150292 1638 INELE 1642
Cdd:pfam05483 766 KEEKE 770
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
986-1938 |
1.07e-06 |
|
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: 53.90 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 986 AKEHQIRALQDEMRQQDENISKLnKERKNQEEQNK----KLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQ-TMEREKRN 1060
Cdd:TIGR00606 228 SKEAQLESSREIVKSYENELDPL-KNRLKEIEHNLskimKLDNEIKALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1061 RADMDKNKRKAEGELKIAQETLEELNKSKSDaenaLRRKETELhtlgmklEDEQAAVaKLQKGIQQDEARVKD---LHDQ 1137
Cdd:TIGR00606 307 YHNHQRTVREKERELVDCQRELEKLNKERRL----LNQEKTEL-------LVEQGRL-QLQADRHQEHIRARDsliQSLA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1138 LADEKDARQRADRSRADQQAEYDELTEQLEDQARATAaqielgkkkdaeltKLRRDLEESGLKFGEQLTVLKKKGSDAIQ 1217
Cdd:TIGR00606 375 TRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA--------------QLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1218 ELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELrLKADEQSrqlqdfvsskgrLN 1297
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTET-LKKEVKS------------LQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1298 SENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLAREL------EQLKESIEDEVAGKN 1371
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSKEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1372 EASRQLSKASVELDQWRTKFETEGligadefDEVKKRQNQKTSEIQDALDACNAKI--VALENARSRL-TAEADANRLEA 1448
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHIN-------NELESKEEQLSSYEDKLFDVCGSQDeeSDLERLKEEIeKSSKQRAMLAG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1449 EH--HAQAVSSLEKKQKAFDKVID-------EWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENK 1519
Cdd:TIGR00606 661 ATavYSQFITQLTDENQSCCPVCQrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1520 SLSDETRDLTESLSEGGRATHALSKNLrrlemEKEELQRGldeaeaALESEESKALRCQIEVSqiraeIEKRIAEKEEEf 1599
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDI-----EEQETLLG------TIMPEEESAKVCLTDVT-----IMERFQMELKD- 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1600 eNHRKVHQQTIdsiqatldsetkakselfrvkkklEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKR 1679
Cdd:TIGR00606 804 -VERKIAQQAA------------------------KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1680 REEFREhllaaerKLAVAKQEQEELIvklEALERARRVVESSVkehqEHNNELNSQNVALAAAKSQLDNEIALLNSDIAE 1759
Cdd:TIGR00606 859 IQHLKS-------KTNELKSEKLQIG---TNLQRRQQFEEQLV----ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1760 AHTELSASEDRGRRAASDAAKLAEDLRheqeqsqQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQ 1839
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKVK-------NIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN 997
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1840 SDLETESR---------RAGEASKTLARADRKVREFE------------FQVAEDKKNYDKLQELV-------------- 1884
Cdd:TIGR00606 998 EDMRLMRQdidtqkiqeRWLQDNLTLRKRENELKEVEeelkqhlkemgqMQVLQMKQEHQKLEENIdlikrnhvlalgrq 1077
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1885 -----EKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRS 1938
Cdd:TIGR00606 1078 kgyekEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
941-1675 |
1.09e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 941 KLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLrkveaeknakEHQIRALQDEMRQQDENISKLNKERKNQEEQNK 1020
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCT----------PCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1021 KLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRAdmdKNKRKAEGELKIAQETLEELNKSKSDAENALRRKE 1100
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER---INRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1101 TELHTLGMKLEDEQAAVAKLQKG------IQQDEARVKDLHDQLADEKD--ARQRADRSRADQQAEYDELTEQLEDQARA 1172
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQrrllqtLHSQEIHIRDAHEVATSIREisCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1173 TAAQIELGKKKDAELTKLRRDLEESgLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEkghMQREFDESSAALD 1252
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQ-LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE---SAQSLKEREQQLQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1253 QEAKLRADQERIAKGYEVRLLELRLKA---DEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELD 1329
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1330 HAKRQAEEESRERQNLSNL------SKNLARELEQLKESIEDEVAGKNEASRQLSKASVELdqwrtkfETEGLIGADEFD 1403
Cdd:TIGR00618 557 QRASLKEQMQEIQQSFSILtqcdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL-------LRKLQPEQDLQD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1404 eVKKRQNQKTSEIQDALdacnakiVALENARSRLTAEadanrlEAEHHAQAVSSLEKKQKAFDKvidewkkkvddlyLEL 1483
Cdd:TIGR00618 630 -VRLHLQQCSQELALKL-------TALHALQLTLTQE------RVREHALSIRVLPKELLASRQ-------------LAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1484 DGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEA 1563
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1564 EAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKV---HQQTIDS-IQATLDSETKAKSELFRVKKKLEaDIN 1639
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLeaeIGQEIPSdEDILNLQCETLVQEEEQFLSRLE-EKS 841
|
730 740 750
....*....|....*....|....*....|....*.
gi 25150292 1640 ELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDE 1675
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1451-1911 |
1.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1451 HAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTE 1530
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1531 SLseggrATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQI---EVSQIRAEIEKRIAEKEEEFENHRKVHQ 1607
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1608 QTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANE-DAQKNIRRYLDQIRELQQTVDEEQKRREEFREH 1686
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1687 LLA-------AERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAE 1759
Cdd:COG4717 279 LFLvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1760 AHTELSASEDRGRRA---ASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLK 1836
Cdd:COG4717 359 LEEELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1837 AFQSDLETESRRA-----------------GEASKTLARADRKVREFEfQVAEDKKNYDKLQELVEKltAKLKLQKKQLE 1899
Cdd:COG4717 439 EELEELEEELEELreelaeleaeleqleedGELAELLQELEELKAELR-ELAEEWAALKLALELLEE--AREEYREERLP 515
|
490
....*....|..
gi 25150292 1900 EAEEQANSHLSK 1911
Cdd:COG4717 516 PVLERASEYFSR 527
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1181-1903 |
1.65e-06 |
|
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: 53.44 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1181 KKKDAELTKLRRDLEESG------LKFGEQLTVLKKKGSDAI----------------------QELSDQIEQLQKQKGR 1232
Cdd:pfam02463 169 RKKKEALKKLIEETENLAeliidlEELKLQELKLKEQAKKALeyyqlkekleleeeyllyldylKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1233 IEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEA 1312
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1313 KIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFE 1392
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1393 TEGLIGADEFDEVKKRQNQKTS---EIQDALDACNAKIVALENARSRLTAEADANRLEAEhhaqAVSSLEKKQKAFDKVI 1469
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEileEEEESIELKQGKLTEEKEELEKQELKLLKDELELK----KSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1470 DEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRL 1549
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1550 EMEKEELQRGLDEAEAALESEESKALRCQI---EVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSE 1626
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIavlEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1627 LFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELiv 1706
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL-- 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1707 KLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLR 1786
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1787 HEQEQSQQLERFKKQLESAVKDLQEradaaeaavmkggaKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREf 1866
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQE--------------EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE- 867
|
730 740 750
....*....|....*....|....*....|....*..
gi 25150292 1867 EFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEE 1903
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1243 |
2.03e-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: 53.10 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGA---ERLNKETADLLAQLEaskgstrEVEERMTAMNEQKVA-----L 931
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkelEQNNKKIKELEKQLN-------QLKSEISDLNNQKEQdwnkeL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 932 EGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQ-------DEMRQQDEN 1004
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1005 ISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEE 1084
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1085 LNKSKSDAENALRRKETELhtlgmklEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDEL-T 1163
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKEL-------KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLeD 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1164 EQLEDQARATAAQIELGK-KKDAELTKLRRDlEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQR 1242
Cdd:TIGR04523 546 ELNKDDFELKKENLEKEIdEKNKEIEELKQT-QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
.
gi 25150292 1243 E 1243
Cdd:TIGR04523 625 E 625
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
926-1723 |
2.12e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 926 EQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLkkncqdvdlslrkvEAEKNAKEHQIRALQDEMRQQD--- 1002
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL--------------EQDYQAASDHLNLVQTALRQQEkie 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1003 ---ENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRnRAdmdKNKRKAEGELKIAQ 1079
Cdd:COG3096 351 ryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQT-RA---IQYQQAVQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1080 ETLEELNKSKSDAEN---ALRRKETELHT----LGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKdARQ-----R 1147
Cdd:COG3096 427 ALCGLPDLTPENAEDylaAFRAKEQQATEevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQT-AREllrryR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1148 ADRSRADQ----QAEYDELTEQLEDQARATAAQIELGKKKD-------------AELTKLRRDLEESGLKFGEQLTVLKK 1210
Cdd:COG3096 506 SQQALAQRlqqlRAQLAELEQRLRQQQNAERLLEEFCQRIGqqldaaeeleellAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1211 KGSDA---IQELSDQIEQLQKQKGRIEKEKGHMQREFdESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQ 1287
Cdd:COG3096 586 QLEQLrarIKELAARAPAWLAAQDALERLREQSGEAL-ADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1288 DFVSSK-GRLNS--------------ENSDL------------ARQ---VEELEAKIQAANRLK-----LQF----SNEL 1328
Cdd:COG3096 665 QPGGAEdPRLLAlaerlggvllseiyDDVTLedapyfsalygpARHaivVPDLSAVKEQLAGLEdcpedLYLiegdPDSF 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1329 DHAKRQAEEE-------SRERQ-NLSNLSK-----NLARE--LEQLKESIEDEVAGKNEASRQLSKASvELDQWRTKFET 1393
Cdd:COG3096 745 DDSVFDAEELedavvvkLSDRQwRYSRFPEvplfgRAAREkrLEELRAERDELAEQYAKASFDVQKLQ-RLHQAFSQFVG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1394 EGLIGADEFD--EVKKRQNQKTSEIQDALDACNAKIV----ALENARSRLTA----EADANRLEAEHHAQavsslekkqk 1463
Cdd:COG3096 824 GHLAVAFAPDpeAELAALRQRRSELERELAQHRAQEQqlrqQLDQLKEQLQLlnklLPQANLLADETLAD---------- 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1464 afdkvidewkkKVDDLYLELDGAQRDARQLSGEAHKLRgqhdTLADQVEGLRR---ENKSLSDETRDLTESLSEGGRATH 1540
Cdd:COG3096 894 -----------RLEELREELDAAQEAQAFIQQHGKALA----QLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIF 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1541 ALSKNL-RRLEMEKEELQRGLDEAEAAleseeskalrcqieVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQ--ATL 1617
Cdd:COG3096 959 ALSEVVqRRPHFSYEDAVGLLGENSDL--------------NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQvlASL 1024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1618 DSETKAKSELFRvkkKLEADINELEIALDhankANEDAQKNIRRyldqiRELQQTVDEEQKRREEfrehllaAERKLAVA 1697
Cdd:COG3096 1025 KSSRDAKQQTLQ---ELEQELEELGVQAD----AEAEERARIRR-----DELHEELSQNRSRRSQ-------LEKQLTRC 1085
|
890 900 910
....*....|....*....|....*....|
gi 25150292 1698 KQEQEELIVKLEALER----ARRVVESSVK 1723
Cdd:COG3096 1086 EAEMDSLQKRLRKAERdykqEREQVVQAKA 1115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1743-1947 |
2.23e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1743 KSQLDN-EIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAeaavm 1821
Cdd:TIGR02168 219 KAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL----- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1822 kggAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEA 1901
Cdd:TIGR02168 294 ---ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 25150292 1902 EeqanshlSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK 1947
Cdd:TIGR02168 371 E-------SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1587-1836 |
2.32e-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: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1587 EIEKRIAEKEEEFENHRKVHQQtIDSIQATLDSETKAKsELFRVKKKLEADINELEIALDHANKanEDAQKNIRRYLDQI 1666
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEA-LEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1667 RELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEEliVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQL 1746
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1747 DNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVmkggAK 1826
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL----AE 451
|
250
....*....|
gi 25150292 1827 AIQKAEQRLK 1836
Cdd:COG4913 452 ALGLDEAELP 461
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1389-1930 |
2.69e-06 |
|
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: 52.87 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1389 TKFETEGLIGADEFDEVKKRQNQKTSEIQDaLDACNAKIVALEN-------ARSRLTAEADANRLEAEHHAQAV------ 1455
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKE-LEKKHQQLCEEKNalqeqlqAETELCAEAEEMRARLAARKQELeeilhe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1456 --SSLEKKQKAFDKVIDEWKK---KVDDLYLELDgAQRDARQ--------LSGEAHKLRGQHDTLADQVEGLRRENKSLS 1522
Cdd:pfam01576 80 leSRLEEEEERSQQLQNEKKKmqqHIQDLEEQLD-EEEAARQklqlekvtTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1523 DETRDLTESLSEGGRATHALSKNLRRLE---------MEKEELQRGLDEAEAALESEESKALRCQI-EVSQIRAEIEKRI 1592
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEamisdleerLKKEEKGRQELEKAKRKLEGESTDLQEQIaELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1593 AEKEEEfenhrkvhqqtIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIR------------ 1660
Cdd:pfam01576 239 AKKEEE-----------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRdlgeelealkte 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1661 ----------------RYLDQIRELQQTVDEEQKRRE---------------EFREHLLAAER---KLAVAKQ----EQE 1702
Cdd:pfam01576 308 ledtldttaaqqelrsKREQEVTELKKALEEETRSHEaqlqemrqkhtqaleELTEQLEQAKRnkaNLEKAKQalesENA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1703 ELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLA 1782
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1783 EDLRHEQEQSQQLERFK-------KQLESAVKDLQERADAAEAAvMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKT 1855
Cdd:pfam01576 468 SQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEA-KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1856 LARADRKVREFEFQVAEDKKNYDK-------LQELVEKLTAKLKLQKK---QLEEAEEQANSHLSKYRTVqlSLETAEER 1925
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDLDHQRQlvsNLEKKQKKFDQMLAEEKAI--SARYAEER 624
|
....*
gi 25150292 1926 aDSAE 1930
Cdd:pfam01576 625 -DRAE 628
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
999-1285 |
2.75e-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: 52.43 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 999 RQQDENISKLNKERKNQEEQNK--KLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKR-NRADMDKNKRKAE--- 1072
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKarEVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERElERIRQEERKRELErir 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1073 -GELKIAQETLEELNKSKSDAE--NALRRKETELHTLGMKLEDEQAAVAKLQKG------IQQDEARVKDLhdQLADEKD 1143
Cdd:pfam17380 367 qEEIAMEISRMRELERLQMERQqkNERVRQELEAARKVKILEEERQRKIQQQKVemeqirAEQEEARQREV--RRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1144 AR--QRADRSRADQQAEYDELTEQLEDQARaTAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQ-ELS 1220
Cdd:pfam17380 445 ARemERVRLEEQERQQQVERLRQQEEERKR-KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEME 523
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1221 D-QIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQ 1285
Cdd:pfam17380 524 ErQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1626-1931 |
4.19e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1626 ELFRVKKKLEADineLEIALDHANKANE--DAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEE 1703
Cdd:COG3096 317 ELSARESDLEQD---YQAASDHLNLVQTalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1704 LIVKL---------------------EALERARRV-------VESSVKEHQEHNNELNS---------QNVALA-AAKSQ 1745
Cdd:COG3096 394 LKSQLadyqqaldvqqtraiqyqqavQALEKARALcglpdltPENAEDYLAAFRAKEQQateevleleQKLSVAdAARRQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1746 LDNEIALLNSDIAEAHTElsasedrgrRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAE--AAVMKG 1823
Cdd:COG3096 474 FEKAYELVCKIAGEVERS---------QAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERllEEFCQR 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1824 GAKAIQKAEQrLKAFQSDLETEsrrageasktLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAK----LKLQKKqLE 1899
Cdd:COG3096 545 IGQQLDAAEE-LEELLAELEAQ----------LEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDA-LE 612
|
330 340 350
....*....|....*....|....*....|..
gi 25150292 1900 EAEEQANSHLSKYRTVQLSLETAEERADSAEQ 1931
Cdd:COG3096 613 RLREQSGEALADSQEVTAAMQQLLEREREATV 644
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
881-1095 |
4.21e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 881 QEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKkleveearavEINKQKKLVE 960
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA----------EIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 961 AECADLKKNCQDVDLSLRKVEAEkNAKE--HQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANK 1038
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSE-SFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25150292 1039 LKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENA 1095
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1582-1913 |
4.30e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1582 SQIRAEIEKRIAEKEEEFENHRkvhQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRR 1661
Cdd:PLN02939 44 SQQKKKRGKNIAPKQRSSNSKL---QSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1662 YLDQIRELQ-----QTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALE------RARRVVESSVKEHQEHNN 1730
Cdd:PLN02939 121 DGEQLSDFQledlvGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEmrlsetDARIKLAAQEKIHVEILE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1731 ELnsqnvaLAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQ---LESAVK 1807
Cdd:PLN02939 201 EQ------LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKErslLDASLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1808 DLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARAD---RKVREFEFQVAEdKKNYDKLQELV 1884
Cdd:PLN02939 275 ELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQdlrDKVDKLEASLKE-ANVSKFSSYKV 353
|
330 340
....*....|....*....|....*....
gi 25150292 1885 EKLTAKLKLQKKQLEEAEEQANSHLSKYR 1913
Cdd:PLN02939 354 ELLQQKLKLLEERLQASDHEIHSYIQLYQ 382
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1737-1947 |
4.56e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1737 VALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAA 1816
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1817 EAAvMKGGAKAIQKAEQRLKAFQSDLETES-----RRAgEASKTLARADRKVREfefQVAEDKKNYDKLQELVEKLTAKL 1891
Cdd:COG3883 85 REE-LGERARALYRSGGSVSYLDVLLGSESfsdflDRL-SALSKIADADADLLE---ELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1892 KLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK 1947
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
796-1223 |
5.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 796 SLAQLITGLQAQIRwyyQTIERKRRVEKITalKIIQRNIRSWAELRTWVwfKLYGKVKPLVNsgkieaQYEKLQEtvatl 875
Cdd:PRK03918 318 RLEEEINGIEERIK---ELEEKEERLEELK--KKLKELEKRLEELEERH--ELYEEAKAKKE------ELERLKK----- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 876 KDTVVQEEEKKRQLQEgAERLNKETADLLAQLEASKGSTR-EVEERMTAMNEQKVA-----LEGKLADASKKLEVEEARA 949
Cdd:PRK03918 380 RLTGLTPEKLEKELEE-LEKAKEEIEEEISKITARIGELKkEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 950 VEINKqkklVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQ--DEMRQQDENISKLNKErknqeeqnkKLTEDLQ 1027
Cdd:PRK03918 459 AELKR----IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLE---------ELEKKAE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1028 AAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRAdMDKNKRKAEGELK--------IAQETLEELNK------------ 1087
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAellkeleeLGFESVEELEErlkelepfyney 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1088 -SKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRAD-----RSRADQQAEYDE 1161
Cdd:PRK03918 605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEylelsRELAGLRAELEE 684
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1162 LTEQLE------DQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQI 1223
Cdd:PRK03918 685 LEKRREeikktlEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEI 752
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1560 |
6.32e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 857 NSGKIEAQYEKLQETVATLKDTVVQEEekkrQLQEGAERLNKETADLLAQLEASKGSTREV---EERMTAMNEQKVALEG 933
Cdd:PRK04863 322 AESDLEQDYQAASDHLNLVQTALRQQE----KIERYQADLEELEERLEEQNEVVEEADEQQeenEARAEAAEEEVDELKS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 934 KLADASKKLEVEEARAVEINKQKKLVEaecaDLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISkLNKERK 1013
Cdd:PRK04863 398 QLADYQQALDVQQTRAIQYQQAVQALE----RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAH 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1014 NQEEQNKKLTEDLQAAEEQNLAANKLKAKL------------MQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQET 1081
Cdd:PRK04863 473 SQFEQAYQLVRKIAGEVSRSEAWDVARELLrrlreqrhlaeqLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1082 LEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEAR----------VKDLHDQLADEKDARQRADRS 1151
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEY 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1152 RADQQAEYDELT---EQLEDQARATAAQIE-LGKKKDAELTKLRRDLEESGlkfGEQLTVLKKKGS--DA---------- 1215
Cdd:PRK04863 633 MQQLLERERELTverDELAARKQALDEEIErLSQPGGSEDPRLNALAERFG---GVLLSEIYDDVSleDApyfsalygpa 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1216 -----IQELSDQIEQLQKQKG------RIEkekGHMQReFDESSAALDQEAKLRADQE-----RIAKGYEV--------- 1270
Cdd:PRK04863 710 rhaivVPDLSDAAEQLAGLEDcpedlyLIE---GDPDS-FDDSVFSVEELEKAVVVKIadrqwRYSRFPEVplfgraare 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1271 -RLLELRLKADEQSRQ----------LQDFVSSKGRLNSENSDLARQVEElEAKIQAANRLKLQFSNEL------DHAKR 1333
Cdd:PRK04863 786 kRIEQLRAEREELAERyatlsfdvqkLQRLHQAFSRFIGSHLAVAFEADP-EAELRQLNRRRVELERALadhesqEQQQR 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1334 QAEEESRERQNLSN----LSKNLARE-LEQLKESIEDEVAGKNEASR---QLSKASVELDQWRTKFETEgligADEFDEV 1405
Cdd:PRK04863 865 SQLEQAKEGLSALNrllpRLNLLADEtLADRVEEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQSD----PEQFEQL 940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1406 KKRQNQKTSEIQDAldacNAKIVALENARSRLT--AEADANRLEAEhHAQAVSSLEKKQKAFDKVIDEWKKkvddlylEL 1483
Cdd:PRK04863 941 KQDYQQAQQTQRDA----KQQAFALTEVVQRRAhfSYEDAAEMLAK-NSDLNEKLRQRLEQAEQERTRARE-------QL 1008
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1484 DGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSL------SDETR------DLTESLSEGGRATHALSKNLRRLEM 1551
Cdd:PRK04863 1009 RQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsGAEERararrdELHARLSANRSRRNQLEKQLTFCEA 1088
|
....*....
gi 25150292 1552 EKEELQRGL 1560
Cdd:PRK04863 1089 EMDNLTKKL 1097
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1216-1688 |
6.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1216 IQELSDQIEQLQKQKGRI-----------EKEKGHMQREFDESSAALDQEAKLRADQERIAKgyEVRLLELRLKADEQSR 1284
Cdd:COG4717 48 LERLEKEADELFKPQGRKpelnlkelkelEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1285 QLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKlqfsNELDHAKRQAEEESRERQNLSNLSKNLAR-ELEQLKESI 1363
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLSLATEeELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1364 EDEVAGKNEASRQLSKASVELDQWRTKFETeglIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADA 1443
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQ---LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1444 NRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSD 1523
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1524 ETRDLTeslseggrathalsknLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHR 1603
Cdd:COG4717 359 LEEELQ----------------LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1604 KVH-----QQTIDSIQATLDSETKAKSELFRVKKKLEADINELEI--ALDHANKANEDAQKNIRRYLDQIRELQ---QTV 1673
Cdd:COG4717 423 EALdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKlalELL 502
|
490
....*....|....*.
gi 25150292 1674 DEEQKR-REEFREHLL 1688
Cdd:COG4717 503 EEAREEyREERLPPVL 518
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1271-1946 |
8.35e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1271 RLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAAN-RLKLqfsneLDHAKRQAEEESRERQNLSNLS 1349
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASdHLNL-----VQTALRQQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1350 KNLARELEQLKESIEDevagKNEASRQLSKASVELDQWRTKFetegligAD---EFDEVKKRQNQKTSEIQ---DALDAC 1423
Cdd:COG3096 361 ERLEEQEEVVEEAAEQ----LAEAEARLEAAEEEVDSLKSQL-------ADyqqALDVQQTRAIQYQQAVQaleKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1424 NAKIVALENARSRLTA------EADANRLEAEHHAqAVSSLEKKQkaFDKVIDEWKKKVDDLylELDGAQRDARQLSGEA 1497
Cdd:COG3096 430 GLPDLTPENAEDYLAAfrakeqQATEEVLELEQKL-SVADAARRQ--FEKAYELVCKIAGEV--ERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1498 HKLRGQhdtlADQVEGLRRENKSLS---DETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKA 1574
Cdd:COG3096 505 RSQQAL----AQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1575 LRCQIEVSQIRAEIEK----------------RIAEK-EEEFENhrkvHQQTIDSIQATLDSETKA---KSELFRVKKKL 1634
Cdd:COG3096 581 SELRQQLEQLRARIKElaarapawlaaqdaleRLREQsGEALAD----SQEVTAAMQQLLEREREAtveRDELAARKQAL 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1635 EADINELeialdHANKANEDAQKN--------------------------------------------IRRYLDQI---- 1666
Cdd:COG3096 657 ESQIERL-----SQPGGAEDPRLLalaerlggvllseiyddvtledapyfsalygparhaivvpdlsaVKEQLAGLedcp 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1667 --------------------RELQQTV----DEEQKRREEFREHLL----AAERKLAVAKQEQEELivklealerARRVV 1718
Cdd:COG3096 732 edlyliegdpdsfddsvfdaEELEDAVvvklSDRQWRYSRFPEVPLfgraAREKRLEELRAERDEL---------AEQYA 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1719 ESS--VKEHQ---EHNNELNSQNVALAAAKSQlDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLaedlrheQEQSQ 1793
Cdd:COG3096 803 KASfdVQKLQrlhQAFSQFVGGHLAVAFAPDP-EAELAALRQRRSELERELAQHRAQEQQLRQQLDQL-------KEQLQ 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1794 QLERFKKQ--------LESAVKDLQERADAAEAAV--MKGGAKAIQKAEQRLKAFQSD---LETESRRAGEASKTLARAD 1860
Cdd:COG3096 875 LLNKLLPQanlladetLADRLEELREELDAAQEAQafIQQHGKALAQLEPLVAVLQSDpeqFEQLQADYLQAKEQQRRLK 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1861 RKV--------REFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQanshlskyrtvqlsLETAEERADSAEQC 1932
Cdd:COG3096 955 QQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQ--------------LRQAQAQYSQYNQV 1020
|
810
....*....|....
gi 25150292 1933 LVRIRSRTRANAEQ 1946
Cdd:COG3096 1021 LASLKSSRDAKQQT 1034
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
880-1146 |
8.79e-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: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 880 VQEEEKKRQLqegaERLNKEtadllaQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLV 959
Cdd:pfam17380 353 IRQEERKREL----ERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 960 EAECADLKKNCQDvdlSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNlaankl 1039
Cdd:pfam17380 423 EQIRAEQEEARQR---EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1040 KAKLMQSLEDSEQTMEREKRNRADMDKnkrkaegELKIAQETL-EELNKSKSDAEnalRRKETELHTlgMKLEDEQAAVA 1118
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKRKLLEK-------EMEERQKAIyEEERRREAEEE---RRKQQEMEE--RRRIQEQMRKA 561
|
250 260
....*....|....*....|....*...
gi 25150292 1119 KLQKGIQQDEARVKDLHDQLADEKDARQ 1146
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1092 |
1.18e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 862 EAQYEKLQETVATLKDTVVQE------------EEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKV 929
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSripeiqaelsklEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 930 ALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLN 1009
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1010 KERKNQEEQNKKLTEDlqaaEEQNLAANKLKAKL------MQSLED----SEQTMEREKRNRADMDKNKRKAEGELKIAQ 1079
Cdd:TIGR02169 931 EELSEIEDPKGEDEEI----PEEELSLEDVQAELqrveeeIRALEPvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
250
....*....|...
gi 25150292 1080 ETLEELNKSKSDA 1092
Cdd:TIGR02169 1007 ERIEEYEKKKREV 1019
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
971-1175 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 971 QDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSL--- 1047
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1048 -------------EDSEQTMEREKRNRADMDKNKRKAEgELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQ 1114
Cdd:COG3883 99 ggsvsyldvllgsESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1115 AAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAA 1175
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1745-1907 |
1.80e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1745 QLDNEIALLNSDIAEAHTELSASEDRgrraasdAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMkgg 1824
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDE-------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1825 akAIQKAEQrLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQ 1904
Cdd:COG1579 84 --NVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
...
gi 25150292 1905 ANS 1907
Cdd:COG1579 161 LEA 163
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1093-1558 |
4.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1093 ENALRRKETELHTL-GMKLEDEQAAVAKLQKGIQQDEARvkdlHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQAR 1171
Cdd:COG4717 48 LERLEKEADELFKPqGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1172 ATAAQielgkKKDAELTKLRRDLEEsglkFGEQLTVLKKKgsdaIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAAL 1251
Cdd:COG4717 124 LLQLL-----PLYQELEALEAELAE----LPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1252 DQEAklradqERIAKGYEvrllELRLKADEQSRQLQdfvsskgRLNSENSDLARQVEELEAKIQAANRLK---------- 1321
Cdd:COG4717 191 EEEL------QDLAEELE----ELQQRLAELEEELE-------EAQEELEELEEELEQLENELEAAALEErlkearllll 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1322 -----LQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGL 1396
Cdd:COG4717 254 iaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1397 IGADEFDEVKKRQNQKTSEIQDALDACN-AKIVALENARSRLTAEADANRLEA-EHHAQAVSSLEKKQKAFDKVIDEWKK 1474
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEeLQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1475 KVDDLYLELDGAQRDarQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESlseggratHALSKNLRRLEMEKE 1554
Cdd:COG4717 414 LLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKA 483
|
....
gi 25150292 1555 ELQR 1558
Cdd:COG4717 484 ELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1464-1685 |
4.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1464 AFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALS 1543
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1544 KNLRRLemeKEELQRGLDEAEAALESEESKALRCQIEVSQIR------AEIEKRIAEKEEEFENHRKVHQQTIDSIQATL 1617
Cdd:COG4942 97 AELEAQ---KEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1618 DSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFRE 1685
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1210 |
4.69e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASK 940
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 941 KLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNK 1020
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1021 KLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEEL--NKSKSDAENALRR 1098
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1099 KETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLadekdarqradrsradqqAEYDELTEQLEDqarataaQIE 1178
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI------------------EEKEKKISSLEK-------ELE 620
|
330 340 350
....*....|....*....|....*....|..
gi 25150292 1179 LGKKKDAELTKLRRDLEESGLKFGEQLTVLKK 1210
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1092-1318 |
5.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1092 AENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQAR 1171
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1172 ATAAQIELGKKKDAELT-----------KLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHM 1240
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1241 QREFDESSAALDQeakLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAAN 1318
Cdd:COG3883 174 EAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1653-1930 |
5.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1653 EDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNEL 1732
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1733 NS---QNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRaasdaaklAEDLRHEQEQSQQLERFKKQLESAVKDL 1809
Cdd:PRK03918 241 EElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1810 QERADAAEAAvmkggAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEfQVAEDKKNYDKLQ-------- 1881
Cdd:PRK03918 313 EKRLSRLEEE-----INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKkrltgltp 386
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 25150292 1882 ELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAE 1930
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1074-1275 |
6.07e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1074 ELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARqradrsra 1153
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1154 dqqaEYDELTEQLEDQARAtaaqielgkkkdaeltklRRDLEESGLKFGEQltvlkkkgsdaIQELSDQIEQLQKQKGRI 1233
Cdd:COG1579 90 ----EYEALQKEIESLKRR------------------ISDLEDEILELMER-----------IEELEEELAELEAELAEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 25150292 1234 EKEKGHMQREFDESSAALDQE-AKLRADQERIAKGYEVRLLEL 1275
Cdd:COG1579 137 EAELEEKKAELDEELAELEAElEELEAEREELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1594-1931 |
6.44e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1594 EKEEEFENHRKVHQQTIDSIQATLDS-ETKAKSELFRVKKKLEADINELEIALDHANKAN--------EDAQKNIRR--- 1661
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEFAKKkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVlekelkhlREALQQTQQsha 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1662 YLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEE---------LIVKLEALERARRVVESSVKEHQEHNNEL 1732
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERinrarkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1733 NS---QNVALAAAKSQLDNEIALLNSDIA-EAHTELSASEDRGRRAASDAAKlaEDLRHEQEQSQQLERFKKQLESAVKD 1808
Cdd:TIGR00618 324 AKllmKRAAHVKQQSSIEEQRRLLQTLHSqEIHIRDAHEVATSIREISCQQH--TLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1809 L-QERADAAEAAVM----------KGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLA-RADRKVREFEFQVAeDKKN 1876
Cdd:TIGR00618 402 LdILQREQATIDTRtsafrdlqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLqESAQSLKEREQQLQ-TKEQ 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1877 YDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQ 1931
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1407-1598 |
7.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1407 KRQNQKTSEIQDALDACNAKIVALENARSRLTAEADA-----NRLEAEHhAQAVSSLEKKQKAFDKVIDEWKKKVDDLYL 1481
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAAleaelAELEKEI-AELRAELEAQKEELAELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1482 ELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLD 1561
Cdd:COG4942 123 ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
|
170 180 190
....*....|....*....|....*....|....*..
gi 25150292 1562 EAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEE 1598
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1035-1805 |
8.51e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1035 AANKLKAKLMQSLEDSE-------QTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSdaenalrrketelhtlg 1107
Cdd:PRK10246 164 AKPKERAELLEELTGTEiygqisaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQ----------------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1108 mKLEDEQAAVAKLQKGIQQDEARVKDlHDQLADEKDARQRAdrsradqqaeydelteQLEDQARATAAQIELGKkkdAEL 1187
Cdd:PRK10246 227 -VLTDEEKQLLTAQQQQQQSLNWLTR-LDELQQEASRRQQA----------------LQQALAAEEKAQPQLAA---LSL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1188 TKLRRDLEESGLKFGEQLTVLKKKGSDaIQELSDQIEQLQKQKGRIEKekgHMQREFDESSAALDQEAKLRADQERIakg 1267
Cdd:PRK10246 286 AQPARQLRPHWERIQEQSAALAHTRQQ-IEEVNTRLQSTMALRARIRH---HAAKQSAELQAQQQSLNTWLAEHDRF--- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1268 yevrllelRLKADEQSRQLQDFvSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFS-NELDHAKRQAEEESRERQNLS 1346
Cdd:PRK10246 359 --------RQWNNELAGWRAQF-SQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTaDEVAAALAQHAEQRPLRQRLV 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1347 NLSKNLA---RELEQLKESIEdevagknEASRQLSKASVELDQWRTKFETegligadefdevkkrqnqKTSEIQDALDAC 1423
Cdd:PRK10246 430 ALHGQIVpqqKRLAQLQVAIQ-------NVTQEQTQRNAALNEMRQRYKE------------------KTQQLADVKTIC 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1424 N--AKIVALENARSRLTAEADANRLEAEHH--AQAVSSLEkkqkafdkvidewkkkVDDLYLELDGAQRDARQLSGEAHK 1499
Cdd:PRK10246 485 EqeARIKDLEAQRAQLQAGQPCPLCGSTSHpaVEAYQALE----------------PGVNQSRLDALEKEVKKLGEEGAA 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1500 LRGQHDTLADQVEGLRRENKSLSDETRDLTE---SLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALeseeskALR 1576
Cdd:PRK10246 549 LRGQLDALTKQLQRDESEAQSLRQEEQALTQqwqAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRH------ELQ 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1577 CQIE-----VSQIRAEIEKRIAEKEEEFeNHRKVHQQTIDSIQATL-DSETKAKSELFRVKK--KLEADINELEIALDHA 1648
Cdd:PRK10246 623 GQIAahnqqIIQYQQQIEQRQQQLLTAL-AGYALTLPQEDEEASWLaTRQQEAQSWQQRQNEltALQNRIQQLTPLLETL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1649 NKANEDAQKNIRRYLDQIRE--------------LQQTVDEEQKRREEFREHLLAAERKLAVAKQE-------QEELIVK 1707
Cdd:PRK10246 702 PQSDDLPHSEETVALDNWRQvheqclslhsqlqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQaflaallDEETLTQ 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1708 LEALERarrvvesSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRH 1787
Cdd:PRK10246 782 LEQLKQ-------NLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQ 854
|
810
....*....|....*...
gi 25150292 1788 EQEQSQQLERFKKQLESA 1805
Cdd:PRK10246 855 DADNRQQQQALMQQIAQA 872
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
868-1155 |
9.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 868 LQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEA 947
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 948 RAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQ 1027
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1028 AAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLG 1107
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25150292 1108 MKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQ 1155
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1219-1914 |
1.28e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1219 LSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKgyevrllELRLKADEQSRQLQDFVSskgrlns 1298
Cdd:pfam05483 76 LSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-------ELQFENEKVSLKLEEEIQ------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1299 ENSDLarqVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNlareleqlkesIEDEVAGKNEASRQLS 1378
Cdd:pfam05483 142 ENKDL---IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNN-----------IEKMILAFEELRVQAE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1379 KASVELdQWRTKFETEGLIGADEfdEVKKRQNQKTSEIQDALdacnAKIVALENARSRLTAEADANRleaehhaQAVSSL 1458
Cdd:pfam05483 208 NARLEM-HFKLKEDHEKIQHLEE--EYKKEINDKEKQVSLLL----IQITEKENKMKDLTFLLEESR-------DKANQL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1459 EKKQKAFDKVIDEWKKKVDDLYLELDGAQRdARQLSGEAHKlrgqhdTLADQVEGLRRENKSLSDETRDLTESLSEGgRA 1538
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLTKELEDIKM-SLQRSMSTQK------ALEEDLQIATKTICQLTEEKEAQMEELNKA-KA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1539 THALS-KNLRRLEMEKEELQRgldeaeaaleSEESKALRCQIEVSQIRAEIEKRIAEKEE--EFENHRKVHQQTIDSIQA 1615
Cdd:pfam05483 346 AHSFVvTEFEATTCSLEELLR----------TEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVELEELKKILA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1616 TLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNI-------RRYLDQIRELQQTVDEEQKRREEFREH-- 1686
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIELTAHcd 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1687 LLAAERKLAVA---------KQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDI 1757
Cdd:pfam05483 496 KLLLENKELTQeasdmtlelKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1758 AEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMK---GGAKAIQKAEQR 1834
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlelELASAKQKFEEI 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1835 LKAFQSDLE----TESRRAGEASKTLARADRKVRefeFQVAEDKKNYDKLQELVekltAKLKLQKKQLEEAEEQANSHLS 1910
Cdd:pfam05483 656 IDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVK---LQKEIDKRCQHKIAEMV----ALMEKHKHQYDKIIEERDSELG 728
|
....
gi 25150292 1911 KYRT 1914
Cdd:pfam05483 729 LYKN 732
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1622-1927 |
1.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1622 KAKSELFRVK-KKLEADINELEiALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAV---- 1696
Cdd:COG4717 53 KEADELFKPQgRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1697 -----AKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRG 1771
Cdd:COG4717 132 qeleaLEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1772 RRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRL-KAFQSDLETESRRAG 1850
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIaGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25150292 1851 EASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQanshLSKYRTVQLSLETAEERAD 1927
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEELEEELQ 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1446-1679 |
1.79e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1446 LEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDET 1525
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1526 RDLTESLSEggrATHALSKNLRRLEM--EKEELQRGLDEAEAALESEESKALRcqiEVSQIRAEIEKRIAEKEEEFENHR 1603
Cdd:COG4942 93 AELRAELEA---QKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLK---YLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1604 KVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKR 1679
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
929-1159 |
2.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 929 VALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENIskl 1008
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1009 nkerknqEEQNKKLTEDLQAAEEQNLAANKL--------------KAKLMQSLEDSEQ-TMEREKRNRADMDKNKRKAEG 1073
Cdd:COG3883 82 -------EERREELGERARALYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADAdLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1074 ELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRA 1153
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*.
gi 25150292 1154 DQQAEY 1159
Cdd:COG3883 235 AAAAAA 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
851-1359 |
2.31e-04 |
|
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: 46.50 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 851 KVKPLVNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETadllaQLEASKGSTREVEERmtamneqkva 930
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE-----QQLQTKEQIHLQETR---------- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 931 legkladaskKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSlrkveaeknakehqiRALQDEMRQQDENISKLNK 1010
Cdd:TIGR00618 488 ----------KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP---------------GPLTRRMQRGEQTYAQLET 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1011 ERKNQEEQNKKLTEDLQAAEEQnlaanklkaklMQSLEDSEQTM-EREKRNRADMDKNKRKAEGELKIAQETLEELNKSK 1089
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQ-----------MQEIQQSFSILtQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1090 SDAENALRRKETELHTLGMKLEDEQaavakLQKGIQQDEARVKDLHDQLADEkDARQRADRSRaDQQAEYDELTEQLEDQ 1169
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQ-----CSQELALKLTALHALQLTLTQE-RVREHALSIR-VLPKELLASRQLALQK 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1170 ARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHM--------Q 1241
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahF 764
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1242 REFDESSAAL---DQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFvssKGRLNSENSDLARQVEELEAKIqaan 1318
Cdd:TIGR00618 765 NNNEEVTAALqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD---EDILNLQCETLVQEEEQFLSRL---- 837
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 25150292 1319 RLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQL 1359
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1012-1557 |
2.31e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1012 RKNQEEQNKKLTEDLQAAEEQNLAA-NKLKAKLMQSLEDSEQTMEREKRNRadmdKNKRKAEG-ELKIAQETLEELNKSK 1089
Cdd:pfam07111 131 RKNLEEGSQRELEEIQRLHQEQLSSlTQAHEEALSSLTSKAEGLEKSLNSL----ETKRAGEAkQLAEAQKEAELLRKQL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1090 SDAENALRRKETELHTLgMKLEDEQAAVaklQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQ 1169
Cdd:pfam07111 207 SKTQEELEAQVTLVESL-RKYVGEQVPP---EVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1170 ARATAAQIELGKKKDAELTK----LRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFD 1245
Cdd:pfam07111 283 EEELTRKIQPSDSLEPEFPKkcrsLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1246 ESSAALDQE-AKLRADQERIAKGYEVRLLElRLKADEQSRQLQDFVSSkgrLNSENSDLARQVEELEakiQAANRLKlQF 1324
Cdd:pfam07111 363 DKAAEVEVErMSAKGLQMELSRAQEARRRQ-QQQTASAEEQLKFVVNA---MSSTQIWLETTMTRVE---QAVARIP-SL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1325 SNELDHAKRQaeeesrerqnLSNLSKNLARELeqlkesiedevagkneASRQLSKASVELDQWRTKFETEGLIgadEFDE 1404
Cdd:pfam07111 435 SNRLSYAVRK----------VHTIKGLMARKV----------------ALAQLRQESCPPPPPAPPVDADLSL---ELEQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1405 VKKRQNQKTSEIQdaldaCNAKIVALENARSRLTAEADANRLeAEHHAQAVSSLEKKQKAFDKVidewkkkvddlYLELD 1484
Cdd:pfam07111 486 LREERNRLDAELQ-----LSAHLIQQEVGRAREQGEAERQQL-SEVAQQLEQELQRAQESLASV-----------GQQLE 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1485 GAQRDARQLSGEAHKLRgQHDTLADQVEGLRRENK----------SLSDETRDLTESLSEGGRATHALSKNLRRLEMEKE 1554
Cdd:pfam07111 549 VARQGQQESTEEAASLR-QELTQQQEIYGQALQEKvaevetrlreQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKE 627
|
...
gi 25150292 1555 ELQ 1557
Cdd:pfam07111 628 RNQ 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1738-1941 |
2.47e-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: 45.53 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1738 ALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAE 1817
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1818 AAVMKGgAKAIQKAEQRLKA---FQSDLETESRRAGEASKTLARADRKvrefefQVAEDKKNYDKLQELVEKLTAKLKLQ 1894
Cdd:COG4942 104 EELAEL-LRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPARRE------QAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25150292 1895 KKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTR 1941
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
977-1145 |
2.77e-04 |
|
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: 45.81 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 977 LRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQ-AAEEQNLAANKLKaKLMQSLEDSEQTME 1055
Cdd:pfam10168 549 LKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEeIKDKQEKLMRRCK-KVLQRLNSQLPVLS 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1056 REKRnraDMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQaavAKLQKGIQQDEArvKDLH 1135
Cdd:pfam10168 628 DAER---EMKKELETINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQ---RKTIKEILKQLG--SEID 699
|
170
....*....|
gi 25150292 1136 DQLADEKDAR 1145
Cdd:pfam10168 700 ELIKQVKDIN 709
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
971-1145 |
2.96e-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: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 971 QDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQnlaANKLKAKLMQSLEDS 1050
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1051 E-QTMEREKrnrADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETElhtlgmkLEDEQAAVAKLQKGIQQDEA 1129
Cdd:COG1579 90 EyEALQKEI---ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE-------LEEKKAELDEELAELEAELE 159
|
170
....*....|....*.
gi 25150292 1130 RVKDLHDQLADEKDAR 1145
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1216-1379 |
3.24e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1216 IQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKgr 1295
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1296 lnsENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASR 1375
Cdd:COG1579 90 ---EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....
gi 25150292 1376 QLSK 1379
Cdd:COG1579 167 ELAA 170
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1585-1811 |
3.26e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1585 RAEIEKRI--AEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRY 1662
Cdd:PRK11281 38 EADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1663 LDQ--IRELQQTVDEEQKRREEFREHLLAAERKLAVAKQeqeelivkleALERARRVVESSVKEHQEHNNELNSQNVA-- 1738
Cdd:PRK11281 118 LSTlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT----------QPERAQAALYANSQRLQQIRNLLKGGKVGgk 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1739 --LAAAKSQLDNEIALLNsdiaeAHTELSASEDRGRRAASDAAKLAEDLRHEQEQsqqlerfkkQLESAVKDLQE 1811
Cdd:PRK11281 188 alRPSQRVLLQAEQALLN-----AQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---------RLEHQLQLLQE 248
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1662-1794 |
3.61e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1662 YLDQIRelQQTVDEEQKRREEfrehlLAAERKLAVAKQEQEELIV--------KLEALERARR----VVESSVKEHQEHN 1729
Cdd:PRK11637 163 YLNQAR--QETIAELKQTREE-----LAAQKAELEEKQSQQKTLLyeqqaqqqKLEQARNERKktltGLESSLQKDQQQL 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1730 NELNSqnvalaaaksqldNEIALLNSdIAEAHTELSAsedRGRRAASDAAKlaedLRHEQEQSQQ 1794
Cdd:PRK11637 236 SELRA-------------NESRLRDS-IARAEREAKA---RAEREAREAAR----VRDKQKQAKR 279
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1302-1517 |
3.64e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1302 DLARQVEELEAKIQAANRLK--LQFS-NELDHAKRQAEEE---SRERQNLSNLSKnLARELEQLKESIEDEVAGkneASR 1375
Cdd:COG0497 169 ALKKELEELRADEAERARELdlLRFQlEELEAAALQPGEEeelEEERRRLSNAEK-LREALQEALEALSGGEGG---ALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1376 QLSKASVELDQwrtkfetegLIGADE-FDEVKKRQNQKTSEIQDALDAcnakivaLENARSRLtaEADANRLEA-EHHAQ 1453
Cdd:COG0497 245 LLGQALRALER---------LAEYDPsLAELAERLESALIELEEAASE-------LRRYLDSL--EFDPERLEEvEERLA 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1454 AVSSLEKK-QKAFDKVI---DEWKKKVDdlylELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRE 1517
Cdd:COG0497 307 LLRRLARKyGVTVEELLayaEELRAELA----ELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
998-1344 |
3.86e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 998 MRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEdSEQTMEREKRNRADMDKNKrkaegelKI 1077
Cdd:PLN02939 37 ARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELP-QKSTSSDDDHNRASMQRDE-------AI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1078 AQETLEELNKSKSDAEnalrrketelhTLGMKLEDEQAAVAKLQKGIQQ-DEARVKDLHD--QLADEKDARQRadrsrad 1154
Cdd:PLN02939 109 AAIDNEQQTNSKDGEQ-----------LSDFQLEDLVGMIQNAEKNILLlNQARLQALEDleKILTEKEALQG------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1155 qqaEYDELTEQL-EDQARA-TAAQIELGKK-KDAELTKLRRDLEESG-------LKFGEQLTVLKKKG---SDAIQELSD 1221
Cdd:PLN02939 171 ---KINILEMRLsETDARIkLAAQEKIHVEiLEEQLEKLRNELLIRGateglcvHSLSKELDVLKEENmllKDDIQFLKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1222 QIEQLQKQKGRI---EKEKGHMQrefdesSAALDQEAKLRADQERIAK----GYEV---RLLELRLKADEQSRQLQDFVS 1291
Cdd:PLN02939 248 ELIEVAETEERVfklEKERSLLD------ASLRELESKFIVAQEDVSKlsplQYDCwweKVENLQDLLDRATNQVEKAAL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 25150292 1292 SKGRlnseNSDLARQVEELEAKIQAANRLKLQ-FSNELDHAKRQAEEESRERQN 1344
Cdd:PLN02939 322 VLDQ----NQDLRDKVDKLEASLKEANVSKFSsYKVELLQQKLKLLEERLQASD 371
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1478-1723 |
4.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1478 DLYLE--LDGAQRDARQ----LSGEAHKLRGQHDTLADQVEGLRRENK--SLSDETRDLTESLSEggrathaLSKNLRRL 1549
Cdd:COG3206 159 EAYLEqnLELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------LESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1550 EMEKEELQRGLDE--AEAALESEESKALRCQIEVSQIRAEI---EKRIAEKEEEF-ENHRKV--HQQTIDSIQATLDSET 1621
Cdd:COG3206 232 RAELAEAEARLAAlrAQLGSGPDALPELLQSPVIQQLRAQLaelEAELAELSARYtPNHPDViaLRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1622 KakselfRVKKKLEADINELEIALdhankanEDAQKNIRRYLDQIRELQQTVDEeqkrreefrehLLAAERKLAVAKQEQ 1701
Cdd:COG3206 312 Q------RILASLEAELEALQARE-------ASLQAQLAQLEARLAELPELEAE-----------LRRLEREVEVARELY 367
|
250 260
....*....|....*....|..
gi 25150292 1702 EELIVKLEALERARRVVESSVK 1723
Cdd:COG3206 368 ESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1455-1939 |
4.52e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1455 VSSLEKKQKAFDKVIDEWKKKV---DDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTES 1531
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEIsniDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1532 LSEggraTHALSKNLRRLEMEKEELQRGLDEAEAALESEEskalrcQIEVSQIRAEIEKRIAeKEEEFENHRKVHQQTID 1611
Cdd:PRK01156 241 LNE----LSSLEDMKNRYESEIKTAESDLSMELEKNNYYK------ELEERHMKIINDPVYK-NRNYINDYFKYKNDIEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1612 --SIQATLDSETKAKSELFRVKKKLEADINELEIA------LDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRRE-- 1681
Cdd:PRK01156 310 kkQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKksryddLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErm 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1682 --EFREHLLAAERKLAVAKQEQEELIVKLE-------ALERARRVVESSVKEHQEHNNELNSQNVA------LAAAKSQ- 1745
Cdd:PRK01156 390 saFISEILKIQEIDPDAIKKELNEINVKLQdisskvsSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttLGEEKSNh 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1746 ----LDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLA-EDLRHEQEQSQQLERFKKQLESAVKDLQERADA---AE 1817
Cdd:PRK01156 470 iinhYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLEDIKIKINELKDKhdkYE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1818 AAVMKGGAKAIQKAEQRLKAFQS--------DLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVE---- 1885
Cdd:PRK01156 550 EIKNRYKSLKLEDLDSKRTSWLNalavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEnean 629
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1886 ------KLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSR 1939
Cdd:PRK01156 630 nlnnkyNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKA 689
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1274-1528 |
4.72e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1274 ELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQaanrlklQFSNELDHAKRQAEEESRERQNLSNLSKNLA 1353
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-------ELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1354 RELEQLKESIED---EVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEfDEVKKRQNQKTSEIQDALDACNAKIVAL 1430
Cdd:COG1340 85 EKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE-KELVEKIKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1431 EnarsrLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQ 1510
Cdd:COG1340 164 E-----LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|....*...
gi 25150292 1511 VEGLRRENKSLSDETRDL 1528
Cdd:COG1340 239 LRELRKELKKLRKKQRAL 256
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
860-1176 |
4.74e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTV------VQEEEKKRQLQEGAERLNKET------------ADL---LAQLEASKGSTREVE 918
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVaeatkkVEEAEKKAKDQKEEDRRNYPTntyktleleiaeSDVevkKAELELVKEEAKEPR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 919 ERMTaMNEQKVALEGKLADAS--KKLEVEEARAVEINKQK---KLVEAECADLKKNCQDVDLSLRK-----VEAEKNAKE 988
Cdd:NF033838 202 DEEK-IKQAKAKVESKKAEATrlEKIKTDREKAEEEAKRRadaKLKEAVEKNVATSEQDKPKRRAKrgvlgEPATPDKKE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 989 HQIRALQDEMRQQDENISKLNKERKNQE-----EQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMERE------ 1057
Cdd:NF033838 281 NDAKSSDSSVGEETLPSPSLKPEKKVAEaekkvEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAElelvke 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1058 --KRNRADMDKNKRKAEGELKIAQET-LEELNKSKSDAENALRRKETELHTLGMK-LEDEQAAVAKlqkgiQQDEARVKD 1133
Cdd:NF033838 361 eaKEPRNEEKIKQAKAKVESKKAEATrLEKIKTDRKKAEEEAKRKAAEEDKVKEKpAEQPQPAPAP-----QPEKPAPKP 435
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 25150292 1134 lhdqladEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQ 1176
Cdd:NF033838 436 -------EKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQQ 471
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1005-1254 |
4.86e-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: 44.42 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1005 ISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSE-QTMEREKRNraDMDKNKRKAEGELKIAQETLE 1083
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEkQLLELTRVN--ELLKAKFSEDGTQKKMSSLSM 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1084 ELNKSKSdaenalrRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRaDRSRADQQAEYDE-- 1161
Cdd:pfam15905 160 ELMKLRN-------KLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE-EKSETEKLLEYITel 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1162 --LTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESglkfgeqltvlkkkgsdaIQELSDQIEQLQKQKGRIEKEKGH 1239
Cdd:pfam15905 232 scVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEK------------------EQELSKQIKDLNEKCKLLESEKEE 293
|
250
....*....|....*
gi 25150292 1240 MQREFDESSAALDQE 1254
Cdd:pfam15905 294 LLREYEEKEQTLNAE 308
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1819 |
5.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1663 LDQIRELQQT---VDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQnvaL 1739
Cdd:COG1579 6 LRALLDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1740 AAAKSQ-----LDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLrheQEQSQQLERFKKQLESAVKDLQERAD 1814
Cdd:COG1579 83 GNVRNNkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELE 159
|
....*
gi 25150292 1815 AAEAA 1819
Cdd:COG1579 160 ELEAE 164
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
880-1817 |
6.60e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 880 VQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLE-VEEARAveinKQKKL 958
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlVQTALR----QQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 959 VEAEcADLKKncqdvdLSLRKVEAEknakehQIRALQDEmrQQDENisklnkerknqEEQnkkltedLQAAEEQNLAANK 1038
Cdd:PRK04863 351 ERYQ-ADLEE------LEERLEEQN------EVVEEADE--QQEEN-----------EAR-------AEAAEEEVDELKS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1039 LKAKLMQSLeDSEQTMEREKRN--RAdmdknKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAA 1116
Cdd:PRK04863 398 QLADYQQAL-DVQQTRAIQYQQavQA-----LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1117 VAKLQKGIQqdearvkdLHDQLADEkdarqrADRSRADQQAEydELTEQLEDQaRATAAQIElgkKKDAELTKLRRDLEE 1196
Cdd:PRK04863 472 HSQFEQAYQ--------LVRKIAGE------VSRSEAWDVAR--ELLRRLREQ-RHLAEQLQ---QLRMRLSELEQRLRQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1197 SglkfgeqltvlkkkgsdaiQELSDQIEQLQKQKGRiekekghmqrefDESSAALDQEakLRADQERIAKGYEVRLLELR 1276
Cdd:PRK04863 532 Q-------------------QRAERLLAEFCKRLGK------------NLDDEDELEQ--LQEELEARLESLSESVSEAR 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1277 LKADEQSRQLQDfvsskgrLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAkrqaeeesrerQNLSNLSKNLA--- 1353
Cdd:PRK04863 579 ERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-----------QDVTEYMQQLLere 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1354 RELEQLKESIEDEVAGKNEASRQLSKAS-VELDQWRTKFET-EGLIGADEFDEVkkrqnqktsEIQDAL-------DACN 1424
Cdd:PRK04863 641 RELTVERDELAARKQALDEEIERLSQPGgSEDPRLNALAERfGGVLLSEIYDDV---------SLEDAPyfsalygPARH 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1425 AKIVA-LENARSRLTAEADA----------------NRLEAEHHAQAVSslekkqkafDKVID-EWK-KKVDDLYLeLDG 1485
Cdd:PRK04863 712 AIVVPdLSDAAEQLAGLEDCpedlyliegdpdsfddSVFSVEELEKAVV---------VKIADrQWRySRFPEVPL-FGR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1486 AQRDAR--QLSGEAHKLRGQHDTLADQVEGLRRENKSLSD----------------ETRDLTESLSEGGRATHALSKNLR 1547
Cdd:PRK04863 782 AAREKRieQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigshlavafeadpeaELRQLNRRRVELERALADHESQEQ 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1548 RLEMEKEELQRGLDEAEaaleseeskalRCQIEVSQIRAE-IEKRIAEKEEEFENhrkvhqqtIDSIQATLDSETKAKSE 1626
Cdd:PRK04863 862 QQRSQLEQAKEGLSALN-----------RLLPRLNLLADEtLADRVEEIREQLDE--------AEEAKRFVQQHGNALAQ 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1627 LFRVKKKLEADINELEiALDHANKANEDAQKNIRRYLDQIRELQQtvdeeqkRREEFREHllAAERKLAVAKQEQEELIV 1706
Cdd:PRK04863 923 LEPIVSVLQSDPEQFE-QLKQDYQQAQQTQRDAKQQAFALTEVVQ-------RRAHFSYE--DAAEMLAKNSDLNEKLRQ 992
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1707 KLEALERARRVVESSVKEHQehnNELNSQNVALAAAKSQLDNEIALLnsdiAEAHTELS-----ASEDRGRRAASDAAKL 1781
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQ---AQLAQYNQVLASLKSSYDAKRQML----QELKQELQdlgvpADSGAEERARARRDEL 1065
|
970 980 990
....*....|....*....|....*....|....*.
gi 25150292 1782 AEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAE 1817
Cdd:PRK04863 1066 HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1665-1889 |
7.16e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1665 QIRELQQTVDEEQKRREEfrehllaaerklavakQEQEelivKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKs 1744
Cdd:PRK09510 88 QAEELQQKQAAEQERLKQ----------------LEKE----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1745 qldneiallnsdiAEAHTELSASEDRGRRAASDAAKLAEdlrhEQEQSQQLERFKKQLESAVKdlqerADAAEAAVMKGG 1824
Cdd:PRK09510 147 -------------AKAEAEAKRAAAAAKKAAAEAKKKAE----AEAAKKAAAEAKKKAEAEAA-----AKAAAEAKKKAE 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1825 AKAIQKAEQRLKAfQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTA 1889
Cdd:PRK09510 205 AEAKKKAAAEAKK-KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDS 268
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1690-1931 |
1.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1690 AERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEhnnELNSQNVALAAAKSQLDNeialLNSDIAEAHTELSASED 1769
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK----LQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1770 rgrraasdaaKLAEDLRHEQEQSQQLERFKKQLESA-VKDLQERADA------AEAAVMKGGAKAIQKAEQRLKAFQSDL 1842
Cdd:COG3883 87 ----------ELGERARALYRSGGSVSYLDVLLGSEsFSDFLDRLSAlskiadADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1843 ETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETA 1922
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*....
gi 25150292 1923 EERADSAEQ 1931
Cdd:COG3883 237 AAAAAAAAS 245
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
878-1560 |
1.12e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 878 TVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINK-QK 956
Cdd:COG3096 341 TALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQaVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 957 KLVEAecadlKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISkLNKERKNQEEQNKKLTEDLQAAEEQNLAA 1036
Cdd:COG3096 421 ALEKA-----RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS-VADAARRQFEKAYELVCKIAGEVERSQAW 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1037 NKLKAKLMQ--SLEDSEQTMEREKRNRADMdknkRKAEGELKIAQETLEELNKSKS-------DAENALRRKETELHTLG 1107
Cdd:COG3096 495 QTARELLRRyrSQQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGqqldaaeELEELLAELEAQLEELE 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1108 MKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSR-------ADQQAEYDELTEQLEDQARATAAQIELG 1180
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLReqsgealADSQEVTAAMQQLLEREREATVERDELA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1181 KKKDAELTKLRRDLEESGLKFGEQLTVLKKKG-------------SDA---------------IQELSDQIEQLQKQKG- 1231
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALAERLGgvllseiyddvtlEDApyfsalygparhaivVPDLSAVKEQLAGLEDc 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1232 -----RIEKEkghmQREFDESSAALDQE-----AKLRADQERIAK----------GYEVRLLELRLKADEQSRQ------ 1285
Cdd:COG3096 731 pedlyLIEGD----PDSFDDSVFDAEELedavvVKLSDRQWRYSRfpevplfgraAREKRLEELRAERDELAEQyakasf 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1286 ----LQDFVSSKGRLNSENSDLARQvEELEAKIQAANRLKLQFSNEL------DHAKRQAEEESRERQNLSN----LSKN 1351
Cdd:COG3096 807 dvqkLQRLHQAFSQFVGGHLAVAFA-PDPEAELAALRQRRSELERELaqhraqEQQLRQQLDQLKEQLQLLNkllpQANL 885
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1352 LARE-LEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETeglIGAD--EFDEVKkrqnQKTSEIQDALDACNAKIV 1428
Cdd:COG3096 886 LADEtLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAV---LQSDpeQFEQLQ----ADYLQAKEQQRRLKQQIF 958
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1429 ALENARSRLT--AEADANRLEAEHhaqavSSLEKKQKAFDKVIDEWKKKVDDlylELDGAQRDARQLSGEAHKLRGQHDT 1506
Cdd:COG3096 959 ALSEVVQRRPhfSYEDAVGLLGEN-----SDLNEKLRARLEQAEEARREARE---QLRQAQAQYSQYNQVLASLKSSRDA 1030
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150292 1507 LADQVEGLRRENKSLS------------DETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGL 1560
Cdd:COG3096 1031 KQQTLQELEQELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
996-1230 |
1.15e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 996 DEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLaanklkAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGEL 1075
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQ------KELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1076 KIAQEtleelNKSKSDAENALRRKEtelhTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLAdEKDARQRADRSRADQ 1155
Cdd:TIGR02794 127 KQAAE-----AKAKAEAEAERKAKE----EAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA-KAEAEAKAKAEEAKA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1156 QAEYDELTEQLEDQARATAAQIELG----KKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQK 1230
Cdd:TIGR02794 197 KAEAAKAKAAAEAAAKAEAEAAAAAaaeaERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
742-1196 |
1.39e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 742 ESIIGKTDAKKGSALMlaRLVKEKKLEEENFRVGLTKVFFKAG-IVAHLEDLRD-QSLAQLITGLQAQIRWYYQTIERKR 819
Cdd:PRK01156 255 ESEIKTAESDLSMELE--KNNYYKELEERHMKIINDPVYKNRNyINDYFKYKNDiENKKQILSNIDAEINKYHAIIKKLS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 820 RVEKITALKIIQRnirswaelrtwvwfKLYGKVKPLVNSGK-IEAQYEKLQETVATLKDTVVQEE-EKKRQLQEGAERLN 897
Cdd:PRK01156 333 VLQKDYNDYIKKK--------------SRYDDLNNQILELEgYEMDYNSYLKSIESLKKKIEEYSkNIERMSAFISEILK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 898 KETAD---LLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKncqDVD 974
Cdd:PRK01156 399 IQEIDpdaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN---HYN 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 975 LSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAA------EEQNLAANKLKAKLMQS-- 1046
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADledikiKINELKDKHDKYEEIKNry 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1047 ----LEDSEQTMER-----EKRNRADMDKN-KRKAEGELKI------AQETLEELNKSKSDAENALRRKETELHTLGMK- 1109
Cdd:PRK01156 556 kslkLEDLDSKRTSwlnalAVISLIDIETNrSRSNEIKKQLndlesrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKy 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1110 --LEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARaTAAQIELGKKKDAEL 1187
Cdd:PRK01156 636 neIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-LESTIEILRTRINEL 714
|
....*....
gi 25150292 1188 TKLRRDLEE 1196
Cdd:PRK01156 715 SDRINDINE 723
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1065-1459 |
1.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1065 DKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETElhtlgmklEDEQAAVAKLQKGIQQDEARVKDLHDQL---ADE 1141
Cdd:COG5185 156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGIS--------ELKKAEPSGTVNSIKESETGNLGSESTLlekAKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1142 KDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSD 1221
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1222 Q--IEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEvrllelRLKAD-EQSRQLQDFVSSKGRLNS 1298
Cdd:COG5185 308 KkaTESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLE------AIKEEiENIVGEVELSKSSEELDS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1299 ENSDLARQVEELEAKIQAANRLKLQFSneldhakrqaeeesrerQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLS 1378
Cdd:COG5185 382 FKDTIESTKESLDEIPQNQRGYAQEIL-----------------ATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLN 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1379 KASVELDQWRTKFETEGLIGADEfdevkkRQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSL 1458
Cdd:COG5185 445 ELISELNKVMREADEESQSRLEE------AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
.
gi 25150292 1459 E 1459
Cdd:COG5185 519 L 519
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
841-947 |
1.50e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 841 RTWVWF-KLYGK-----VKPLVNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETA---DLLAQLEASK 911
Cdd:PRK11448 114 RLAVWFhRTYGKdwdfkPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValeGLAAELEEKQ 193
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 25150292 912 GSTREVEERMTAMNEQKVALEGK-----LADASKKLEVEEA 947
Cdd:PRK11448 194 QELEAQLEQLQEKAAETSQERKQkrkeiTDQAAKRLELSEE 234
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1207-1368 |
1.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1207 VLKKKGSDAIQELSDQIEQLQKQKGRIEKEKghmqrefdeSSAALDQEAKLRADQERiakgyevrllELRLKADEQSRQL 1286
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEA---------LLEAKEEIHKLRNEFEK----------ELRERRNELQKLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1287 QDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARE--LEQLKESIE 1364
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEEAR 168
|
....
gi 25150292 1365 DEVA 1368
Cdd:PRK12704 169 HEAA 172
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1006-1336 |
1.82e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 43.30 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1006 SKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKlmQSLEDSEQTMereKRNRADMDKNkRKAEGELKiaqetlEEL 1085
Cdd:pfam09726 358 SSSSKNSKKQKGPGGKSGARHKDPAENCIPNNQLSKP--DALVRLEQDI---KKLKAELQAS-RQTEQELR------SQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1086 NkSKSDAENALRrkeTELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQaEYDELTEQ 1165
Cdd:pfam09726 426 S-SLTSLERSLK---SELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEA 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1166 LEDQARATAAQIElgkkkdaeltklrrdleesglkfGEQLTVLKKKgsdaIQELSDQIEQLQKqkgriekekghmqrefd 1245
Cdd:pfam09726 501 TAARAVALAAASR-----------------------GECTESLKQR----KRELESEIKKLTH----------------- 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1246 essaaldqEAKLRADQeriAKGYEVRLLELRlKADEQSRQLQDFVSSKGRLNSENsdlarqvEELEAKIQAANRLKLQFS 1325
Cdd:pfam09726 537 --------DIKLKEEQ---IRELEIKVQELR-KYKESEKDTEVLMSALSAMQDKN-------QHLENSLSAETRIKLDLF 597
|
330
....*....|.
gi 25150292 1326 NELDHAKRQAE 1336
Cdd:pfam09726 598 SALGDAKRQLE 608
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1203-1386 |
1.96e-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: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1203 EQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQ-EAKLRADQERIAK--------GYEVRLL 1273
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGEraralyrsGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1274 ELRLkadeQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLA 1353
Cdd:COG3883 106 DVLL----GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|...
gi 25150292 1354 RELEQLKESIEDEVAGKNEASRQLSKASVELDQ 1386
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1001-1138 |
1.97e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.13 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1001 QDENISkLNKERKNQEEQNKKLTEDLQAAEEQNlaanklkAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQE 1080
Cdd:pfam05911 680 TEENKR-LKEEFEQLKSEKENLEVELASCTENL-------ESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAE 751
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 25150292 1081 TLEELNKSKSDAENALRRKETELHTLGMKLEDEQaavaklqKGIQQDEARVKDLHDQL 1138
Cdd:pfam05911 752 SYEDLETRLTELEAELNELRQKFEALEVELEEEK-------NCHEELEAKCLELQEQL 802
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1185-1558 |
2.01e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1185 AELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEkekghmQREFDESSAaldqEAKLRADQERi 1264
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR------LLEKREAEA----EEALREQAEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1265 AKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQN 1344
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1345 LSNLSKNLARELEQLKEsIEDEVAGKNEASRQLSKASVELDQWRtkfETEGLIGADEFDEVKKRQNQKTSEIqdaldacn 1424
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKE-LEFEIQSQEQDSEIVKNSKSELARIP---ELEKELERLREHNKHLNENIENKLL-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1425 akivaLENARSRLTAeadanRLEAEHHAQA-VSSLEKKQKAFDKVIDEWKKKVDDLYLELdgaqRDARQLSGEAHKLRGQ 1503
Cdd:pfam05557 226 -----LKEEVEDLKR-----KLEREEKYREeAATLELEKEKLEQELQSWVKLAQDTGLNL----RSPEDLSRRIEQLQQR 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1504 HDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQR 1558
Cdd:pfam05557 292 EIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1622-1906 |
2.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1622 KAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQ 1701
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1702 EELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKL 1781
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1782 AEDLRHEQEqsQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADR 1861
Cdd:COG4372 170 EQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 25150292 1862 KVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQAN 1906
Cdd:COG4372 248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1059-1901 |
2.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1059 RNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAkLQKGIQQDEARVKDLHDQL 1138
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR-QQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1139 ADEKDARQRAD------RSRADQ-QAEYDELTEQLEDQARAtaaqIELGKKKDAELTKLRRDLEESglkfgEQLTVLKkk 1211
Cdd:PRK04863 365 EEQNEVVEEADeqqeenEARAEAaEEEVDELKSQLADYQQA----LDVQQTRAIQYQQAVQALERA-----KQLCGLP-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1212 gSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEvrllelRLKADEQSRQLQdfvs 1291
Cdd:PRK04863 434 -DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVS------RSEAWDVARELL---- 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1292 skgRLNSENSDLARQVEELEAKIQAANRlKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKN 1371
Cdd:PRK04863 503 ---RRLREQRHLAEQLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1372 EASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSrLTAEADANRLEAEHH 1451
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERE-LTVERDELAARKQAL 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1452 AQAVSSLEKKQKAFDKVIDEWKKKV---------DDLYLE-------LDGAQRDA---RQLSGEAHKLRGQHDTLAD--Q 1510
Cdd:PRK04863 658 DEEIERLSQPGGSEDPRLNALAERFggvllseiyDDVSLEdapyfsaLYGPARHAivvPDLSDAAEQLAGLEDCPEDlyL 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1511 VEGlrrenkslsdetrDLTeSLSEGGrathalsknlrrleMEKEELQRGLdeaeaaLESEESKALRcqieVSQI------ 1584
Cdd:PRK04863 738 IEG-------------DPD-SFDDSV--------------FSVEELEKAV------VVKIADRQWR----YSRFpevplf 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1585 -RAEIEKRIAEkeeefenhrkvhqqtidsiqatLDSETKAKSELFrvkKKLEADINELEIALDHANKA------------ 1651
Cdd:PRK04863 780 gRAAREKRIEQ----------------------LRAEREELAERY---ATLSFDVQKLQRLHQAFSRFigshlavafead 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1652 NEDAQKNIRRYLDQI-RELQQTVDEEQKRREEF---REHLLAAERKLAVAK--------QEQEELIVKLEALERARRVVE 1719
Cdd:PRK04863 835 PEAELRQLNRRRVELeRALADHESQEQQQRSQLeqaKEGLSALNRLLPRLNlladetlaDRVEEIREQLDEAEEAKRFVQ 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1720 -------------SSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLnSDIAEAHTELSASEDRGRRAASDAA--KLAED 1784
Cdd:PRK04863 915 qhgnalaqlepivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHFSYEDAAEMLAKNSDLneKLRQR 993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1785 LRH-EQEQSQQLERFKKQ-------------LESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETEsrrag 1850
Cdd:PRK04863 994 LEQaEQERTRAREQLRQAqaqlaqynqvlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHAR----- 1068
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1851 easktLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEA 1901
Cdd:PRK04863 1069 -----LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1241-1837 |
2.41e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1241 QREFDESSAALDQE-AKLRADQERIAKGYEVRL-------------LELRLKADEQ------SRQLQDFVSSKGRLNS-- 1298
Cdd:NF041483 166 RRLLDESRAEAEQAlAAARAEAERLAEEARQRLgseaesaraeaeaILRRARKDAErllnaaSTQAQEATDHAEQLRSst 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1299 -ENSDLAR-QVEEL----EAKIQAANRLKLQFSNELDH---------AKRQAEEESRERQNLSNLSKNLAReleQLKESI 1363
Cdd:NF041483 246 aAESDQARrQAAELsraaEQRMQEAEEALREARAEAEKvvaeakeaaAKQLASAESANEQRTRTAKEEIAR---LVGEAT 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1364 EDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSE---IQDALDACNAKIVALENA-RSRLTA 1439
Cdd:NF041483 323 KEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEevlTKASEDAKATTRAAAEEAeRIRREA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1440 EADANRLEAEHHAQAvsslEKKQKAFDKVIDEWKKKVDDLyleldgaQRDARQLSGEAHKLRGQHDTLADQVEG-LRREN 1518
Cdd:NF041483 403 EAEADRLRGEAADQA----EQLKGAAKDDTKEYRAKTVEL-------QEEARRLRGEAEQLRAEAVAEGERIRGeARREA 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1519 KSLSDETRDLTESLSEGGRATHALSKNLRRLEMEK---EELQRGldeaeaaleseesKALRCQIE--VSQIRAEIEKRIA 1593
Cdd:NF041483 472 VQQIEEAARTAEELLTKAKADADELRSTATAESERvrtEAIERA-------------TTLRRQAEetLERTRAEAERLRA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1594 EKEEEFENHRKVHQQTI-----DSIQATLDSETKAKSELFRVKKKLEADINELEIALDHA--------NKANEDAQKNIR 1660
Cdd:NF041483 539 EAEEQAEEVRAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAraeaerirREAAEETERLRT 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1661 RYLDQIRELQQTVDEEQKR-REEfrehlLAAERKLAVAKQEQEELIVKLEALERARRVvessVKEHQEHNNELNSQNVAL 1739
Cdd:NF041483 619 EAAERIRTLQAQAEQEAERlRTE-----AAADASAARAEGENVAVRLRSEAAAEAERL----KSEAQESADRVRAEAAAA 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1740 AAAKSqldneiallnsdiAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQqlERFKKQLESAVKDLQERADAAEAA 1819
Cdd:NF041483 690 AERVG-------------TEAAEALAAAQEEAARRRREAEETLGSARAEADQER--ERAREQSEELLASARKRVEEAQAE 754
|
650
....*....|....*...
gi 25150292 1820 VMKGGAKAIQKAEQRLKA 1837
Cdd:NF041483 755 AQRLVEEADRRATELVSA 772
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
860-1059 |
2.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKgstREVEERMTAMNEQK-------VALE 932
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERARALYRSGgsvsyldVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 933 GK-LADASKKLE----VEEARAVEINKQKKLVEAecadLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISK 1007
Cdd:COG3883 111 SEsFSDFLDRLSalskIADADADLLEELKADKAE----LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 25150292 1008 LNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKR 1059
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1005-1177 |
2.62e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1005 ISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIA-QETLE 1083
Cdd:PRK12705 22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDArAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1084 ELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAklqkGIQQDEAR---VKDLHDQLADEKDARQRADRSRADQQAEYD 1160
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVA----GLTPEQARkllLKLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
170 180
....*....|....*....|
gi 25150292 1161 E---LTEQLEDQARATAAQI 1177
Cdd:PRK12705 178 AqniLAQAMQRIASETASDL 197
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1007-1239 |
2.73e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1007 KLNKER-KNQEEQNKKLTEDLQAAEEQNlaanKLKAKLMQSLEdsEQTMEREKRNRADMDKNKRKAE---GELKIAQETL 1082
Cdd:PHA02562 170 KLNKDKiRELNQQIQTLDMKIDHIQQQI----KTYNKNIEEQR--KKNGENIARKQNKYDELVEEAKtikAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1083 EELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKG---------IQQDEARVKDLHD-------QLADEKDARQ 1146
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDklkelqhSLEKLDTAID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1147 RADR---SRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELtklrrdleesglkfgEQLTVLKKKGSDAIQELSDQI 1223
Cdd:PHA02562 324 ELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI---------------EELQAEFVDNAEELAKLQDEL 388
|
250
....*....|....*.
gi 25150292 1224 EQLQKQKGRIEKEKGH 1239
Cdd:PHA02562 389 DKIVKTKSELVKEKYH 404
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1109-1319 |
2.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1109 KLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEdqarATAAQIElgkKKDAELT 1188
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----EAEAEIE---ERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1189 KLRRDLEESGLKFGEQLTVLkkkGSDAIQELSDQIEQLQkqkgRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGY 1268
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1269 EVRLLELRLKADEQSRQLQDFVSskgRLNSENSDLARQVEELEAKIQAANR 1319
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLA---QLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1280-1365 |
2.99e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1280 DEQSRQLQDFVsskGRLNSENSDLARQVEELEAKIQaanrlKLQfsNELDHAKRQAEEESRERQNLSNLS---KNLAREL 1356
Cdd:COG2433 412 EEEIRRLEEQV---ERLEAEVEELEAELEEKDERIE-----RLE--RELSEARSEERREIRKDREISRLDreiERLEREL 481
|
....*....
gi 25150292 1357 EQLKESIED 1365
Cdd:COG2433 482 EEERERIEE 490
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1581-1728 |
3.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1581 VSQIRAEIEKRIAEKEEEFENHRKvhqqtidsiqatlDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIR 1660
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKK-------------EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1661 RYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEAL--ERARRVVESSVKEHQEH 1728
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaEEAKEILLEKVEEEARH 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1776-1946 |
3.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1776 SDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKT 1855
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1856 LARADRKVREFEFQVAEDKknYDKLQELvekltaklklqKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVR 1935
Cdd:COG4913 318 LDALREELDELEAQIRGNG--GDRLEQL-----------EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170
....*....|.
gi 25150292 1936 IRSRTRANAEQ 1946
Cdd:COG4913 385 LRAEAAALLEA 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1485-1939 |
3.25e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1485 GAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQ------- 1557
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRnqlqntv 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1558 ------RGLDEAEAALESEESKALRCQI--------EVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDS----IQATLDS 1619
Cdd:pfam15921 152 heleaaKCLKEDMLEDSNTQIEQLRKMMlshegvlqEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSaiskILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1620 E-TKAKSELFRVKKKLEAdineleialdhankANEDAQKNIRRYLDQIRE-LQQTVDEEQKRREEFREHLLAAeRKLAVA 1697
Cdd:pfam15921 232 EiSYLKGRIFPVEDQLEA--------------LKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSA-RSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1698 KQEQEELIvkleaLERARRVVESSVKEHQEHNNELNSQNVALAAAK-------SQLDNEIALLNSDIAEAHTELSAS--- 1767
Cdd:pfam15921 297 IQSQLEII-----QEQARNQNSMYMRQLSDLESTVSQLRSELREAKrmyedkiEELEKQLVLANSELTEARTERDQFsqe 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1768 ----EDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVmkggakaiQKAEQRLKAFQSDLE 1843
Cdd:pfam15921 372 sgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV--------QRLEALLKAMKSECQ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1844 TESRRAGEASKTLARADRKVREFEFQVAEDKknyDKLQELVEKLTAklklqKKQLEEAEEQANSHLSKyrtvqlSLETAE 1923
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTK---EMLRKVVEELTA-----KKMTLESSERTVSDLTA------SLQEKE 509
|
490
....*....|....*.
gi 25150292 1924 ERADSAEQCLVRIRSR 1939
Cdd:pfam15921 510 RAIEATNAEITKLRSR 525
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
875-1142 |
3.53e-03 |
|
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: 42.65 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 875 LKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINK 954
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 955 QKKLVEAECADLKKNCQDVDLSLRKVEAEK--NAKEHQIRALQDEMRQQDENISK---LNKERKNQEEQNKKLTEDLQAA 1029
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEelLQELLLKEEELEEQKLKDELESKeekEKEEKKELEEESQKLNLLEEKE 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1030 EEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMK 1109
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
250 260 270
....*....|....*....|....*....|...
gi 25150292 1110 LEDEQAAVAKLQKGIQQDEARVKDLHDQLADEK 1142
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1548-1817 |
3.66e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1548 RLEMEKEELQRGLDEAEAALESEesKALRCQIE-VSQIRAEIEKRIAEKEEEFENHR---------KVHQQTIDSIQAT- 1616
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAE--KARQAEMDrQAAIYAEQERMAMERERELERIRqeerkreleRIRQEEIAMEISRm 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1617 -----LDSETKAKSElfRVKKKLEA--DINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLA 1689
Cdd:pfam17380 378 relerLQMERQQKNE--RVRQELEAarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1690 AERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEH---NNELNSQNVALAAAKsqldNEIALLNSDIAEAHTELSA 1766
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilEKELEERKQAMIEEE----RKRKLLEKEMEERQKAIYE 531
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1767 SEDRgrraasdaaKLAEDLRHEQEQSQQLERFKKQLESAVKDlQERADAAE 1817
Cdd:pfam17380 532 EERR---------REAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAME 572
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
861-1091 |
3.85e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 42.03 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKLQETVATLKDTVVQEEEKKRQL---QEGAERLNKETADLLAQLeASKGSTREVEERM--TAMNEQKVALEGKl 935
Cdd:COG5059 331 SRAKSIKNKIQVNSSSDSSREIEEIKFDLsedRSEIEILVFREQSQLSQS-SLSGIFAYMQSLKkeTETLKSRIDLIMK- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 936 adaSKKLEVEEARAVEINKQKKLVEAEcaDLKKNCQDVDLSLRKVEAEKNA-KEHQIRALQDEmRQQDENISKLNKERKN 1014
Cdd:COG5059 409 ---SIISGTFERKKLLKEEGWKYKSTL--QFLRIEIDRLLLLREEELSKKKtKIHKLNKLRHD-LSSLLSSIPEETSDRV 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150292 1015 QEEQNKKLTEDL--QAAEEQNLAANKLKAKLMQSLEDSEQTMErekrNRADMDKNKRKAEGELKIAQETLEELNKSKSD 1091
Cdd:COG5059 483 ESEKASKLRSSAstKLNLRSSRSHSKFRDHLNGSNSSTKELSL----NQVDLAGSERKVSQSVGELLRETQSLNKSLSS 557
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
851-1131 |
3.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 851 KVKPLVNSGKIEAQY-----EKLQETVATLKDTVVQE--EEKKRQLQEGAERLNKETADLLAQLEAS---------KGST 914
Cdd:COG3206 128 TVEPVKGSNVIEISYtspdpELAAAVANALAEAYLEQnlELRREEARKALEFLEEQLPELRKELEEAeaaleefrqKNGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 915 REVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNcqdvdlslrkveaeknakeHQIRAL 994
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-------------------PVIQQL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 995 QDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQnlaankLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGE 1074
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------LQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 25150292 1075 LKIAQETLEELNKSKSDAENAlrrkETELHTLGMKLEDeqaavAKLQKGIQQDEARV 1131
Cdd:COG3206 343 LAELPELEAELRRLEREVEVA----RELYESLLQRLEE-----ARLAEALTVGNVRV 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
860-1007 |
4.04e-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: 41.06 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQK--VALEGKLAD 937
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 938 ASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISK 1007
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
861-1260 |
4.10e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 861 IEAQYEKL--QETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVAlegKLADA 938
Cdd:PRK11281 41 VQAQLDALnkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE---ETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 939 SKKLEVE--EARAVEINKQKKLVEAECADLkkNCQDVDLSLRKVEAEKNAKEHQIRALQdeMRQQDENiSKLNKERKNQE 1016
Cdd:PRK11281 118 LSTLSLRqlESRLAQTLDQLQNAQNDLAEY--NSQLVSLQTQPERAQAALYANSQRLQQ--IRNLLKG-GKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1017 EQNKKLTEdlQAAEEQNLAANKlkaklmQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLeelnksksdaeNAL 1096
Cdd:PRK11281 193 QRVLLQAE--QALLNAQNDLQR------KSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAI-----------NSK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1097 RRKETElhtlgmkledEQAavaklQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQ-------LEdq 1169
Cdd:PRK11281 254 RLTLSE----------KTV-----QEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQnlrvknwLD-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1170 aRATAAQielgkkkdaeltklrRDLEesglkfgEQLTVLkkKGS-----------------DAIQELSDQI--------- 1223
Cdd:PRK11281 317 -RLTQSE---------------RNIK-------EQISVL--KGSlllsrilyqqqqalpsaDLIEGLADRIadlrleqfe 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 25150292 1224 -----EQLQKQKGRIEK-EKGHMQREFDESSAALDQEAKLRAD 1260
Cdd:PRK11281 372 inqqrDALFQPDAYIDKlEAGHKSEVTDEVRDALLQLLDERRE 414
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
885-1045 |
4.26e-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: 41.06 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 885 KKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKL--VEAE 962
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 963 CADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQnlAANKLKAK 1042
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE--LAAKIPPE 175
|
...
gi 25150292 1043 LMQ 1045
Cdd:COG1579 176 LLA 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1737-1947 |
4.84e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1737 VALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAA 1816
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1817 EAAvmkggaKAIQKAE--QRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAklklQ 1894
Cdd:COG4942 96 RAE------LEAQKEElaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----L 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 25150292 1895 KKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK 1947
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1769-1947 |
5.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1769 DRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAvmkggaKAIQKAEQRLKAFQSDLETESRR 1848
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1849 AGEASKTLARadrkVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQK-KQLEEAEEQANSHLSKYRTVQLSLETAEERAD 1927
Cdd:COG4717 148 LEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180
....*....|....*....|
gi 25150292 1928 SAEQCLVRIRSRTRANAEQK 1947
Cdd:COG4717 224 ELEEELEQLENELEAAALEE 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1042 |
5.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 860 KIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEA------------------SKGSTREVEERM 921
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 922 TAMNEQKVALEGKLADASKKLEveearavEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQ 1001
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25150292 1002 DENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAK 1042
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1010-1832 |
6.30e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1010 KERKNQEEQNKKLTEDlqaAEEQNLAanKLKAKLMQSLEDSEQTMEREKRnRADMDKNKRKAEGELKIAQETLEELNKSK 1089
Cdd:TIGR01612 473 EEEWGSYDIKKDIDEN---SKQDNTV--KLILMRMKDFKDIIDFMELYKP-DEVPSKNIIGFDIDQNIKAKLYKEIEAGL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1090 SDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIqqdearvKDLHDQLADEKDARQRADRSRadqqAEYDELTEQLEDQ 1169
Cdd:TIGR01612 547 KESYELAKNWKKLIHEIKKELEEENEDSIHLEKEI-------KDLFDKYLEIDDEIIYINKLK----LELKEKIKNISDK 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1170 ARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELS----DQIEQLQKQKGRIEKEKghmqrEFD 1245
Cdd:TIGR01612 616 NEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSkiyeDDIDALYNELSSIVKEN-----AID 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1246 ESsaalDQEAKLRADQERIAKGY------EVRLLELRLKADEQSRQ--LQDFVSSKGRLNSE-NSDLARQVEELEAKiqa 1316
Cdd:TIGR01612 691 NT----EDKAKLDDLKSKIDKEYdkiqnmETATVELHLSNIENKKNelLDIIVEIKKHIHGEiNKDLNKILEDFKNK--- 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1317 anrlKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEqlKESIEDEVAGKN-EASRQLSKAsveldqwrtkfeteg 1395
Cdd:TIGR01612 764 ----EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN--IDNIKDEDAKQNyDKSKEYIKT--------------- 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1396 lIGADEfDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADA-----NRLEAEHHAQAVSSLEKKQKAFDKVID 1470
Cdd:TIGR01612 823 -ISIKE-DEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQfaeltNKIKAEISDDKLNDYEKKFNDSKSLIN 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1471 EWKKKVDDLYL------ELDGAQRDARQLSGEAHKLRGQHDTLAD----QVEGLRREN---KSLSDETRD-LTESLSEGG 1536
Cdd:TIGR01612 901 EINKSIEEEYQnintlkKVDEYIKICENTKESIEKFHNKQNILKEilnkNIDTIKESNlieKSYKDKFDNtLIDKINELD 980
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1537 RATHALSknLRRLEMEKEELQRGLDEAEAALESEESKALRCQI-EVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQA 1615
Cdd:TIGR01612 981 KAFKDAS--LNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFdEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIID 1058
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1616 TLDSETKAKSELF--RVKKKLEADI---NELEIALDHANKANEDAQKNIR------RYLDQIRELQQTVDEEQKRREEFr 1684
Cdd:TIGR01612 1059 EIEKEIGKNIELLnkEILEEAEINItnfNEIKEKLKHYNFDDFGKEENIKyadeinKIKDDIKNLDQKIDHHIKALEEI- 1137
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1685 ehllaaerklavaKQEQEELIVKLEA-LERARRVVESSVKEHQEHNNELNSQNVALAAAKSQ-LDNEIALLNSDIAEAHT 1762
Cdd:TIGR01612 1138 -------------KKKSENYIDEIKAqINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKnIYDEIKKLLNEIAEIEK 1204
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1763 ELSASEDRGRRAASDAAKLAE-DLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAE 1832
Cdd:TIGR01612 1205 DKTSLEEVKGINLSYGKNLGKlFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAE 1275
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1757-1896 |
6.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1757 IAEAHTELSASE--DRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERadaaeaavmkggakaIQKAEQR 1834
Cdd:COG2433 378 IEEALEELIEKElpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE---------------LEEKDER 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 1835 LKafqsDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKK 1896
Cdd:COG2433 443 IE----RLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1580-1725 |
6.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1580 EVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIA-----LDHANKANED 1654
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150292 1655 AQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEA----LERARRVVESSVKEH 1725
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAeleeLEAEREELAAKIPPE 175
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
898-1257 |
7.04e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 898 KETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKK---LEVEEARAVEINKQKKLVEAECADLKKNCQDVD 974
Cdd:pfam05622 124 RESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRtlqLEEELKKANALRGQLETYKRQVQELHGKLSEES 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 975 LSLRKVEAEKNAKEHQIRALQDE---MRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSleDSE 1051
Cdd:pfam05622 204 KKADKLEFEYKKLEEKLEALQKEkerLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPA--EIR 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1052 QTMEREKRnradmdKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARV 1131
Cdd:pfam05622 282 EKLIRLQH------ENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1132 KD---LHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELG-KKKDAELtklrRDLEESGLKFGEQL-T 1206
Cdd:pfam05622 356 EDsslLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEAlRKKDEDM----KAMEERYKKYVEKAkS 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 25150292 1207 VLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKL 1257
Cdd:pfam05622 432 VIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
991-1262 |
7.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 991 IRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRK 1070
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1071 AEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRAD- 1149
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAl 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1150 ---RSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQL 1226
Cdd:COG4372 186 delLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270
....*....|....*....|....*....|....*.
gi 25150292 1227 QKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQE 1262
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1031-1177 |
7.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1031 EQNLAANKLKAKLMqsLEDSEQTMEREKRN-----RADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHT 1105
Cdd:PRK12704 30 EAKIKEAEEEAKRI--LEEAKKEAEAIKKEalleaKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150292 1106 LGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQladekdARQRADRSRADQQAE-YDELTEQLEDQARATAAQI 1177
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEE------QLQELERISGLTAEEaKEILLEKVEEEARHEAAVL 174
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1632-1903 |
7.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1632 KKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEAL 1711
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1712 ERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRaasdaAKLAEDLRHEQEQ 1791
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE-----QALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1792 SQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVA 1871
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270
....*....|....*....|....*....|..
gi 25150292 1872 EDKKNYDKLQELVEKLTAKLKLQKKQLEEAEE 1903
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1149-1378 |
8.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1149 DRSRADQQAEYDELTEQLEDQARATAAQIElgkKKDAELTKLRRdlEESGLKFGEQLTVLkkkgSDAIQELSDQIEQLQK 1228
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE---EAEAALEEFRQ--KNGLVDLSEEAKLL----LQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1229 QKGRIEKEKGHMQREFD---ESSAALDQEAKLRADQERIAKgYEVRLLELRLKADEQSRQLQDfvsskgrlnsensdLAR 1305
Cdd:COG3206 234 ELAEAEARLAALRAQLGsgpDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIA--------------LRA 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150292 1306 QVEELEAKIQA-ANRLKLQFSNELDHAKRQAEEesrerqnlsnlsknlareLEQLKESIEDEVAGKNEASRQLS 1378
Cdd:COG3206 299 QIAALRAQLQQeAQRILASLEAELEALQAREAS------------------LQAQLAQLEARLAELPELEAELR 354
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1402-1933 |
8.52e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1402 FDEVKKRQNQ------KTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKK 1475
Cdd:pfam10174 211 LREELHRRNQlqpdpaKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1476 VDdlyleldgaqrdarQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEE 1555
Cdd:pfam10174 291 ID--------------QLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1556 LQRGLDEAEAaleseesKALRCQIEVSQIRAEIE--KRIAEKEEefenhRKVH--QQTIDSIQATLDSETKAKSELFRVK 1631
Cdd:pfam10174 357 KESFLNKKTK-------QLQDLTEEKSTLAGEIRdlKDMLDVKE-----RKINvlQKKIENLQEQLRDKDKQLAGLKERV 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1632 KKLEADINELEIALDHANKANEDAQKNIRRYLDQIRElqqtvdEEQKRREEfrehllaaerkLAVAKQEQEELIVKLEAL 1711
Cdd:pfam10174 425 KSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRER------EDRERLEE-----------LESLKKENKDLKEKVSAL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1712 ERARRVVESSVKEHQEHNNELNSQNValaaaksQLDNEIALLNSDIAEAHTELSASEDRGRRAASdaakLAEDLRHEQEQ 1791
Cdd:pfam10174 488 QPELTEKESSLIDLKEHASSLASSGL-------KKDSKLKSLEIAVEQKKEECSKLENQLKKAHN----AEEAVRTNPEI 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1792 SQQLerfkKQLESAVKDLQERADAAEAAVmkggakaiqkaeQRLKAFQSDLETESRRAGEASKTL-ARADRKVREFEFQV 1870
Cdd:pfam10174 557 NDRI----RLLEQEVARYKEESGKAQAEV------------ERLLGILREVENEKNDKDKKIAELeSLTLRQMKEQNKKV 620
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150292 1871 A--------EDKKNYDKLQE-LVEKLTAKLKLQKKQLEEAEEQanshLSKYRTVqlsLETAEERADSAEQCL 1933
Cdd:pfam10174 621 AnikhgqqeMKKKGAQLLEEaRRREDNLADNSQQLQLEELMGA----LEKTRQE---LDATKARLSSTQQSL 685
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
883-1115 |
8.64e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 41.08 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 883 EEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMnEQKVALEgKLA--DASKKL-EVEEARAVeINKQKKLV 959
Cdd:pfam15818 77 EEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEM-EQKLQLH-LLAkeDHHKQLnEIEKYYAT-ITGQFGLV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 960 EAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEM----------------RQQDENISKLNKERKNQEEQ----- 1018
Cdd:pfam15818 154 KENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELkkvtsdlikskvtcqyKMGEENINLTIKEQKFQELQerlnm 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1019 ----NKKLTEDLQAAEEQnlaanklKAKLMQSLEDSEQTMEREKRNRADMdknkrkaEGELKIAQETLEELNKsksdaEN 1094
Cdd:pfam15818 234 elelNKKINEEITHIQEE-------KQDIIISFQHMQQLLQQQTQANTEM-------EAELKALKENNQTLER-----DN 294
|
250 260
....*....|....*....|....
gi 25150292 1095 ALRR---KETELHTLGMKLEDEQA 1115
Cdd:pfam15818 295 ELQRekvKENEEKFLNLQNEHEKA 318
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1062-1320 |
9.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1062 ADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADE 1141
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1142 KDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSD 1221
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1222 QIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENS 1301
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250
....*....|....*....
gi 25150292 1302 DLARQVEELEAKIQAANRL 1320
Cdd:COG4372 267 ILVEKDTEEEELEIAALEL 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1607-1783 |
9.85e-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: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1607 QQTIDSIQATLDSETKAKSELfrvkKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKR------- 1679
Cdd:COG3883 19 QAKQKELSELQAELEAAQAEL----DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150292 1680 -------------------------REEFREHLLAAERK-LAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELN 1733
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25150292 1734 SQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAE 1783
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| |
