|
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, ... |
100-779 |
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: 1259.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQAASGKEakdGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKS-KRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKP-LGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKqg 578
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKSE-- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 579 dAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYqtqeeaaeaAKAGQTAGGKRGKSSSFAT 658
Cdd:cd01377 475 -AHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSS-DPLVASLFKDY---------EESGGGGGKKKKKGGSFRT 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 659 VSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILA 738
Cdd:cd01377 544 VSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILA 623
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127737 739 ADAAKES--DPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd01377 624 PNAIPKGfdDGKAACEKILKALQLD----PELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-779 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1115.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 88 TEDMANLTFLNEASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMV 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 168 QDKENQSMLITGESGAGKTENTKKVISYFAIVGATQAAsgkeakdgKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA--------GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 248 GKFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQ-AELTIEGM 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTN-PKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 327 DDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 407 VRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVN 486
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 487 ERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQHlGKHP 565
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 566 NFQKPKPpkgkQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQeeAAEAAKAGQT 645
Cdd:pfam00063 470 HFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSS-DPLLAELFPDYETA--ESAAANESGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 646 AGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRM 725
Cdd:pfam00063 543 STPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRI 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 726 LYPDFKHRYAILAADAAKE--SDPKKASVGILDKIsvdgNLTDEEFKVGETKIFFK 779
Cdd:pfam00063 623 TFQEFVQRYRILAPKTWPKwkGDAKKGCEAILQSL----NLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-791 |
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: 985.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 81 NPPKFDKTEDMANLTFLNEASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 161 EAYRNMVQDKENQSMLITGESGAGKTENTKKVISYFAIVGATqaasgkeakdGKKGGTLEEQIVQTNPVLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS----------NTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 241 NNNSSRFGKFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQA- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLK-SPEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 320 ELTIEGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQA-EPDGEEDALNAAAMLGIQAEEF 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 399 LKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFE 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKD-GSTYFIGVLDIYGFEIFEVNSFE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 479 QLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKlL 557
Cdd:smart00242 389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEK-L 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 558 DQHLGKHPNFQKPKppkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQeeaa 637
Cdd:smart00242 467 NQHHKKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSK-NPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 638 eaakagqtaggkRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRIC 717
Cdd:smart00242 538 ------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 718 RKGFPNRMLYPDFKHRYAILAAD--AAKESDPKKASVGILDKISVDGnltdEEFKVGETKIFFKAGVLAKLEDLRD 791
Cdd:smart00242 606 RAGFPYRLPFDEFLQRYRVLLPDtwPPWGGDAKKACEALLQSLGLDE----DEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-779 |
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: 972.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGAtqaaSGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA----SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQ-KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQGD 579
Cdd:cd14909 396 LEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 580 AHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQeeaaeAAKAGQTAGGKRGKSSSFATV 659
Cdd:cd14909 476 AHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQ-NKLLIEIFADHAGQ-----SGGGEQAKGGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 660 SMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAA 739
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 127737 740 DAAK-ESDPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14909 630 AGIQgEEDPKKAAEIILESIALD----PDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-779 |
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: 912.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQAASGKEAKDG--KKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSG 257
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 258 SGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQE 337
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKG 417
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 418 QNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKeIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHM 497
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTK-LPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 498 FVLEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQ 577
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 578 GDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEEAAEAAKAGQTaggKRGKSSSFA 657
Cdd:cd14927 480 YEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQ-NKLLATLYENYVGSDSTEDPKSGVKE---KRKKAASFQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 658 TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd14927 556 TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 738 AADAAKES---DPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14927 636 NPSAIPDDkfvDSRKATEKLLGSLDIDHT----QYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
101-779 |
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: 876.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKeaKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKK--KDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKeIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTK-LPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKqGDA 580
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGR-AEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTqeeaaeAAKAGQTAGGKRGKSSSFATVS 660
Cdd:cd14913 478 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSS-NRLLAHLYATFAT------ADADSGKKKVAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 661 MIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAAD 740
Cdd:cd14913 551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127737 741 AAKES---DPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14913 631 AIPEGqfiDSKKACEKLLASIDIDHT----QYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-779 |
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: 862.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATqaasGKEAKDGKkgGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT----GKQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14934 155 KLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14934 235 DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKeIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14934 315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTK-MQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQGD 579
Cdd:cd14934 394 LEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 580 AHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdnSLMLDIWQDYQtqeeaaeaAKAGQTAGGKRGksSSFATV 659
Cdd:cd14934 474 AHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--LGLLALLFKEE--------EAPAGSKKQKRG--SSFMTV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 660 SMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAA 739
Cdd:cd14934 542 SNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNP 621
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127737 740 DAAKES--DPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14934 622 NVIPQGfvDNKKASELLLGSIDLDVN----EYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-779 |
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: 830.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATqaasgKEAKdgKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM-----IESK--KKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDpSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKeIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAK-LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKgKQGD 579
Cdd:cd14929 392 LEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDK-KKFE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 580 AHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEEAAeaakagQTAGGKRGKSSSFATV 659
Cdd:cd14929 471 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSS-NRLLASLFENYISTDSAI------QFGEKKRKKGASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 660 SMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAA 739
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127737 740 ---DAAKESDPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14929 624 rtfPKSKFVSSRKAAEELLGSLEID----HTQYRFGITKVFFK 662
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1420 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 827.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 32 FDSKKNCWIPDPEDGFVAAEIQSTTG------EQVTVVTVKGNQITVKKDQCQEMNPPKFDKTEDMANLTFLNEASVLGN 105
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKEAFnkgkvtEEGKKEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 106 LKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGESGAGK 185
Cdd:COG5022 86 LEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 186 TENTKKVISYFAIVGATqaasgkeakDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGKLAGGD 265
Cdd:COG5022 166 TENAKRIMQYLASVTSS---------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 266 IEHYLLEKSRVVRQAPGERCYHIFYQIMSGnDPSLRGKLKLSNDITYYHFCSQAELT-IEGMDDKEEMRLTQEAFDIMGF 344
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAG-DPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 345 EDNETMDLYRSTAGIMHMGEMKFKQrPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVN 424
Cdd:COG5022 316 DEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 425 WAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEE 504
Cdd:COG5022 395 AIRDSLAKALYSNLFDWIVDRINKSLDHSA-AASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 505 YKREGIAWTFIDFgLDLQACIELIEK--PLGIISILDEECIVPKATDMTYAQKLLDQ-HLGKHPNFQKPkppkgKQGDAH 581
Cdd:COG5022 474 YVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKS-----RFRDNK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 582 FAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLkHSTDNSLMLDIWQDYQtqeeaaeaakagqtaggKRGKSSSFATVSM 661
Cdd:COG5022 548 FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELL-KASTNEFVSTLFDDEE-----------------NIESKGRFPTLGS 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 662 IYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL---- 737
Cdd:COG5022 610 RFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILspsk 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 738 --AADAAKESDPKKASVGILDKISVDgnltDEEFKVGETKIFFKAGVLAKLEDLRDEILSRIVTMFQSRIRSYLAKAEVR 815
Cdd:COG5022 690 swTGEYTWKEDTKNAVKSILEELVID----SSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 816 RRYEQQTGLLVVQRNVRAWCTLRTWEWFKLFGKVKPMLKAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLE-------- 887
Cdd:COG5022 766 QALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEvefslkae 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 888 --SQVADLVEEKNALFLSLETE------KANLADAEER-------NEKLNQLKAT---LESKLSDITGQLE-DMQERNE- 947
Cdd:COG5022 846 vlIQKFGRSLKAKKRFSLLKKEtiylqsAQRVELAERQlqelkidVKSISSLKLVnleLESEIIELKKSLSsDLIENLEf 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 948 ------DLARQKKKTD-QELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKE-KKHQEE--SNR 1017
Cdd:COG5022 926 kteliaRLKKLLNNIDlEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSElKNFKKElaELS 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1018 KLNEDLQSEEDKVNHLEKIRNKLEQQMDELEEnIDREKRSRGDIEKAKRKVE----------GDLKVAQENIDEITKQKH 1087
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEVAELQSASKIISS-ESTELSILKPLQKLKGLLLlennqlqaryKALKLRRENSLLDDKQLY 1084
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1088 ---DVETTLKRKEEDlhhtnaKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLe 1164
Cdd:COG5022 1085 qleSTENLLKTINVK------DLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELD- 1157
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1165 qqGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLrkrhgDSVAELTEQLETLQKlKAKSEAEKSKLQRDLEes 1244
Cdd:COG5022 1158 --GLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSS-----SEVNDLKNELIALFS-KIFSGWPRGDKLKKLI-- 1227
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1245 qhatdSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFaalKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQ 1324
Cdd:COG5022 1228 -----SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSL---LNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFN 1299
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1325 LDETRRNYDEESRERQALAATA----KNLEHENTILREHLDEEAES------------KADLTRQI--SKLNAEIQQWKA 1386
Cdd:COG5022 1300 ALRTKASSLRWKSATEVNYNSEelddWCREFEISDVDEELEELIQAvkvlqllkddlnKLDELLDAcySLNPAEIQNLKS 1379
|
1450 1460 1470
....*....|....*....|....*....|....*
gi 127737 1387 RFD-SEGLNKLEEIEAAKKALQLKVQELTDTNEGL 1420
Cdd:COG5022 1380 RYDpADKENNLPKEILKKIEALLIKQELQLSLEGK 1414
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
101-779 |
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: 811.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKEAKDGKkgGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQgDA 580
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKP-EA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEEAAeaakagQTAGGKRGKSSSFATVS 660
Cdd:cd14917 478 HFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSS-LKLLSNLFANYAGADAPI------EKGKGKAKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 661 MIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAAD 740
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127737 741 AAKES---DPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14917 631 AIPEGqfiDSRKGAEKLLSSLDIDHN----QYKFGHTKVFFK 668
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-779 |
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: 801.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRN-EMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVgatqaASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAAL-----SGSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHF----CSQAELTIEGMDDKEEMRL 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 335 TQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREE--QAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 413 WVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERK-HFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQ 491
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 492 FFNHHMFVLEQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQHlGKHPNFQKP 570
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH-GSHPRFFSK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 571 KppkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDnslmldiwqdyqtqeeaaeaakagqtaggkr 650
Cdd:cd00124 474 K----RKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 651 gksssfatvsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDF 730
Cdd:cd00124 519 ------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 127737 731 KHRYAILAADAAKESDPKKASVGILDKISvdGNLTDEEFKVGETKIFFK 779
Cdd:cd00124 587 LKRYRILAPGATEKASDSKKAAVLALLLL--LKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-779 |
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: 799.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVgATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATI-AVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKqGDA 580
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGK-AEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLdIWQDYqtqeeaaEAAKAGQTAGGKRG---KSSSFA 657
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSF-LFSNY-------AGAEAGDSGGSKKGgkkKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 658 TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd14923 551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 738 AADAAKES---DPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14923 631 NASAIPEGqfiDSKNASEKLLNSIDVD----REQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
101-779 |
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: 799.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGgTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKG-TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQgDA 580
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQ-EA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTqeeaAEAAKAGQTAGGKRgKSSSFATVS 660
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSS-LKLMATLFSTYAS----ADTGDSGKGKGGKK-KGSSFQTVS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 661 MIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAAD 740
Cdd:cd14916 553 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127737 741 AAKES---DPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14916 633 AIPEGqfiDSRKGAEKLLGSLDIDHN----QYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
101-779 |
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: 792.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQgDA 580
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKV-EA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLmldiwqdyqTQEEAAEAAKAGQTAGGKRG---KSSSFA 657
Cdd:cd14910 480 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTL---------ALLFSGAAAAEAEEGGGKKGgkkKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 658 TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd14910 551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 738 AADAAKES---DPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14910 631 NASAIPEGqfiDSKKASEKLLGSIDID----HTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-779 |
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: 790.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKqGDA 580
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGK-AEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLmldiwqdyqTQEEAAEAAKAGQTAGG--KRG---KSSS 655
Cdd:cd14912 480 HFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTL---------AYLFSGAQTAEGASAGGgaKKGgkkKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 FATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA 735
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127737 736 ILAADAAKES---DPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14912 631 VLNASAIPEGqfiDSKKASEKLLASIDID----HTQYKFGHTKVFFK 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
102-779 |
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: 789.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 102 VLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGES 181
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 182 GAGKTENTKKVISYFAIVgatqAASGKEAKD--GKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14918 83 GAGKTVNTKRVIQYFATI----AVTGEKKKEesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKqGD 579
Cdd:cd14918 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 580 AHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMlDIWQDYQTQEEAAEAAKagqtagGKRGKSSSFATV 659
Cdd:cd14918 477 AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLA-SLFSTYASAEADSGAKK------GAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 660 SMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAA 739
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127737 740 DAAKES---DPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14918 630 SAIPEGqfiDSKKASEKLLASIDID----HTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-779 |
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: 788.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNL 420
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 421 EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVL 500
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 501 EQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKqGDA 580
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-AEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 581 HFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLdIWQDYQTqeeaaeaaKAGQTAGGKRG---KSSSFA 657
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAF-LFSGGQT--------AEAEGGGGKKGgkkKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 658 TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd14915 551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 738 AADAAKES---DPKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14915 631 NASAIPEGqfiDSKKASEKLLGSIDID----HTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-779 |
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: 760.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQA-ASGKEAKDGKKG----GTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTH 254
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPkGSGAVPHPAVNPavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 255 FSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLsNDITYYHFCSQAELTIEGMDDKEEMRL 334
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 335 TQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWV 414
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 415 NKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFN 494
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 495 HHMFVLEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHlGKHPNFQKPKppk 574
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTD--- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 575 gKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDnSLMLDIWQDyqTQEEAAEAAKAGQTAGGKRGKSS 654
Cdd:cd14911 476 -FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQD-PFVVNIWKD--AEIVGMAQQALTDTQFGARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 SFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127737 735 AILAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14911 632 ELLTPNVIPKGfmDGKKACEKMIQALELDSNL----YRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-779 |
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: 758.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVgatqAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHV----ASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14920 157 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEG-FNNYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPL---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKGK 576
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNsLMLDIWQDYQTQEEAAEAAKAGQTAGGK--RGKSS 654
Cdd:cd14920 475 ---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDR-FVAELWKDVDRIVGLDQVTGMTETAFGSayKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 SFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127737 735 AILAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14920 631 EILTPNAIPKGfmDGKQACERMIRALELDPNL----YRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-779 |
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: 714.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPL---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKgk 576
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLK-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNsLMLDIWQDYQTQEEAAEAAKAGQTAGGK-RGKSSS 655
Cdd:cd14932 477 -DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDK-FVSELWKDVDRIVGLDKVAGMGESLHGAfKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 FATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA 735
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 127737 736 ILAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14932 635 ILTPNAIPKGfmDGKQACVLMVKALELDPNL----YRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
101-779 |
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: 703.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDL-MIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGAtqaASGKEAkdgkkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGG---SSSGET-------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKH-FIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMF 498
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 499 VLEQEEYKREGIAWTFIDFgLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGK-HPNFQKPKPPKGKq 577
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 578 gdahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNslmldiwqdyqtqeeaaeaakagqtaggKRgksssfa 657
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR----------------------------KK------- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 658 TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 127737 738 A-ADAAKESDPKKASVGILDKisvdgNLTDEE-FKVGETKIFFK 779
Cdd:cd01380 591 LpSKEWLRDDKKKTCENILEN-----LILDPDkYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-779 |
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: 678.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVgatqAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVV----ASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEG-FNNYTFLSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPL---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKGK 576
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDnSLMLDIWQDYQTQEEAAEAAKAGQTA--GGKRGKSS 654
Cdd:cd14921 475 ---TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSD-KFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 SFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd14921 551 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127737 735 AILAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14921 631 EILAANAIPKGfmDGKQACILMIKALELDPNL----YRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-779 |
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: 672.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVgatqAASGKEAKDGkkgGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHV----ASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14919 154 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPL---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKGK 576
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNsLMLDIWQDYQTQEEAAEAAKAGQTA--GGKRGKSS 654
Cdd:cd14919 472 ---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDK-FVSELWKDVDRIIGLDQVAGMSETAlpGAFKTRKG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 SFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd14919 548 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127737 735 AILAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14919 628 EILTPNSIPKGfmDGKQACVLMIKALELDSNL----YRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-779 |
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: 670.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLEN-YNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPL---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKgk 576
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPKKLK-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNsLMLDIWQDYQTQEEAAEAAKAGQTAGGKRGKSSSF 656
Cdd:cd15896 477 -DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDK-FVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 657 ATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAI 736
Cdd:cd15896 555 RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 737 LAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd15896 635 LTPNAIPKGfmDGKQACVLMIKSLELDPNL----YRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-779 |
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: 654.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVgatqAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHV----ASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQAELTIEGmDDKEEMRLTQEAF 339
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETLESL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd14930 235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFGLDLQACIELIEKPL---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKGK 576
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVA-QEQGGHPKFQRPRHLRDQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNsLMLDIWQDYQTQEEAAEAAKAGQTAGGKRGKSSSF 656
Cdd:cd14930 474 ---ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR-LTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 657 ATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAI 736
Cdd:cd14930 550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 737 LAADAAKES--DPKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14930 630 LTPNAIPKGfmDGKQACEKMIQALELDPNL----YRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
101-779 |
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: 651.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKhfMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFIT--AYRQKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATqaasgkeakdgkkGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGG-------------SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLsNDITYYHFCSQAE-LTIEGMDDKEEMRLTQEAF 339
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQN 419
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 420 LEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFV 499
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 500 LEQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKlLDQHLGKHPNFqkpkppKGKQG 578
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANK-LKQHLKSNSCF------KGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 579 DAhFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLkhSTDNSLMLdiwqdyQTQEEAAEAAKAGQTAGGKRGKSSSF-A 657
Cdd:cd01383 458 GA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL--SSCSCQLP------QLFASKMLDASRKALPLTKASGSDSQkQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 658 TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd01383 529 SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127737 738 AADAAKES-DPKKASVGILDKIsvdgNLTDEEFKVGETKIFFK 779
Cdd:cd01383 609 LPEDVSASqDPLSTSVAILQQF----NILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-779 |
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: 616.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAASGKEAKDgkkggtleeQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERVKD---------MLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFD 340
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 341 IMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDAlNAAAMLGIQAEEFLKALTKPRVRVGTEW---VNKG 417
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSVLD-FVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 418 QNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHhm 497
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 498 FVL--EQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECI-VPKATDMTYAQKlLDQHLGKHPNFQKPKPP 573
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLtAGDATDQTFLQK-LNQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 574 KGkQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLkHSTDNSLMLDIWQDyqtqEEAAEAAKAGQTAGGKrgks 653
Cdd:cd01378 468 FE-LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELM-QSSSNPFLRSLFPE----GVDLDSKKRPPTAGTK---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 654 ssfatvsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHR 733
Cdd:cd01378 538 ---------FKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLER 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 127737 734 YAILAADA--AKESDPKKASVGILdkisVDGNLTDEEFKVGETKIFFK 779
Cdd:cd01378 609 YKLLSPKTwpAWDGTWQGGVESIL----KDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-779 |
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: 610.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAivgatqAASGKEAkdgkkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd01381 81 ESGAGKTESTKLILQYLA------AISGQHS-------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPRE--EQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 418 QNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL--DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNH 495
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIykPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 496 HMFVLEQEEYKREGIAWTFIDFgLDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQKLLDQHlGKHPNFQKPKppk 574
Cdd:cd01381 388 HIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPK--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 575 gKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLkHSTDNSLMLDIWQDYqtqeeaaeaAKAGQTAGGKRgkss 654
Cdd:cd01381 463 -SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLV-QSSKNKFLKQLFNED---------ISMGSETRKKS---- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 sfATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd01381 528 --PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERY 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127737 735 AILAADA--AKESDPKKASVGILDKISvdgnLTDEEFKVGETKIFFK 779
Cdd:cd01381 606 RVLVPGIppAHKTDCRAATRKICCAVL----GGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-779 |
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: 607.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATQAasgkeakdgkkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSG--NDPSLRGKLKLsNDITYYHFCSQAE-LTIEGMDDKEEMRLTQE 337
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKL-GEPEDYHYLNQSGcIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAA-MLGIQAEEFLKALTKPRVRVGTEWVNK 416
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKIVAkLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 417 GQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKhFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHH 496
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSR-FIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 497 MFVLEQEEYKREGIAWTFIDFGlDLQACIELIEK-PLGIISILDEECIVPKATDMTYAQKLLDQHlGKHPNFQKPKPPKG 575
Cdd:cd14883 387 VFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 576 KQgdaHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWqDYQTQEEAAEAAKAGQTAGGKRGKSSS 655
Cdd:cd14883 465 KT---EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSK-NKFVKELF-TYPDLLALTGLSISLGGDTTSRGTSKG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 FATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA 735
Cdd:cd14883 540 KPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 127737 736 ILAADAAKESDPKKAsvGILDKISVDGNLTDEEFKVGETKIFFK 779
Cdd:cd14883 620 CLDPRARSADHKETC--GAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-779 |
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: 598.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVGatqaasGKEAKDGKkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLsNDITYYHFCSQAE-LTIEGMDDKEEMRLTQE 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGE--EDAL-NAAAMLGIQAEEFLKALTKpRVRVGT-EW 413
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEksEFHLkAAAELLMCDEKALEDALCK-RVIVTPdGI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 414 VNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLdAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFF 493
Cdd:cd01384 310 ITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSI-GQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 494 NHHMFVLEQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQhLGKHPNFQKPKP 572
Cdd:cd01384 389 NQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 573 PKGKqgdahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLkHSTDNSLMLDIWQdyqtqeeaaeaakagQTAGGKRGK 652
Cdd:cd01384 467 SRTD-----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALL-NASKCPFVAGLFP---------------PLPREGTSS 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 653 SSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKH 732
Cdd:cd01384 526 SSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLD 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 127737 733 RYAILAADAAKESDPKKASV-GILDKISVDGnltdeeFKVGETKIFFK 779
Cdd:cd01384 606 RFGLLAPEVLKGSDDEKAACkKILEKAGLKG------YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
100-779 |
7.47e-175 |
|
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: 546.85 E-value: 7.47e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVGatqaasgkeakdGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLklsndityyhfcsqaeLTIEGMDDKEEMRLTQEA 338
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 339 FDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREE----QAEPDGEEDALNAAAMLGIQAEEFLKALTKpRVRVGTEWV 414
Cdd:cd01382 213 MKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 415 NKGQ------NLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKeiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNER 488
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE--TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 489 LQQFFNHHMFVLEQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQHLgKHPNF 567
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 568 QKPKPPKGK-----QGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLmldiwqdyqtQEEAAEAAKA 642
Cdd:cd01382 448 SIPRKSKLKihrnlRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFI----------RSLFESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 643 GQTAGGKRGKsSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFP 722
Cdd:cd01382 518 NKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127737 723 NRMLYPDFKHRYA-ILAADAAKeSDPK---KASVGILdkisvdgNLTDEEFKVGETKIFFK 779
Cdd:cd01382 597 SRTSFHDLYNMYKkYLPPKLAR-LDPRlfcKALFKAL-------GLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-779 |
1.53e-167 |
|
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: 526.65 E-value: 1.53e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFA-IVGATqaasgkeakdgkkgGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAeVAGST--------------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDityYHFCSQAE-LTIEGMDDKEEMRLTQE 337
Cdd:cd14872 147 GRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA---YGYLSLSGcIEVEGVDDVADFEEVVL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFK--QRPREEQAEPDGEEDAL-NAAAMLGIQAEEFLKALTKPRVRVgtewv 414
Cdd:cd14872 224 AMEQLGFDDADINNVMSLIAAILKLGNIEFAsgGGKSLVSGSTVANRDVLkEVATLLGVDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 415 nKGQNL-------EQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNE 487
Cdd:cd14872 299 -KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 488 RLQQFFNHHMFVLEQEEYKREGIAWTFIDFgLDLQACIELIEK-PLGIISILDEECIVPKATDMTYAQKlLDQHLGKHPN 566
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIA-ANQTHAAKST 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 567 FQkpkPPKGKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKhSTDNSLMLDIWQDYQtqeeaaeaakagqta 646
Cdd:cd14872 456 FV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLS-SSKNKLIAVLFPPSE--------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 647 gGKRgkSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRML 726
Cdd:cd14872 517 -GDQ--KTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYS 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 127737 727 YPDFKHRYAILAADAAKeSDPKKASVGILDKISVDGNLTDeEFKVGETKIFFK 779
Cdd:cd14872 594 HERFLKRYRFLVKTIAK-RVGPDDRQRCDLLLKSLKQDFS-KVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-779 |
1.54e-166 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 524.72 E-value: 1.54e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQ----DKENQS 174
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 175 MLITGESGAGKTENTKKVISYFA-IVGATQAASGKEAKDGKKG-----GTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFG 248
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLArITSGFAQGASGEGEAASEAieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 249 KFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYY---HFCSQaeltIEG 325
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFylrGECSS----IPS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 326 MDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQrprEEQAEPDGEEDALN----AAAMLGIQAEEFLKA 401
Cdd:cd14890 237 CDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFES---ENDTTVLEDATTLQslklAAELLGVNEDALEKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 402 LTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLW 481
Cdd:cd14890 314 LLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPD-DKWGFIGVLDIYGFEKFEWNTFEQLC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 482 INFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-----KPlGIISILDeECIVPKATDM------ 550
Cdd:cd14890 393 INYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLD-DCWRFKGEEAnkkfvs 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 551 ----TYAQKLLDQHLGK----HPNFQKPKppkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSl 622
Cdd:cd14890 470 qlhaSFGRKSGSGGTRRgssqHPHFVHPK----FDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 623 mldiwqdyqtqeeaaeaakagqtaggkRGKSssfatVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVL 702
Cdd:cd14890 545 ---------------------------REVS-----VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCL 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 703 NQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAADAakesDPKKASVGILDKISvdgNLTDEEFKVGETKIFFK 779
Cdd:cd14890 593 RQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA----ENIEQLVAVLSKML---GLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-779 |
3.55e-164 |
|
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: 517.81 E-value: 3.55e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVGATQAasgkEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSL----ELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQAE-LTIEGMDDKEEMRLTQE 337
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQSGcVEDKTISDQESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAepdgEEDAL-NAAAMLGIQAEEFLKALTKPRVRVGTEWVNK 416
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVS----FKTALgRSAELLGLDPTQLTDALTQRSMFLRGEEILT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 417 GQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKeiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHH 496
Cdd:cd14873 312 PLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 497 MFVLEQEEYKREGIAWTFIDFgLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHlGKHPNFQKPkppkgK 576
Cdd:cd14873 390 IFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKP-----R 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 QGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdnslmLD-IWQDYQTQEEAAEAAKAGQTAGGKRgksss 655
Cdd:cd14873 463 VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESR-----FDfIYDLFEHVSSRNNQDTLKCGSKHRR----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 fATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA 735
Cdd:cd14873 533 -PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 127737 736 ILAADAAKESDPKKASVGILDKisVDGnlTDEEFKVGETKIFFK 779
Cdd:cd14873 612 VLMRNLALPEDVRGKCTSLLQL--YDA--SNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-779 |
4.57e-163 |
|
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: 515.10 E-value: 4.57e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVgatqaASGKEAKDGKKggtleeqIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATI-----AGGLNDSTIKK-------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHfcSQAELTIEGMDDKEEMRLTQEA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG--ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 339 FDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAE--PDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 417 GQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHfIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHH 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANH-IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 497 MFVLEQEEYKREGIAWTFIDFgLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKgk 576
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 577 qgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKhSTDNSLMLDIWqDYQTQEEAAEAAKAGQTAGGKRGKSSSF 656
Cdd:cd14903 463 ---TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMR-GSSKPFLRMLF-KEKVESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 657 ATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAI 736
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 127737 737 -LAADAAKESDPKKASVGILDKISVDgnlTDEEFKVGETKIFFK 779
Cdd:cd14903 618 fLPEGRNTDVPVAERCEALMKKLKLE---SPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
101-779 |
2.91e-161 |
|
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: 509.12 E-value: 2.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGATqaasgkeakdgkKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA------------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSG---NDPSLRGKLKLSNDITYYHFCSQAELTIEGMD-DKEEMRLTQ 336
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGlaeDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSgNREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 337 EAFDIMGFEDNETMDLYRSTAGIMHMGEMKFkqrpREEQAEPDGEEDAL--------NAAAMLGIQAEEFLKALTKPRVR 408
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEF----TEVESNHQTDKSSRisnpealnNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 409 VGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL--DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVN 486
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 487 ERLQQFFNHHMFVLEQEEYKREGIAWTFIDFG-----LDLqacieLIEKPLGIISILDEECIVPKATDMTYAQKLldQHL 561
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF--HNN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 562 GKHPNFQKPkppkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStDNSLmldIWQdyqtqeeaaeaak 641
Cdd:cd01379 459 IKSKYYWRP-----KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS-ENPL---VRQ------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 642 agqtaggkrgksssfaTVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGF 721
Cdd:cd01379 517 ----------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGF 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 722 PNRMLYPDFKHRYAILAADAAKESDPKKAS-VGILDKISVDGnltdeeFKVGETKIFFK 779
Cdd:cd01379 581 SHRILFADFLKRYYFLAFKWNEEVVANRENcRLILERLKLDN------WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
100-779 |
4.28e-160 |
|
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: 508.07 E-value: 4.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQAASGkeakdgkkggtLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALSQKGYGSG-----------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRP--REEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKG 417
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 418 QNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL---DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFN 494
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 495 HHMFVLEQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKlLDQHLGKHPNFQkpKPP 573
Cdd:cd01385 390 QHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYE--KPQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 574 KGKQGdahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKhSTDNSLMLDI----------W---------------- 627
Cdd:cd01385 466 VMEPA---FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLR-SSSSAFVRELigidpvavfrWavlrafframaafrea 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 628 ---QDYQTQEEAAEAAKAGQTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQ 704
Cdd:cd01385 542 grrRAQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQ 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127737 705 LTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAADAAKESdpKKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd01385 622 LRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISS--KEDIKDFLEKLNLD----RDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
100-779 |
1.64e-159 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 505.45 E-value: 1.64e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEM---PPHLFAVSDEAYRNMVQD----KEN 172
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVgkgqGTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 173 QSMLITGESGAGKTENTKKVISYFAIvgATQAASGKEAKDGKKGG--TLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKF 250
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAT--ASKLAKGASTSKGAANAheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 251 IRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQAE-LTIEGMDDK 329
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELT-PAESFLFLNQGNcVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 330 EEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQR--PREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKpRV 407
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVT-QT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 408 RVGTewvnKGQNLE------QVNWAVSGLAKAIYARMFKWIITRCNK---------TLDAKEIERKHFIGVLDIAGFEIF 472
Cdd:cd14892 317 TSTA----RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAchkqqtsgvTGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 473 DLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIEK-PLGIISILDEECIVP-KATDM 550
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 551 TYAQKLLDQHLGKHPNFQKPKppkgKQGDaHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDnslmldiwqdy 630
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPR----FECD-EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 631 qtqeeaaeaakagqtaggkrgksssfatvsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGV 710
Cdd:cd14892 536 --------------------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 711 LEGIRICRKGFPNRMLYPDFKHRYAILA---ADAAKESDPKKASVGI-LDKISVDGNLTDEEFKVGETKIFFK 779
Cdd:cd14892 584 LEVVRIRREGFPIRRQFEEFYEKFWPLArnkAGVAASPDACDATTARkKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-779 |
1.19e-158 |
|
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: 503.46 E-value: 1.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMgKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVGAtqaasgkeaKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFS-- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGS---------EDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 257 -------GSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAEL-------- 321
Cdd:cd14888 151 kskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 322 ---------------TIEGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFK-QRPREEQA--EPDGEED 383
Cdd:cd14888 231 ephlkfryltksschELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAvvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 384 ALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGV 463
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 464 LDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELI-EKPLGIISILDEEC 542
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 543 IVPKATDMTYAQKLLDQHLGkHPNFqkpKPPKGKQGDahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSL 622
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKG-HKRF---DVVKTDPNS--FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK-NPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 623 MLDIWQDYqtqeeaaeaAKAGQTAGGKRGKsssFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVL 702
Cdd:cd14888 543 ISNLFSAY---------LRRGTDGNTKKKK---FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVN 610
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 703 NQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAadaakesdpkkasvgildkiSVDGNLTDEEFKVGETKIFFK 779
Cdd:cd14888 611 EQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL--------------------NGEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-779 |
1.41e-158 |
|
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: 502.75 E-value: 1.41e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVgatqaasgkeakdGKKGGTL-EEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGs 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV-------------NQRRNNLvTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEA 338
Cdd:cd01387 147 GVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 339 FDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPRE---EQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVN 415
Cdd:cd01387 227 MQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 416 KGQNLEQVNWAVSGLAKAIYARMFKWIITRCNkTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNH 495
Cdd:cd01387 307 TPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 496 HMFVLEQEEYKREGIAWTFIDFgLDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQKLLDQHlGKHPNFQKPkppk 574
Cdd:cd01387 386 HVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKP---- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 575 gKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStDNSLMLDIWQDYQTQEeaaeaakagQTAGGKRGKSS 654
Cdd:cd01387 460 -RMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSS-RTRVVAHLFSSHRAQT---------DKAPPRLGKGR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 SFA------TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYP 728
Cdd:cd01387 529 FVTmkprtpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQ 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 127737 729 DFKHRYAILAADAAKESDPKKASVGILDkiSVDGNLTDEEFKVGETKIFFK 779
Cdd:cd01387 609 VFIDRYRCLVALKLPRPAPGDMCVSLLS--RLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-777 |
1.61e-158 |
|
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: 502.78 E-value: 1.61e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFM--GKRR----NEMPPHLFAVSDEAYRNMVQD---- 169
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYehGERRaageRKLPPHVYAVADKAFRAMLFAsrgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 170 KENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGkkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGK 249
Cdd:cd14901 81 KCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERE----NVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 250 FIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHF-CSQAELTIEGMDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 329 KEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREeqAEPDGEEDALNAAA---MLGIQAEEFLKALTKP 405
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGE--GGTFSMSSLANVRAacdLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 406 RVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKE-IERKHFIGVLDIAGFEIFDLNSFEQLWINF 484
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEsTGASRFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 485 VNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQhLGK 563
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 564 HPNFQKPKPpkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStdnslmldiwqdyqtqeeaaeaakag 643
Cdd:cd14901 473 HASFSVSKL---QQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTS-------------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 644 qtaggkrgkSSSF--ATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGF 721
Cdd:cd14901 524 ---------SNAFlsSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 722 PNRMLYPDFKHRYAILAADAAKESDPKKASVGILDKISVDGNLTDEE---FKVGETKIF 777
Cdd:cd14901 595 PVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHlppFQVGKTKVF 653
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
100-779 |
1.70e-150 |
|
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: 479.96 E-value: 1.70e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKR-RNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVgatqaaSGKEAKDgkkggtLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL------SPSDDSD------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLsNDITYYHFCSQAELTIEGMDDKEEMRLTQEA 338
Cdd:cd14897 149 GQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 339 F----DIM---GFEDNETMDLYRSTAGIMHMGEMKFkqrprEEQAEPDG----EEDAL-NAAAMLGIQAEEFLKALTKPR 406
Cdd:cd14897 228 FhdltNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGvtvaDEYPLhAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 407 VRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL----DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWI 482
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 483 NFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQKLLDqHL 561
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YC 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 562 GKHPNFqkpKPPKGkqGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStDNSLMLDIWQDYqtqeeaaeaak 641
Cdd:cd14897 461 GESPRY---VASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNS-NNEFISDLFTSY----------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 642 agqtaggkrgksssfatvsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGF 721
Cdd:cd14897 524 ---------------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGY 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 722 PNRMLYPDFKHRYAILAADAAKE-SDPKKASVGILDKISVdgnltdEEFKVGETKIFFK 779
Cdd:cd14897 583 PIRIKYEDFVKRYKEICDFSNKVrSDDLGKCQKILKTAGI------KGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-764 |
3.97e-145 |
|
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: 464.78 E-value: 3.97e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFM-----------GKRRNEMPPHLFAVSDEAYRNMVQ 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLlsfearssstrNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 169 ----DKENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAkdGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNS 244
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSM--GKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 245 SRFGKFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRgKLKLSNDITyyhfcsqaeltie 324
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-KRDMYRRVM------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 325 gmddkeemrltqEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALN-------AAAMLGIQAEE 397
Cdd:cd14900 226 ------------DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 398 FLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKH----FIGVLDIAGFEIFD 473
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHgglhFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 474 LNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELI-EKPLGIISILDEECIVPKATDMTY 552
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 553 AQKLLdQHLGKHPNFQKPKPPKGKqgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStdnslmldiWQdyqt 632
Cdd:cd14900 453 ASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG---------LQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 633 qeeaaeaakagqtaggkrgksssfatvsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLE 712
Cdd:cd14900 516 ------------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 127737 713 GIRICRKGFPNRMLYPDFKHRYAILAADAAKESDpKKASVGILDKISVDGNL 764
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSLARAKNRLLA-KKQGTSLPDTDSDHGPA 616
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-779 |
6.84e-140 |
|
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: 450.65 E-value: 6.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYK--DLMIYTYSGLFCVVINPYKRLPiysESVIKHFMGKRRNEMPPHLFAVSDEAYRNMV---QDKENQS 174
Cdd:cd14891 1 AGILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMClgsGRMQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 175 MLITGESGAGKTENTKKVISYF---AIVGATQAASGKEAKDGKK---GGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLttrAVGGKKASGQDIEQSSKKRklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 249 KFIRTHFSGSG-KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMD 327
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 328 DKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREE-QAEPDGEED--AL-NAAAMLGIQAEEFLKALT 403
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgEAEIASESDkeALaTAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 404 KPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDL-NSFEQLWI 482
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDP-DPLPYIGVLDIFGFESFETkNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 483 NFVNERLQQFFNHHMFVLEQEEYKREGI-----AWTfidfglDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQKL 556
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIdvgviTWP------DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 557 LDQHlGKHPNFQKPKpPKGKQgdAHFAIVHYAGTVRYNATNFLEKNkdplNDTavallkhstdnslmldIWQDYqtqeea 636
Cdd:cd14891 471 HKTH-KRHPCFPRPH-PKDMR--EMFIVKHYAGTVSYTIGSFIDKN----NDI----------------IPEDF------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 637 aeaakagqtaggkrgksSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRI 716
Cdd:cd14891 521 -----------------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 717 CRKGFPNRMLYPDFKHRYAILAADAAK--ESDPKKA-SVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd14891 584 LKVGLPTRVTYAELVDVYKPVLPPSVTrlFAENDRTlTQAILWAFRVP----SDAYRLGRTRVFFR 645
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
100-737 |
2.01e-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: 447.56 E-value: 2.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP---------IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDK 170
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 171 ENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKD-------GKKGGTLEEQIVQTNPVLEAFGNAKTVRNNN 243
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLtssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 244 SSRFGKFIRTHFS-GSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDIT--YYHFCSQAE 320
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 321 -LTIEGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRP--REEQAEPDGEEDALNAAAMLGIQAEE 397
Cdd:cd14907 241 cYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 398 FLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHF-------IGVLDIAGFE 470
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQLfqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 471 IFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTF--IDFgLDLQACIELIEK-PLGIISILDEECIVPKA 547
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 548 TDMTYAQKLLDQHlgkhPNFQKPKPPKGKQGDAhFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLmLDIW 627
Cdd:cd14907 480 TDEKLLNKIKKQH----KNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRII-SSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 628 QDYQTQEEAAEAAKAGQTAGGKrgksssfaTVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTC 707
Cdd:cd14907 554 SGEDGSQQQNQSKQKKSQKKDK--------FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|
gi 127737 708 NGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-779 |
6.90e-136 |
|
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: 440.11 E-value: 6.90e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 102 VLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMV----QDKENQSMLI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 178 TGESGAGKTENTKKVIsyfaivgatqaasgKEAKDGKKGGT-LEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFS 256
Cdd:cd14889 83 SGESGAGKTESTKLLL--------------RQIMELCRGNSqLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 257 gSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSG---NDPSLRGKLklsnDITYYHFCSQaeltieGMDDKEEMR 333
Cdd:cd14889 149 -NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisaEDRENYGLL----DPGKYRYLNN------GAGCKREVQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 334 LTQ-------EAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAA-MLGIQAEEFLKALTKP 405
Cdd:cd14889 218 YWKkkydevcNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAAgQFGVSEEDLLKTLTCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 406 RVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKE---IERKHfIGVLDIAGFEIFDLNSFEQLWI 482
Cdd:cd14889 298 VTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDdssVELRE-IGILDIFGFENFAVNRFEQACI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 483 NFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFgLDLQACIEL-IEKPLGIISILDEECIVPKATDMTYAQKlLDQHL 561
Cdd:cd14889 377 NLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDK-LNIHF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 562 GKHPNFQKP--KPPKgkqgdahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEEAAEA 639
Cdd:cd14889 455 KGNSYYGKSrsKSPK-------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSA-TPLLSVLFTATRSRTGTLMP 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 640 AKAGQTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRK 719
Cdd:cd14889 527 RAKLPQAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRRE 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 720 GFPNRMLYPDFKHRYAILAADAAKESDpKKASVGILDKISVDGnltdeeFKVGETKIFFK 779
Cdd:cd14889 607 GFSWRPSFAEFAERYKILLCEPALPGT-KQSCLRILKATKLVG------WKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-779 |
4.67e-135 |
|
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: 438.57 E-value: 4.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHF--MGKRRNE-------MPPHLFAVSDEAYRNMVQD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqEGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 170 KENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGgTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKL-SIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 250 FIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDIT-------YYHFCSQAEL- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITgglqlpnEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 322 TIEGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPD--GEEDALN-AAAMLGIQAEEF 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAeeGNEKCLArVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 399 LKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLD-AKEIERKHFIGVLDIAGFEIFDLNSF 477
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 478 EQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVP-KATDMTYAQK 555
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 556 LLDQHLGK----HPNFQKPKPPKGKQGDAHFAIVHYAGTVRYNA-TNFLEKNKDPLNDTAVALLKHSTDnslmldiwqdy 630
Cdd:cd14908 479 LYETYLPEknqtHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ----------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 631 qtqeeaaeaakagqtaggkrgksssfatvsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGV 710
Cdd:cd14908 548 --------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 711 LEGIRICRKGFPNRMLYPDFKHRYAILAADAAKES--------DPKKASVGILDKISVDG----------NLTDEEFKVG 772
Cdd:cd14908 596 LEAVRVARSGYPVRLPHKDFFKRYRMLLPLIPEVVlswsmerlDPQKLCVKKMCKDLVKGvlspamvsmkNIPEDTMQLG 675
|
....*..
gi 127737 773 ETKIFFK 779
Cdd:cd14908 676 KSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
42-832 |
2.30e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 432.92 E-value: 2.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 42 DPEDGFVAAEIQ-STTGEQVTVVTV---KGNQITVKKD---QCQEM-NPPKFDkteDMANLTFLNEASVLGNLKDRYKDL 113
Cdd:PTZ00014 47 DPDLMFAKCLVLpGSTGEKLTLKQIdppTNSTFEVKPEhafNANSQiDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 114 MIYTYSGLFCVVINPYKRLPIYSESVIKHFM-GKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGESGAGKTENTKKV 192
Cdd:PTZ00014 124 QIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 193 ISYFAivgatqaasgkEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGKLAGGDIEHYLLE 272
Cdd:PTZ00014 204 MRYFA-----------SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 273 KSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQAELTIEGMDDKEEMRLTQEAFDIMGFEDNETMDL 352
Cdd:PTZ00014 273 KSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKS-LEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 353 YRSTAGIMHMGEMKFKQRPREEQAE-----PDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVNWAV 427
Cdd:PTZ00014 352 FSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 428 SGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKR 507
Cdd:PTZ00014 432 DSLSKAVYEKLFLWIIRNLNATIEPPG-GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 508 EGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQhLGKHPNFQKPKppkgKQGDAHFAIVHY 587
Cdd:PTZ00014 511 EGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKYKPAK----VDSNKNFVIKHT 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 588 AGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEeaaeaakagqtagGKRGKSSSFATVSMiyrESL 667
Cdd:PTZ00014 586 IGDIQYCASGFLFKNKDVLRPELVEVVKASP-NPLVRDLFEGVEVEK-------------GKLAKGQLIGSQFL---NQL 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 668 NNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAADAAKES-- 745
Cdd:PTZ00014 649 DSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSsl 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 746 DPKKASVGILDKIsvdgNLTDEEFKVGETKIFFKAGVLAKLEDLRDEILSR---IVTMFQSRIRSYLAKAEVRRRYEQqt 822
Cdd:PTZ00014 729 DPKEKAEKLLERS----GLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIKS-- 802
|
810
....*....|
gi 127737 823 gLLVVQRNVR 832
Cdd:PTZ00014 803 -LVRIQAHLR 811
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-730 |
2.75e-131 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 429.31 E-value: 2.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVI---KHFM-----GKRRNEMPPHLFAVSDEAYRNMVQ-D 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLnayKASMtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 170 KENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTleeQIVQTNPVLEAFGNAKTVRNNNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 250 FIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITY----YHFCSQAELTIEG 325
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 326 MDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALN---AAAMLGIQAEEFLKAL 402
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHlakCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 403 TKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDA--------KEIERKHFIGVLDIAGFEIFDL 474
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYfdsavsisDEDEELATIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 475 NSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVPKATDMTYA 553
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 554 QKLLDQHLgkhpnfqkpkppkgkqGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDnslmlDIWQDYQTQ 633
Cdd:cd14902 477 TKFYRYHG----------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN-----EVVVAIGAD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 634 EEAAEAAKAGQTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEG 713
Cdd:cd14902 536 ENRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEA 615
|
650
....*....|....*..
gi 127737 714 IRICRKGFPNRMLYPDF 730
Cdd:cd14902 616 VRIARHGYSVRLAHASF 632
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-779 |
8.26e-131 |
|
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: 425.51 E-value: 8.26e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAIVGAtqaasgkeakdGKKGGTLEeQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----------GRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITY-YHFCSQAELTIEGMDDKEEMRLTQE 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYqYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALnAAAMLGIQAEEFLKALTKPRVRVGTEWVNKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 418 QNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHM 497
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 498 FVLEQEEYKREGIAWTFIDFGlDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQH--LGKHPNFQKPKPPKg 575
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 576 kqgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEeaaeaakagQTAGGKRGKSSS 655
Cdd:cd14904 466 ----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSS-LDLLTELFGSSEAPS---------ETKEGKSGKGTK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 FA-TVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd14904 532 APkSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127737 735 AILAADAAKESDPKKASVGILDKIsvdGNLTDEEFKVGETKIFFK 779
Cdd:cd14904 612 AIMFPPSMHSKDVRRTCSVFMTAI---GRKSPLEYQIGKSLIYFK 653
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
857-1937 |
1.00e-128 |
|
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: 433.45 E-value: 1.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDIT 936
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 937 GQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESN 1016
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1017 RKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRK 1096
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1097 EEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEA 1176
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1177 NKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQ 1256
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1257 DLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEES 1336
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1337 RERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNkLEEIEAAKKALQLKVQELTDT 1416
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1417 NEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFK 1496
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1497 AKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQI 1576
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1577 EVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTI 1656
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1657 KKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSAL 1736
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1737 TGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENA 1816
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1817 ALKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVE 1896
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 127737 1897 EA-EEVAASNLNKYKvLTAQFEQAEERADIAENALSKMRNKI 1937
Cdd:pfam01576 1041 EAeEEASRANAARRK-LQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
106-779 |
3.97e-128 |
|
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: 419.74 E-value: 3.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 106 LKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSesvikhfMGKRRNEMP------PHLFAVSDEAYRNM-------VQDKE 171
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD-------LHKYREEMPgwtalpPHVFSIAEGAYRSLrrrlhepGASKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 172 NQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTleeQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 251
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 252 RTHFSG-----SGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSG--NDPSLRGKLKLSNDITYYHFC-SQAELTI 323
Cdd:cd14895 157 RMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGaaDDMKLELQLELLSAQEFQYISgGQCYQRN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 324 EGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDA---LNAAAM---------- 390
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrLASASPssltvqqhld 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 391 -----LGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKH------ 459
Cdd:cd14895 317 ivsklFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNPnkaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 460 ----FIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGLDlQACIELIE-KPLGI 534
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 535 ISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPpkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALL 614
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASRT---DQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 615 KhSTDNSLMLDIWQDYQTqeEAAEAAKAGQTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASG 694
Cdd:cd14895 552 G-KTSDAHLRELFEFFKA--SESAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 695 VIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAAdAAKESDPKKASvgILDKISVDGnltdeeFKVGET 774
Cdd:cd14895 629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA-AKNASDATASA--LIETLKVDH------AELGKT 699
|
....*
gi 127737 775 KIFFK 779
Cdd:cd14895 700 RVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-779 |
7.77e-128 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 416.87 E-value: 7.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQaasgkeakDGKKGGTLEEQIvqtnPVLEAFGNAKTVRNNNSSRFGKFIRTHFSgSG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQ--------TEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHLQ-HG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPRE--EQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKG 417
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 418 QNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAK-EIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHH 496
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPgEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 497 MFVLEQEEYKREGIAWTFIDfGLDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQKlLDQHLGKHPNFQKPKPPKg 575
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQK-CHYHHGDHPSYAKPQLPL- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 576 kqgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStDNSLMLDIWQDYQTQeeaaeaakagqtAGGKRGKSss 655
Cdd:cd14896 465 ----PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQS-QLQLVGSLFQEAEPQ------------YGLGQGKP-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 faTVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA 735
Cdd:cd14896 526 --TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFG 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 127737 736 ILAADAAKESDPKKASVGILDKisVDGNLTDeEFKVGETKIFFK 779
Cdd:cd14896 604 ALGSERQEALSDRERCGAILSQ--VLGAESP-LYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-779 |
4.81e-125 |
|
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: 408.99 E-value: 4.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKhfmgKRRN-----EMPPHLFAVSDEAYRNMVQDKENQS 174
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIR----KYRDapdltKLPPHVFYTARRALENLHGVNKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 175 MLITGESGAGKTENTKKVISYFAivgatqaasgkEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTH 254
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFA-----------SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 255 FSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQAELTIEGMDDKEEMRL 334
Cdd:cd14876 146 VASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLL-GLKEYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 335 TQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKqrPREEQAEPD-----GEEDAL--NAAAMLGIQAEEFLKALTKPRV 407
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKIT--GKTEQGVDDaaaisNESLEVfkEACSLLFLDPEALKRELTVKVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 408 RVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNE 487
Cdd:cd14876 303 KAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPG-GFKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 488 RLQQFFNHHMFVLEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDmtyaQKLLDQHLGKHPNF 567
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSD----EKFVSACVSKLKSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 568 QKPKPPKGKQgDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEeaaeaakagqtag 647
Cdd:cd14876 458 GKFKPAKVDS-NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQAST-NPVVKALFEGVVVEK------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 648 GKRGKSSSFATVSMiyrESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLY 727
Cdd:cd14876 523 GKIAKGSLIGSQFL---KQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPF 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 127737 728 PDF--KHRYAILAADAAKESDPKKASVGILDKisvdGNLTDEEFKVGETKIFFK 779
Cdd:cd14876 600 EEFlyQFKFLDLGIANDKSLDPKVAALKLLES----SGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
100-738 |
5.45e-116 |
|
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: 383.82 E-value: 5.45e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRR-NEMPPHLFAVSDEAYRNMVQDKE--NQSM 175
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 176 LITGESGAGKTENTKKVISYFAIVgatqAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHF 255
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVV----AASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 256 SGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDiTYYHFCSQAELTIEgmddKEEMRLT 335
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEG-AAFSWLPNPERNLE----EDCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 336 QEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQA---EPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTE 412
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 413 WV--NKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQ 490
Cdd:cd14880 312 QQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 491 QFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQK 569
Cdd:cd14880 392 QHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 570 PKPPKgkqgDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLDIWQDyqtqeeaaeAAKAGQTAGGK 649
Cdd:cd14880 471 NKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN---------PEEKTQEEPSG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 650 RGKSSSFATVSMiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPD 729
Cdd:cd14880 538 QSRAPVLTVVSK-FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616
|
....*....
gi 127737 730 FKHRYAILA 738
Cdd:cd14880 617 FVERYKLLR 625
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
100-779 |
2.79e-112 |
|
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: 372.68 E-value: 2.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRN-----EMPPHLFAVSDEAYRNMVQDKENQ 173
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 174 SMLITGESGAGKTENTKKVISYFAiVGATQAASgkeakdgkkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRT 253
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFA-YGHSTSST-----------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 254 HFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQAE-LTIEGMDDKEEM 332
Cdd:cd14886 149 LVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKS-LESYNFLNASKcYDAPGIDDQKEF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 333 RLTQEAFDIMgFEDNETMDLYRSTAGIMHMGEMKFKQRPR---EEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRV 409
Cdd:cd14886 228 APVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 410 GTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKhFIGVLDIAGFEIFDLNSFEQLWINFVNERL 489
Cdd:cd14886 307 NNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARP-WIGILDIYGFEFFERNTYEQLLINYANERL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 490 QQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIEKP-LGIISILDEECIVPKATDMTYAQKlldqhLGKHPNFQ 568
Cdd:cd14886 386 QQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSS-----CKSKIKNN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 569 KPKPPKGKQgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTdNSLMLDIWQDYQTQEeaaeaakagqtaGG 648
Cdd:cd14886 460 SFIPGKGSQ--CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGST-NPIVNKAFSDIPNED------------GN 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 649 KRGKsssfaTVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYP 728
Cdd:cd14886 525 MKGK-----FLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 127737 729 DFKHRYAIL----AADAAKESDPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14886 600 EFFHRNKILishnSSSQNAGEDLVEAVKSILENLGIPCS----DYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-734 |
2.21e-108 |
|
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: 363.65 E-value: 2.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHF-------MGKR---RNEMPPHLFAVSDEAYRNMVQ 168
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRvtsTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 169 DKENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGG-----TLEEQIVQTNPVLEAFGNAKTVRNNN 243
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPAspsrtTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 244 SSRFGKFIRTHFSGSG-KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSL----RGKLKLSNDITYYHFCSQ 318
Cdd:cd14899 161 SSRFGKFIELRFRDERrRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVskeqKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 319 AELTI--EGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRP--REEQAEPDGEEDALN-------- 386
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARVMSSttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 387 --AAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL-------------- 450
Cdd:cd14899 321 tkAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 451 DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE- 529
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 530 KPLGIISILDEECIVPKATDMTYAQK--LLDQHLGKHPNFqkpKPPKGKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLN 607
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKyyLEFEKKNSHPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 608 DTAVALLKHSTdNSLMLDIWQDYQTQEEAAEAAKAGQTAGGKRGKSSSFATVSM--IYRESLNNLMNMLYQTHPHFIRCI 685
Cdd:cd14899 557 ESAAQLLAGSS-NPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVgtQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 127737 686 IPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRY 734
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
100-779 |
2.48e-106 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 356.04 E-value: 2.48e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMI-YTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEM-PPHLFAVSDEAYRNM-VQDKENQSML 176
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 177 ITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKggtLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHF- 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADK---IDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 256 SGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLR---GKLKLSNDityyHFCSQAELTI-------EG 325
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKkelGGLKTAQD----YKCLNGGNTFvrrgvdgKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 326 MDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQrPREEQAEPDGEEDALNAAAMLGIqAEEFLKA--LT 403
Cdd:cd14875 234 LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQL-DPAKLREcfLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 404 KPRVRVGTEWVNKgQNLEQVNWAvsgLAKAIYARMFKWIITRCNKTLDAK-EIERKHFIGVLDIAGFEIFDLNSFEQLWI 482
Cdd:cd14875 312 KSKTSLVTILANK-TEAEGFRNA---FCKAIYVGLFDRLVEFVNASITPQgDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 483 NFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGlDLQACIELIE-KPLGIISILDEECIVPKATDMTYAQKLLDQHL 561
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 562 GKHPNFQKPKPPKGKQgdahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDN---SLMLDiwqdyqtqeeaae 638
Cdd:cd14875 467 NKSPYFVLPKSTIPNQ----FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEfirTLLST------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 639 aakagqtaggKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICR 718
Cdd:cd14875 530 ----------EKGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127737 719 KGFPNRMLYPDF-KHRYAILAADAA---KESDPKKASVGILDKISVDGNLTDEEFKVGETKIFFK 779
Cdd:cd14875 600 QGYPVRRPIEQFcRYFYLIMPRSTAslfKQEKYSEAAKDFLAYYQRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
100-737 |
8.17e-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: 341.57 E-value: 8.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRN-EMPPHLFAVSDEAYRNMVQDKENQSMLI 177
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 178 TGESGAGKTENTKKVISYfaIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHF-S 256
Cdd:cd14906 81 SGESGSGKTEASKTILQY--LINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 257 GSGKLAGGDIEHYLLEKSRVV-RQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGM--------- 326
Cdd:cd14906 159 SDGKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnkns 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 327 ------DDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQ---RPREEQAEPDGEEDALNAAAMLGIQAEE 397
Cdd:cd14906 239 nhnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdsdFSKYAYQKDKVTASLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 398 FLKALTKPRVRVGTEWVNKGQNLE--QVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKH----------FIGVLD 465
Cdd:cd14906 319 FKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLaggsnkknnlFIGVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 466 IAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFgLDLQACIELIE-KPLGIISILDEECIV 544
Cdd:cd14906 399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 545 PKATDMTYAQKLLDQHlgkhpnFQKPKPPKGKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNslml 624
Cdd:cd14906 478 PKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNF---- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 625 dIWQDYQTQEEAAEAAKAGQTAGGkrgksssfATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQ 704
Cdd:cd14906 548 -LKKSLFQQQITSTTNTTKKQTQS--------NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQ 618
|
650 660 670
....*....|....*....|....*....|...
gi 127737 705 LTCNGVLEGIRICRKGFPNRMLYPDFKHRYAIL 737
Cdd:cd14906 619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCI 651
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
100-779 |
5.10e-95 |
|
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: 323.88 E-value: 5.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAIVGATQaasgkeakdgkkGGTLE-EQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGS 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSV------------GGVLSvEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKL----SNDITYYHFCSQAEltiegmdDKEE--- 331
Cdd:cd01386 149 GQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLnqlaESNSFGIVPLQKPE-------DKQKaaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 332 --MRLtQEAFDIMGFEDNETMDLYRSTAGIMHM---GEMKFKQRPREEQAEPdgeEDALNAAAMLGIQAEEFLKALTKPR 406
Cdd:cd01386 222 afSKL-QAAMKTLGISEEEQRAIWSILAAIYHLgaaGATKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 407 VRVGTEWVNKGQNLEQVNW------------AVSGLAKAIYARMFKWIITRCNKTLDAKeIERKHFIGVLDIAGFEifdl 474
Cdd:cd01386 298 LSGGPQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSS-HHSTSSITIVDTPGFQ---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 475 N----------SFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGLDLQACIELIEKPL------------ 532
Cdd:cd01386 373 NpahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrde 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 533 ---GIISILDEECIVPKATDMTYAQKLLdQHLGKHPNFQKPKPPKGKQGDAHFAIVHYAGT--VRYNATNFLEKNK-DPL 606
Cdd:cd01386 453 drrGLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 607 NDTAVALLKHSTDnslmldiwqdyqtqeeaaeaakagQTAGGKRgkSSSFATVSMiyreSLNNLMNMLYQTHPHFIRCII 686
Cdd:cd01386 532 AQNATQLLQESQK------------------------ETAAVKR--KSPCLQIKF----QVDALIDTLRRTGLHFVHCLL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 687 PN------EKKASGVIDSALVLN------QLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAADAAKES-------DP 747
Cdd:cd01386 582 PQhnagkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLglnsevaDE 661
|
730 740 750
....*....|....*....|....*....|..
gi 127737 748 KKASVGILDKISVDgnltDEEFKVGETKIFFK 779
Cdd:cd01386 662 RKAVEELLEELDLE----KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-779 |
3.47e-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: 314.83 E-value: 3.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFM---GKRRNEMPPHLFAVSDEAYRNMVQDKENQSML 176
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 177 ITGESGAGKTENTKKVISYFAivgatqaasgkeAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFS 256
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 257 GSGK-LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNdITYYHFCSQAEL----TIEGMDDKEE 331
Cdd:cd14878 149 ERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNN-LCAHRYLNQTMRedvsTAERSLNREK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 332 MRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGT 411
Cdd:cd14878 228 LAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 412 EWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL---DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNER 488
Cdd:cd14878 308 DMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 489 LQQFFNHHMFVLEQEEYKREGIAW-TFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPN- 566
Cdd:cd14878 388 MHHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNa 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 567 -FQKPK------PPKGkQGDAhFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStDNSLMLDIWQdyqtqeeaaea 639
Cdd:cd14878 468 vYSPMKdgngnvALKD-QGTA-FTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTS-ENVVINHLFQ----------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 640 akagqtaggkrgksSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRK 719
Cdd:cd14878 534 --------------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127737 720 GFPNRMLYPDFKHRYAILAADAAKESdpKKASVG-----ILDKISVDGnltdeeFKVGETKIFFK 779
Cdd:cd14878 600 GYPVRLSFSDFLSRYKPLADTLLGEK--KKQSAEercrlVLQQCKLQG------WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-779 |
5.18e-91 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 310.79 E-value: 5.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLpiysESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAivgatqaaSGKeakdgKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL--------SGV-----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDiTYYHFCSQAELTIEGMDDKEEMRLTQEAF 339
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSE-NEYKYIVNKNVVIPEIDDAKDFGNLMISF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 340 DIMGFEDNETmDLYRSTAGIMHMGEMKFKQRPREEQ---AEPDGEEDAL--NAAAMLGIQAEEFLKALTKPRVRVGTEWV 414
Cdd:cd14937 223 DKMNMHDMKD-DLFLTLSGLLLLGNVEYQEIEKGGKtncSELDKNNLELvnEISNLLGINYENLKDCLVFTEKTIANQKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 415 NKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEiERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFN 494
Cdd:cd14937 302 EIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 495 HHMFVLEQEEYKREGIAWTFIDFGLDlQACIELIEKPLGIISILDEECIVPKATDMTYAqKLLDQHLGKHPNFQKPKppk 574
Cdd:cd14937 381 YIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIV-SVYTNKFSKHEKYASTK--- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 575 gKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHStDNSLMLDIWQDYQTQeeaaeaakagQTAGGKRgkss 654
Cdd:cd14937 456 -KDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVS-NNKLVRSLYEDVEVS----------ESLGRKN---- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 655 sfaTVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRIcRKGFPNRMLYPDFKHRY 734
Cdd:cd14937 520 ---LITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 127737 735 AILAADAAKESD-PKKASVGILDKISVDGNLtdeeFKVGETKIFFK 779
Cdd:cd14937 596 EYLDYSTSKDSSlTDKEKVSMILQNTVDPDL----YKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
97-788 |
2.79e-87 |
|
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: 299.85 E-value: 2.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 97 LNEASVLGNLKDRY-KDLmIYTY---SGLfcVVINPYKRLPIYSESVIKHF------MGKRRNEM-PPHLFAVSDEAYRN 165
Cdd:cd14879 1 PSDDAITSHLASRFrSDL-PYTRlgsSAL--VAVNPYKYLSSNSDASLGEYgseyydTTSGSKEPlPPHAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 166 MVQDKENQSMLITGESGAGKTEN----TKKVISYfaivgatQAASGKEAKdgkkggtLEEQIVQTNPVLEAFGNAKTVRN 241
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESrrllLRQLLRL-------SSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 242 NNSSRFGKFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHF----CS 317
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasygCH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 318 QAELTIeGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQrpreeqaEPDGEEDA--------LN-AA 388
Cdd:cd14879 224 PLPLGP-GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvLDiVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 389 AMLGIQAEEFLKALTKPRVRVGTEWV----NKGQNLEQVNwavsGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVL 464
Cdd:cd14879 296 AFLGVSPEDLETSLTYKTKLVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 465 DIAGFEIFD---LNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFgLDLQACIELI-EKPLGIISILDE 540
Cdd:cd14879 372 DFPGFQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 541 EC-IVPKATDMTYAQKlLDQHLGKHPNFQKPKPPKGKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHstd 619
Cdd:cd14879 451 QTrRMPKKTDEQMLEA-LRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRG--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 620 nslmldiwqdyQTQEeaaeaakagqtaggkrgksssfatvsmiyRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSA 699
Cdd:cd14879 527 -----------ATQL-----------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKR 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 700 LVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYailaadaaKESDPKKASVGILDKISVDGNLTDEEFKVGETKIFFK 779
Cdd:cd14879 567 RVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY--------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFLS 638
|
....*....
gi 127737 780 AGVLAKLED 788
Cdd:cd14879 639 YAAWRMLED 647
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
91-779 |
6.38e-87 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 301.57 E-value: 6.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 91 MANLtFLNEASVLGNLKDRYKdlmIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDK 170
Cdd:cd14887 4 LENL-YQRYNKAYINKENRNC---IYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 171 ENQSMLITGESGAGKTENTKKVISYFAIVGATQaasgkeakDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKF 250
Cdd:cd14887 80 RSQSILISGESGAGKTETSKHVLTYLAAVSDRR--------HGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 251 IRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYqimsgndpSLRGKLKLSNdityyhfcSQAELTIEGMDDKE 330
Cdd:cd14887 152 LLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFY--------ALCNAAVAAA--------TQKSSAGEGDPEST 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 331 EMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKF--KQRPREEQAEP------------------------------ 378
Cdd:cd14887 216 DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFttDQEPETSKKRKltsvsvgceetaadrshssevkclssglkv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 379 -DGEEDALNAAAML-----GIQAEEFLK-ALTKPRVRVgtewVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLD 451
Cdd:cd14887 296 tEASRKHLKTVARLlglppGVEGEEMLRlALVSRSVRE----TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 452 --AKEIERK-----------HFIGVLDIAGFEIF---DLNSFEQLWINFVNERLQQFF------NHHMfVLEQEEYKREG 509
Cdd:cd14887 372 rsAKPSESDsdedtpsttgtQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLleqlilNEHM-LYTQEGVFQNQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 510 IAWTFiDFGLDLQAC--------IELIEKP--------------LGIISIL-DEECIVPKATDMTYAQKLLDQHLGKH-P 565
Cdd:cd14887 451 DCSAF-PFSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLsSSLSSSPPVWEGRDNSDLFYEKLNKNiI 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 566 NFQKPK--PPKGKQGDAHFAIVHYAGTVRYNATNFLEKNKDPL-NDTAVALLKHSTDNSLMLDiwqdyqtqeeaaeaaka 642
Cdd:cd14887 530 NSAKYKniTPALSRENLEFTVSHFACDVTYDARDFCRANREATsDELERLFLACSTYTRLVGS----------------- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 643 gQTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFP 722
Cdd:cd14887 593 -KKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 723 NRMLYPDFKHRYA-ILAADAAKESDPKKASVGILDKISVDGNltdeEFKVGETKIFFK 779
Cdd:cd14887 672 CRLPYVELWRRYEtKLPMALREALTPKMFCKIVLMFLEINSN----SYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-749 |
3.16e-84 |
|
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: 289.10 E-value: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSEsviKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKeNQSMLITGE 180
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGA---MKAYLKNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAivgatqaasgkeakDGKKGGT-LEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGsg 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV--------------ERTASTTsIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDpslrgkLKLSND-ITYYHFCSQAELTIEgmdDKEEMRLTQEA 338
Cdd:cd14898 142 KITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDfIDTSSTAGNKESIVQ---LSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 339 FDIMG---FEDNETMDLyrstaGIMHMGEMKFKQrprEEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVN 415
Cdd:cd14898 213 MKSLGianFKSIEDCLL-----GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 416 KGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLdakEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNH 495
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCL---EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 496 HMFVLEQEEYKREGIAWTFIDFgLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKhpnfqkpkpPKG 575
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGF---------INT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 576 KQGDAhFAIVHYAGTVRYNATNFLEKNKDPLNdtaVALLKhstdNSLMLDiwqdyqtqeeaaeaakagqtaggkRGKSSS 655
Cdd:cd14898 432 KARDK-IKVSHYAGDVEYDLRDFLDKNREKGQ---LLIFK----NLLIND------------------------EGSKED 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 656 FATVsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA 735
Cdd:cd14898 480 LVKY---FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556
|
650
....*....|....
gi 127737 736 ILAADAAKESDPKK 749
Cdd:cd14898 557 ILGITLFEVVDYRK 570
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-738 |
1.35e-78 |
|
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: 274.30 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPiysesVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG-----NPLTLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVI-SYFAIVGatqaasGKEAKDGKKggtleeQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSgSG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVAG------GGPETDAFK------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT-DG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLS----NDITYYhfcSQAELTIEGMDDKEEMRLT 335
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspANLRYL---SHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 336 QEAFDIMGFednETMDLYRSTAGIMHMGEMKFKQrPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVN 415
Cdd:cd14881 221 KACLGILGI---PFLDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 416 KGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKH----FIGVLDIAGFEIFDLNSFEQLWINFVNERLQQ 491
Cdd:cd14881 297 SVCDANMSNMTRDALAKALYCRTVATIVRRANSLKRLGSTLGTHatdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 492 FFNHHMFVLEQEEYKREGIAwTFIDFG-LDLQACIELIEK-PLGIISILDEECiVPKATDMTYAQKLLDQHLGkHPNFQK 569
Cdd:cd14881 377 FYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ-NPRLFE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 570 PKPpkgkQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLDIWQDYQTQeeaaeaakagqtaggk 649
Cdd:cd14881 454 AKP----QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFATHTQDFHTR---------------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 650 rgksssfatvsmiyresLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPD 729
Cdd:cd14881 514 -----------------LDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
....*....
gi 127737 730 FKHRYAILA 738
Cdd:cd14881 577 FNARYRLLA 585
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-726 |
2.03e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 275.25 E-value: 2.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFMGKRRNE-------MPPHLFAVSDEAYRNMVQDKE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 172 NQSMLITGESGAGKTENTKKVISYFAIVGATQAASgkeakdgkkggTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFI 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMT-----------ERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 252 RTHFS---------GSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHF------- 315
Cdd:cd14884 150 LLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdesh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 316 --------CSQAELTI-----EGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQrpreeqaepdgee 382
Cdd:cd14884 230 qkrsvkgtLRLGSDSLdpseeEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 383 dalnAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL----DAKEIERK 458
Cdd:cd14884 297 ----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckEKDESDNE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 459 H-------FIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDF--GLDLQACIELIE 529
Cdd:cd14884 373 DiysineaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 530 KPLGIISILDEECivPKATDMTYAQKLLD-----QHLGKH------PNFQKPKPPKGKQGDAHFAIVHYAGTVRYNATNF 598
Cdd:cd14884 453 RRLDDITKLKNQG--QKKTDDHFFRYLLNnerqqQLEGKVsygfvlNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 599 LEKNKDPLNDTAVALLKHSTDNSLmldiwqdyqtqeeaaeaakagqTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTH 678
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFL----------------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 127737 679 PHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRML 726
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-779 |
2.45e-72 |
|
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: 255.57 E-value: 2.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 100 ASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFmgkrrnemppHLFAVSDEAYRNMVQDKENQSMLI-T 178
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 179 GESGAGKTENTKKVISYFAivgatqaasgKEAKdgKKGGTLEEQIVQTnpVLEAFGNAKTVRNNNSSRFGKFIRTHFSgS 258
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT----------SQPK--SKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYK-R 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 259 GKLAGGDIEHYL-LEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLsNDITYYHFCSQAELTIEGMDDKEEMRLTQE 337
Cdd:cd14874 136 NVLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI-KGLQKFFYINQGNSTENIQSDVNHFKHLED 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 338 AFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRpreeqAEPDGEEDALN---------AAAMLGIQAEEFLKALTkPRVR 408
Cdd:cd14874 215 ALHVLGFSDDHCISIYKIISTILHIGNIYFRTK-----RNPNVEQDVVEignmsevkwVAFLLEVDFDQLVNFLL-PKSE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 409 VGTEwVNKGQNLEQVNwavsGLAKAIYARMFKWIITRCNktLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNER 488
Cdd:cd14874 289 DGTT-IDLNAALDNRD----SFAMLIYEELFKWVLNRIG--LHLKCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNER 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 489 LQQFFNHHMFVLEQEEYKREGIAwtfIDF----GLDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQKLLDQHLGK 563
Cdd:cd14874 362 IENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 564 hPNFQKPKppkgKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLdIWQDYQTQEeaaeaakag 643
Cdd:cd14874 439 -SSYGKAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGL-LFESYSSNT--------- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 644 qtaggkrgkSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPN 723
Cdd:cd14874 504 ---------SDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPV 574
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 724 RMLYPDFKHRY-AILAADAAKESDPKKAsvgILDKISVDGNLTDEEFKVGETKIFFK 779
Cdd:cd14874 575 KISKTTFARQYrCLLPGDIAMCQNEKEI---IQDILQGQGVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
101-779 |
1.01e-69 |
|
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: 249.24 E-value: 1.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLP-IYSESVIKHFmgKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFAivgatqaasgkeAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSG 259
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL------------TTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 260 KLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSnDITYYHFCSQ-AELTIEGMDDKEEMRLTQEA 338
Cdd:cd14905 148 EIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-DINSYHYLNQgGSISVESIDDNRVFDRLKMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 339 FDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRpreeqaepDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQ 418
Cdd:cd14905 227 FVFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--------NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 419 NLEQVNwavsGLAKAIYARMFKWIITRCNKTLdaKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMF 498
Cdd:cd14905 299 AVENRD----SLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 499 VLEQEEYKREGIAW-TFIDFGlDLQACIELIEKplgIISILDEECIVPKATDMTYAQKlLDQHLGKHPNFQKpKPPKgkq 577
Cdd:cd14905 373 KQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEK-LQNFLSRHHLFGK-KPNK--- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 578 gdahFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTD------------NSLMLDIWQDYQTQEEAAEAAKA--- 642
Cdd:cd14905 444 ----FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITkylfsrdgvfniNATVAELNQMFDAKNTAKKSPLSivk 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 643 -------------------------GQTAGGKRGKSSSFATVSMIYRESLNNlmnmlYQTHPHFIRCIIPNEKKASGVID 697
Cdd:cd14905 520 vllscgsnnpnnvnnpnnnsgggggGGNSGGGSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPNSKKTHLTFD 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 698 SALVLNQLTCNGVLEGIRICRKGFP----NRMLYPDF-----KHRYAILAADAAKESDpkkasvgildkISVDgNLTDEE 768
Cdd:cd14905 595 VKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRFsfffqNQRNFQNLFEKLKEND-----------INID-SILPPP 662
|
730
....*....|.
gi 127737 769 FKVGETKIFFK 779
Cdd:cd14905 663 IQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-778 |
2.05e-68 |
|
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: 247.19 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 103 LGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRR----------NEMPPHLFAVSDEAYRNMVQDKEN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 173 QSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 253 THFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSG--NDPSLRGKLKLSNDITYYHFCSQAELTIEGMD-DK 329
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 330 EEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQ--AEEFLKAL---TK 404
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpAQILLAAKlleVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 405 PRV------------RVGTEWVN--KGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTL--------DAKEIERKHFIG 462
Cdd:cd14893 324 PVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryeKSNIVINSQGVH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 463 VLDIAGFEIFD--LNSFEQLWINFVNERLQQFFNHHMFV-----LEQEEYKREG--IAWTFIDFGLDLQACIELIE-KPL 532
Cdd:cd14893 404 VLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEdKPF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 533 GIISILDEECIVPKATDMTYAQKLL--DQHLG--KHPNF------QKPKPPkgKQGDAHFAIVHYAGTVRYNATNFLEKN 602
Cdd:cd14893 484 GIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNMgadttnEYLAPS--KDWRLLFIVQHHCGKVTYNGKGLSSKN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 603 KDPLNDTAVALLkHSTDNSLMLDIWQDY-----------QTQEEAAEAAKAGQTAGGKR-GKSSSFATVSMIYRESlNNL 670
Cdd:cd14893 562 MLSISSTCAAIM-QSSKNAVLHAVGAAQmaaassekaakQTEERGSTSSKFRKSASSAReSKNITDSAATDVYNQA-DAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 671 MNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYA-ILAADAAKESdpkk 749
Cdd:cd14893 640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKnVCGHRGTLES---- 715
|
730 740
....*....|....*....|....*....
gi 127737 750 asvgILDKISVDGNLTDEEFKVGETKIFF 778
Cdd:cd14893 716 ----LLRSLSAIGVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-779 |
8.94e-62 |
|
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: 225.00 E-value: 8.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGE 180
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 181 SGAGKTENTKKVISYFAIVGatqaasgkeakDGKKGGTleEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGK 260
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----------DGNRGAT--GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 261 LAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSlrGKLK---LSNDITYYHFCSQAELTIEGM----DDKEE-- 331
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQ--NRLKeynLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGnv 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 332 --MRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRprEEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRV 409
Cdd:cd14882 227 erYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQN--GGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 410 GTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKE--IERKHFIGVLDIAGFEIFDLNSFEQLWINFVNE 487
Cdd:cd14882 305 GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRavFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 488 RLQQFFNHHMFVLEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEecivpKATDMTYAQKLLDQHLGKHPNF 567
Cdd:cd14882 385 QMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKHSQF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 568 QKPkppkgkQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLdIWQDYQTQEEaaeaakagqtag 647
Cdd:cd14882 460 VKK------HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKL-MFTNSQVRNM------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 648 gkRGKSSSFATVSMiyrESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLY 727
Cdd:cd14882 521 --RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 127737 728 PDFKHRYAILAADAAKESDPKKASVGILDKisvdgNLTDEEFKVGETKIFFK 779
Cdd:cd14882 596 QEFLRRYQFLAFDFDETVEMTKDNCRLLLI-----RLKMEGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-252 |
3.41e-54 |
|
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: 187.17 E-value: 3.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 122 FCVVINPYKRLPIYSESVIKHF-MGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGESGAGKTENTKKVISYFAIVG 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFyRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 127737 201 ATQAASGKEA---KDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIR 252
Cdd:cd01363 81 FNGINKGETEgwvYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIE 135
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-743 |
1.42e-46 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 180.80 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 101 SVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVI-KHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITG 179
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIeKYKCIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 180 ESGAGKTENTKKVISYFA------IVGATQAASGKEAKD-----GKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFG 248
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsRRLPTNLNDQEEDNIhneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 249 KFIRTHFSGSgKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDD 328
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 329 K---EEMRLTQEAFD--------------IMGFEDNETMDLYRSTAGIM-------------HMGEMKFKqrprEEQAEP 378
Cdd:cd14938 241 GkilELLKSLNYIFDddkeidfifsvlsaLLLLGNTEIVKAFRKKSLLMgknqcgqninyetILSELENS----EDIGLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 379 DGEEDALNAAAMLGIQAEEFLKALTKPRVrVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDA--KEIE 456
Cdd:cd14938 317 ENVKNLLLACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQlqNINI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 457 RKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGLD-LQACIELIEKPLGII 535
Cdd:cd14938 396 NTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 536 SILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQgdAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLK 615
Cdd:cd14938 476 FSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 616 HStDNSLMLDIWQDYQTQeeaaeaaKAGQTAGGKRGKSSSFA--------------TVSMIyRESLNNLMNMLYQTHPHF 681
Cdd:cd14938 554 QS-ENEYMRQFCMFYNYD-------NSGNIVEEKRRYSIQSAlklfkrrydtknqmAVSLL-RNNLTELEKLQETTFCHF 624
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 682 IRCIIPNEKKAS-GVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAADAAK 743
Cdd:cd14938 625 IVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNEDLKE 687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1182-1933 |
8.87e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.23 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1182 AEIAKLRREKEEDSLNHETAISSLrKRHGDSVAELTEQLETLQ-------KLKAKSEAEKSK-----------LQRDLEE 1243
Cdd:TIGR02168 165 AGISKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLErqaekaeRYKELKAELRELelallvlrleeLREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1244 SQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQS 1323
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1324 QLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGL------NKLE 1397
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiaslnNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1398 EIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFK-----LMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKK 1472
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1473 TDDLSSELDAAQRDNRQLSTDLFKAKTANDE----------------------------LAEYLDSTRRENKSLAQEVKD 1524
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVVVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1525 LTDQLGEGGRSVAELQKIV-RKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVS----------QIRSEIEKRIQEKE 1593
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1594 EEFENTRRNHQ---------RALESMQATLEAETKQKEEALRIkKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQ 1664
Cdd:TIGR02168 644 GYRIVTLDGDLvrpggvitgGSAKTNSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1665 ELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLE 1744
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1745 GELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAEnAALKGGKKI 1824
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1825 IAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKifkrqvEEAEEVAAS 1904
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS------EEYSLTLEE 955
|
810 820
....*....|....*....|....*....
gi 127737 1905 NLNKYKVLTAQFEQAEERADIAENALSKM 1933
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1037-1816 |
1.15e-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: 109.76 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1037 RNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIdEITKQKHDVETTL-----KRKEEDLHHTNAKLAENN 1111
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELELALlvlrlEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1112 SIIAKLQRLIKELTARNAELEEEleaeRNSRQKSdrsrseaereleeltERLEQQGGATAAQLEANKKREAEIAKLRREK 1191
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLE----VSELEEE---------------IEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1192 EEDSLnhetaisslrKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSE 1271
Cdd:TIGR02168 314 LERQL----------EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1272 LQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLhrLKSTLQSQLDETRRNYDEESRERqalaataKNLEH 1351
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL-------EELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1352 ENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDS--EGLNKLEEIEAAKKALQLKVQELTdtneGLFAKIASQEK 1429
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSleRLQENLEGFSEGVKALLKNQSGLS----GILGVLSELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1430 VRFK----------------LMQDLDDAQSDVE----KAAAQVAFYE-----------------KHRRQFESIIAEWKKK 1472
Cdd:TIGR02168 531 VDEGyeaaieaalggrlqavVVENLNAAKKAIAflkqNELGRVTFLPldsikgteiqgndreilKNIEGFLGVAKDLVKF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1473 TDDLS-------------SELDAAQRDNRQLSTDlFKAKTANDEL-----AEYLDSTRRENKSLA--QEVKDLTDQLGEG 1532
Cdd:TIGR02168 611 DPKLRkalsyllggvlvvDDLDNALELAKKLRPG-YRIVTLDGDLvrpggVITGGSAKTNSSILErrREIEELEEKIEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1533 GRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKE-EEFENTRRNHQRalESMQ 1611
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqLSKELTELEAEI--EELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1612 ATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIK-------KYMETVQELQFQIEEEQRQKDEIREQF 1684
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLRERLESLERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1685 LASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNA 1764
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 127737 1765 VEQGQKASADAARLAEELRQEQEHSM-HIERIRKGLELQIKEMQIRLDDAENA 1816
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLeEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
853-1638 |
2.52e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 853 LKAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKL 932
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 933 SDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSrdhnirsLQDEMANQDEAVAKLNKEKKHQ 1012
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1013 EESNRKLNEDLQSEEDKVNHLEK----IRNK---LEQQMDELEENIDREKRSRGDIEkaKRKVEGDLKVAQENIDEITKQ 1085
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELqiasLNNEierLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1086 KHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTArnaeleeeLEAERNSRQKSDRSRSEAERELEELTERLEQ 1165
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA--------RLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1166 QGGATAAQLEANKKREAEIAKLRREK-----EEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEK------ 1234
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAALGGRlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILkniegf 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1235 -----------SKLQRDLE----------------ESQHATDSEVR------------------------SRQDLEKALK 1263
Cdd:TIGR02168 601 lgvakdlvkfdPKLRKALSyllggvlvvddldnalELAKKLRPGYRivtldgdlvrpggvitggsaktnsSILERRREIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1264 TIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALA 1343
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1344 ATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDseglnkleEIEAAKKALQLKVQELTDTNEGLFAK 1423
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--------ELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1424 IASQEKVRFKLMQDLDDAQSDVEKAAAQvafyekhrrqfesiIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDE 1503
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1504 LAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAEL-QKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIR 1582
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 1583 SEIEK-------RIQEKEEefENTRRNHQralesmqatleaeTKQKEEALRIKKKLESDINDL 1638
Cdd:TIGR02168 979 NKIKElgpvnlaAIEEYEE--LKERYDFL-------------TAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1007-1921 |
2.02e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1007 KEKKHQEESN-RKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEenidREKRSRGDIEKAKRKVEG-DLKVAQENIDEITK 1084
Cdd:TIGR02168 171 KERRKETERKlERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALLVlRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1085 QKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAeleeeleaernsrqksdrsrseaereleelterle 1164
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----------------------------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1165 qqggaTAAQLEANKKREAEIAKLRREKEEDSLnhetaisslrKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEES 1244
Cdd:TIGR02168 292 -----ALANEISRLEQQKQILRERLANLERQL----------EELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1245 QHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLhrLKSTLQSQ 1324
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL--LKKLEEAE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1325 LDETRRNYDEESRERqalaataKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDS--EGLNKLEEIEAA 1402
Cdd:TIGR02168 435 LKELQAELEELEEEL-------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSleRLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1403 KKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDL-DDAQS----DVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLS 1477
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALgGRLQAvvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1478 S---ELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVkDLTDQLGEGGRSVAELQKIVRKlevekeelq 1554
Cdd:TIGR02168 588 GndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL-ELAKKLRPGYRIVTLDGDLVRP--------- 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1555 kaldeaEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTrrnhQRALESMQATLEAETKQKEEALRIKKKLESD 1634
Cdd:TIGR02168 658 ------GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL----EKALAELRKELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1635 INDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRn 1714
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD- 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1715 aeaeciELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIER 1794
Cdd:TIGR02168 807 ------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1795 IRKGLELQIKEMQIRLDDAENAalkggkkiIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEE---- 1870
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEE--------LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEyslt 952
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 1871 ----KKNEERLTELVDKLQCKLKIFKRQV-----------EEAEEVAAsnlnKYKVLTAQFEQAEE 1921
Cdd:TIGR02168 953 leeaEALENKIEDDEEEARRRLKRLENKIkelgpvnlaaiEEYEELKE----RYDFLTAQKEDLTE 1014
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
106-718 |
1.48e-20 |
|
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: 99.05 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 106 LKDRYKDLMIYTYSGLFCV-VINPYKRL------PIYSESVIKHFMGKRRNE--MPPHLFAVSDEAYRNMVQDKEN---- 172
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLFFDNEHtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 173 ---------------QSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTL------------------ 219
Cdd:cd14894 87 pstissnrsmtegrgQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSEETCKVSGSTRqpkiklftsstkstiqmr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 220 ---------------------------------------------------------------EEQ-------------- 222
Cdd:cd14894 167 teeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQlrmyfknphaakkl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 223 --IVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFS-----GSGKLAGGDIEHYLLEKSRVVRQA------PGERCYHIF 289
Cdd:cd14894 247 siVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAfglhpWEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHIL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 290 YQIMSGND--PSLR---GKLKLSN-DITYYHFCSQAELTIEGMDDKEEM------RLTQ--EAFDIMGFEDNETMDLYRS 355
Cdd:cd14894 327 YAMVAGVNafPFMRllaKELHLDGiDCSALTYLGRSDHKLAGFVSKEDTwkkdveRWQQviDGLDELNVSPDEQKTIFKV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 356 TAGIMHMGEMKFKQRPREEQAEPDgEEDALNAAAM------LGiQAEEFLKALTKPRVRVGTEWVNKGQNLE--QVNWAV 427
Cdd:cd14894 407 LSAVLWLGNIELDYREVSGKLVMS-STGALNAPQKvvelleLG-SVEKLERMLMTKSVSLQSTSETFEVTLEkgQVNHVR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 428 SGLAKAIYARMFKWIITRCNKTL----------------DAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLqq 491
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL-- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 492 ffnhhmfvleqeeYKRE----GIAWTFID--FGLDLQACIELI-EKPLGIISILDEECIVPKATDMTYAQ-----KLLDQ 559
Cdd:cd14894 563 -------------YAREeqviAVAYSSRPhlTARDSEKDVLFIyEHPLGVFASLEELTILHQSENMNAQQeekrnKLFVR 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 560 HLGKHPNFQKPKPPKG-KQGDAH---------FAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLDIWQD 629
Cdd:cd14894 630 NIYDRNSSRLPEPPRVlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 630 YQTQEEAAEAAKAGQTAGGKRGKSSSFATVsmiYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNG 709
Cdd:cd14894 710 SQLGWSPNTNRSMLGSAESRLSGTKSFVGQ---FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQR 786
|
....*....
gi 127737 710 VLEGIRICR 718
Cdd:cd14894 787 LIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
860-1782 |
2.12e-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: 98.98 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 860 EAMGELAVKIQKlEEAVQRGEIARSQLEsQVADLVEEknalflsLETEKANLADAEERNEKLNQLKATLES-KLSDITGQ 938
Cdd:TIGR02168 163 EAAGISKYKERR-KETERKLERTRENLD-RLEDILNE-------LERQLKSLERQAEKAERYKELKAELRElELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 939 LEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRK 1018
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1019 LNEDLQSeedkvnhLEKIRNKLEQQMDELEENIDRekrsrgdIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEE 1098
Cdd:TIGR02168 314 LERQLEE-------LEAQLEELESKLDELAEELAE-------LEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1099 DLHHTNAKLAEnnsiiaklqrlikeltarnaeleeeleaernsrqksdrsrseaereleelterLEQQGGATAAQLEANK 1178
Cdd:TIGR02168 380 QLETLRSKVAQ-----------------------------------------------------LELQIASLNNEIERLE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1179 KREAEIAK-LRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDS---EVRS 1254
Cdd:TIGR02168 407 ARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAaerELAQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1255 RQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLnnenSDLNRSLEEMDNQLNSLhrLKSTLQSQLDETrrnyde 1334
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL----SELISVDEGYEAAIEAA--LGGRLQAVVVEN------ 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1335 ESRERQALAATAKNLEHENTILREHLDEEAESKADltrqisklNAEIQQWKARFDSEGLNKLEEIEAAKKALQlkvqelt 1414
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGN--------DREILKNIEGFLGVAKDLVKFDPKLRKALS------- 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1415 dtneGLFAKIAsqekvrfkLMQDLDDAQSDVEKAAAQVAF-------------YEKHRRQFESIIAEWKKKTDDLSSELD 1481
Cdd:TIGR02168 620 ----YLLGGVL--------VVDDLDNALELAKKLRPGYRIvtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIE 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1482 AAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAE 1561
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1562 AALEAEEAkvlrAQIEVSQIRSEIEKRIQEKEEEFENTRRNHqRALESMQATLEAETKQKEEALrikKKLESDINDLEIA 1641
Cdd:TIGR02168 768 ERLEEAEE----ELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERL---ESLERRIAATERR 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1642 LDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIE 1721
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127737 1722 LREQNNDLNAHVSALTGQRRKLEGELLAAHA-ELEEIANELKNAVEQGQKASADAARLAEEL 1782
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1291-1939 |
7.98e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1291 NRLNNENSDLNRS---LEEMDNQLNSLHRlkstlQSQLDETRRNYDEESRERQALAATAKNLEhentiLREHLDEEAESK 1367
Cdd:COG1196 179 RKLEATEENLERLediLGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLRE-----LEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1368 ADLTRQISKLNAEIQQWKARfdseglnkLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEK 1447
Cdd:COG1196 249 EELEAELEELEAELAELEAE--------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1448 AAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTD 1527
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1528 QLGEGGRSVAELQKIVRKLEVEKEELQkaldeaeaaleaeeakvlRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRAL 1607
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELE------------------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1608 ESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLAs 1687
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1688 ekrnailqsekDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQ 1767
Cdd:COG1196 542 -----------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1768 GQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKGGKKIIAQLEARIRAIEQELDGEQRRHQ 1847
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1848 DTEKNWRKAERRVKEVEfQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKykvLTAQFEQAEERADIAE 1927
Cdd:COG1196 691 EELELEEALLAEEEEER-ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE---EALEELPEPPDLEELE 766
|
650
....*....|..
gi 127737 1928 NALSKMRNKIRA 1939
Cdd:COG1196 767 RELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
999-1701 |
1.24e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 999 DEA--VAKLnKEKKHqeESNRKLNEdlqsEEDKVNHLEKIRNKLEQQMDELEEniDREK-RSRGDIEKAKRKVEGDLKV- 1074
Cdd:COG1196 162 EEAagISKY-KERKE--EAERKLEA----TEENLERLEDILGELERQLEPLER--QAEKaERYRELKEELKELEAELLLl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1075 ----AQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQksdrsrs 1150
Cdd:COG1196 233 klreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1151 eaereleelterleqqggATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRhgdsVAELTEQLETLQKLKAKS 1230
Cdd:COG1196 306 ------------------RLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1231 EAEKSKLQRDLEESQHATDSEVRSRQDLEKALktievqySELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQ 1310
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAA-------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1311 LNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDS 1390
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1391 EGLNKLeeieAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFY--EKHRRQFESIIAE 1468
Cdd:COG1196 517 AGLRGL----AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLplDKIRARAALAAAL 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1469 WKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEV 1548
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1549 EKEELQkaldeaeaaleaeeakvlraqievsQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIK 1628
Cdd:COG1196 673 ALLEAE-------------------------AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1629 KKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEI----------------REQFLASEKrnA 1692
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeeleeRYDFLSEQR--E 805
|
....*....
gi 127737 1693 ILQSEKDEL 1701
Cdd:COG1196 806 DLEEARETL 814
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
853-1695 |
9.57e-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: 93.59 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 853 LKAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKL-----NQLKAT 927
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 928 LES---KLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMA---NQDEA 1001
Cdd:TIGR02169 296 IGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlrAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1002 VAKLNKEKKHQEESNRKLNEDLQSEedkVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDE 1081
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKRE---INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1082 ITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTArnaeleeeleaernsRQKSDRSRSEAERELEELTE 1161
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA---------------QARASEERVRGGRAVEEVLK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1162 RLEQQGGATAAQLEANKKREA---EIAKLRREKE---EDSLNHETAISSLRKRHGDSVAELTeqletLQKLKAKsEAEKS 1235
Cdd:TIGR02169 518 ASIQGVHGTVAQLGSVGERYAtaiEVAAGNRLNNvvvEDDAVAKEAIELLKRRKAGRATFLP-----LNKMRDE-RRDLS 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1236 KLQRD--LEESQHATDSEVRSR-------------QDLEKA--------LKTIE---VQYSELQTKADEQSRQLQDFAAl 1289
Cdd:TIGR02169 592 ILSEDgvIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAArrlmgkyrMVTLEgelFEKSGAMTGGSRAPRGGILFSR- 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1290 knRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKAD 1369
Cdd:TIGR02169 671 --SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1370 LTRQISKLNAEIQQWKARfdseglnkLEEIEAAKKALQLKVQELTDtneglfakiasqekvrfklmqdlDDAQSDVEKAA 1449
Cdd:TIGR02169 749 LEQEIENVKSELKELEAR--------IEELEEDLHKLEEALNDLEA-----------------------RLSHSRIPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1450 AQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQrDNRQlstdlfkaktandELAEYLDSTRRENKSLAQEVKDLTDQL 1529
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-KEIQ-------------ELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1530 GEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIR---SEIEKRIQEKEEEFENTRRNHQRA 1606
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlSELKAKLEALEEELSEIEDPKGED 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1607 LESMQATLEAETKQKEealriKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELqfqiEEEQRQKDEIREQFlA 1686
Cdd:TIGR02169 944 EEIPEEELSLEDVQAE-----LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL----EEERKAILERIEEY-E 1013
|
....*....
gi 127737 1687 SEKRNAILQ 1695
Cdd:TIGR02169 1014 KKKREVFME 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1184-1838 |
2.17e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1184 IAKLRREKEEdslnhetaisSLRK---------RHGDSVAELTEQLETLQKlkaksEAEKSKLQRDLEESQHATDSEVRS 1254
Cdd:COG1196 167 ISKYKERKEE----------AERKleateenleRLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1255 RQdlekaLKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDE 1334
Cdd:COG1196 232 LK-----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1335 ESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEgLNKLEEIEAAKKALQLKVQELT 1414
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1415 DTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDL 1494
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1495 FKAKTANDELAEYLDSTRRE------NKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEE 1568
Cdd:COG1196 466 AELLEEAALLEAALAELLEElaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1569 AKVLRAQIEVSQIRSEIEKRIQEK-----------EEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDIND 1637
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAkagratflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1638 LEIALDHANRAY-----ADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNA-ILQSEKDELAQQAEAAERA 1711
Cdd:COG1196 626 TLVAARLEAALRravtlAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAeRLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1712 RRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQ------- 1784
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnll 785
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 127737 1785 -EQEHsmhiERIRKGLElqikEMQIRLDDAENAalkggkkiIAQLEARIRAIEQE 1838
Cdd:COG1196 786 aIEEY----EELEERYD----FLSEQREDLEEA--------RETLEEAIEEIDRE 824
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
947-1684 |
3.86e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 91.24 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 947 EDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQdemANQDEAVAKLNKEKKHQEESNR---KLNEDL 1023
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDKINKLNSdlsKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1024 QSEEDKVNHLEKIRNKLEQQMDELEENIDrekrsrgDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHT 1103
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNID-------KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1104 NAKLAENNSIIAKLQRLIKELTARNaeleeeleaernsrqksdrsrseaereleelterleqqggataaqlEANKKREAE 1183
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKI----------------------------------------------QKNKSLESQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1184 IAKLrrekEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATdsevRSRQDLEKALK 1263
Cdd:TIGR04523 220 ISEL----KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN----KKIKELEKQLN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1264 TIEVQYSELQTKADEqsrqlqdfaalknrlnNENSDLNRSLEEMDNQLnslhrlkSTLQSQLDETRRNYDEESRERQALA 1343
Cdd:TIGR04523 292 QLKSEISDLNNQKEQ----------------DWNKELKSELKNQEKKL-------EEIQNQISQNNKIISQLNEQISQLK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1344 ATAKNLEHENTILREHLDEEaeskadlTRQISKLNAEIQQWKarfdseglNKLEEIEAAKKALQLKVQELTDTNEGLFAK 1423
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEK-------QNEIEKLKKENQSYK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1424 IASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDE 1503
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1504 LAEYLDSTRRENKSLAQEVKDLTDQlgeggrsVAELQKIVRKLEVEKEELQKALDEAEAALEaeeakvlraQIEVSQIRS 1583
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKK-------ISSLKEKIEKLESEKKEKESKISDLEDELN---------KDDFELKKE 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1584 EIEKRIQEKEEEFENTRRNhQRALESMQATLEAETKQKE-EALRIKKKLESD---INDLEIALDHANRAYADAQKTIKKY 1659
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQT-QKSLKKKQEEKQELIDQKEkEKKDLIKEIEEKekkISSLEKELEKAKKENEKLSSIIKNI 636
|
730 740
....*....|....*....|....*
gi 127737 1660 METVQELQFQIEEEQRQKDEIREQF 1684
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
783-1416 |
8.41e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 783 LAKLEDLRDEILSRIVTmfqsrirsyLAK-AEVRRRYEQQTGLLvvqRNVRAWCTLRTWEWFKL-FGKVKpmLKAGKEQE 860
Cdd:COG1196 188 LERLEDILGELERQLEP---------LERqAEKAERYRELKEEL---KELEAELLLLKLRELEAeLEELE--AELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 861 AMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLE 940
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 941 DMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLN 1020
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1021 EDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDL 1100
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1101 HHTNA------------KLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGG 1168
Cdd:COG1196 494 LLLLEaeadyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1169 ATAAQLEANKKREAEIAKLRREKEED--SLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKlQRDLEESQH 1246
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAavDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA-GRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1247 ATDSEVRSRQdLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLD 1326
Cdd:COG1196 653 GEGGSAGGSL-TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1327 ETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAEskaDLTRQISKLNA-------EIQQWKARFDSegLN-KLEE 1398
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELE---RLEREIEALGPvnllaieEYEELEERYDF--LSeQRED 806
|
650
....*....|....*...
gi 127737 1399 IEAAKKALQLKVQELTDT 1416
Cdd:COG1196 807 LEEARETLEEAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1013-1897 |
1.24e-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: 90.13 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1013 EESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEEniDREKRSR-GDIEKAKRKVEGDLKVAQENIDEitKQKHDVET 1091
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR--EREKAERyQALLKEKREYEGYELLKEKEALE--RQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1092 TLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATA 1171
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1172 AQLeankkrEAEIAKLRREKEedslnhetaisslrkrhgdsvaELTEQLETLQKLKAKSEAEKSKLQRDLEESqhatdse 1251
Cdd:TIGR02169 325 AKL------EAEIDKLLAEIE----------------------ELEREIEEERKRRDKLTEEYAELKEELEDL------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1252 VRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRN 1331
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1332 YDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARfDSEGLNKLEEIEAAKKALQLKVQ 1411
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1412 ELTDTNEGLFAKI--ASQEKVRFKLMQDLDDAQSDVE----KAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQR 1485
Cdd:TIGR02169 529 QLGSVGERYATAIevAAGNRLNNVVVEDDAVAKEAIEllkrRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1486 DNRQLStdLFKAKTANDELAEYLDSTRRENK-----SLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEA 1560
Cdd:TIGR02169 609 DPKYEP--AFKYVFGDTLVVEDIEAARRLMGkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1561 EAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEefentRRNHQRALESMQATLEAETKQKEEALRikkKLESDINDLEI 1640
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGE-----IEKEIEQLEQEEEKLKERLEELEEDLS---SLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1641 ALDHANRAYADAQKTIKKYMETVQEL-----QFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNA 1715
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1716 EAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKnaveqgqkasadaarlaeelrqeqehsmHIERI 1795
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG----------------------------DLKKE 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1796 RKGLELQIKEMQIRLDDAEnAALKGGKKIIAQLEARIRAIEQELD-------------GEQRRHQDTEKNWRKAERRVK- 1861
Cdd:TIGR02169 891 RDELEAQLRELERKIEELE-AQIEKKRKRLSELKAKLEALEEELSeiedpkgedeeipEEELSLEDVQAELQRVEEEIRa 969
|
890 900 910
....*....|....*....|....*....|....*....
gi 127737 1862 --EVEFQVVEE-KKNEERLTELVDKLQcKLKIFKRQVEE 1897
Cdd:TIGR02169 970 lePVNMLAIQEyEEVLKRLDELKEKRA-KLEEERKAILE 1007
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
907-1508 |
8.74e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 86.61 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 907 EKANLADAEERNEKLNQLKaTLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDH 986
Cdd:TIGR04523 60 DKNLNKDEEKINNSNNKIK-ILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 987 NIRSLQDEMANQDEAVAKLN-------KEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRG 1059
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNnkyndlkKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1060 DIEKAKRKVegdlKVAQENIDEITKQKHDVETTLKRKEEDLHHTnakLAENNSIIAKLQRLIKELtarnaeleeeleaer 1139
Cdd:TIGR04523 219 QISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQL---KDEQNKIKKQLSEKQKEL--------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1140 nsrqksdrsrseaereleelterleQQGGATAAQLEAN-KKREAEIAKLRREKEEDSLNH---------------ETAIS 1203
Cdd:TIGR04523 277 -------------------------EQNNKKIKELEKQlNQLKSEISDLNNQKEQDWNKElkselknqekkleeiQNQIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1204 SLRKrhgdSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQ---- 1279
Cdd:TIGR04523 332 QNNK----IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQekln 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1280 -----------------SRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQAL 1342
Cdd:TIGR04523 408 qqkdeqikklqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1343 AATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQwkarFDSEGLNKLEEIEAAKKALQLKVQELtdTNEGLFA 1422
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----LESEKKEKESKISDLEDELNKDDFEL--KKENLEK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1423 KIASQEKVRFKLMQD---LDDAQSDVEKAAAQvafYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKT 1499
Cdd:TIGR04523 562 EIDEKNKEIEELKQTqksLKKKQEEKQELIDQ---KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
....*....
gi 127737 1500 ANDELAEYL 1508
Cdd:TIGR04523 639 KKNKLKQEV 647
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
4.80e-16 |
|
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: 73.62 E-value: 4.80e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 127737 33 DSKKNCWIPDPEDGFVAAEIQSTTGEQVTVVTVKGNQITVKKDQC 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
873-1553 |
5.01e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 873 EEAVQRGEIARSQLEsQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKlsditgQLEDMQERNEDLARQ 952
Cdd:COG1196 175 EEAERKLEATEENLE-RLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLL------KLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 953 KKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNH 1032
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1033 LEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNS 1112
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1113 IIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKE 1192
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1193 EDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKS---EAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQY 1269
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1270 SELQTKAdeqsrqlqDFAALknrlnneNSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNL 1349
Cdd:COG1196 568 AAKAGRA--------TFLPL-------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1350 EHENTILREHLDEEAESKADLTRQisklnAEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEK 1429
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGG-----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1430 VRFKLMQDLDDAQSDVEKAAAQVafyEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDEL----- 1504
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQL---EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnl 784
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 127737 1505 --AEYLDSTRRENKSLAQEVKDLTdqlgeggRSVAELQKIVRKLEVEKEEL 1553
Cdd:COG1196 785 laIEEYEELEERYDFLSEQREDLE-------EARETLEEAIEEIDRETRER 828
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1034-1938 |
1.58e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 83.10 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1034 EKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVegdlkvaqENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNsi 1113
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLA--------ELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1114 iAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEE 1193
Cdd:pfam02463 222 -EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1194 DSLNHETAISSLRkrhgdsvaeltEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQdlekALKTIEVQYSELQ 1273
Cdd:pfam02463 301 ELLKLERRKVDDE-----------EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE----AEEEEEEELEKLQ 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1274 TKAdeqsRQLQDFAALKNRLNNENsdLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHEN 1353
Cdd:pfam02463 366 EKL----EQLEEELLAKKKLESER--LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1354 TILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQELT------DTNEGLFAKIASQ 1427
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1428 EKVRFKLMQ-DLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELae 1506
Cdd:pfam02463 520 VGGRIISAHgRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL-- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1507 YLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIE 1586
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1587 KRIQEKEEEFENTRRNHQRALESMQatLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETvqel 1666
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIK--KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE---- 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1667 qfqiEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGE 1746
Cdd:pfam02463 752 ----EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1747 LLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKGGKKIIA 1826
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1827 QLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNL 1906
Cdd:pfam02463 908 KLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE 987
|
890 900 910
....*....|....*....|....*....|..
gi 127737 1907 NKYKVLTAQFEQAEERADIAENALSKMRNKIR 1938
Cdd:pfam02463 988 ERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1297-1940 |
4.43e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1297 NSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNydEESRERQALAATAKNLEHENTilrehldEEAESKADLTRQISK 1376
Cdd:PTZ00121 1038 NDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGL--KPSYKDFDFDAKEDNRADEAT-------EEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1377 LNAEIQQWK--ARFDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQ-SDVEKAAAQVA 1453
Cdd:PTZ00121 1109 GKAEEARKAeeAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKkAEAARKAEEVR 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1454 FYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGG 1533
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1534 RSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQAT 1613
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1614 LEAETKQKEEALRIKKKLESDINDLEIAldhanRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQflASEKRNAI 1693
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA--AAAKKKAD 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1694 LQSEKDElAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKaSA 1773
Cdd:PTZ00121 1422 EAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK-KA 1499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1774 DAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKGGKKIIAQLEaRIRAIEQELDGEQRRHQDTEKNW 1853
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1854 --RKAErrvkevEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEE---AEEVAASNLNKYKVLTAQFEQAEERADIAEN 1928
Cdd:PTZ00121 1579 alRKAE------EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
650
....*....|..
gi 127737 1929 ALSKMRNKIRAS 1940
Cdd:PTZ00121 1653 KKAEEENKIKAA 1664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1000-1807 |
7.66e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 80.93 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1000 EAVAKLNKEKKHQ-EESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEenidREKRSRGDIEKAKRKVEGDLKvaqen 1078
Cdd:pfam15921 74 EHIERVLEEYSHQvKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQ----MERDAMADIRRRESQSQEDLR----- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1079 iDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKEL--------TARNAELEEELEAERNSRQKSDRSRS 1150
Cdd:pfam15921 145 -NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIrsilvdfeEASGKKIYEHDSMSTMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1151 EAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLN-----HETAISSLRKRHGDSVAELTEQLETLQK 1225
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEqliseHEVEITGLTEKASSARSQANSIQSQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1226 LKAKSEAEKSKLQRDLEESQhATDSEVRSrqDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLE 1305
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLE-STVSQLRS--ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1306 EMdnqLNSLHRLKSTLQSQLDETRRNYDEESrerqalaataknlehENTILREHLDEEAEskaDLTRQISKLNAEIQQWK 1385
Cdd:pfam15921 381 KL---LADLHKREKELSLEKEQNKRLWDRDT---------------GNSITIDHLRRELD---DRNMEVQRLEALLKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1386 ARFDSEGLNKLEEIEAAKKALQlKVQELTdtneglfAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESI 1465
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLE-KVSSLT-------AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1466 IAEWKKKTDDLSSELDAAQRDNRQLSTD---LFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQki 1542
Cdd:pfam15921 512 IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ-- 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1543 VRKLEVEKE------ELQ-----------KALDEAEAALEAEEAKV---------LRAQIEVSQIRSEIEKRIQEKE--- 1593
Cdd:pfam15921 590 VEKAQLEKEindrrlELQefkilkdkkdaKIRELEARVSDLELEKVklvnagserLRAVKDIKQERDQLLNEVKTSRnel 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1594 ----EEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQ 1669
Cdd:pfam15921 670 nslsEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1670 IeeeqrqkdeireQFLASEKRNAilQSEKDELaqqaeaaerarrnaeaecielREQNNDLNAHVSALTGQRRKLEGELLA 1749
Cdd:pfam15921 750 I------------QFLEEAMTNA--NKEKHFL---------------------KEEKNKLSQELSTVATEKNKMAGELEV 794
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1750 AHAELEEIANELKNAVEQGQKASADAARLAEEL-RQEQEHSmhieRIRKGLELQIKEMQ 1807
Cdd:pfam15921 795 LRSQERRLKEKVANMEVALDKASLQFAECQDIIqRQEQESV----RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1178-1934 |
1.01e-14 |
|
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: 80.50 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1178 KKREAEIAKLRREKEEdslnHETAISSLRKRhgdsVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQ- 1256
Cdd:TIGR02169 219 EKREYEGYELLKEKEA----LERQKEAIERQ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQl 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1257 DLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEES 1336
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1337 RERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARfdseglnkLEEIEAAKKALQLKVQELTDT 1416
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE--------LADLNAAIAGIEAKINELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1417 NEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFK 1496
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1497 AKTANDELAEYldstrRENKSLAQEVkdltdqlGEGGRsvaeLQKIVrkleVEKEELQKALDEAEAALEAEEA------K 1570
Cdd:TIGR02169 523 VHGTVAQLGSV-----GERYATAIEV-------AAGNR----LNNVV----VEDDAVAKEAIELLKRRKAGRAtflplnK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1571 VLRAQIEVSQIRSE----IEKRIQEKEEEFENTRRnhqralESMQATLEAETKQKEEALRIKKK---LESDINDLEIALD 1643
Cdd:TIGR02169 583 MRDERRDLSILSEDgvigFAVDLVEFDPKYEPAFK------YVFGDTLVVEDIEAARRLMGKYRmvtLEGELFEKSGAMT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1644 HANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDeireqFLASEKRNaiLQSEKDELAQQAEAAERarrnaeaeciELR 1723
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELS-----SLQSELRR--IENRLDELSQELSDASR----------KIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1724 EQNNDLNAhvsaLTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERirKGLELQI 1803
Cdd:TIGR02169 720 EIEKEIEQ----LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1804 KEMQIRLDDAEnaalkggkKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDK 1883
Cdd:TIGR02169 794 PEIQAELSKLE--------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 127737 1884 LQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAEERADIAENALSKMR 1934
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1342-1939 |
2.71e-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: 78.95 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1342 LAATAKNLEHENTILREhldeeaeskadLTRQISKLnaEIQQWKArfdseglNKLEEIEAAKKALQLKVqeLTDTNEGLF 1421
Cdd:TIGR02168 181 LERTRENLDRLEDILNE-----------LERQLKSL--ERQAEKA-------ERYKELKAELRELELAL--LVLRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1422 AKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTAN 1501
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1502 DELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQI 1581
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1582 RSEI---EKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEAL-RIKKKLESDINDLEIALDHANRAYADAQKTIK 1657
Cdd:TIGR02168 399 NNEIerlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1658 KYMETVQELQFQIEEEQRQKDE-------IREQFLASEKRNAILQS--------EKDE------LAQQAEAAERARRNAE 1716
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENlegfsegVKALLKNQSGLSGILGVlselisvdEGYEaaieaaLGGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1717 AECIELREQNNDLNAHVSALT-----------GQRRKLEGELLAAHAELEEIANELKNAVEQ--GQKASADAARLAEELR 1783
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDsikgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1784 QEQEHSMHI-----ERIRKG---------LELQIKEMQIRLDDAENAalkggkkiIAQLEARIRAIEQELDGEQRRHQDT 1849
Cdd:TIGR02168 639 KKLRPGYRIvtldgDLVRPGgvitggsakTNSSILERRREIEELEEK--------IEELEEKIAELEKALAELRKELEEL 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1850 EKNWRKA-------ERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAEER 1922
Cdd:TIGR02168 711 EEELEQLrkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
650
....*....|....*..
gi 127737 1923 ADIAENALSKMRNKIRA 1939
Cdd:TIGR02168 791 IEQLKEELKALREALDE 807
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
987-1807 |
1.87e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 987 NIRSLQD--EMANQDEAVaklnKEKKHQEESNRKLNEDLQSEEDKVNHLEKIR-NKLEQQMDELEENIDREKrsrgdIEK 1063
Cdd:PTZ00121 1025 NIEKIEEltEYGNNDDVL----KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKpSYKDFDFDAKEDNRADEA-----TEE 1095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1064 AKRKVEGDLKVAQENIDEITKQKHdvetTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQ 1143
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEE----AKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARK 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1144 KSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAE--IAKLRREKEEDSLNHETAISSLRKRHGDSV-AELTEQL 1220
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErkAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERNN 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1221 ETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKAlktIEVQYSELQTKADEQSRQLQDfaalknrlNNENSDL 1300
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA---DEAKKAEEKKKADEAKKKAEE--------AKKADEA 1320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1301 NRSLEEMDNQLNSLHRlKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAE 1380
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1381 IQQWKARfdSEGLNKLEEIEAAKKALQLKVQELTDTNEglfAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAfyEKHRR 1460
Cdd:PTZ00121 1400 AEEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADE---AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1461 QFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLfKAKTANDELAEYLDSTRRENKSLAQEVKDltdqlGEGGRSVAELQ 1540
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA-EAKKKADEAKKAEEAKKADEAKKAEEAKK-----ADEAKKAEEKK 1546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1541 KI--VRKLEVEKEELQKALDEAEAALEAEEAKVLRaqievsqiRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAET 1618
Cdd:PTZ00121 1547 KAdeLKKAEELKKAEEKKKAEEAKKAEEDKNMALR--------KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1619 KQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQflASEKRNAILQSEK 1698
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKK 1696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1699 DELAQQAEAaerarrnaeaecielreqnndlnahvsaltgQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARL 1778
Cdd:PTZ00121 1697 EAEEAKKAE-------------------------------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
810 820
....*....|....*....|....*....
gi 127737 1779 AEELRQEQEHSMHIERIRKGLELQIKEMQ 1807
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1135-1922 |
2.16e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1135 LEAERNS----RQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEdslnHETAISSLRKRhg 1210
Cdd:TIGR02169 172 KEKALEEleevEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA----LERQKEAIERQ-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1211 dsVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQ-DLEKALKTIEVQYSELQTKADEQSRQLQDFAAL 1289
Cdd:TIGR02169 246 --LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1290 KNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKAD 1369
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1370 LTRQISKLNAEIQQWKARF-----DSEGL-NKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQS 1443
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELadlnaAIAGIeAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1444 DVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQL-STDLFKAKTANDELAEYLDSTRRENKSLAQEV 1522
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1523 KDLTDQLGEGGRSVAELQKIvRKLEVEKEELQKALDEA--------EAALEAEEAKVLRAQIEVSQI----RSEIEKRIQ 1590
Cdd:TIGR02169 564 IELLKRRKAGRATFLPLNKM-RDERRDLSILSEDGVIGfavdlvefDPKYEPAFKYVFGDTLVVEDIeaarRLMGKYRMV 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1591 EKEEE-FE---------NTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYM 1660
Cdd:TIGR02169 643 TLEGElFEksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1661 ETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRnaeaeciELREQNNDLNAHVS-----A 1735
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLShsripE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1736 LTGQRRKLEGEllaaHAELEEIANELKNAVEqgqkasadaaRLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAeN 1815
Cdd:TIGR02169 796 IQAELSKLEEE----VSRIEARLREIEQKLN----------RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL-N 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1816 AALKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQV 1895
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
810 820
....*....|....*....|....*..
gi 127737 1896 EEAEEVAASNLNkYKVLTAQFEQAEER 1922
Cdd:TIGR02169 941 GEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1587-1944 |
2.51e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1587 KRIQEKEEEFENTRRNHQRA------LESMQATLEAETKQKEEALRIKKKLEsdINDLEIALdhanRAYADAQKTIKKYM 1660
Cdd:COG1196 172 ERKEEAERKLEATEENLERLedilgeLERQLEPLERQAEKAERYRELKEELK--ELEAELLL----LKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1661 ETVQELQFQIEEEQRQKDEIREQflasekrnaiLQSEKDELAqqaeaaerarrnaeaeciELREQNNDLNAHVSALTGQR 1740
Cdd:COG1196 246 AELEELEAELEELEAELAELEAE----------LEELRLELE------------------ELELELEEAQAEEYELLAEL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1741 RKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKG 1820
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1821 GKKIIAQLEARIRAIEQELDgEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEE 1900
Cdd:COG1196 378 EEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 127737 1901 VAASNLNKYKVLTAQFEQAEERADIAENALSKMRNKIRASASMA 1944
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
859-1413 |
3.31e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 859 QEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKnalfLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQ 938
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 939 LEDMQERNEDLARQKK------KTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQ 1012
Cdd:PRK03918 268 IEELKKEIEELEEKVKelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1013 EESNRKLNEdlqsEEDKVNHLEKIRNKLEqQMDELE-----ENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKH 1087
Cdd:PRK03918 348 KELEKRLEE----LEERHELYEEAKAKKE-ELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1088 DVETTLKR------------KEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKsDRSRSEAERE 1155
Cdd:PRK03918 423 ELKKAIEElkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKEL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1156 LEELTERLEQQGGATAAQLEANkkreaeiAKLRREKEEDSLNHETAISSLRKRHgDSVAELTEQLETLQKLKAKSEAEKS 1235
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEELEKK-------AEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1236 KLQRDLEESQHATDSEVRSR-QDLEKALKtievQYSELQTKADEQSRqlqdfaaLKNRLNNENSDLNRSLEEMDNQLNSL 1314
Cdd:PRK03918 574 ELLKELEELGFESVEELEERlKELEPFYN----EYLELKDAEKELER-------EEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1315 HRLKstlqSQLDETRRNYDEESRERQALAATAKNLEHENtiLREHLDEEAESKADLTRQISKLNAEIQQWKarfdseglN 1394
Cdd:PRK03918 643 EELR----KELEELEKKYSEEEYEELREEYLELSRELAG--LRAELEELEKRREEIKKTLEKLKEELEERE--------K 708
|
570
....*....|....*....
gi 127737 1395 KLEEIEAAKKALQlKVQEL 1413
Cdd:PRK03918 709 AKKELEKLEKALE-RVEEL 726
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
874-1555 |
6.07e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 874 EAVQRGEIARSQLESQVADLVeeKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNED---LA 950
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAV--KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 951 RQKKKTDQelsdtkkhvqdlelsLRKAEQEKQSRDhnIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKv 1030
Cdd:PTZ00121 1287 EEKKKADE---------------AKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA- 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1031 nhlekiRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQE--NIDEITKQKHDVettlKRKEEDLHHTNAKLA 1108
Cdd:PTZ00121 1349 ------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEED----KKKADELKKAAAAKK 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1109 ENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLR 1188
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1189 ----REKEEDSLNHETAISSLRKRHGDSV--AELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKA- 1261
Cdd:PTZ00121 1499 adeaKKAAEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNm 1578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1262 -------LKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDE 1334
Cdd:PTZ00121 1579 alrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1335 ----------ESRERQALAATAKNLEHENTILREHLDEEAESKADlTRQISKLNAEIQQwkarfDSEGLNKLEEiEAAKK 1404
Cdd:PTZ00121 1659 nkikaaeeakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKK-----KAEELKKAEE-ENKIK 1731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1405 ALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQ 1484
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127737 1485 RDNRQLSTDLFKAK----TANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQK 1555
Cdd:PTZ00121 1812 EGGKEGNLVINDSKemedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1169-1908 |
6.13e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1169 ATAAQLEANKKREaEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHAT 1248
Cdd:PTZ00121 1089 ADEATEEAFGKAE-EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1249 DS-EVRSRQDLEKALKTIEVQYSELQTKADEQSRqlqdfAALKNRLNNENSDLNRSLEEMDNQLNSLHRLkstlqsqldE 1327
Cdd:PTZ00121 1168 EArKAEDAKKAEAARKAEEVRKAEELRKAEDARK-----AEAARKAEEERKAEEARKAEDAKKAEAVKKA---------E 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1328 TRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKArfdsEGLNKLEEIEAAKKALQ 1407
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA----DEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1408 lKVQELTDTNEglfAKIASQEKvrfKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSEldaaqrdN 1487
Cdd:PTZ00121 1310 -KAEEAKKADE---AKKKAEEA---KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE-------E 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1488 RQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTD--QLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALE 1565
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAakKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1566 AEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRiKKKLESDINDLEIALDHA 1645
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK-KAEEAKKADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1646 NRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREqflASEKRNAILQ----SEKDELAQQAEAAERARRNAEAECIE 1721
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---AEEDKNMALRkaeeAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1722 LR-EQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLE 1800
Cdd:PTZ00121 1612 AKkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1801 LQIKEMQIRLDDAENAALKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVE-FQVVEEKKNEERLTE 1879
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkKKIAHLKKEEEKKAE 1771
|
730 740
....*....|....*....|....*....
gi 127737 1880 LVDKLqcKLKIFKRQVEEAEEVAASNLNK 1908
Cdd:PTZ00121 1772 EIRKE--KEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
860-1701 |
1.13e-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: 73.85 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 860 EAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQL 939
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 940 EDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSR-------DHNIRSLQDEMANQDEAVAKLNKEKKHQ 1012
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeeelkllAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1013 EESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKhDVETT 1092
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK-EEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1093 LKRKEEDLHHTNAKLAENNSIIAKLQRLIKELtarnaeleeeLEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAA 1172
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELE----------ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1173 QLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEV 1252
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1253 RSRQDLEKA---LKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNensdlnrSLEEMDNQLNSLHRLKSTLQSQLDETR 1329
Cdd:pfam02463 549 VIVEVSATAdevEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-------AVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1330 RNYDEESRERQALA-----ATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKK 1404
Cdd:pfam02463 622 AKVVEGILKDTELTklkesAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1405 ALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQ 1484
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1485 RDNRQ-LSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLE-VEKEELQKALDEAEA 1562
Cdd:pfam02463 782 KTEKLkVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEqKLEKLAEEELERLEE 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1563 ALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIAL 1642
Cdd:pfam02463 862 EITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL 941
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1643 DHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDEL 1701
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1126 |
2.45e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 858 EQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITG 937
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 938 QLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNR 1017
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1018 KLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENI-DREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKH-------DV 1089
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAA 991
|
250 260 270
....*....|....*....|....*....|....*..
gi 127737 1090 ETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTA 1126
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1144 |
3.18e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.56 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 897 KNALFLSLETEKANLADAEERNEKLNQLKAtLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRK 976
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAAEAEAELEQ-LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 977 AEQEKQSRDHNIRSLQDEMANQDEAVAK-LNKEKKHQEESNRKL---NEDLQSEEDKVNHLEKIRNKLEQQMDELEENID 1052
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1053 REKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELE 1132
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|..
gi 127737 1133 EELEAERNSRQK 1144
Cdd:COG4942 241 ERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
910-1447 |
8.98e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 910 NLADAEERNEKLNQLKATLESKLSditgQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQsrdhNIR 989
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE----KLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 990 SLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSR----------- 1058
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklsefyeeyld 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1059 --GDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEE------DLHHTNAKLAENNSIIAKLQRLIKELTARNAE 1130
Cdd:PRK03918 308 elREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1131 LEEELEAERNSRQKsdrSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDslnHEtaisslrkrhG 1210
Cdd:PRK03918 388 KLEKELEELEKAKE---EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE---HR----------K 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1211 DSVAELTEQLETLQKLKAKSEAEKSKLQRDLE--ESQHATDSEVRSRQDLEKALKTIE-----VQYSELQTKADEQSRQL 1283
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRelEKVLKKESELIKLKELAEQLKELEeklkkYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1284 QDFAALKNRLNNENSDLNR------SLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRER-QALAA------TAKNLE 1350
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKleelkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPfyneylELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1351 HENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFdsEGLNKLEEIEAAKKALQLKVqELTDTNEGLFAKIASQEKV 1430
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL--EELEKKYSEEEYEELREEYL-ELSRELAGLRAELEELEKR 688
|
570
....*....|....*..
gi 127737 1431 RFKLMQDLDDAQSDVEK 1447
Cdd:PRK03918 689 REEIKKTLEKLKEELEE 705
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1255 |
1.03e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 859 QEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQ 938
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 939 LEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRK 1018
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1019 LNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDRekrsrgdIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEE 1098
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEA-------LLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1099 DLHHTNAKLAENNSIIAKLQRLIKEltarnaeleeeleaernsrqksdrsrseaereleeLTERLEQQGGATAAQLEANK 1178
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDN-----------------------------------LQERLSEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1179 -KREAEIAKLRREKEEdslnHETAISSLRKRHGDSVAELTEQLETLQKLKAKSE-AEKSKlqRDLEESQHATDSEVRSR 1255
Cdd:TIGR02168 961 nKIEDDEEEARRRLKR----LENKIKELGPVNLAAIEEYEELKERYDFLTAQKEdLTEAK--ETLEEAIEEIDREARER 1033
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1456-1937 |
2.61e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1456 EKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLstdlfkaktanDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRS 1535
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKEL-----------EELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1536 VAELQKIVRKLEVEKEELQKaldeaeaaleaeEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNhqraLESMQATLE 1615
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE----INGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1616 AETKQKEEALRIKKKLESDINDLEIaLDHANRAYADAqKTIKKYMETVQElqfqiEEEQRQKDEIREQFLASEKRNAILQ 1695
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEA-KAKKEELERLKK-----RLTGLTPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1696 SEKDELAQQAEaaerarrnaeaeciELREQNNDLNAHVSALTGQRRKL-----------EGELLAA-HAELEEIANELKN 1763
Cdd:PRK03918 405 EEISKITARIG--------------ELKKEIKELKKAIEELKKAKGKCpvcgrelteehRKELLEEyTAELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1764 AVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAA--LKGGKKIIAQLEARIRAIEQELdg 1841
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAeeYEKLKEKLIKLKGEIKSLKKEL-- 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1842 eqRRHQDTEKNWRKAERRVKEVEFQVVE-EKKNEERLTELVDKLQCKLK----IFKRQVE--EAEEVAASNLNKYKVLTA 1914
Cdd:PRK03918 549 --EKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKelepFYNEYLElkDAEKELEREEKELKKLEE 626
|
490 500
....*....|....*....|...
gi 127737 1915 QFEQAEERADIAENALSKMRNKI 1937
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKEL 649
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
974-1834 |
5.95e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.07 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 974 LRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDL-QSEEDKVNHLEKIRNKLEQQMDELEENID 1052
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1053 REKRSRGDIEKAKRKVegdlkvaQENIDEITKQKHDVETTLKRKEEDLhhtNAKLAENNSIIAKLQRLIKELTARNAELE 1132
Cdd:pfam02463 255 SSKQEIEKEEEKLAQV-------LKENKEEEKEKKLQEEELKLLAKEE---EELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1133 EELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDS-----LNHETAISSLRK 1207
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSsaaklKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1208 RHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKtIEVQYSELQTKADEQSRQLQdfa 1287
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL-LKDELELKKSEDLLKETQLV--- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1288 aLKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAesK 1367
Cdd:pfam02463 481 -KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT--A 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1368 ADLTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEK 1447
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1448 AAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTD 1527
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1528 QLGEggRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRAL 1607
Cdd:pfam02463 718 EAEE--LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1608 E-SMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKymetvqELQFQIEEEQRQKDEIREQFLA 1686
Cdd:pfam02463 796 LkAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK------LEKLAEEELERLEEEITKEELL 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1687 SEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANElKNAVE 1766
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-EADEK 948
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1767 QGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKGGKKIIAQLEARIRA 1834
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1039-1421 |
7.18e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1039 KLEQQMDELEENIDrekrsrgDIEKAkrkvegdLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQ 1118
Cdd:TIGR02168 681 ELEEKIEELEEKIA-------ELEKA-------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1119 RLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRRE---KEEDS 1195
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1196 LNHETAISSLRKRhgdsVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTK 1275
Cdd:TIGR02168 827 ESLERRIAATERR----LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1276 ADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNslhrlksTLQSQLDEtrrnydEESRERQALAATAKNLEHENTI 1355
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRID-------NLQERLSE------EYSLTLEEAEALENKIEDDEEE 969
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 1356 LREHLDEeaeskadLTRQISKLN-------AEIQQWKARFDsEGLNKLEEIEAAKKALQLKVQELTDTNEGLF 1421
Cdd:TIGR02168 970 ARRRLKR-------LENKIKELGpvnlaaiEEYEELKERYD-FLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
962-1883 |
1.24e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.99 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 962 DTKKHVQDLELSLRKAEQEKQSRDHnIRslqdemanqDEAVAKLNKEKKHQEESNRKLNEdLQSEEDKVNHLEKIRNKLE 1041
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACE-IR---------DQITSKEAQLESSREIVKSYENE-LDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1042 QQMDELEENIDREKRSRGDIEKAKRKVEgdlKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNsiiaKLQRLI 1121
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKME---KVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLN----KERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1122 KELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANkkreaeIAKLRREKEEDSlnheta 1201
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN------FHTLVIERQEDE------ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1202 isslRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSR 1281
Cdd:TIGR00606 407 ----AKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1282 QLQDFAALKNR------------LNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQalaataKNL 1349
Cdd:TIGR00606 483 AERELSKAEKNsltetlkkevksLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRK------IKS 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1350 EHENTILreHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLN--KLEEIE-AAKKALQLKVQELTDTNEGLFAKIAS 1426
Cdd:TIGR00606 557 RHSDELT--SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKElaSLEQNKnHINNELESKEEQLSSYEDKLFDVCGS 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1427 QEkvrfkLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESII---------------------AEWKKKTDDLSSELDAAQR 1485
Cdd:TIGR00606 635 QD-----EESDLERLKEEIEKSSKQRAMLAGATAVYSQFItqltdenqsccpvcqrvfqteAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1486 DNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALE 1565
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1566 AEEAkVLRAQIEVSQIRSEIEKRIQEKE--------EEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDIND 1637
Cdd:TIGR00606 790 DVTI-MERFQMELKDVERKIAQQAAKLQgsdldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1638 LEIALDHANRAYADAQKtikkYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEA 1717
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQ----FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1718 eciELREQNNDLNAHVSALTG--------QRRKLEGELLAAHAELEEIANELKNAVE--QGQKASADAARLAEELRQEQE 1787
Cdd:TIGR00606 945 ---DIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNL 1021
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1788 HSMHIERIRKGLELQIKEMQIRLDDAENAALKGGKKiiaQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQV 1867
Cdd:TIGR00606 1022 TLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQ---KLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRD 1098
|
970 980
....*....|....*....|
gi 127737 1868 VEEKKNEE----RLTELVDK 1883
Cdd:TIGR00606 1099 AEEKYREMmivmRTTELVNK 1118
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1213-1901 |
1.66e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1213 VAELTEQLETLQKLKAKSEAEKSKlqrdleESQHATDSEVRSRQDLEKALKTievQYSELQTKADEQSRQLQDFAALKNR 1292
Cdd:PTZ00121 1029 IEELTEYGNNDDVLKEKDIIDEDI------DGNHEGKAEAKAHVGQDEGLKP---SYKDFDFDAKEDNRADEATEEAFGK 1099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1293 LNNENSDLNRSLEEMDNQLNSLHRLKSTlqSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAEsKADLTR 1372
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDA--RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR-KAEDAK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1373 QISKLNAEIQQWKArfdsEGLNKLEE---IEAAKKALQLK----VQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDV 1445
Cdd:PTZ00121 1177 KAEAARKAEEVRKA----EELRKAEDarkAEAARKAEEERkaeeARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1446 EKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSS-----ELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQ 1520
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1521 EVKDLTDQlGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTR 1600
Cdd:PTZ00121 1333 AAKKKAEE-AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1601 RNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTikkymetvqelqfqieEEQRQKDEI 1680
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA----------------EEAKKADEA 1475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1681 REQflASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGellAAHAELEEIANE 1760
Cdd:PTZ00121 1476 KKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE---AKKAEEKKKADE 1550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1761 LKNA-----------VEQGQKASAD---AARLAEELRQEQEHsmHIERIRKGLELQIKEMQIRLDDAENAALKGgkkiia 1826
Cdd:PTZ00121 1551 LKKAeelkkaeekkkAEEAKKAEEDknmALRKAEEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------ 1622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1827 qleARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVV----------EEKKNEERLTELVDKLQCKLKIFKRQVE 1896
Cdd:PTZ00121 1623 ---EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaeeakkaeEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
....*
gi 127737 1897 EAEEV 1901
Cdd:PTZ00121 1700 EAKKA 1704
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
887-1681 |
1.68e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 887 ESQVADLVEEKNALFLSLETEKANLADAEERNEK----LNQLKATLESKLSDITGQLEDMQE--RNEDLARQKKKTDQEL 960
Cdd:TIGR00606 300 DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKerrlLNQEKTELLVEQGRLQLQADRHQEhiRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 961 ------SDTKKHVQD-LELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHL 1033
Cdd:TIGR00606 380 dgfergPFSERQIKNfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1034 EKIRNKLEQQMDELEEnidrekrsrgdIEKAKRKVEGDLKVAQENIDEITKQKHdvETTLKRKEEDLHHTNAKLAENNsi 1113
Cdd:TIGR00606 460 IKELQQLEGSSDRILE-----------LDQELRKAERELSKAEKNSLTETLKKE--VKSLQNEKADLDRKLRKLDQEM-- 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1114 iAKLQRLIKELTarnaeleeelEAERNSRQKSDRSRSEAERELEELTERLEQQGG-ATAAQLEANKKREAEIAKLRREKE 1192
Cdd:TIGR00606 525 -EQLNHHTTTRT----------QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfPNKKQLEDWLHSKSKEINQTRDRL 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1193 EDsLNHETAISSLRKRH-GDSVAELTEQLETLQKL---KAKSEAEKSKLQRDLEESQHATdsevRSRQDLEKALKTIEVQ 1268
Cdd:TIGR00606 594 AK-LNKELASLEQNKNHiNNELESKEEQLSSYEDKlfdVCGSQDEESDLERLKEEIEKSS----KQRAMLAGATAVYSQF 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1269 YSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKN 1348
Cdd:TIGR00606 669 ITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1349 LEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLnkLEEIEAAKKALQLKVQELTDTNEGLFAKIASQE 1428
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI--MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1429 kvrfkLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSEldaaqrdNRQLSTDLFKAKtandELAEYL 1508
Cdd:TIGR00606 827 -----VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-------KLQIGTNLQRRQ----QFEEQL 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1509 DSTRRENKSLAQEVKDLTDQlgeggrsVAELQKIVRKLEVEKEELQKALDEAEAaleaeeakvlRAQIEVSQIRSEIEKR 1588
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1589 IQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALD--HANRAYADAQKTIKKYMETVQEL 1666
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqKIQERWLQDNLTLRKRENELKEV 1033
|
810
....*....|....*
gi 127737 1667 QFQIEEEQRQKDEIR 1681
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQ 1048
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
865-1125 |
2.34e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 865 LAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQE 944
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 945 RNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQ 1024
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1025 SEEDkvnhlEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTN 1104
Cdd:TIGR04523 549 KDDF-----ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260
....*....|....*....|.
gi 127737 1105 AKLAENNSIIAKLQRLIKELT 1125
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLK 644
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
908-1339 |
5.88e-10 |
|
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: 64.69 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 908 KANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHN 987
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 988 IRSLQDEMANQDEAVAKLNKEKKHQEEsnrklneDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDiekakrk 1067
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN------- 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1068 vegdlkvAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNaeleeeleaernsrqksdr 1147
Cdd:TIGR02168 822 -------LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL------------------- 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1148 srseaerelEELTERLEQQGGATAAQLEANKKREAEIAKLRREkeedslnhetaisslrkrhgdsVAELTEQLETLQKLK 1227
Cdd:TIGR02168 876 ---------EALLNERASLEEALALLRSELEELSEELRELESK----------------------RSELRRELEELREKL 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1228 AKSEAEKSKLQRDLEESQhatdSEVRSRQDLEkaLKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNEN-------SDL 1300
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQ----ERLSEEYSLT--LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyEEL 998
|
410 420 430
....*....|....*....|....*....|....*....
gi 127737 1301 NRSLEEMDNQLNSLHRLKSTLQSQLDETrrnyDEESRER 1339
Cdd:TIGR02168 999 KERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1045-1686 |
8.31e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1045 DELEENIDREKRSRGDIEKAKR---KVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLhhtNAKLAENNSIIAKLQRLI 1121
Cdd:PRK03918 144 DESREKVVRQILGLDDYENAYKnlgEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL---EEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1122 KELTARNAELEEELEAERN--SRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSlnhe 1199
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI---- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1200 tAISSLRKrhgdsvaELTEQLETLQKLKAKSEAEKSKLQRDLEESQhatdSEVRSRQDLEKALKTIEVQYSELQTKAdeq 1279
Cdd:PRK03918 297 -KLSEFYE-------EYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERH--- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1280 sRQLQDFAALKNRLNNENSDL-NRSLEEMDNQLNSLHRLKSTLQSQLDET---RRNYDEESRERQALAATAKNLEHENTI 1355
Cdd:PRK03918 362 -ELYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1356 LREHLDEE--AESKADLTRQISKLNAEIQQWKARfDSEGLNKLEEIEAAkkalqLKVQELTDTNEGLFAKIASQEKVRFK 1433
Cdd:PRK03918 441 CGRELTEEhrKELLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKV-----LKKESELIKLKELAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1434 LmqdlddaqsDVEKAAAQVAFYEKHRRQFESIiaewKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRR 1513
Cdd:PRK03918 515 Y---------NLEELEKKAEEYEKLKEKLIKL----KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1514 ENKSLAQEVKDLTDQLGEGGRSVAELQKIVRklevEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQE-K 1592
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEK----ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyS 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1593 EEEFENTRRNH---QRALESMQATLEAETKQKEEALRIKKKLESDINDLEialdhanrAYADAQKTIKKYMETVQELqfq 1669
Cdd:PRK03918 658 EEEYEELREEYlelSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE--------KAKKELEKLEKALERVEEL--- 726
|
650
....*....|....*..
gi 127737 1670 IEEEQRQKDEIREQFLA 1686
Cdd:PRK03918 727 REKVKKYKALLKERALS 743
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
857-1475 |
8.37e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNAL---FLSLETEKANLADAEERNEKLNQLKATLESKLS 933
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 934 DITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKkhQE 1013
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK--EQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1014 ESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTL 1093
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1094 KRKEEDLHHTNAKLAENNSIIAKLQRLIKELtarnaeleeeleaernsrqksdrsrseaereleelterleqqggataaQ 1173
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKL------------------------------------------------Q 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1174 LEANKKrEAEIAKLRREKE------EDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHA 1247
Cdd:TIGR04523 419 QEKELL-EKEIERLKETIIknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1248 TDSEVRSRQDLEKALKTIEVQYSELQTKADEQSrqlqdfaALKNRLNNENSDLNRSLEEMDNQLNS--LHRLKSTLQSQL 1325
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE-------SEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEI 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1326 DETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQIS---------------------KLNAEIQQW 1384
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEkakkeneklssiiknikskknKLKQEVKQI 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1385 KARFDsEGLNKLEEIEAAKKALQLKVQELTDT-----NEGLFA-KIASQEKVRFKLMQDLDDAQSDVEKAAAQVafyEKH 1458
Cdd:TIGR04523 651 KETIK-EIRNKWPEIIKKIKESKTKIDDIIELmkdwlKELSLHyKKYITRMIRIKDLPKLEEKYKEIEKELKKL---DEF 726
|
650
....*....|....*..
gi 127737 1459 RRQFESIIAEWKKKTDD 1475
Cdd:TIGR04523 727 SKELENIIKNFNKKFDD 743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
904-1701 |
1.59e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 904 LETEKANLADAEERNEKLnqlkatlESKLSDITGQLEDMQERnedlaRQKKKTDQELSDTKKHVQDLELSLRKAEQEKQs 983
Cdd:TIGR02169 172 KEKALEELEEVEENIERL-------DLIIDEKRQQLERLRRE-----REKAERYQALLKEKREYEGYELLKEKEALERQ- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 984 rdhnIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHL-EKIRNKLEQQMDELEENIDREKRSRGDIE 1062
Cdd:TIGR02169 239 ----KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1063 KAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAEleeeleaernSR 1142
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE----------TR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1143 QKSDrsrsEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLrREKEEDSLNHETAISSLRKRHGDSVAELTEQLET 1222
Cdd:TIGR02169 385 DELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADL-NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1223 LQKLKAKSEAEKSKLQRDLeesqhatdsevrsrQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNEN----- 1297
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEY--------------DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhg 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1298 --SDLNRSLEEMDNQLNSL--HRLKSTLQSQlDETRRNYDEESRERQALAATAKNLeheNTILREHLDEEAESKA----- 1368
Cdd:TIGR02169 526 tvAQLGSVGERYATAIEVAagNRLNNVVVED-DAVAKEAIELLKRRKAGRATFLPL---NKMRDERRDLSILSEDgvigf 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1369 --DLTRQISKLNAEIQQwkaRFDSEGLnkLEEIEAAkKALQLKVQELTDTNE---------GLFAKIASQEKVRFKLMQD 1437
Cdd:TIGR02169 602 avDLVEFDPKYEPAFKY---VFGDTLV--VEDIEAA-RRLMGKYRMVTLEGElfeksgamtGGSRAPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1438 LDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKS 1517
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1518 LAQEVKDLTDQLGEGGRSVAELQKIVRKLEVE--KEELQKALDEAEAALEAEEAKVLRAQ-IEVSQIRSEIEKRIQEKE- 1593
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLReIEQKLNRLTLEKEYLEKEi 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1594 EEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEE 1673
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
810 820
....*....|....*....|....*...
gi 127737 1674 QRQKDEIREQFLASEKRNAILQSEKDEL 1701
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1433-1939 |
1.63e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1433 KLMQDLDDAQSDVEKAAAQV-------AFYEKHRRQFESI------------------IAEWKKKTDDLSSELDAAQRDN 1487
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIellepirELAERYAAARERLaeleylraalrlwfaqrrLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1488 RQLSTDLFKAKTANDEL-AEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEK-------EELQKALDE 1559
Cdd:COG4913 312 ERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1560 AEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRR---NHQRALESMQATLEAETKQKEEALRIKKKLesdin 1636
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPARLLALRDALAEALGLDEAELPFVGEL----- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1637 dLEIALDH------ANRA--------------YADAqktiKKYMETVQ---ELQFQIEEEQRQKDEIR---EQFLASE-- 1688
Cdd:COG4913 467 -IEVRPEEerwrgaIERVlggfaltllvppehYAAA----LRWVNRLHlrgRLVYERVRTGLPDPERPrldPDSLAGKld 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1689 -KRNAILQSEKDELaqqaeaaeraRRNAEAECIELREQnndLNAHVSALT--GQ-------------------------- 1739
Cdd:COG4913 542 fKPHPFRAWLEAEL----------GRRFDYVCVDSPEE---LRRHPRAITraGQvkgngtrhekddrrrirsryvlgfdn 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1740 RRKLEgELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRkGLELQIKEMQIRLD--DAENAA 1817
Cdd:COG4913 609 RAKLA-ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELErlDASSDD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1818 LKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVE-EKKNEERLTELVDKLQCKLKIFKRQVE 1896
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVERE 766
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 127737 1897 EAEEvaasnlnkykvLTAQFEQAEERADIAENALSKMRNKIRA 1939
Cdd:COG4913 767 LREN-----------LEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1179-1800 |
2.11e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1179 KREAEIAKLRREKEEDSLNHETAISSLRKRhgdsVAELTEQLETLQKLKAKSEAEKSKLqrdlEESQHATDSEVRSRQDL 1258
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKEEI----EELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1259 EKALKTIEVQYSELQTKADEQSRQLQDFAALKnRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRE 1338
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1339 RQALAATAKNLEHentILREHldEEAESKADLTRQISKLNAEIQQWKARFDSEGL----NKLEEIEAAKKALQLKVQELT 1414
Cdd:PRK03918 337 EERLEELKKKLKE---LEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPekleKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1415 DTNEGLFAKIASQEKVrfklMQDLDDAQSDVEKAAAQVAfyEKHRrqfESIIAEWKKKTDDLSSELDAAQRDNRQLSTDL 1494
Cdd:PRK03918 412 ARIGELKKEIKELKKA----IEELKKAKGKCPVCGRELT--EEHR---KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1495 FKAKTANDElaeylDSTRRENKSLAQEVKDLTDQLGEGGrsVAELQKIVRKLEVEKEELQKaldeaeaaleaeeakvLRA 1574
Cdd:PRK03918 483 RELEKVLKK-----ESELIKLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIK----------------LKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1575 QIEVsqirseIEKRIqEKEEEFENTRRNHQRALEsmqatlEAETKQKEEALRIKKKLESDINDLEIALDHANRAYadaqk 1654
Cdd:PRK03918 540 EIKS------LKKEL-EKLEELKKKLAELEKKLD------ELEEELAELLKELEELGFESVEELEERLKELEPFY----- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1655 tiKKYME---TVQELQFQIEEEQRQKDEIREQFLASEKRNAILQsekdelaqqaeaaerarrnaeaeciELREQNNDLNA 1731
Cdd:PRK03918 602 --NEYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------------------------ELRKELEELEK 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1732 HVSALTgqRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLE 1800
Cdd:PRK03918 655 KYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1519-1924 |
3.25e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1519 AQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKvlraQIEVSQIRSEIEKrIQEKEEEFEN 1598
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REELETLEAEIED-LRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1599 TRRNHQRALESMQATLEAETKQKEEALRikkklESDINDLEIALDHANRAYADAQKTikKYMETVQELQFQIEEEQRQKD 1678
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLA-----EAGLDDADAEAVEARREELEDRDE--ELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1679 EIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEG---ELLAAHAELE 1755
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDfleELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1756 EIANELKNAVEQGQKASADAARLAEELR-----QEQEHSMHIERIRKGLElQIKEMQIRLDDAENAalkggkkiIAQLEA 1830
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRE-RVEELEAELEDLEEE--------VEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1831 RIRAIEqELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKYK 1910
Cdd:PRK02224 497 RLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410
....*....|....
gi 127737 1911 VLTAQFEQAEERAD 1924
Cdd:PRK02224 576 ELNSKLAELKERIE 589
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1438-1888 |
3.48e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1438 LDDAQSDVEKAAAQVAfyEKHRRQFESIIAEWKKKTDDLSSELD--AAQRDNRQLSTDlfkakTANDELAEYlDSTRREN 1515
Cdd:PRK02224 182 LSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIEryEEQREQARETRD-----EADEVLEEH-EERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1516 KSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEeakvlRAQIE-VSQIRSEIEKRIQEKEE 1594
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD-----DADAEaVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1595 EFENTRRNHQRALESMQATLEAETKQKEEAlrikKKLESDINDLEIALDHANRAYADAQktikkymETVQELQFQIEEEQ 1674
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERA----EELREEAAELESELEEAREAVEDRR-------EEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1675 RQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELRE-----------QNNDLNAHVSALTGQRRKL 1743
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVETIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1744 EgELLAAHAELEEIANELKNAVEQGQKASADAARL---------AEELRQEQ-----EHSMHIERIRKGLELQIKEMQIR 1809
Cdd:PRK02224 478 E-ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIerleerredLEELIAERretieEKRERAEELRERAAELEAEAEEK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1810 LDDAENAALKGGKKI--IAQLEARIRAIEQELDG--------------------------------EQRRHQDTEKNWRK 1855
Cdd:PRK02224 557 REAAAEAEEEAEEAReeVAELNSKLAELKERIESlerirtllaaiadaedeierlrekrealaelnDERRERLAEKRERK 636
|
490 500 510
....*....|....*....|....*....|...
gi 127737 1856 AERRVKEVEFQVVEEKKNEERLTELVDKLQCKL 1888
Cdd:PRK02224 637 RELEAEFDEARIEEAREDKERAEEYLEQVEEKL 669
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
890-1337 |
4.54e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 890 VADLVEEKNALF-LSLETEKANLADAEERNEKLNQLKATLEsKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQ 968
Cdd:COG4717 48 LERLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 969 DLEL--SLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQ----SEEDKVNHLEKIRNKLEQ 1042
Cdd:COG4717 127 LLPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1043 QMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENiDEITKQK---------HDVETTLKRKEEDLHHTNAKLAENNSI 1113
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1114 IAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEE 1193
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1194 DSLNHETAiSSLRKRHGDSVAELTEQLETLQKLKAKsEAEKSKLQRDLEE--SQHATDSEVRSRQDLEKALKTIEVQYSE 1271
Cdd:COG4717 366 EELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQEL-KEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127737 1272 LQTKADEQSRQLQDFAALKNRLNNEN--SDLNRSLEEMDNQLNSLHRLKSTLQ---SQLDETRRNYDEESR 1337
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREERL 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
868-1604 |
4.68e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 61.91 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 868 KIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNE 947
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 948 DLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEmanqdeAVAKLNKEKKHQEESNRKLNEDLQSEE 1027
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL------KQGKLTEEKEELEKQELKLLKDELELK 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1028 DKVNHLEKIRNKLEQQMDELEENIDREKRSRgdieKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEdLHHTNAKL 1107
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERS----QKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-VAVENYKV 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1108 AENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKL 1187
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1188 RREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQhatdsevrsrQDLEKALKTIEV 1267
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL----------QEKAESELAKEE 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1268 QYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAK 1347
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1348 NLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFD-SEGLNKLEEIEAAKKALQLKVQELTDTNEGLfAKIAS 1426
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAElLEEEQLLIEQEEKIKEEELEELALELKEEQK-LEKLA 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1427 QEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAE 1506
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1507 YLDSTRRENKS-LAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEI 1585
Cdd:pfam02463 933 YEEEPEELLLEeADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAII 1012
|
730
....*....|....*....
gi 127737 1586 EKRIQEKEEEFENTRRNHQ 1604
Cdd:pfam02463 1013 EETCQRLKEFLELFVSINK 1031
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
871-1531 |
4.97e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 871 KLEEAVQRGEiarsqlesqvaDLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLA 950
Cdd:pfam05483 135 KLEEEIQENK-----------DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 951 RQKKKTDQELSdtkkhvqdlelslRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKV 1030
Cdd:pfam05483 204 VQAENARLEMH-------------FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1031 NHLEKIRNKLEQQMDELEENIDREKRSRGDIE-------KAKRKVEGDLKVAQENIDEITKQKH---------------- 1087
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKELEDIKmslqrsmSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfv 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1088 --DVETTLKRKEEDLHHTNAKLAENNSiiaKLQRLIKELtaRNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQ 1165
Cdd:pfam05483 351 vtEFEATTCSLEELLRTEQQRLEKNED---QLKIITMEL--QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1166 QGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLET--LQKLKAKSEAEKSKLQRDlEE 1243
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKekLKNIELTAHCDKLLLENK-EL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1244 SQHATDS--EVRSRQ-DLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKST 1320
Cdd:pfam05483 505 TQEASDMtlELKKHQeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1321 LQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNKLEEIE 1400
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1401 AAKKALQLKVQELTDtneglfAKIASQEKVrfKLMQDLDDAQSdvEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSEL 1480
Cdd:pfam05483 665 DKKISEEKLLEEVEK------AKAIADEAV--KLQKEIDKRCQ--HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKE 734
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 127737 1481 DAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGE 1531
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
854-1420 |
6.21e-09 |
|
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: 61.34 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 854 KAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLS 933
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 934 DITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQE-------KQSRDHNIRSLQ------DEMANQDE 1000
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdLDHQRQLVSNLEkkqkkfDQMLAEEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1001 AVAKLNKEKKHQEESNRK--------LNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDL 1072
Cdd:pfam01576 615 AISARYAEERDRAEAEAReketralsLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1073 KVAQENIDEITKQKHDVETTLKRKEEDLH--------HTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQK 1144
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAKLRLEVNMQalkaqferDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1145 SDrsrseaerelEELTERLEQQGGATAAQLEANK---KREAEIAKLRREKEEDSLNHETAISSLR------KRHGDSVAE 1215
Cdd:pfam01576 775 LE----------LDLKELEAQIDAANKGREEAVKqlkKLQAQMKDLQRELEEARASRDEILAQSKesekklKNLEAELLQ 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1216 LTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQT----------KADEQSRQL-- 1283
Cdd:pfam01576 845 LQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSntellndrlrKSTLQVEQLtt 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1284 ---------QDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLK-STLQSQLDETRRNYDEESRERQALAATAKNLEHEN 1353
Cdd:pfam01576 925 elaaerstsQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKL 1004
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 1354 TILREHLDEEAESKADLTRQISKLNAEIQQWKARFDsEGLNKLEEIEAAKKALQLKVQELTDTNEGL 1420
Cdd:pfam01576 1005 KEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKLQRELDDATESNESM 1070
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
859-1329 |
6.79e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 859 QEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQ 938
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 939 LEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQekqsrdhnirsLQDEmanqdeavAKLNKEKKHQEESNRK 1018
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----------LLEA--------GKCPECGQPVEGSPHV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1019 lnEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKrsrgdiekakrkvegDLKVAQENIDEITKQKHDVETTLKRKEE 1098
Cdd:PRK02224 468 --ETIEEDRERVEELEAELEDLEEEVEEVEERLERAE---------------DLVEAEDRIERLEERREDLEELIAERRE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1099 DLHHTNAKLAENNSIIAKLQrlikeltarnaeleeeleaeRNSRQKSDRsrseaereleelterleqqggATAAQLEANK 1178
Cdd:PRK02224 531 TIEEKRERAEELRERAAELE--------------------AEAEEKREA---------------------AAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1179 KREaEIAKLRREKEE-----DSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSE---AEKSKLQRDLEESQHATDS 1250
Cdd:PRK02224 570 ARE-EVAELNSKLAElkeriESLERIRTLLAAIADAEDEIERLREKREALAELNDERRerlAEKRERKRELEAEFDEARI 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1251 EvRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENS--DLNRSLEEMDNQLNSLHRLKSTLQSQLDET 1328
Cdd:PRK02224 649 E-EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEElrERREALENRVEALEALYDEAEELESMYGDL 727
|
.
gi 127737 1329 R 1329
Cdd:PRK02224 728 R 728
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
848-1380 |
7.69e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 848 KVKPMLKAGKEQEAMGELAVKIQ----KLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQ 923
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEeakkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 924 LKATLES--KLSDITGQLEDMQERNEDL--ARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQ------- 992
Cdd:PTZ00121 1383 AKKKAEEkkKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkaeea 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 993 ----------DEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENidREKRSRGDIE 1062
Cdd:PTZ00121 1463 kkkaeeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--EEAKKADEAK 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1063 KAKRKVEGD-------LKVAQE--NIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIA-----KLQRLIKELTARN 1128
Cdd:PTZ00121 1541 KAEEKKKADelkkaeeLKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEeekkmKAEEAKKAEEAKI 1620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1129 AELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETA------- 1201
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkeaee 1700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1202 ---ISSLRKRHGDSV--AELTEQLETLQKLKA-----KSEAEKSK---LQRDLEESQHATDSEVRSRQDLEKALKTIEVQ 1268
Cdd:PTZ00121 1701 akkAEELKKKEAEEKkkAEELKKAEEENKIKAeeakkEAEEDKKKaeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1269 YSELQTKADEQSRQLQD---------FAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRER 1339
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEN 1860
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 127737 1340 QALAATAKNLEHENTILREhlDEEAESKADLTRQISKLNAE 1380
Cdd:PTZ00121 1861 GEDGNKEADFNKEKDLKED--DEEEIEEADEIEKIDKDDIE 1899
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1037-1293 |
8.17e-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: 59.78 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1037 RNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQkhdvettlkrkeedLHHTNAKLAENNSIIAK 1116
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR--------------IRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1117 LQRLIKELTARNAELEEELEAERNSRQKSDRsrseAERELEELTERLEQQGGATAAQLEA-NKKREAEIAKLRREKEEDS 1195
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGR----QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1196 LNhETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTK 1275
Cdd:COG4942 164 AL-RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|....*...
gi 127737 1276 ADEQSrqlqdFAALKNRL 1293
Cdd:COG4942 243 TPAAG-----FAALKGKL 255
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1212-1504 |
1.05e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 60.70 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1212 SVAELTEQLETLQKLKAKSEAEKSkLQRDLEESQHATDSEVRSRQDLEKALKTIEvqyselqtKADEQSRQLQ-DFAALK 1290
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEAEDKL-VQQDLEQTLALLDKIDRQKEETEQLKQQLA--------QAPAKLRQAQaELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1291 NRLNNE-NSDL-NRSLEEMDNQLNSLHRLKSTLQSQLDE------TRRNYDEesRERQALAATAKNLEHENTILREHLDE 1362
Cdd:PRK11281 108 DDNDEEtRETLsTLSLRQLESRLAQTLDQLQNAQNDLAEynsqlvSLQTQPE--RAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1363 EAESKADltrQISKLNAEIQQWKA-----RFDSEGLNKLEEIeaakkaLQLKVQELTdtneglfAKIASQEkvrfKLMQD 1437
Cdd:PRK11281 186 GKALRPS---QRVLLQAEQALLNAqndlqRKSLEGNTQLQDL------LQKQRDYLT-------ARIQRLE----HQLQL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1438 LDDAQSdvEKAAAQVafyEKHRRQFESIIAEWKKKTDDL-SSELDAaqrdNRQLSTDLFKAKTANDEL 1504
Cdd:PRK11281 246 LQEAIN--SKRLTLS---EKTVQEAQSQDEAARIQANPLvAQELEI----NLQLSQRLLKATEKLNTL 304
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1471-1692 |
1.45e-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: 59.01 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1471 KKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQK----IVRKL 1546
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKeiaeLRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1547 EVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQI--RSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEA 1624
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1625 LrikKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNA 1692
Cdd:COG4942 180 L---AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
907-1554 |
1.59e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 907 EKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDH 986
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 987 NIRSLQ--------------------DEMANQDEAVAKLNKE-------------KKHQEESNRKLNEDLQSEEDKVNHL 1033
Cdd:TIGR00618 244 YLTQKReaqeeqlkkqqllkqlrariEELRAQEAVLEETQERinrarkaaplaahIKAVTQIEQQAQRIHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1034 EKIR--------------------NKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQenIDEITKQKHDVETTL 1093
Cdd:TIGR00618 324 AKLLmkraahvkqqssieeqrrllQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ--QKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1094 KRKEEDLHHT-NAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGgataa 1172
Cdd:TIGR00618 402 LDILQREQATiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ----- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1173 QLEANKKREAEIAKLrREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEV 1252
Cdd:TIGR00618 477 TKEQIHLQETRKKAV-VLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1253 RSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNEnsdLNRSLEEMDNQLNSLHRLKSTLQSQLDETR-RN 1331
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEAEDMLACEQHALLRKLQPEQDLQDvRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1332 YDEESRERQALAATAKNLEHENTI---LREHL----DEEAESKADLTRQISKLNAEIQQwkARFDSEGLN----KLEEIE 1400
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTqerVREHAlsirVLPKELLASRQLALQKMQSEKEQ--LTYWKEMLAqcqtLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1401 AAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAqvafyEKHRRQFESIIAEwkKKTDDLSSEL 1480
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKART-----EAHFNNNEEVTAA--LQTGAELSHL 783
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1481 DA-AQRDNRQLSTDLFKAKTANDELAEYLDSTRR----ENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQ 1554
Cdd:TIGR00618 784 AAeIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1669-1910 |
1.74e-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: 59.01 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1669 QIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELl 1748
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1749 aaHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDD--AENAALKGGKKIIA 1826
Cdd:COG4942 100 --EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1827 QLEARIRAIEQELDGEQRRHQDTEKnwrKAERRVKEVEFQVVEEKKNEERLTELVDKLQcklkifKRQVEEAEEVAASNL 1906
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE------AEAAAAAERTPAAGF 248
|
....
gi 127737 1907 NKYK 1910
Cdd:COG4942 249 AALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
958-1413 |
1.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 958 QELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQE--ESNRKLNEDLQSEEDKVNHLEK 1035
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1036 IRNKLEQQMDELEENIDREKRSRGDIEKAKRKV----EGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLA--E 1109
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1110 NNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREaEIAKLRR 1189
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE-ELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1190 EKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKsEAEKSKLQRDLEESQHATdsevRSRQDLEKALKTIEVQY 1269
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEQ----EIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1270 SELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDnqlnslhrlKSTLQSQLDEtrrnydeesrerqalaataknl 1349
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEE---------------------- 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127737 1350 ehentiLREHLDEEAESKADLTRQISKLNAEIQQWkarfdsEGLNKLEEIEAAKKALQLKVQEL 1413
Cdd:COG4717 437 ------LEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEELKAELREL 488
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1165-1849 |
1.83e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1165 QQGGATAAQLEANKKR---EAEIAKLRREKEEDSLNHETAISSLRKRH-GDSVAELTEQL----ETLQKLKAKSEA--EK 1234
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSlhgKAELLTLRSQLLTLCTPCMPDTYHERKQVlEKELKHLREALqqtqQSHAYLTQKREAqeEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1235 SKLQRDLEESQhatdSEVRSRQDLEKALktievqysELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSL 1314
Cdd:TIGR00618 256 LKKQQLLKQLR----ARIEELRAQEAVL--------EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1315 --------------------HRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTI--LREHLDEEAESKADLTR 1372
Cdd:TIGR00618 324 akllmkraahvkqqssieeqRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLqqQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1373 QISKLNAEIQQWKARFDSEGLNKL---EEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKL---MQDLDDAQSDVE 1446
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAhakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLkerEQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1447 KAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAA------QRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSL-- 1518
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLke 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1519 -AQEVKDLTDQLGEGGRSVAELQKIVRKLEVE-KEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEF 1596
Cdd:TIGR00618 564 qMQEIQQSFSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1597 ENTrrnhqrALESMQATLEAEtKQKEEALRIK--KKLESDINDLEI-ALDHANRAYADAQKTIKKYMETVQELQFQIEEE 1673
Cdd:TIGR00618 644 KLT------ALHALQLTLTQE-RVREHALSIRvlPKELLASRQLALqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1674 QRQKDEIReqfLASEKRNAILQSEkDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQrrklegellaahaE 1753
Cdd:TIGR00618 717 DREFNEIE---NASSSLGSDLAAR-EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA-------------E 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1754 LEEIANELKNAVEQGQKASADAARLAEELRQEQEHsmhierirkglELQIKEMQIRLDDAENAALKGGKKIIAQLEARIR 1833
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-----------DEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
730
....*....|....*.
gi 127737 1834 AiEQELDGEQRRHQDT 1849
Cdd:TIGR00618 849 H-QLLKYEECSKQLAQ 863
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1340-1920 |
2.42e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1340 QALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAeiQQWKARFDSEGLNKLEEIEAAKKALQL--KVQELTDTN 1417
Cdd:TIGR00618 215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--QLKKQQLLKQLRARIEELRAQEAVLEEtqERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1418 EGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKA 1497
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1498 KTANDelaeyldstRRENKSLAQEVKDLTDQLgeggrsvaelQKIVRKLEVEKEELQKALDEAEAALEAEEAKV-LRAQI 1576
Cdd:TIGR00618 373 QQHTL---------TQHIHTLQQQKTTLTQKL----------QSLCKELDILQREQATIDTRTSAFRDLQGQLAhAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1577 EVSQIRSEIEKRIQEKEEEFENTRRNHQR-----------ALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHA 1645
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQesaqslkereqQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1646 NRAYADA------QKTIKKYMETVQELQFQIEEEQRQKDEIREQFlasekrnAILQSEKDELAQQAEAAERARRNAEAEC 1719
Cdd:TIGR00618 514 NPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR-------ASLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1720 IELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADA------ARLAEELRQE-QEHSMHI 1792
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlkltalHALQLTLTQErVREHALS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1793 ERIRKGLELQIKEMQIRLDDAENAALKGGKKIIAQLEARIRAIEQELdgeqrrhqdtEKNWRKAERRVKEVEFQVVEEKK 1872
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI----------EEYDREFNEIENASSSLGSDLAA 736
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 127737 1873 NEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAE 1920
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1037-1695 |
3.24e-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: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1037 RNKLEQQMDELEENIDREKRSRGDIEKAKRKVEgDLKVAQENIDEITKQKHDVET--------TLKRKEEDLHHTNAKLA 1108
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAEleylraalRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1109 ENNSIIAKLQRLIKELTARNAELEEELEAERNSRqksdrsrseaereleelterlEQQGGATAAQLeankkrEAEIAKLR 1188
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQI---------------------RGNGGDRLEQL------EREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1189 REKEE---DSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLeesqhatDSEVRSRQDLEKALKTI 1265
Cdd:COG4913 352 RELEErerRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELREL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1266 EVQYSELQTKADEQSRQLQDF-AALKNRLNNENSDLNRSLEEMDNQLNS----------LHRLKSTL---QSQLDETRRN 1331
Cdd:COG4913 425 EAEIASLERRKSNIPARLLALrDALAEALGLDEAELPFVGELIEVRPEEerwrgaiervLGGFALTLlvpPEHYAAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1332 YDEESRERQAlaatakNLEHENTILREHLDEEAESKAdLTRQISKLNAEIQQW-----KARFDSEGLNKLEEIEAAKKAL 1406
Cdd:COG4913 505 VNRLHLRGRL------VYERVRTGLPDPERPRLDPDS-LAGKLDFKPHPFRAWleaelGRRFDYVCVDSPEELRRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1407 QlkVQELTDTNEGLFAK-----IASQ--------EKVRFKLmQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKT 1473
Cdd:COG4913 578 T--RAGQVKGNGTRHEKddrrrIRSRyvlgfdnrAKLAALE-AELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1474 DDLSSELD--AAQRDNRQLSTDLFKAKTANDELAEY---LDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEV 1548
Cdd:COG4913 655 EYSWDEIDvaSAEREIAELEAELERLDASSDDLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1549 EKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQE-------KEEEFENTRRNHQRALESMQATLEAETKQK 1621
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAlrarlnrAEEELERAMRAFNREWPAETADLDADLESL 814
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127737 1622 EEALRIKKKLESDinDLEialdhanRAYADAQKTIKKYMET-VQELQFQIEEEQRqkdEIREQFlasEKRNAILQ 1695
Cdd:COG4913 815 PEYLALLDRLEED--GLP-------EYEERFKELLNENSIEfVADLLSKLRRAIR---EIKERI---DPLNDSLK 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1598-1821 |
3.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1598 NTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQK 1677
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1678 DEIREQfLASEKRNAILQSEKDELAQQAEAAERARRNAEAECI-----ELREQNNDLNAHVSALTGQRRKLEGELLAAHA 1752
Cdd:COG4942 100 EAQKEE-LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylapARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1753 ELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKGG 1821
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
937-1518 |
3.85e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 937 GQLEDMQERNED--LARQKKKTDQE--LSDTKKHVQDLElslrkaEQEKQSRdhnIRSLQDEMANQDEAVAKLNKEKKHQ 1012
Cdd:PRK02224 162 GKLEEYRERASDarLGVERVLSDQRgsLDQLKAQIEEKE------EKDLHER---LNGLESELAELDEEIERYEEQREQA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1013 EESNRKLNEDLQSEEDKVNHLEKirnkLEQQMDELEENI-----DRE---------KRSRGDIEKAKRKVEGDLKVAQEN 1078
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELET----LEAEIEDLRETIaeterEREelaeevrdlRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1079 IDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELeeeleaernsRQKSDRSRSEAERELEE 1158
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL----------REEAAELESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1159 LTERLEQQgGATAAQLEANKKREAEiAKLRREKEEDSLnhETAISSLRKRHGDsVAELTEQLETLQKLKAKSEA--EKSK 1236
Cdd:PRK02224 379 VEDRREEI-EELEEEIEELRERFGD-APVDLGNAEDFL--EELREERDELRER-EAELEATLRTARERVEEAEAllEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1237 ---LQRDLEESQHA---TDSEVRsRQDLEKALKTIEVQYSELQTKAdEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQ 1310
Cdd:PRK02224 454 cpeCGQPVEGSPHVetiEEDRER-VEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1311 LNSlhrlKSTLQSQLDETRRNYDEESRERQALAATAknlehentilREHLDEEAESKADLTRQISKLNAEIQQWKARFDS 1390
Cdd:PRK02224 532 IEE----KRERAEELRERAAELEAEAEEKREAAAEA----------EEEAEEAREEVAELNSKLAELKERIESLERIRTL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1391 egLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQsdVEKAAAQVAFYEKHRRQFESIIAEWK 1470
Cdd:PRK02224 598 --LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELR 673
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 127737 1471 KKTDDLSSELDAAQRDNRQLStDLFKAKTANDELAEYLDSTRRENKSL 1518
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEEL 720
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1639 |
4.70e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1038 NKLEQQMDELEENIDREKRSRGDIEkakrKVEGDLKVAQENIDEITKQKHDVET----TLKRKEEDLHHTNAKLAENNSI 1113
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNID----YLEEKLKSSNLELENIKKQIADDEKshsiTLKEIERLSIEYNNAMDDYNNL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1114 IAKLQRLIKELTARNAELEEEleaernsrQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEE 1193
Cdd:PRK01156 238 KSALNELSSLEDMKNRYESEI--------KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1194 DSLNHETAISSLRKRHgdsvaELTEQLETLQK-----LKAKSEAEKSKLQR-DLEESQHATDSEVRSrqdLEKALKTIEV 1267
Cdd:PRK01156 310 KKQILSNIDAEINKYH-----AIIKKLSVLQKdyndyIKKKSRYDDLNNQIlELEGYEMDYNSYLKS---IESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1268 QYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDE-ESRERQALAATA 1346
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlNGQSVCPVCGTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1347 KNLEHENTIlREHLDEEA---ESKAD-LTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLfA 1422
Cdd:PRK01156 462 LGEEKSNHI-INHYNEKKsrlEEKIReIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKI-N 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1423 KIASQE------KVRFKLM--QDLDDAQSDVEKAAAQVAF--YEKHRRQFESIiaewKKKTDDLSSELDaaqrdnrqlst 1492
Cdd:PRK01156 540 ELKDKHdkyeeiKNRYKSLklEDLDSKRTSWLNALAVISLidIETNRSRSNEI----KKQLNDLESRLQ----------- 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1493 dlfKAKTANDELAEYLDSTRREnksLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDeaeaaleaeeakVL 1572
Cdd:PRK01156 605 ---EIEIGFPDDKSYIDKSIRE---IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS------------II 666
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 1573 RAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQR------ALESMQATLEAETKQKEEALRIKKKLESDINDLE 1639
Cdd:PRK01156 667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARlestieILRTRINELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1183-1688 |
5.14e-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: 58.31 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1183 EIAKLrrekEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDsevRSRQDLEKAL 1262
Cdd:pfam12128 242 EFTKL----QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD---ELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1263 KTIEVQYSELQtKADEQSRQLQDFAALKNRLNNENSDLNRS-LEEMDNqlnslhRLKSTLQSQLDETRRNYDEESRERQA 1341
Cdd:pfam12128 315 AAVAKDRSELE-ALEDQHGAFLDADIETAAADQEQLPSWQSeLENLEE------RLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1342 LAATAKNLEHENTILREHLDEE-AESKADLTRQISKLNAEIQQWKARFDSEGlnklEEIEAAKKALQLKVQELTDTNEGL 1420
Cdd:pfam12128 388 NNRDIAGIKDKLAKIREARDRQlAVAEDDLQALESELREQLEAGKLEFNEEE----YRLKSRLGELKLRLNQATATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1421 FAKIASQEKVrfklmqdlDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTA 1500
Cdd:pfam12128 464 LQLENFDERI--------ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1501 ndeLAEYLDSTR---REN--KSLAQE-------VKDLTDQLGEGGRSVAELQKIVRKLEVEK-----EELQKALDEAEAA 1563
Cdd:pfam12128 536 ---LLHFLRKEApdwEQSigKVISPEllhrtdlDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaaseEELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1564 LEAEEAKVLRAQIEVSQIRSEIEKriQEKEEEF-----ENTRRNHQRALESMQATLEAETKQKEEAlriKKKLESDINDL 1638
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEK--ASREETFartalKNARLDLRRLFDEKQSEKDKKNKALAER---KDSANERLNSL 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 127737 1639 EI---ALDHANRAYADAQKTIKK--YMETVQELQFQIEEEQRQKDEIREQFLASE 1688
Cdd:pfam12128 688 EAqlkQLDKKHQAWLEEQKEQKReaRTEKQAYWQVVEGALDAQLALLKAAIAARR 742
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1350-1885 |
6.46e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1350 EHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDS---------EGLNKLEEIEAAKKALQLKVQELTDTNEGL 1420
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEadevleeheERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1421 FAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRrqfesiiaewkkktDDLSSELDAAQRDNRQLSTDLFKAKTA 1500
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR--------------EELEDRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1501 NDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEaeeakvlRAQIEVSQ 1580
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-------NAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1581 IRSEIEkRIQEKEEEFENTRRNHQRALESMQATLEA--------------------ETKQKEEALRIK-KKLESDINDLE 1639
Cdd:PRK02224 417 LREERD-ELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetieEDRERVEELEAElEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1640 IALDHANRAyADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQflASEKRnailqSEKDELAQQAEAAERARRNAEAEC 1719
Cdd:PRK02224 496 ERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRER--AEELR-----ERAAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1720 IELREQNNDLNAHVSALTGQRRKLE--GELLAAHAELEEIANELKNAVEQgqkasadaarLAEELRQEQEH-SMHIERIR 1796
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREA----------LAELNDERRERlAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1797 kglelqikEMQIRLDDAENAALKGGKkiiAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEfqvvEEKKNEER 1876
Cdd:PRK02224 638 --------ELEAEFDEARIEEAREDK---ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE----ELRERREA 702
|
....*....
gi 127737 1877 LTELVDKLQ 1885
Cdd:PRK02224 703 LENRVEALE 711
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1397-1932 |
1.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1397 EEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRfKLMQDLDDAQSDVEKAAAQVAFYEKHR-------RQFESIIAEW 1469
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIEELEKELESLEGSKrkleekiRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1470 KKKTDDLSS------ELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIV 1543
Cdd:PRK03918 272 KKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1544 RKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKrIQEKEEEFENTRRNhqraLESMQATLEAETKQKEE 1623
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-LEKAKEEIEEEISK----ITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1624 AL-RIKK-KLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIrEQFLASEKRNAILQSEKDEL 1701
Cdd:PRK03918 427 AIeELKKaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1702 AQQAEAAERARRNAEAECIE----LREQNNDLNAHVS----------ALTGQRRKLEGELLAAHAELEEIANELKnavEQ 1767
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKslkkelekleELKKKLAELEKKLDELEEELAELLKELE---EL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1768 GQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAalkggKKIIAQLEARIRAIEQELDGEQRRHq 1847
Cdd:PRK03918 583 GFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-----FEELAETEKRLEELRKELEELEKKY- 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1848 dTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEvAASNLNKYKVLTAQFEQAEE-----R 1922
Cdd:PRK03918 657 -SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREkvkkyK 734
|
570
....*....|
gi 127737 1923 ADIAENALSK 1932
Cdd:PRK03918 735 ALLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1167-1396 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1167 GGATAAQLEANKKREAEIAKLRREKEEdslnHETAISSLRKRHGDSVAELTE---QLETLQKLKAKSEAEKSKLQRDLEE 1243
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAAlerRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1244 SQhatdsevRSRQDLEKALKTIEVQYSEL------------------QTKADEQSRQLQDFAALKNRLNNENSDLNRSLE 1305
Cdd:COG4942 88 LE-------KEIAELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1306 EMDNQLNSLHRLKSTLQSQLDET---RRNYDEESRERQALAATaknLEHENTILREHLDEEAESKADLTRQISKLNAEIQ 1382
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELeeeRAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....
gi 127737 1383 QWKARFDSEGLNKL 1396
Cdd:COG4942 238 AAAERTPAAGFAAL 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
846-1555 |
1.51e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 846 FGKVKPMLKAGKEQEAMGELAVKIQKLEEAV---QRGEIARSQLESQVADLVEEK----NALFLSLETEKANLADAEERN 918
Cdd:pfam12128 195 FRDVKSMIVAILEDDGVVPPKSRLNRQQVEHwirDIQAIAGIMKIRPEFTKLQQEfntlESAELRLSHLHFGYKSDETLI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 919 EKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKT-DQELSDTKKHVQDLELSLRKAEQEKQSRDH----NIRSLQD 993
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAaDAAVAKDRSELEALEDQHGAFLDADIETAAadqeQLPSWQS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 994 EMANQDEAVAKL--NKEKKHQEESNRKLNEDLQ--------------SEEDKVNHLEKIRNKLEQQMDELEENIDREKRS 1057
Cdd:pfam12128 355 ELENLEERLKALtgKHQDVTAKYNRRRSKIKEQnnrdiagikdklakIREARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1058 RGDIEKAKRKVEGDLKVaqeNIDEITKQKhDVETTLKRKEEDLHHTNAKLAENNsiiAKLQRLIKELTARnaeleeelea 1137
Cdd:pfam12128 435 FNEEEYRLKSRLGELKL---RLNQATATP-ELLLQLENFDERIERAREEQEAAN---AEVERLQSELRQA---------- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1138 ernsRQKSDRSrseAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELT 1217
Cdd:pfam12128 498 ----RKRRDQA---SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1218 EQletlqklKAKSEAEKSKLQRDLEESQHatDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNEN 1297
Cdd:pfam12128 571 DG-------SVGGELNLYGVKLDLKRIDV--PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1298 SDLNRSLEEMDNQLNSLHRLKSTLQSQLDETR-RNYDEESRERQALAATAKNLEHENTILREHLDEEAeskadLTRQISK 1376
Cdd:pfam12128 642 TFARTALKNARLDLRRLFDEKQSEKDKKNKALaERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK-----REARTEK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1377 LNAEIQQWKARFDSEGLNKlEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAA---AQVA 1453
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLK-AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAvrrQEVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1454 FYEK--------HRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDL 1525
Cdd:pfam12128 796 RYFDwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740 750
....*....|....*....|....*....|....*.
gi 127737 1526 -----TDQL-GEGGRSVAELQKIVRKLEVEKEELQK 1555
Cdd:pfam12128 876 kedanSEQAqGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1459-1937 |
1.67e-07 |
|
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: 56.67 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1459 RRQFESIIAEWKKKTDDL------SSELDAAQRDN-RQ----LSTDLFKAKTANDELAeylDSTRRENKSlaQEvkDLTD 1527
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLqrrlneSNELHEKQKFYlRQsvidLQTKLQEMQMERDAMA---DIRRRESQS--QE--DLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1528 QLgeggrsvaelQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRS---EIEKRIQEKEEEFENTRRNHQ 1604
Cdd:pfam15921 146 QL----------QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvDFEEASGKKIYEHDSMSTMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1605 RALESMQATLEAETKQKEEALR-----IKKKLES----DINDLEIAL----DHANRAYADAQKTIKKYMETVQELQFQIE 1671
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKgrifpVEDQLEAlkseSQNKIELLLqqhqDRIEQLISEHEVEITGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1672 EEQRQKDEIREQflaSEKRNAILQSEKDELAQQAEAAERarrnaeaeciELREQNNDLNAHVSALTGQRRKLEGELLAAH 1751
Cdd:pfam15921 296 SIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTVSQLRS----------ELREAKRMYEDKIEELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1752 AELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAalkggkkiIAQLEAR 1831
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME--------VQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1832 IRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKkneERLTELVDKLQCKlkifKRQVEEAEEVAASnlnkykv 1911
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK---EMLRKVVEELTAK----KMTLESSERTVSD------- 500
|
490 500
....*....|....*....|....*..
gi 127737 1912 LTAQFeQAEERADIAENA-LSKMRNKI 1937
Cdd:pfam15921 501 LTASL-QEKERAIEATNAeITKLRSRV 526
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
867-1463 |
1.71e-07 |
|
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: 56.59 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 867 VKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLEteKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERN 946
Cdd:TIGR00606 447 EILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER--ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 947 EDLARQKKKTDQELSDTKKhvqdlelslrKAEQEKQSRDHNIRSlQDEMANQ----------DEAVAKLNKEKKHQEESN 1016
Cdd:TIGR00606 525 EQLNHHTTTRTQMEMLTKD----------KMDKDEQIRKIKSRH-SDELTSLlgyfpnkkqlEDWLHSKSKEINQTRDRL 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1017 RKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIdrekrsrgdiekakrkvegdlkvaqenIDEITKQkhDVETTLKRK 1096
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---------------------------FDVCGSQ--DEESDLERL 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1097 EEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEEleaernsrqkSDRSRSEAERELEELTERLEQQGGATAAQlea 1176
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPV----------CQRVFQTEAELQEFISDLQSKLRLAPDKL--- 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1177 nKKREAEIAKLRREKEEDSLNHETAISSLRKRhgdsVAELTEQLETLQKLKAKSEAEKSKLQRdlEESQHATdseVRSRQ 1256
Cdd:TIGR00606 712 -KSTESELKKKEKRRDEMLGLAPGRQSIIDLK----EKEIPELRNKLQKVNRDIQRLKNDIEE--QETLLGT---IMPEE 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1257 DLEKALKTIEVQYSELQTKADEQSRQLQDFAAlknrlNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEES 1336
Cdd:TIGR00606 782 ESAKVCLTDVTIMERFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1337 RERQALAATAKNLEHENTILREHLDEE---AESKADLTRQISKLNAEIQQWK------ARFDSEGLNKLEEIEAAKKALQ 1407
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKeqdsplETFLEKDQQEKEELISSKETSN 936
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127737 1408 LKVQ-ELTDTNEGLFAKIASQEKVrFKLMQD-----LDDAQSDVEKAAAQVAFYEKHRRQFE 1463
Cdd:TIGR00606 937 KKAQdKVNDIKEKVKNIHGYMKDI-ENKIQDgkddyLKQKETELNTVNAQLEECEKHQEKIN 997
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
994-1730 |
2.04e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 994 EMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKvEGDLK 1073
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK-QQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1074 VAQENIDEITKQKHDVETTlkRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQksdrsrseaE 1153
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEET--QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA---------A 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1154 RELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRkrhgdsvaeltEQLETLQKLKAKSEAE 1233
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ-----------QQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1234 KSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDfAALKNRLNNEnsdLNRSLEEMDNQLns 1313
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC-EKLEKIHLQE---SAQSLKEREQQL-- 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1314 lhrlkSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGl 1393
Cdd:TIGR00618 476 -----QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1394 nKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAaqvafyeKHRRQFESIIAEWKKKT 1473
Cdd:TIGR00618 550 -QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS-------EAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1474 DDLSSELDAAQRDnRQLSTDLFKAKTANDELAEYLDSTRRENKSLAqeVKDLTDQLGEGG-RSVAELQKIVRKLEVEKEE 1552
Cdd:TIGR00618 622 QPEQDLQDVRLHL-QQCSQELALKLTALHALQLTLTQERVREHALS--IRVLPKELLASRqLALQKMQSEKEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1553 LQKaLDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLE 1632
Cdd:TIGR00618 699 LAQ-CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1633 SDINDLEIALDHANRAYADAQKTIKKYMETVQ------ELQFQIEEEQRQKDeiREQFLASEKRNAILQSEKDELAQQAE 1706
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipsdEDILNLQCETLVQE--EEQFLSRLEEKSATLGEITHQLLKYE 855
|
730 740
....*....|....*....|....
gi 127737 1707 AAERARRNAEAECIELREQNNDLN 1730
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
852-1527 |
2.50e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 852 MLKAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLS-LETEKANLADAEERNEKLNQLKATLES 930
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 931 KLSDITGQ--------LEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQE-----KQSRDHNIRSLQDEMAN 997
Cdd:COG4913 324 ELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalrAEAAALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 998 QDEAVAKLNKEKKHQEESnRKLNEDLQS-EEDKVN---HLEKIRNKLEQQMDELEENI----------DREKRSRGDIEK 1063
Cdd:COG4913 404 EEALAEAEAALRDLRREL-RELEAEIASlERRKSNipaRLLALRDALAEALGLDEAELpfvgelievrPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1064 AKRKV-------EGDLKVAQENIDEI-TKQKHDVEttlkRKEEDLHHTNAKLAENNSIIAKL-------QRLIKELTARN 1128
Cdd:COG4913 483 VLGGFaltllvpPEHYAAALRWVNRLhLRGRLVYE----RVRTGLPDPERPRLDPDSLAGKLdfkphpfRAWLEAELGRR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1129 AE------------------LEEELEAERNSRQKSDRSrseaereleeLTERLEQQGGATAAQLEAnkkREAEIAKLRRE 1190
Cdd:COG4913 559 FDyvcvdspeelrrhpraitRAGQVKGNGTRHEKDDRR----------RIRSRYVLGFDNRAKLAA---LEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1191 KEEdslnHETAISSLRKRHgdsvAELTEQLETLQKLKAKSEAEK--SKLQRDLEESQHAtdsevrsRQDLEKA---LKTI 1265
Cdd:COG4913 626 LAE----AEERLEALEAEL----DALQERREALQRLAEYSWDEIdvASAEREIAELEAE-------LERLDASsddLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1266 EVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKST-LQSQLDETRRNYDEESRERQAlaa 1344
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVEREL--- 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1345 tAKNLEHENTILREHLDEEAEskaDLTRQISKLN----AEIQQWKARFDSEG-----LNKLEEIEAAKKALQLKvQELTD 1415
Cdd:COG4913 768 -RENLEERIDALRARLNRAEE---ELERAMRAFNrewpAETADLDADLESLPeylalLDRLEEDGLPEYEERFK-ELLNE 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1416 TNEGLFAKIASqekvrfKLMQDLDDAQSDVE---KAAAQVAFYEKHRRQFE---SIIAEWKKKTDDLSSELDAAQRDNRQ 1489
Cdd:COG4913 843 NSIEFVADLLS------KLRRAIREIKERIDplnDSLKRIPFGPGRYLRLEarpRPDPEVREFRQELRAVTSGASLFDEE 916
|
730 740 750
....*....|....*....|....*....|....*...
gi 127737 1490 LSTDLFKAKtanDELAEYLDStrRENKSLAQEVKDLTD 1527
Cdd:COG4913 917 LSEARFAAL---KRLIERLRS--EEEESDRRWRARVLD 949
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
929-1126 |
2.50e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 929 ESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKE 1008
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1009 KKHQEESNRKLNEDLQSE--EDKVNHLEKIRNKLEQQMDELEENidreKRSRGDIEKAKRKVEGDLKVAQENIDEITKQK 1086
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 127737 1087 HDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTA 1126
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
854-1124 |
2.57e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 854 KAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQL--------- 924
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagkcpec 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 925 -------------------KATLESKLSDITGQLEDMQ---ERNEDLARQKKKTDqELSDTKKHVQDLELSLRKAEQEKQ 982
Cdd:PRK02224 458 gqpvegsphvetieedrerVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKR 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 983 SRDHNIRS----LQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEqQMDELEENIDREKRSR 1058
Cdd:PRK02224 537 ERAEELREraaeLEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKR 615
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1059 GDI------------EKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKEL 1124
Cdd:PRK02224 616 EALaelnderrerlaEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1288-1900 |
3.70e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1288 ALKNRLNNENSDLnrslEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESK 1367
Cdd:TIGR04523 23 GYKNIANKQDTEE----KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1368 ADLTRQISKLNAEIQ---QWKARFDSEgLNKLEEIEAAKKALQLKV-----------QELTDTNEGLFAKIASQEKVRFK 1433
Cdd:TIGR04523 99 NKLNSDLSKINSEIKndkEQKNKLEVE-LNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1434 LMQDLDDAQSDVEKAAAQVAFYEkhrrQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRR 1513
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLE----LLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1514 ENKSLAQEVKDLTDQLGE-------GGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIR-SEI 1585
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEkqkeleqNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQiSQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1586 EKRIQEKEEEF----------ENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEialdhanrayadaqKT 1655
Cdd:TIGR04523 334 NKIISQLNEQIsqlkkeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE--------------SK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1656 IKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSA 1735
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1736 LTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLD---- 1811
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenl 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1812 ----DAENAALKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCK 1887
Cdd:TIGR04523 560 ekeiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
650
....*....|...
gi 127737 1888 LKIFKRQVEEAEE 1900
Cdd:TIGR04523 640 KNKLKQEVKQIKE 652
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1207-1517 |
3.73e-07 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 55.61 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1207 KRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSR-----QDLEKALKTIeVQYSELQTKADEQSR 1281
Cdd:NF012221 1471 RRAGLSTNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAKAGSNRLEFKgtghnDGLGYILDNV-VATSESSQQADAVSK 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1282 QLQDFAALKNRLNN-ENSDLNRS-LE-EMDNQLNSLhrlkSTLQSQLDETRRNYDEES--RERQALAATAKNLEHENTIL 1356
Cdd:NF012221 1550 HAKQDDAAQNALADkERAEADRQrLEqEKQQQLAAI----SGSQSQLESTDQNALETNgqAQRDAILEESRAVTKELTTL 1625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1357 REHLDEeaeskadLTRQISKLNAEIQQWKARFdSEGL--NKLEEIEAAKKALQLKVQELTDTNEGLfakiasqekvrfkl 1434
Cdd:NF012221 1626 AQGLDA-------LDSQATYAGESGDQWRNPF-AGGLldRVQEQLDDAKKISGKQLADAKQRHVDN-------------- 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1435 MQDLDDAqsdVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLF----KAKTANDElaeylDS 1510
Cdd:NF012221 1684 QQKVKDA---VAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANaaanDAQSRGEQ-----DA 1755
|
....*..
gi 127737 1511 TRRENKS 1517
Cdd:NF012221 1756 SAAENKA 1762
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
848-1095 |
5.10e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 848 KVKPMLKAGKEQEAMGELAVKIQKLEEAVqrGEIARSQLEsQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKAT 927
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKELEEKL--KKYNLEELE-KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 928 LESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNK 1007
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1008 ------------EKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEgDLKVA 1075
Cdd:PRK03918 641 rleelrkeleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKA 719
|
250 260
....*....|....*....|
gi 127737 1076 QENIDEITKQKHDVETTLKR 1095
Cdd:PRK03918 720 LERVEELREKVKKYKALLKE 739
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1253-1443 |
5.68e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1253 RSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAAlKNR---LNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETR 1329
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-KNGlvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1330 RNYDE---------ESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNKLEEIE 1400
Cdd:COG3206 247 AQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 127737 1401 AAKKALQLKVQELtdtnEGLFAKIASQEKVRFKLMQDLDDAQS 1443
Cdd:COG3206 327 AREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARE 365
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
1208-1384 |
5.89e-07 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 54.22 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1208 RHGDSVAELTEQLETLqklkaksEAEKSKLQRDLEESQHATD------SEVRSRQD----LEKALKTIEVQYSELQTKAD 1277
Cdd:PRK10361 26 QHAQQKAEQLAEREEM-------VAELSAAKQQITQSEHWRAecellnNEVRSLQSintsLEADLREVTTRMEAAQQHAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1278 EQSRQL--------QDFAALKNRLNNENsdlNRSLEEMDNQlnSLHRLKSTLQSQLDETRR----NYDEESRERQALAAT 1345
Cdd:PRK10361 99 DKIRQMinseqrlsEQFENLANRIFEHS---NRRVDEQNRQ--SLNSLLSPLREQLDGFRRqvqdSFGKEAQERHTLAHE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 127737 1346 AKNLEHENTilrehldEEAESKADLTRQISKLNAEIQQW 1384
Cdd:PRK10361 174 IRNLQQLNA-------QMAQEAINLTRALKGDNKTQGNW 205
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
857-1097 |
6.34e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAvqrgEIAR-SQLESQVADLVE-EKNALFLSLETEKANLADAEERNEKLNQLKATLE-SKLS 933
Cdd:pfam17380 303 QEKEEKAREVERRRKLEEA----EKARqAEMDRQAAIYAEqERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 934 DITGQLEDMQERNEDL-----ARQKKKTDQELSDTKKHVQDLELSLRKAEQEkQSRDHNIRSLQDEMANQDEAVAKLNKE 1008
Cdd:pfam17380 379 ELERLQMERQQKNERVrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1009 KKHQ----------------------------EESNRK-LNEDLQSEEDKVNHLEKIRNKLEQQMDELEENI-DREKRSR 1058
Cdd:pfam17380 458 RQQQverlrqqeeerkrkklelekekrdrkraEEQRRKiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIyEEERRRE 537
|
250 260 270
....*....|....*....|....*....|....*....
gi 127737 1059 GDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKE 1097
Cdd:pfam17380 538 AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1332-1701 |
8.99e-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: 54.30 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1332 YDEESRE-RQALAATAKNLEHENTILREHLD-----EEAESKADLTRQISKLNAEIQQWkarfdsEGLNKLEEIEAAKKA 1405
Cdd:TIGR02169 168 FDRKKEKaLEELEEVEENIERLDLIIDEKRQqlerlRREREKAERYQALLKEKREYEGY------ELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1406 LQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAA--QVAFYEKhRRQFESIIAEWKKKTDDLSSELDAA 1483
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeQLRVKEK-IGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1484 QRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDqlgeggrsvaELQKIVRKLEVEKEELQkaldeaeaa 1563
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----------ELEDLRAELEEVDKEFA--------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1564 leaeeakvlRAQIEVSQIRSEIEKRIQEKEEefentrrnHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALD 1643
Cdd:TIGR02169 382 ---------ETRDELKDYREKLEKLKREINE--------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1644 hanrayaDAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDEL 1701
Cdd:TIGR02169 445 -------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
907-1529 |
9.66e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 907 EKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQElsdtkkhvqdlELSLRKAEQEKQSRDH 986
Cdd:PRK01156 157 EILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADD-----------EKSHSITLKEIERLSI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 987 NIRSLQDEMANQDEAVAKLN---KEKKHQEESNRKLNEDLQSEEDKVNHLEKIrnklEQQMDELEENIDREKRSRGDIEK 1063
Cdd:PRK01156 226 EYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKEL----EERHMKIINDPVYKNRNYINDYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1064 AKRKVEGDLKVAQENIDEITKQKHDVettlKRKEEDLHHTNAKLAENNSIIAKLQRLIKELtarnaeleeelEAERNSRQ 1143
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAI----IKKLSVLQKDYNDYIKKKSRYDDLNNQILEL-----------EGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1144 KSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETL 1223
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1224 QKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELqtkaDEQSRQLQdfaALKNRLNNENsdlnrs 1303
Cdd:PRK01156 447 EMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI----DEKIVDLK---KRKEYLESEE------ 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1304 LEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQAlaataknLEHENTILREHLDEEAESKADLTRQISklNAEIQQ 1383
Cdd:PRK01156 514 INKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI-------KNRYKSLKLEDLDSKRTSWLNALAVIS--LIDIET 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1384 WKARFDsEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFE 1463
Cdd:PRK01156 585 NRSRSN-EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID 663
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 1464 SIIaewkKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQL 1529
Cdd:PRK01156 664 SII----PDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL 725
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
857-1908 |
9.74e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAVQRGEIArsQLESQVADLVEEKNALFLSLETEKANLADaeERNEKLNQLKATLESKLSDIT 936
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETA--TVELHLSNIENKKNELLDIIVEIKKHIHG--EINKDLNKILEDFKNKEKELS 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 937 GQLEDMQERNEDLARQKKKtdqeLSDTKKHVQD-LELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEES 1015
Cdd:TIGR01612 769 NKINDYAKEKDELNKYKSK----ISEIKNHYNDqINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDF 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1016 NRKLN----------EDLQSEEDKVNHL-EKIRNKL-EQQMDELEENIDREKRSRGDIEKA----------KRKVEGDLK 1073
Cdd:TIGR01612 845 LNKVDkfinfennckEKIDSEHEQFAELtNKIKAEIsDDKLNDYEKKFNDSKSLINEINKSieeeyqnintLKKVDEYIK 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1074 VAqENIDEITKQKHDVETTLKR---------KEEDLHHTNAKLAENNSIIAK---LQRLIKELTARNAELEEELEAERNS 1141
Cdd:TIGR01612 925 IC-ENTKESIEKFHNKQNILKEilnknidtiKESNLIEKSYKDKFDNTLIDKineLDKAFKDASLNDYEAKNNELIKYFN 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1142 RQKSDRSRseaereleelterleQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAI-SSLRKRHGDSVAELTEQL 1220
Cdd:TIGR01612 1004 DLKANLGK---------------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIhTSIYNIIDEIEKEIGKNI 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1221 ETLQK-LKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKA--LKTIEVQYSELQTKADEQSRQLQDfaaLKNRLNNen 1297
Cdd:TIGR01612 1069 ELLNKeILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYAdeINKIKDDIKNLDQKIDHHIKALEE---IKKKSEN-- 1143
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1298 sdlnrSLEEMDNQLNSLHRLKstlqsqlDETRRNYDEESRERQALAATAKNLEHENTI--LREHLDEEAESKADLT--RQ 1373
Cdd:TIGR01612 1144 -----YIDEIKAQINDLEDVA-------DKAISNDDPEEIEKKIENIVTKIDKKKNIYdeIKKLLNEIAEIEKDKTslEE 1211
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1374 ISKLNAEIQQwkarfdseGLNKL--EEIEAAKKALQLKVQELTDTNEGLfAKIASQEKVRFKLMQDLDDAQSDVE----- 1446
Cdd:TIGR01612 1212 VKGINLSYGK--------NLGKLflEKIDEEKKKSEHMIKAMEAYIEDL-DEIKEKSPEIENEMGIEMDIKAEMEtfnis 1282
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1447 --KAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAaQRDNRQLSTDLFKAKTANDELAEYLDS-TRRENKSLAQEVK 1523
Cdd:TIGR01612 1283 hdDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDI-NDIKKELQKNLLDAQKHNSDINLYLNEiANIYNILKLNKIK 1361
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1524 DLTDQLGEGGRSVAELQKIVrkleveKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEE-------- 1595
Cdd:TIGR01612 1362 KIIDEVKEYTKEIEENNKNI------KDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELknhilsee 1435
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1596 ------FENTRRNHQRALESMQaTLEAETKQKEEALRIKKK-----LESDINDLEIALDHANRAYADAQKTiKKYMETVQ 1664
Cdd:TIGR01612 1436 snidtyFKNADENNENVLLLFK-NIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKN-AKAIEKNK 1513
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1665 ELqfqIEEEQRQKDEIREQFLASEKRNAILQSEKDElaqqaeaaerarrnaEAECIELREQNNDLNahvsaltgqrrkLE 1744
Cdd:TIGR01612 1514 EL---FEQYKKDVTELLNKYSALAIKNKFAKTKKDS---------------EIIIKEIKDAHKKFI------------LE 1563
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1745 GEllAAHAELEEIANE---LKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRK----------GLELQIKEMQIrld 1811
Cdd:TIGR01612 1564 AE--KSEQKIKEIKKEkfrIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKkindclketeSIEKKISSFSI--- 1638
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1812 DAENAALKGGKKIIAQLEARIraieQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEErlTELVDKLQCKLKIF 1891
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSLQEFL----ESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE--IGIIEKIKEIAIAN 1712
|
1130
....*....|....*..
gi 127737 1892 KRQVEEAEEVAASNLNK 1908
Cdd:TIGR01612 1713 KEEIESIKELIEPTIEN 1729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1374-1833 |
1.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1374 ISKLNAEIQQW---KARFDSEGLNKLEEIEAAKKALQLKV---QELTDTNEGLFAKIASQEKVRFKLMQDLDDAQsDVEK 1447
Cdd:COG4717 48 LERLEKEADELfkpQGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLE-KLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1448 AAAQVAFYEKHRRQFESIIAEWKKKTDDLSsELDAAQRDNRQLSTDLFKAKTANDELAEYLD-STRRENKSLAQEVKDLT 1526
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1527 DQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLR----AQIEVSQIRSEIEKRIQEKEE-------- 1594
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaALLALLGLGGSLLSLILTIAGvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1595 ---EFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADaqktikkyMETVQELQFQIE 1671
Cdd:COG4717 286 lalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR--------IEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1672 EEQRQKDEIREQflasEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLaaH 1751
Cdd:COG4717 358 ELEEELQLEELE----QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--E 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1752 AELEEIANELKNAVEQGQKASADAARLAEELRQeQEHSMHIERIRkgLELQIKEMQIRLDDAENAALKGGKKIIAQLEAR 1831
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQ-LEEDGELAELL--QELEELKAELRELAEEWAALKLALELLEEAREE 508
|
..
gi 127737 1832 IR 1833
Cdd:COG4717 509 YR 510
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
915-1479 |
1.36e-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: 53.57 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 915 EERNEKLNQLKATL------ESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNI 988
Cdd:pfam05483 233 KEINDKEKQVSLLLiqitekENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 989 RSLQDEMANQDEAVAKLNKEKKHQ-EESNRKlnedlqseedKVNHlEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRK 1067
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQmEELNKA----------KAAH-SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1068 VEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNsiiaKLQRLIKELTARNAELEEELEaernSRQKSDR 1147
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK----QFEKIAEELKGKEQELIFLLQ----AREKEIH 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1148 SRSEAERELEELTERLEQQGGATAAQLEANKKREAEIA-----------KLRREKEEDSL---NHETAISSLRKRHGDSV 1213
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcdklllenkELTQEASDMTLelkKHQEDIINCKKQEERML 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1214 AELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRL 1293
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1294 NNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQalaataKNLEhENTILREHLDEEAESKADLTRQ 1373
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ------KEIE-DKKISEEKLLEEVEKAKAIADE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1374 ISKLNAEIqqwkarfDSEGLNKLEEIEA---AKKALQLKVQELTDTNEGLF-AKIASQEKVRFKLMQDLDDAQSDVEKAA 1449
Cdd:pfam05483 687 AVKLQKEI-------DKRCQHKIAEMVAlmeKHKHQYDKIIEERDSELGLYkNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
570 580 590
....*....|....*....|....*....|
gi 127737 1450 AQVafyEKHRRQFESIIAEWKKKTDDLSSE 1479
Cdd:pfam05483 760 KQL---EIEKEEKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1683 |
1.38e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1476 LSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQK 1555
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1556 ALDEAEAALEAEEA---KVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLE 1632
Cdd:COG4942 91 EIAELRAELEAQKEelaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 127737 1633 SDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQ 1683
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1280-1683 |
1.46e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1280 SRQLQDFaalknrLNNENSDLNRSLEEMDNqlnSLHRLKSTLQSqLDETRRNYDEESR---ERQALAAtAKNLEHENTiL 1356
Cdd:PRK04863 214 TRSLRDY------LLPENSGVRKAFQDMEA---ALRENRMTLEA-IRVTQSDRDLFKHlitESTNYVA-ADYMRHANE-R 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1357 REHLDEEAESKADLTRQISKLNAEiQQWKARFDSEglnkLEEIEAAKKALQLKVQELTD------TNEGLFAKIASQEKV 1430
Cdd:PRK04863 282 RVHLEEALELRRELYTSRRQLAAE-QYRLVEMARE----LAELNEAESDLEQDYQAASDhlnlvqTALRQQEKIERYQAD 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1431 RFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDN---RQLSTDLFKAKTAN------ 1501
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAiqyQQAVQALERAKQLCglpdlt 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1502 -DELAEYLDSTRRENKSLAQEVKDLTDQL---------------------GEGGRSVAELQKIVRKLEVEKEELQKALDE 1559
Cdd:PRK04863 437 aDNAEDWLEEFQAKEQEATEELLSLEQKLsvaqaahsqfeqayqlvrkiaGEVSRSEAWDVARELLRRLREQRHLAEQLQ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1560 AEAALEAEEAKVLRAQIEVSQIRSEIEKRIQ---EKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDIN 1636
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRAERLLAEFCKRLGknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 1637 DLEI-------ALDHANRAYA---DAQKTIKKYMETVQELQFQIEEEQRQKDEIREQ 1683
Cdd:PRK04863 597 RLAArapawlaAQDALARLREqsgEEFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1181-1691 |
1.61e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.21 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1181 EAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLkaksEAEKSKLQRDLEESQHATDSEVRSRQDLEK 1260
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQEL----QKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1261 ALKTIevqyselQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQ 1340
Cdd:pfam05557 84 YLEAL-------NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1341 ALAATAKNLEHENTILREhLDEEAESKADLTRQISKLNAEIQQWkARFDSEgLNKLEEIEAAKKALQLKVQELTDTNEGL 1420
Cdd:pfam05557 157 NLEKQQSSLAEAEQRIKE-LEFEIQSQEQDSEIVKNSKSELARI-PELEKE-LERLREHNKHLNENIENKLLLKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1421 FAKIASQEKVRfklmqdlddaqsdvekaaAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAqrdnrqlstdlfkakta 1500
Cdd:pfam05557 234 KRKLEREEKYR------------------EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP----------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1501 nDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQ 1580
Cdd:pfam05557 279 -EDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1581 IRSEIE---KRIQEKEEEFENTRRNHQRA--LESMQATLEAETKQKEEALRIKK--KLESDINDLEIALDHANRAYADAQ 1653
Cdd:pfam05557 358 YRAILEsydKELTMSNYSPQLLERIEEAEdmTQKMQAHNEEMEAQLSVAEEELGgyKQQAQTLERELQALRQQESLADPS 437
|
490 500 510
....*....|....*....|....*....|....*...
gi 127737 1654 KTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRN 1691
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRC 475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1299-1862 |
2.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1299 DLNRSLEEMDNQLNSLHRLKSTLQSQLDETRrnYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQIskln 1378
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI---- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1379 aeiqqwkarfDSEGLNKLEEIEAAKKALQLKVQEltdtneglfakiasQEKVRFKLMQDLDDAQSDVEKAAAqvafyekh 1458
Cdd:COG4913 333 ----------RGNGGDRLEQLEREIERLERELEE--------------RERRRARLEALLAALGLPLPASAE-------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1459 rrQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEG-GRSVA 1537
Cdd:COG4913 381 --EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1538 ELQKIVRKLEVEKEE------------------------------------------LQKALDEAEAALEAEEAK---VL 1572
Cdd:COG4913 459 ELPFVGELIEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvYERVRTGLPDPERPRLDPdslAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1573 RAQIEVSQIRSEIEKRIQ--------EKEEEFentrRNHQRALesmqaTLEAETKQKEEALRIKKKlesdindleialDH 1644
Cdd:COG4913 539 KLDFKPHPFRAWLEAELGrrfdyvcvDSPEEL----RRHPRAI-----TRAGQVKGNGTRHEKDDR------------RR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1645 ANRAY---ADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQsekdelaqqaeaaerarrnaeaECIE 1721
Cdd:COG4913 598 IRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ----------------------RLAE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1722 LREQNNDLNAHVSALTGQRRKLEgELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHsmhieriRKGLEL 1801
Cdd:COG4913 656 YSWDEIDVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEE 727
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127737 1802 QIKEMQIRLDDAENAALKG---------GKKIIAQLEARIRA-IEQELDGEQRRHQDTEKNWRKAERRVKE 1862
Cdd:COG4913 728 ELDELQDRLEAAEDLARLElralleerfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1253-1486 |
3.07e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1253 RSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNY 1332
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1333 deesreRQALAATAKNLEHENTILREHldeeAESKADLTRQISKLNAEIQQWKARfdseglnkLEEIEAAKKALQLKVQE 1412
Cdd:COG4942 107 ------AELLRALYRLGRQPPLALLLS----PEDFLDAVRRLQYLKYLAPARREQ--------AEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127737 1413 LTDTNEGLFAKIASQEKVRfklmQDLDDAQSDVEKAAAQVafyEKHRRQFESIIAEWKKKTDDLSSELDAAQRD 1486
Cdd:COG4942 169 LEAERAELEALLAELEEER----AALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1582-1934 |
3.43e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1582 RSEIEKRIQEKEE-EFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDleiALDHANRAYAD--AQKTIKK 1658
Cdd:PRK04863 276 RHANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA---ASDHLNLVQTAlrQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1659 YMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELR------EQNNDLNaH 1732
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqalERAKQLC-G 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1733 VSALTGQrrKLEGELLAAHAELEEIANEL----------KNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQ 1802
Cdd:PRK04863 432 LPDLTAD--NAEDWLEEFQAKEQEATEELlsleqklsvaQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1803 IKEMQirlddaenaalkggkkiIAQLEARIRAIEQELDGEQRrhqdteknwrkAERRVKEVEFQVVEEKKNEERLTELVD 1882
Cdd:PRK04863 510 HLAEQ-----------------LQQLRMRLSELEQRLRQQQR-----------AERLLAEFCKRLGKNLDDEDELEQLQE 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 127737 1883 KLQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAEERADI---AENALSKMR 1934
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLR 616
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
857-1451 |
3.79e-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: 52.28 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAVQRGEIARSQlESQVADLVEEKNalflsLETEKANLADAEERNEKLNQLKATLESKLSDIT 936
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQ-EAVLEETQERIN-----RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 937 GQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEmanqdEAVAKLNKEKKH---QE 1013
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT-----QHIHTLQQQKTTltqKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1014 ESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKV-------EGDLKVAQENIDEITKQK 1086
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaqcekleKIHLQESAQSLKEREQQL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1087 HDVETTLKRKEE---------------------DLHHTNAKLA---ENNSIIAKLQRLIKELtARNAELEEELEAERNSR 1142
Cdd:TIGR00618 476 QTKEQIHLQETRkkavvlarllelqeepcplcgSCIHPNPARQdidNPGPLTRRMQRGEQTY-AQLETSEEDVYHQLTSE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1143 QKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRRE--KEEDSLNHETAISSLRKRHGDSVAELTEQL 1220
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKlsEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1221 ETLQKLKAKSEAEKSKLQRDLEEsQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDL 1300
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLTQ-ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1301 NRSLEEMDNQLNSLHRLKSTLQSQlDETRRNYDEESRERQALAATAKNLEHENTILRE-----HLDEEAESKADLTRQIs 1375
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAAR-EDALNQSLKELMHQARTVLKARTEAHFNNNEEVtaalqTGAELSHLAAEIQFFN- 791
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 1376 KLNAEIQQWKARFDSEGLNKLEEIEAAKKALQLK-VQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQ 1451
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETlVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
918-1100 |
4.10e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 918 NEKLNQLK--ATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEM 995
Cdd:COG1579 3 PEDLRALLdlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 996 ANqdeavAKLNKEKkhqeesnrklnEDLQSEEDKvnhLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVA 1075
Cdd:COG1579 83 GN-----VRNNKEY-----------EALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180
....*....|....*....|....*
gi 127737 1076 QENIDEITKQKHDVETTLKRKEEDL 1100
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREEL 168
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
869-1451 |
5.25e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 869 IQKLEEAVQRGEIARSQLESQVADlvEEKNALFLSLETEKAnladAEERNEKLNQlKATLESKLSDITGQLEDMQERNED 948
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIAD--DEKSHSITLKEIERL----SIEYNNAMDD-YNNLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 949 LARQKKKTDQELSDTKKhVQDLELSLRKAEQEKQSRDHN-IR---SLQDEMANQDEAVAKLNKEKKHQEESNRKLnEDLQ 1024
Cdd:PRK01156 258 IKTAESDLSMELEKNNY-YKELEERHMKIINDPVYKNRNyINdyfKYKNDIENKKQILSNIDAEINKYHAIIKKL-SVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1025 SEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTN 1104
Cdd:PRK01156 336 KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1105 AKLAENNSIIAKLQRLIKELTARNAELEEELEA-----------ERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQ 1173
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvcgTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1174 LEANKKREAEIAKLRREKEEDSLNHETAISSLRkrhgdsvAELTEQLETLQKLK---AKSEAEKSKLQrdleeSQHATDS 1250
Cdd:PRK01156 496 DEKIVDLKKRKEYLESEEINKSINEYNKIESAR-------ADLEDIKIKINELKdkhDKYEEIKNRYK-----SLKLEDL 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1251 EVRsRQDLEKALKTIE-VQYSELQTKADEQSRQLQDFAALKNRLNNENSDLN----RSLEEMDNQLNSLHRLKSTLQsql 1325
Cdd:PRK01156 564 DSK-RTSWLNALAVISlIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEANNLNNKYNEIQ--- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1326 detrrnydEESRERQALAATAKNLEHENTilreHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNkLEEIEAAKKA 1405
Cdd:PRK01156 640 --------ENKILIEKLRGKIDNYKKQIA----EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAN-RARLESTIEI 706
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 127737 1406 LQLKVQELTDTNEGLFAKIASQEKVRfKLMQDLDDAQSDVEKAAAQ 1451
Cdd:PRK01156 707 LRTRINELSDRINDINETLESMKKIK-KAIGDLKRLREAFDKSGVP 751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1283-1787 |
5.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1283 LQDF--AALKNRLNNENSDLNR-SLEEMDNQLNSLHRLKSTLQsQLDETRRNYDEESRERQALAATAKNLEHENTILREH 1359
Cdd:COG4717 39 LLAFirAMLLERLEKEADELFKpQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1360 LD--EEAESKADLTRQISKLNAEIQQWKARFDsEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKiasQEKVRFKLMQD 1437
Cdd:COG4717 118 LEklEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1438 LDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTAndeLAEYLDSTRRENKS 1517
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA---ALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1518 LAQEVKD---------------LTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIR 1582
Cdd:COG4717 271 LILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1583 sEIEKRIQEKEEEFENTRRNHQRA--LESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKym 1660
Cdd:COG4717 351 -ELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1661 etvQELQFQIEEEQRQKDEIREQFLasekrnailqsekdelaqqaeaaerarrnaeaeciELREQNNDLNAHVSALTGqr 1740
Cdd:COG4717 428 ---EELEEELEELEEELEELEEELE-----------------------------------ELREELAELEAELEQLEE-- 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 127737 1741 rklEGELLAAHAELEEIANELKNAVEQGQKASAdAARLAEELRQEQE 1787
Cdd:COG4717 468 ---DGELAELLQELEELKAELRELAEEWAALKL-ALELLEEAREEYR 510
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1188-1462 |
5.78e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.17 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1188 RREKEEDSLNHETaISSLRKRHGDSVAELTEQLETLQkLKAKSEAEKSKLQRDLEESQHATDSEVRSRqdlekalktiev 1267
Cdd:PHA02562 152 RRKLVEDLLDISV-LSEMDKLNKDKIRELNQQIQTLD-MKIDHIQQQIKTYNKNIEEQRKKNGENIAR------------ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1268 qyseLQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRR----------------N 1331
Cdd:PHA02562 218 ----KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1332 YDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNaEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQ 1411
Cdd:PHA02562 294 ISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL-ELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 127737 1412 ELTDTNEGLfAKIASQEKvrfklmqDLDDAQSDVEKaaaqvafyEKHRRQF 1462
Cdd:PHA02562 373 EFVDNAEEL-AKLQDELD-------KIVKTKSELVK--------EKYHRGI 407
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
660-687 |
9.56e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.72 E-value: 9.56e-06
10 20
....*....|....*....|....*...
gi 127737 660 SMIYRESLNNLMNMLYQTHPHFIRCIIP 687
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1174-1766 |
9.77e-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: 50.88 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1174 LEANKKreaEIAKLRREKEEDSLNHETAISSLRKRHGDSVAelTEQLETLQKLKAKSEAEK-SKLQRDLEESQHATdsev 1252
Cdd:pfam05483 115 IEAQRK---AIQELQFENEKVSLKLEEEIQENKDLIKENNA--TRHLCNLLKETCARSAEKtKKYEYEREETRQVY---- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1253 rsrQDLEKALKTIEVQYSELQTKAdEQSRQLQDFaalknRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNY 1332
Cdd:pfam05483 186 ---MDLNNNIEKMILAFEELRVQA-ENARLEMHF-----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1333 D------EESRERqalaatAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQqwkaRFDSEGLNKLEEIEAAKKAL 1406
Cdd:pfam05483 257 KdltfllEESRDK------ANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ----RSMSTQKALEEDLQIATKTI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1407 -QLKVQELTDTNEGLFAKIASQ------EKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSE 1479
Cdd:pfam05483 327 cQLTEEKEAQMEELNKAKAAHSfvvtefEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1480 LDAAQRDNRQLSTDLFKAKTAnDELAEYLDSTRRENKSLAQ----EVKDLTDQLGEGGRSVAELQKIVR--KLEVEKEEL 1553
Cdd:pfam05483 407 LEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIFLLQarekEIHDLEIQLTAIKTSEEHYLKEVEdlKTELEKEKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1554 QKALDEAEAALEAEEAKvlraqiEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLES 1633
Cdd:pfam05483 486 KNIELTAHCDKLLLENK------ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1634 DINDLEIALDHAnrayadaqktikkymetvqelqfqiEEEQRQkdeIREQFLASEKRNAILQSEKDELAQQAEAAERARR 1713
Cdd:pfam05483 560 KGDEVKCKLDKS-------------------------EENARS---IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 127737 1714 NAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVE 1766
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1435-1923 |
1.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1435 MQDLDDAQSDVEKAAAQVAFYEKHRRQfesiIAEWKKKTDDLSSELDAAQRDNRQLstdlfkaktandELAEYLDSTRRE 1514
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1515 NKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEE 1594
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1595 EFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQF-QIEEE 1673
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAlLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1674 QRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLaahae 1753
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL----- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1754 LEEIANELKNAveqGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENaalkggkkiiAQLEARIR 1833
Cdd:COG4717 369 EQEIAALLAEA---GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE----------EELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1834 AIEQELDGEQRRHQDTEKNWRKAERRVKEVEfqvveekkNEERLTELVDKLQCKlkifKRQVEEAEEVAASnlnkYKVLT 1913
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLE--------EDGELAELLQELEEL----KAELRELAEEWAA----LKLAL 499
|
490
....*....|
gi 127737 1914 AQFEQAEERA 1923
Cdd:COG4717 500 ELLEEAREEY 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
911-1112 |
1.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 911 LADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRdhnIRS 990
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---ARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 991 LQ------------------DEMANQDEAVAKLNkekkhqeESNRKLNEDLQSEEDKvnhLEKIRNKLEQQMDELEENID 1052
Cdd:COG3883 95 LYrsggsvsyldvllgsesfSDFLDRLSALSKIA-------DADADLLEELKADKAE---LEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1053 REKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNS 1112
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1623-1914 |
1.22e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1623 EALRIKKKLESDIndLEIALDHAN--RAYADAQKTIKKYMETVQELQFQIEEE-----QRQKDEIREQFLASEKRNAILQ 1695
Cdd:COG3206 125 KNLTVEPVKGSNV--IEISYTSPDpeLAAAVANALAEAYLEQNLELRREEARKaleflEEQLPELRKELEEAEAALEEFR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1696 SEKDElaqqaeaaerarrnaeaecIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADA 1775
Cdd:COG3206 203 QKNGL-------------------VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1776 ArLAEELRQEQEHSMHIERIR----------KGLELQIKEMQIRLDDAENAALKGGKKIIAQLEARIRAIEQELDGEQRR 1845
Cdd:COG3206 264 V-IQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1846 HQDTEKNWRKAERRVKEVEFqvveekkNEERLTELVDKLQcklkifkrqveEAEEVAASNLNKYKVLTA 1914
Cdd:COG3206 343 LAELPELEAELRRLEREVEV-------ARELYESLLQRLE-----------EARLAEALTVGNVRVIDP 393
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1241-1665 |
1.34e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1241 LEESQHATDSEVRSRQDLEKALKtieVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKST 1320
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALR---LRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1321 LQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLdeeaeskADLTRQISKLnaeiQQWKARFDSEglnKLEEIE 1400
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAL-------SEKERIIERL----KEQREREDRE---RLEELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1401 AAKKALqlkvQELTDTNEGLFAKIASQEkvrfklmQDLDDAQsdvEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSsel 1480
Cdd:pfam10174 472 SLKKEN----KDLKEKVSALQPELTEKE-------SSLIDLK---EHASSLASSGLKKDSKLKSLEIAVEQKKEECS--- 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1481 daaqrdnrQLSTDLFKAKTANDELAEYLDSTRREnKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEK-------EEL 1553
Cdd:pfam10174 535 --------KLENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdkkiAEL 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1554 QKALDEAEAALEAEEAKV-LRAQIEVSQIRSEIEKRIQEKEEEFENTrrnHQRALESMQATLEaETKQKEEAlrIKKKLE 1632
Cdd:pfam10174 606 ESLTLRQMKEQNKKVANIkHGQQEMKKKGAQLLEEARRREDNLADNS---QQLQLEELMGALE-KTRQELDA--TKARLS 679
|
410 420 430
....*....|....*....|....*....|...
gi 127737 1633 SDINDLEIALDHANRAYADAQKTIKKYMETVQE 1665
Cdd:pfam10174 680 STQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1721-1950 |
1.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1721 ELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEhsmHIERIRKGLE 1800
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1801 LQIKEMQiRLDDAENAALKGGKKIIAQLEARIRAIEQELDGEQRRhqdteknWRKAERRVKEVEFQVVEEKKNEERLTEL 1880
Cdd:COG4942 108 ELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ-------AEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1881 VDKLQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAEERADIAENALSKMRNKIRASASMAPPDGFP 1950
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
905-1315 |
1.89e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 905 ETEKANLADAEERNEKLNQLKATLES-----KLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQ------DLELS 973
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKkikddiNLEEC 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 974 LRKAEQEKQSRD-----HNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIR-----NKLEQQ 1043
Cdd:TIGR01612 1405 KSKIESTLDDKDideciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFN 1484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1044 MDELEENIDREKRSRGDIEKAKRKVEgdlkvaqENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNS--IIAKLQRLI 1121
Cdd:TIGR01612 1485 INELKEHIDKSKGCKDEADKNAKAIE-------KNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSeiIIKEIKDAH 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1122 KELTarnaeleeelEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQ--LEANKKREAEIAKLRRE-----KEED 1194
Cdd:TIGR01612 1558 KKFI----------LEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQlsLENFENKFLKISDIKKKindclKETE 1627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1195 SLnhETAISSLR--------KRHGDSVAELTEQLETLQKLKAKSEAEKSKLQR--------DLEESQHATDSEVRSrqdL 1258
Cdd:TIGR01612 1628 SI--EKKISSFSidsqdtelKENGDNLNSLQEFLESLKDQKKNIEDKKKELDEldseiekiEIDVDQHKKNYEIGI---I 1702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 127737 1259 EKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLH 1315
Cdd:TIGR01612 1703 EKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIY 1759
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
859-1351 |
1.96e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 859 QEAmGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADaeeRNEKLNQLKATLESKLSDITGQ 938
Cdd:pfam15921 370 QES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD---RNMEVQRLEALLKAMKSECQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 939 LED----MQERNEDLARQKKKTDQeLSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKE-KKHQE 1013
Cdd:pfam15921 446 MERqmaaIQGKNESLEKVSSLTAQ-LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEiTKLRS 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1014 ESNRKLNE--DLQSEEDKVNHLE--------------KIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQE 1077
Cdd:pfam15921 525 RVDLKLQElqHLKNEGDHLRNVQtecealklqmaekdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1078 NIDE--ITKQKHDVET-TLKRKEEDLHHTNAKLAENNSIIAKLQRLIKEltarnaeleeeLEAERNSRQKSDRSrseaer 1154
Cdd:pfam15921 605 ELQEfkILKDKKDAKIrELEARVSDLELEKVKLVNAGSERLRAVKDIKQ-----------ERDQLLNEVKTSRN------ 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1155 eleelterleqqggataaqlEANKKREaEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLK-AKSEAE 1233
Cdd:pfam15921 668 --------------------ELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgSDGHAM 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1234 KSK--LQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNEnsdlnrsLEEMDNQL 1311
Cdd:pfam15921 727 KVAmgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE-------LEVLRSQE 799
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 127737 1312 NSLHRLKSTLQSQLDETRRNYDE--ESRERQALAATAKNLEH 1351
Cdd:pfam15921 800 RRLKEKVANMEVALDKASLQFAEcqDIIQRQEQESVRLKLQH 841
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
899-1834 |
2.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 899 ALFLSLETEKAN------LADAEERNEKLNQlKATLESKLSDITGQLEDMQERNEDLARQkkktdqelsdtkkhVQDLEL 972
Cdd:PRK04863 257 DLFKHLITESTNyvaadyMRHANERRVHLEE-ALELRRELYTSRRQLAAEQYRLVEMARE--------------LAELNE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 973 SLRKAEQEKQS-RDHnirsLQDEManqdEAVAKLNKEKKHQEEsnrklnedlqseedkvnhLEKIRNKLEQQMDELEEni 1051
Cdd:PRK04863 322 AESDLEQDYQAaSDH----LNLVQ----TALRQQEKIERYQAD------------------LEELEERLEEQNEVVEE-- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1052 drekrSRGDIEKAKRKVEgdlkVAQENIDEITKQKHDVETTLkrkeeDLHHTNAkLAENNSIiaklQRLIKeltarnael 1131
Cdd:PRK04863 374 -----ADEQQEENEARAE----AAEEEVDELKSQLADYQQAL-----DVQQTRA-IQYQQAV----QALER--------- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1132 eeeleaernSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEA-NKKREAEIAKLRrekeedslnHETAISSLRKRHG 1210
Cdd:PRK04863 426 ---------AKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLeQKLSVAQAAHSQ---------FEQAYQLVRKIAG 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1211 D---SVA-----ELTEQLETLQKLKAKSEAEKSKLqRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQ 1282
Cdd:PRK04863 488 EvsrSEAwdvarELLRRLREQRHLAEQLQQLRMRL-SELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1283 LQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKS---TLQSQLDETRRNYDEESRERQALAATAKN-LEHENTiLRE 1358
Cdd:PRK04863 567 LESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlAAQDALARLREQSGEEFEDSQDVTEYMQQlLERERE-LTV 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1359 HLDEEAESKADLTRQISKL-------NAEIQQWKARFDSEGLNKLEE---------IEAAKKALQ--LKVQELTDTNEGL 1420
Cdd:PRK04863 646 ERDELAARKQALDEEIERLsqpggseDPRLNALAERFGGVLLSEIYDdvsledapyFSALYGPARhaIVVPDLSDAAEQL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1421 FAKIASQEKVrfkLM-----QDLDDAQSDVEKAAAQVAFYEKHRR----QFESII----AEWKKKTDDLSSELDAAQRDN 1487
Cdd:PRK04863 726 AGLEDCPEDL---YLiegdpDSFDDSVFSVEELEKAVVVKIADRQwrysRFPEVPlfgrAAREKRIEQLRAEREELAERY 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1488 RQLSTDLFKAKTANDELAEYLDStrreNKSLA------QEVKDLTDQLGEGGRSVAEL----QKIVRKLEVEKEELQkal 1557
Cdd:PRK04863 803 ATLSFDVQKLQRLHQAFSRFIGS----HLAVAfeadpeAELRQLNRRRVELERALADHesqeQQQRSQLEQAKEGLS--- 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1558 deaeaaleaeeakVLRAQIEVSQI--RSEIEKRIQEKEEEFENTR------RNHQRALESMQ-------------ATLEA 1616
Cdd:PRK04863 876 -------------ALNRLLPRLNLlaDETLADRVEEIREQLDEAEeakrfvQQHGNALAQLEpivsvlqsdpeqfEQLKQ 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1617 ETKQKEEALRIKKKLESDINDLEIALDHAnrAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEkrnailqs 1696
Cdd:PRK04863 943 DYQQAQQTQRDAKQQAFALTEVVQRRAHF--SYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQ-------- 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1697 ekdelaqqaeaaerarrnaeaecielrEQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIanelknaveqGQKASADAA 1776
Cdd:PRK04863 1013 ---------------------------AQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL----------GVPADSGAE 1055
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1777 RLAEELRQEQEHSMHIERIRKG-LELQIKEMQIRLDDAENAALKGGKKIIAQLEARIRA 1834
Cdd:PRK04863 1056 ERARARRDELHARLSANRSRRNqLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1124 |
2.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 841 EWFKLFGKVKPM------LKAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSL-ETEKAN--- 910
Cdd:PRK03918 359 ERHELYEEAKAKkeelerLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeELKKAKgkc 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 911 -----LADAEERNEKLNQLKAtlesKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRD 985
Cdd:PRK03918 439 pvcgrELTEEHRKELLEEYTA----ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 986 HNIRSLQDEMANQDEAVAKLNKEKKHQeesnRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDR-EKRSRGDIEKA 1064
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEI----KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEEL 590
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 1065 KRKVEgDLKVAQENIDEITKQKHDVETTLKR---KEEDLHHTNAKLAENNSIIAKLQRLIKEL 1124
Cdd:PRK03918 591 EERLK-ELEPFYNEYLELKDAEKELEREEKElkkLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1538-1701 |
2.21e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1538 ELQKIVRKLEVEKEELQKAldeaeaaleaeeaKVLRAQIEVSQIRSEIEKRIQEKEEEFENtrrnhqralesmqatLEAE 1617
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKE-------------ALLEAKEEIHKLRNEFEKELRERRNELQK---------------LEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1618 TKQKEEALriKKKLEsDINDLEIALDHANRAYADAQKTIKKYMETVQELQfqieEEQRQKDEIREQFLASEKRNAILQSE 1697
Cdd:PRK12704 91 LLQKEENL--DRKLE-LLEKREEELEKKEKELEQKQQELEKKEEELEELI----EEQLQELERISGLTAEEAKEILLEKV 163
|
....
gi 127737 1698 KDEL 1701
Cdd:PRK12704 164 EEEA 167
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1279-1490 |
2.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1279 QSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILRE 1358
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1359 HLDEEAESKADLTRQISKlNAEIQQWKARFDSEGLNKLEE----IEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKL 1434
Cdd:COG4942 98 ELEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDAVRrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 1435 MQDLDDAQsdvekaaAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQL 1490
Cdd:COG4942 177 EALLAELE-------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1503-1927 |
3.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1503 ELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEA-KVLRAQIEVSQI 1581
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1582 RSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYME 1661
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1662 TVQELQFQIEEEQRQKDEIREQFLASEKRNAILQsekdelAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRR 1741
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKE------ARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1742 KLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALkgg 1821
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1822 kkiIAQLEARIRAIEQELDGEQ----RRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKI--FKRQV 1895
Cdd:COG4717 365 ---LEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEEL 441
|
410 420 430
....*....|....*....|....*....|..
gi 127737 1896 EEAEEVAASNLNKYKVLTAQFEQAEERADIAE 1927
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
905-1126 |
3.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 905 ETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNE--DLARQKKKTDQELSdtkkhvqDLELSLRKAEQEKQ 982
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLS-------ELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 983 SRDHNIRSLQDEMANQDEAVAKLNK----EKKHQEESNRKLNEDLQSEEDKVNHLEKIRnkLEQQMDELEENIDREkrsr 1058
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQspviQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQLQQE---- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1059 gdIEKAKRKVEGDLKVAQENIDEITKQKHDVEttlkrkeedlhhtnAKLAENNSIIAKLQRLIKELTA 1126
Cdd:COG3206 311 --AQRILASLEAELEALQAREASLQAQLAQLE--------------ARLAELPELEAELRRLEREVEV 362
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
857-1376 |
4.28e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAVQRGEIA--RSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLE----- 929
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESelREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDEriera 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 930 -SKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHN-IRSLQDEMANQDEAVAKL-N 1006
Cdd:pfam12128 477 rEEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTlLHFLRKEAPDWEQSIGKViS 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1007 KEKKHQEESNRKLNEDLQSEEDKVN----HLEKIR-NKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDE 1081
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGELNLYgvklDLKRIDvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1082 ITKQKHDVETTLKRKEEDL-----HHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAEREL 1156
Cdd:pfam12128 637 ASREETFARTALKNARLDLrrlfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1157 EELTERLEqqgGATAAQLEANKkreAEIAKLR--REKEEDSLNHETAiSSLRKR--HGDSVAELTEQLETLQKLKAKSEA 1232
Cdd:pfam12128 717 QAYWQVVE---GALDAQLALLK---AAIAARRsgAKAELKALETWYK-RDLASLgvDPDVIAKLKREIRTLERKIERIAV 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1233 EKSKLQRDLEESQHATDSEvrsRQDLEKALKTIEVQYSEL--QTKADEQSRQLQDFAALKNRLNNENS--DLNRSLEEMD 1308
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQR---RPRLATQLSNIERAISELqqQLARLIADTKLRRAKLEMERKASEKQqvRLSENLRGLR 866
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1309 NQLNSLHRLK-----STLQSQLDETRRNYDEESRERQALAATA-KNLEHENTILREH----LDEEAESKADLTRQISK 1376
Cdd:pfam12128 867 CEMSKLATLKedansEQAQGSIGERLAQLEDLKLKRDYLSESVkKYVEHFKNVIADHsgsgLAETWESLREEDHYQND 944
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
992-1413 |
6.49e-05 |
|
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: 48.41 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 992 QDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDkvnHLEKIRNKLEQQmdeleENIDRekrSRGDIEKAkrkvEGD 1071
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASD---HLNLVQTALRQQ-----EKIER---YQEDLEEL----TER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1072 LKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAEnnsiiakLQRLIKEltarnaeleeeleaernsrqksdrsrse 1151
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD-------YQQALDV---------------------------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1152 aereleelterleQQGGATAAQLEANKKREAeiaklRREKEEDSLnhetAISSLRKRHGDSVAELTEQLETLQKLKAK-- 1229
Cdd:COG3096 408 -------------QQTRAIQYQQAVQALEKA-----RALCGLPDL----TPENAEDYLAAFRAKEQQATEEVLELEQKls 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1230 -SEAEKSKLQRDLEESQHATDSEVRS------RQDLEKA---------LKTIEVQYSELQTKADEQS---RQLQDFAALK 1290
Cdd:COG3096 466 vADAARRQFEKAYELVCKIAGEVERSqawqtaRELLRRYrsqqalaqrLQQLRAQLAELEQRLRQQQnaeRLLEEFCQRI 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1291 NRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKN-------LEHentiLREHLDEE 1363
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqdaLER----LREQSGEA 621
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 127737 1364 AESKADLTRQISK-LNAEIQQWKARfdseglnklEEIEAAKKALQLKVQEL 1413
Cdd:COG3096 622 LADSQEVTAAMQQlLEREREATVER---------DELAARKQALESQIERL 663
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1468-1862 |
6.75e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1468 EWKKKTDDLSSE--------LDAAQRDNRQLStdLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDqlgeggrSVAEL 1539
Cdd:pfam06160 49 EWRKKWDDIVTKslpdieelLFEAEELNDKYR--FKKAKKALDEIEELLDDIEEDIKQILEELDELLE-------SEEKN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1540 QKIVRKLEVEKEELQKaldeaeaaleaeeaKVLRAQIEVSQIRSEIEKRIQEKEEEFEntrrnhqralesmQATLEAETK 1619
Cdd:pfam06160 120 REEVEELKDKYRELRK--------------TLLANRFSYGPAIDELEKQLAEIEEEFS-------------QFEELTESG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1620 QKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKkymETVQELQFQIEEEQRQKDEIREQFLASEkrnaiLQSEKD 1699
Cdd:pfam06160 173 DYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELP---DQLEELKEGYREMEEEGYALEHLNVDKE-----IQQLEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1700 ELAQQAEAAERARRNaeaeciELREQNNDLNAHVSALTGQrrkLEGELLA---AHAELEEIANELKNAVEQGQKASADAA 1776
Cdd:pfam06160 245 QLEENLALLENLELD------EAEEALEEIEERIDQLYDL---LEKEVDAkkyVEKNLPEIEDYLEHAEEQNKELKEELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1777 RLAEELR-QEQEhsmhIERIRkGLELQIKEMQIRLDDAENaALKGGKKIIAQLEARIRAIEQELDG---EQRRHQDTEKN 1852
Cdd:pfam06160 316 RVQQSYTlNENE----LERVR-GLEKQLEELEKRYDEIVE-RLEEKEVAYSELQEELEEILEQLEEieeEQEEFKESLQS 389
|
410
....*....|
gi 127737 1853 WRKAERRVKE 1862
Cdd:pfam06160 390 LRKDELEARE 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
884-1086 |
7.00e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 884 SQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSdt 963
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 964 kkhvqDLELSLrkaeqekQSRD-----HNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRN 1038
Cdd:COG3883 104 -----YLDVLL-------GSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 127737 1039 KLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQK 1086
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1321-1701 |
8.91e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1321 LQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEaesKADLTRQISKLNAEIQQWKarfdseglNKLEEIE 1400
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ---RRELESRVAELKEELRQSR--------EKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1401 AAKKALQLKVQELTDTNEGLfakIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDD---LS 1477
Cdd:pfam07888 101 EKYKELSASSEELSEEKDAL---LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1478 SELDAAQRDNRQLSTDLFKAKTAndeLAEYLDSTRRenksLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKal 1557
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNS---LAQRDTQVLQ----LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNA-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1558 deaeaaleaeeakvlrAQIEVSQIRSEIEKRIQEKEEEFENTrrnHQRALESMQATL---EAETKQKEEALRIKKKLESD 1634
Cdd:pfam07888 249 ----------------SERKVEGLGEELSSMAAQRDRTQAEL---HQARLQAAQLTLqlaDASLALREGRARWAQERETL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1635 INDLEIALDHANRAYADAQKTIKKYMETVQELQ--------------FQIEEEQRQKDEIREQFLASEKRNAILQSEKDE 1700
Cdd:pfam07888 310 QQSAEADKDRIEKLSAELQRLEERLQEERMEREklevelgrekdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
.
gi 127737 1701 L 1701
Cdd:pfam07888 390 L 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
973-1193 |
1.15e-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: 46.68 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 973 SLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENID 1052
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1053 REKRSRGD----IEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARN 1128
Cdd:COG4942 101 AQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 1129 AELEEeleaernsRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKR-EAEIAKLRREKEE 1193
Cdd:COG4942 181 AELEE--------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1539-1929 |
1.23e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1539 LQKIVRKLEVEKEELQKALDEAEAALEaeeakvLRAQIEVSQIRseiekriqekeeefentrrnhqralesmqatleaet 1618
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAAIER------LRKNLTVEPVK------------------------------------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1619 kqkeealrikkklESDIndLEIALDHAN--RAYADAQKTIKKYMETVQELQFQIEEE-----QRQKDEIREQFLASEKRN 1691
Cdd:COG3206 134 -------------GSNV--IEISYTSPDpeLAAAVANALAEAYLEQNLELRREEARKaleflEEQLPELRKELEEAEAAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1692 AILQSEKDElaqqaeaaerarrnaeaecIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKA 1771
Cdd:COG3206 199 EEFRQKNGL-------------------VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1772 SADAArLAEELRQEQEhsmhierirkgLELQIKEMQIRLDDAENAalkggkkiIAQLEARIRAIEQELDGE-QRRHQDTE 1850
Cdd:COG3206 260 LQSPV-IQQLRAQLAE-----------LEAELAELSARYTPNHPD--------VIALRAQIAALRAQLQQEaQRILASLE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1851 KNWRKAERRVKEVEFQVVEEKKneeRLTELVDKLQcKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAEERADIAENA 1929
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEA---RLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
895-1252 |
1.55e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 895 EEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSL 974
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 975 RKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDRE 1054
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1055 KRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEE 1134
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1135 LEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVA 1214
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*...
gi 127737 1215 ELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEV 1252
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
940-1055 |
1.75e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 46.00 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 940 EDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLR-KAEQEK--QSRDHNiRSLQDEMAN-QDEAVAKLNKEKKHQEES 1015
Cdd:pfam03148 254 EETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRdKEAPLKlaQTRLEN-RTYRPNVELcRDEAQYGLVDEVKELEET 332
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 127737 1016 NRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEE--NIDREK 1055
Cdd:pfam03148 333 IEALKQKLAEAEASLQALERTRLRLEEDIAVKANslFIDREK 374
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1321-1582 |
2.23e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1321 LQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARfdseglnkLEEIE 1400
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE--------IAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1401 AAKKALQLKVQELTDTNEglfaKIASQEKVRFKLmqdlddAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSEL 1480
Cdd:COG4942 97 AELEAQKEELAELLRALY----RLGRQPPLALLL------SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1481 DAAQrdnrqlstdlfkakTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEA 1560
Cdd:COG4942 167 AELE--------------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250 260
....*....|....*....|..
gi 127737 1561 EAALEAEEAKVLRAQIEVSQIR 1582
Cdd:COG4942 233 EAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
731-1086 |
2.50e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 731 KHRYAILAADAAKESDPKKASVGILDKISVDGNLTDEEFKVGETKIFFKAGVLAKLEDLRDEILSRIvTMFQSRIRSYLA 810
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL-KQKIDEEEEEEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 811 KAEVRRRYEQQTGLLVVQRNVRAWCTLRTWEWFKLFGKVKPMLKAGKEQEAMgelAVKIQKLEEAVQRGEIARSQLESQV 890
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA---LEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 891 ADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERN-----EDLARQKKKTDQELSDTKK 965
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDeleskEEKEKEEKKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 966 HVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVN--------HLEKIR 1037
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNlmaieefeEKEERY 990
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 127737 1038 NKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQK 1086
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY 1039
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1599-1938 |
2.63e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1599 TRRNHQRALESM-QATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIkkyMETVQELQ-FQIEEEQRQ 1676
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA---MERERELErIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1677 KDEIREQFLASEKRNaILQSEKDELAQQAEAAERARRNAEAECIELREQNndlnahvsaltgQRRKLEGELLaahaELEE 1756
Cdd:pfam17380 362 LERIRQEEIAMEISR-MRELERLQMERQQKNERVRQELEAARKVKILEEE------------RQRKIQQQKV----EMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1757 IANELKNAveqgqkasadaaRLAEELRQEQEHSMHIERIRkgLELQIKEMQIrlddaenaalkggkKIIAQLEARIRAIE 1836
Cdd:pfam17380 425 IRAEQEEA------------RQREVRRLEEERAREMERVR--LEEQERQQQV--------------ERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1837 QELDGEQRRHQDTEKNWRKA-ERRVKEVEFQVVEEKKNEERL-TELVDKLQCKLKIFKRQVEEAEEVAASNLNKYKVLTA 1914
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLeKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
330 340
....*....|....*....|....*
gi 127737 1915 QFEQA-EERADIaeNALSKMRNKIR 1938
Cdd:pfam17380 557 QMRKAtEERSRL--EAMEREREMMR 579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1752-1944 |
3.42e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1752 AELEEIANELKNAVEQGQKASADAARLAEEL----RQEQEHSMHIERIRKGLElQIKEMQIRLDDAENAALKggKKI--- 1824
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELekltEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVK--EKIgel 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1825 ---IAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEV 1901
Cdd:TIGR02169 300 eaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 127737 1902 AASNLNKYKVLTAQFEQA-EERADIAENALSKMRNKIRASASMA 1944
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLkREINELKRELDRLQEELQRLSEELA 423
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
854-1053 |
4.52e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 854 KAGKEQEaMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLAD-AEERNEKLNQLKaTLESKL 932
Cdd:pfam15921 592 KAQLEKE-INDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDiKQERDQLLNEVK-TSRNEL 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 933 SDIT-----------GQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKA-------EQEKQSRDHNIRSLQDE 994
Cdd:pfam15921 670 NSLSedyevlkrnfrNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAmkvamgmQKQITAKRGQIDALQSK 749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127737 995 MANQDEAVAKLNKEKKHQEESNRKLNEDLQ---SEEDKV-NHLEKIRN---KLEQQMDELEENIDR 1053
Cdd:pfam15921 750 IQFLEEAMTNANKEKHFLKEEKNKLSQELStvaTEKNKMaGELEVLRSqerRLKEKVANMEVALDK 815
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1212-1406 |
5.02e-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: 43.76 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1212 SVAELTEQLETLQKL---KAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDfaa 1288
Cdd:COG1579 1 AMPEDLRALLDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1289 LKNRLNNENSdlNRSLEEMDNQLNSLHRLKSTLQsqlDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKA 1368
Cdd:COG1579 78 YEEQLGNVRN--NKEYEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 127737 1369 DLTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKKAL 1406
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPELLALYERIRKRKNGL 190
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
854-1123 |
5.03e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 854 KAGKEQEA---MGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLES 930
Cdd:PLN02939 119 SKDGEQLSdfqLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 931 klsdITGQLEDMqeRNEDLARqkkktdQELSDTKKHVQDLELSLRKAEQEKQSRDHN-IRSLQDEMANQDEAVAKLNKEK 1009
Cdd:PLN02939 199 ----LEEQLEKL--RNELLIR------GATEGLCVHSLSKELDVLKEENMLLKDDIQfLKAELIEVAETEERVFKLEKER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1010 KHQEESNRKLNEDL-QSEED--------------KVNHLEKIRNKLEQQMDELEENIDREKrsrgDIEKAKRKVEGDLKV 1074
Cdd:PLN02939 267 SLLDASLRELESKFiVAQEDvsklsplqydcwweKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLKE 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 127737 1075 AqeNIDEITKQKHDV-ETTLKRKEEDLHHTNaklAENNSIIAKLQRLIKE 1123
Cdd:PLN02939 343 A--NVSKFSSYKVELlQQKLKLLEERLQASD---HEIHSYIQLYQESIKE 387
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1304-1462 |
5.59e-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: 43.76 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1304 LEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISK------- 1376
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1377 --LNAEIQQWKAR---FDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQ 1451
Cdd:COG1579 92 eaLQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
170
....*....|....*.
gi 127737 1452 V-----AFYEKHRRQF 1462
Cdd:COG1579 172 IppellALYERIRKRK 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1725-1966 |
5.61e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1725 QNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEhsmhierirkglelQIK 1804
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--------------EIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1805 EMQIRLDDAENAALKGGKKI-----------IAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKN 1873
Cdd:COG3883 83 ERREELGERARALYRSGGSVsyldvllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1874 EERLTELVDKLQcklkifkRQVEEAEEVAASNLNKYKVLTAQFEQAEERADIAENALSKMRNKIRASASMAPPDGFPMVP 1953
Cdd:COG3883 163 KAELEAAKAELE-------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
250
....*....|...
gi 127737 1954 SASSALIRSSSNA 1966
Cdd:COG3883 236 AAAAAAAAASAAG 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1595-1935 |
5.61e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1595 EFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDindLEIALDHANR---AYAdAQKTIKKYMETVQELQFQIE 1671
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQD---YQAASDHLNLvqtALR-QQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1672 EEQRQKDEIREQFLASEKRNAILQSEKDELAQqaeaaerarrnaeaeciELREQNNDLNA-HVSALTGQ---RRKLEGEL 1747
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS-----------------QLADYQQALDVqQTRAIQYQqavQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1748 LAAHAELeeianELKNAVEQGQKASADAARLAEELRQEQEH----SMHIERIRKGLELQIKemqIRLDDAENAALKGGKK 1823
Cdd:COG3096 428 LCGLPDL-----TPENAEDYLAAFRAKEQQATEEVLELEQKlsvaDAARRQFEKAYELVCK---IAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1824 IIAQ------LEARIRAIEQEL-DGEQRRHQDteknwRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVE 1896
Cdd:COG3096 500 LLRRyrsqqaLAQRLQQLRAQLaELEQRLRQQ-----QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 127737 1897 EAEEVAASNLNKYKVLTAQFEQAEERADI---AENALSKMRN 1935
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDALERLRE 616
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
857-1078 |
6.94e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 857 KEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKanlaDAEERNEKLNQLKATLESKLSDIT 936
Cdd:COG5185 319 AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV----ELSKSSEELDSFKDTIESTKESLD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 937 GQLEDMQERNEDLARQKKKTDQEL-SDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEM-ANQDEAVAKLNKEKKHQE- 1013
Cdd:COG5185 395 EIPQNQRGYAQEILATLEDTLKAAdRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDEINr 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1014 ---ESNRKLNEDLQSEEDKVN----HLEKIRNKLEQQ-------MDELEENIDREKRSRGDIEKAKRKVEGDLKVAQEN 1078
Cdd:COG5185 475 svrSKKEDLNEELTQIESRVStlkaTLEKLRAKLERQlegvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQA 553
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
881-995 |
9.73e-04 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 43.82 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 881 IARSQLESQVADLVEEKNALFLSLETEKANLADAEE-RNE---------KLNQLKATLESKLSDITGQLEDMQERNEDLA 950
Cdd:PRK10361 22 FASYQHAQQKAEQLAEREEMVAELSAAKQQITQSEHwRAEcellnnevrSLQSINTSLEADLREVTTRMEAAQQHADDKI 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 127737 951 RQKKKTDQELSDTKKHVQD--LELSLRKA-EQEKQSRDHNIRSLQDEM 995
Cdd:PRK10361 102 RQMINSEQRLSEQFENLANriFEHSNRRVdEQNRQSLNSLLSPLREQL 149
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
932-1090 |
1.01e-03 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 42.29 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 932 LSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHnirsLQDEManqDEAVAKLNKEKKH 1011
Cdd:pfam16043 9 LDQLQALILDLQEELEKLSETTSELSERLQQRQKHLEALYQQIEKLEKVKADKEV----VEEEL---DEKADKEALASKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1012 Q----EESNRKLNEDLQSEEDKV-NHLEKIRNKLEQQMDELEENIDREkrsrgDIEKAKRKVEGDLKVAQENIDEITKQK 1086
Cdd:pfam16043 82 SrdqfDETLEELNQMLQELLDKLeGQEDAWKKALETLSEELDTKLDRL-----ELDPLKELLERRIKALQKLLQEGSEEL 156
|
....
gi 127737 1087 HDVE 1090
Cdd:pfam16043 157 DEAE 160
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1172-1482 |
1.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1172 AQLEANKKREAEIA--KLRREKEEDSL-------NHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEK----SKL- 1237
Cdd:PRK11281 43 AQLDALNKQKLLEAedKLVQQDLEQTLalldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETretlSTLs 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1238 QRDLEESQHATDSEVrsrQDLEKALKTIEVQYSELQTKAD-------EQSRQLQDFAALKNRLNNENSDLNRSLEE---- 1306
Cdd:PRK11281 123 LRQLESRLAQTLDQL---QNAQNDLAEYNSQLVSLQTQPEraqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVllqa 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1307 ---MDNQLNSLHR--------LKSTLQSQLDETRRNYDEESRERQAL--AATAKNLE------------------HENTI 1355
Cdd:PRK11281 200 eqaLLNAQNDLQRkslegntqLQDLLQKQRDYLTARIQRLEHQLQLLqeAINSKRLTlsektvqeaqsqdeaariQANPL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1356 LREHLDEEAESKADLTRQISKLNAEIQQ---WKARFDSegLNK----LEE-IEAAKKALQL------KVQEL--TDTNEG 1419
Cdd:PRK11281 280 VAQELEINLQLSQRLLKATEKLNTLTQQnlrVKNWLDR--LTQsernIKEqISVLKGSLLLsrilyqQQQALpsADLIEG 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127737 1420 LFAKIASQEKVRFKLMQ---DLDDAQSDVEK--AAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDA 1482
Cdd:PRK11281 358 LADRIADLRLEQFEINQqrdALFQPDAYIDKleAGHKSEVTDEVRDALLQLLDERRELLDQLNKQLNN 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
854-1017 |
1.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 854 KAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNA--LFLSLETEKANLADAEERNEKLNQLKATLESK 931
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 932 LSDITGQLEDMQERNEDLARQKKKTD----QELSDTKKHVQDLELSLRKAEQEkqsrdhnIRSLQDEMANQDEAVAKLNK 1007
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEE-------LEEAQEELEELEEELEQLEN 234
|
170
....*....|
gi 127737 1008 EKKHQEESNR 1017
Cdd:COG4717 235 ELEAAALEER 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
867-1046 |
1.26e-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: 42.60 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 867 VKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLedMQERN 946
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL--GNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 947 EDlarqkkktdqELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSE 1026
Cdd:COG1579 88 NK----------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|
gi 127737 1027 EDKvnhLEKIRNKLEQQMDE 1046
Cdd:COG1579 158 LEE---LEAEREELAAKIPP 174
|
|
| CCDC90-like |
pfam07798 |
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ... |
1254-1372 |
1.33e-03 |
|
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.
Pssm-ID: 462268 [Multi-domain] Cd Length: 175 Bit Score: 41.73 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1254 SRQDLEKALKTIEVQYSELqtKADEQSRQLQDFAALKnrlnNENSDLNRSLEEMDNQLNS-LHRLKSTLQSQLDETR-RN 1331
Cdd:pfam07798 44 TKEDLENETYLQKADLAEL--RSELQILEKSEFAALR----SENEKLRRELEKLKQRLREeITKLKADVRLDLNLEKgRI 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 127737 1332 YDEESRERQALAATAKNLEHENTILREHLDeeaESKADLTR 1372
Cdd:pfam07798 118 REELKAQELKIQETNNKIDTEIANLRTQIE---SVKWDVIR 155
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
921-1126 |
1.35e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 921 LNQLKATLESKLSDITGQLeDMQERNEDlaRQKKKTDQELSDTKKHVQDLelsLRKAEQEKQSrdhnIRSLQDEMANqde 1000
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQI-KTYNKNIE--EQRKKNGENIARKQNKYDEL---VEEAKTIKAE----IEELTDELLN--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1001 avakLNKEKKHQEESNRKLNE---DLQSEEDKVNHLEKIRNK----------LEQQMDELEENIDREKRSRGDIEKAKRK 1067
Cdd:PHA02562 246 ----LVMDIEDPSAALNKLNTaaaKIKSKIEQFQKVIKMYEKggvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 127737 1068 VEgDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKlaennsiIAKLQRLIKELTA 1126
Cdd:PHA02562 322 ID-ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK-------AKKVKAAIEELQA 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1763-1939 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1763 NAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAalkggkKIIAQLEARIRAIEQELDGE 1842
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1843 QRRhqdteknWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKykvLTAQFEQAEER 1922
Cdd:COG4717 145 PER-------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEE 214
|
170
....*....|....*..
gi 127737 1923 ADIAENALSKMRNKIRA 1939
Cdd:COG4717 215 LEEAQEELEELEEELEQ 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1259-1501 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1259 EKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRe 1338
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1339 rqALAATAKNLEHENTILrehldeEAESKADLTRQISKLNAEIQQwkarfdseGLNKLEEIEAAKKALQLKVQELTDTNE 1418
Cdd:COG3883 94 --ALYRSGGSVSYLDVLL------GSESFSDFLDRLSALSKIADA--------DADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1419 GLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAK 1498
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
...
gi 127737 1499 TAN 1501
Cdd:COG3883 238 AAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1632-1944 |
1.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1632 ESDINDLEIALDHANRAYADAQ-KTIKKYMETVQELQFQIEEEQRQKDEIREQF-LASEKRNAIL-----QSEKDELAQQ 1704
Cdd:PTZ00121 1044 EKDIIDEDIDGNHEGKAEAKAHvGQDEGLKPSYKDFDFDAKEDNRADEATEEAFgKAEEAKKTETgkaeeARKAEEAKKK 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1705 AEAAERARRNAEAECI----ELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIAN---ELKNAvEQGQKAS----A 1773
Cdd:PTZ00121 1124 AEDARKAEEARKAEDArkaeEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARkaeEVRKA-EELRKAEdarkA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1774 DAARLAEELRQEQE-----HSMHIERIRKGLELQIKEMQ------IRLDDAENAALKGGKKIIAQLEARIRAIEQELDGE 1842
Cdd:PTZ00121 1203 EAARKAEEERKAEEarkaeDAKKAEAVKKAEEAKKDAEEakkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1843 QRRHQDTEK--NWRKAERRVKEVEFQV-VEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQA 1919
Cdd:PTZ00121 1283 LKKAEEKKKadEAKKAEEKKKADEAKKkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
330 340
....*....|....*....|....*
gi 127737 1920 EERADIAENALSKMRNKIRASASMA 1944
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKA 1387
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1211-1504 |
1.66e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.13 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1211 DSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALK 1290
Cdd:pfam19220 27 ADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1291 NRLNNENSDLNRSLEEMDNQLN-------SLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEE 1363
Cdd:pfam19220 107 EELRIELRDKTAQAEALERQLAaeteqnrALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1364 AESKADLTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKKAlqlkVQELTDTNEGLFAKIASqekvrfkLMQDLDDAQS 1443
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERA----EAQLEEAVEAHRAERAS-------LRMKLEALTA 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127737 1444 DVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDEL 1504
Cdd:pfam19220 256 RAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEM 316
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1300-1555 |
2.00e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1300 LNRSL-EEMDNQLNSLHRLKSTLQSQLDeTRRNYDEESRerqalAATAKNLEHENTILREHLDEEAESKAD---LTRQIS 1375
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIK-TYNKNIEEQR-----KKNGENIARKQNKYDELVEEAKTIKAEieeLTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1376 KLNAEIQQWkarfdSEGLNKLEEiEAAKKALQLKvqeltdtnegLFAKIASQEK---VRFKLMQDLDDAQSDVEKAAAQV 1452
Cdd:PHA02562 245 NLVMDIEDP-----SAALNKLNT-AAAKIKSKIE----------QFQKVIKMYEkggVCPTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1453 AFYEKHRRQFESIIAEWKKKTDdlssELDAAQRDNRQLSTDLFKAKTAndelaeyLDSTRRENKSLAQEVKDLTDQLGEG 1532
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMD----EFNEQSKKLLELKNKISTNKQS-------LITLVDKAKKVKAAIEELQAEFVDN 377
|
250 260
....*....|....*....|...
gi 127737 1533 GRSVAELQKIVRKLEVEKEELQK 1555
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVK 400
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
859-1085 |
2.03e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 859 QEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQ 938
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 939 LEDMQERnedlARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIrSLQDEMANQDEAVAKLNKEKKHQEESNRK 1018
Cdd:COG1340 87 LNELREE----LDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSP-EEEKELVEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1019 LNEDLQSEEDKVNHLEKIRNKLE---QQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQ 1085
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKelaEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1601-1797 |
2.21e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1601 RNHQRALESMQATL----EAETKQKEEALRIKKkLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQ 1676
Cdd:COG1579 3 PEDLRALLDLQELDseldRLEHRLKELPAELAE-LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1677 KDEIR--EQFLASEKRNAILQSEKDELAQQAeaaerarrnaeaecIELREQNNDLNAHVSALTGQRRKLEGELLAAHAEL 1754
Cdd:COG1579 82 LGNVRnnKEYEALQKEIESLKRRISDLEDEI--------------LELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 127737 1755 EEIANELKNAVEQGQKASAD-AARLAEELRQEqehsmhIERIRK 1797
Cdd:COG1579 148 DEELAELEAELEELEAEREElAAKIPPELLAL------YERIRK 185
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1741-1937 |
2.40e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1741 RKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAaLKG 1820
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERG-RKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1821 GKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVK--EVEFQVVEEK--KNEERLTELVDKLQC---KLKIFKR 1893
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVvvEGDLERAEERaeLAESKIVELEEELKVvgnNLKSLEA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 127737 1894 QVEEAEEVAASNLNKYKVLTAQFEQAEERADIAENALSKMRNKI 1937
Cdd:pfam00261 163 SEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEV 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
866-1118 |
2.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 866 AVKIQKLEEAVQRGEIARSQLESQVADLVEEknalflsLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQER 945
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREE-------LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 946 NEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQS 1025
Cdd:COG4372 96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1026 EEDkvnhlEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNA 1105
Cdd:COG4372 176 LSE-----AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250
....*....|...
gi 127737 1106 KLAENNSIIAKLQ 1118
Cdd:COG4372 251 LLEEVILKEIEEL 263
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1219-1494 |
3.18e-03 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 41.88 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1219 QLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEV----QYSELqTKADEQSRQL-----QDFAAL 1289
Cdd:pfam09311 10 QLQAIQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEDKMNQLSEetsnQVSTL-AKRNQKSETLldelqQAFSQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1290 KNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQldeTRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKAD 1369
Cdd:pfam09311 89 KRNFQDQLAVLMDSREQVSDELVRLQKDNESLQGK---HSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1370 LTRQ----ISKLNAEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQdLDDAQSDV 1445
Cdd:pfam09311 166 MEEKlkaeILFLKEQIQAEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQ-LEDLQTTK 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 127737 1446 EKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAA---QRDNRQLSTDL 1494
Cdd:pfam09311 245 GSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELDVSeqvQRDFVKLSQTL 296
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1447-1789 |
3.61e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1447 KAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLT 1526
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1527 DQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRA 1606
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1607 LESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLA 1686
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1687 SEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVE 1766
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340
....*....|....*....|...
gi 127737 1767 QGQKASADAARLAEELRQEQEHS 1789
Cdd:COG4372 341 DLLQLLLVGLLDNDVLELLSKGA 363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1166-1405 |
3.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1166 QGGATAAQLEANKKREAEIaklrrEKEEDSLNHEtaISSLRKRhgdsVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQ 1245
Cdd:COG3883 17 QIQAKQKELSELQAELEAA-----QAELDALQAE--LEELNEE----YNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1246 HATDSEVRSRQDLEKALKTIEV------------QYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNS 1313
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1314 LHRLKSTLQSQLDEtrrnydeesreRQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGL 1393
Cdd:COG3883 166 LEAAKAELEAQQAE-----------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250
....*....|..
gi 127737 1394 NKLEEIEAAKKA 1405
Cdd:COG3883 235 AAAAAAAAAASA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
891-1411 |
3.94e-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: 42.04 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 891 ADLVEEKNALfLSLETEKANLADAEERNeklnqlKATLESKLSDITGQLEDMQERNEDL--------------------- 949
Cdd:pfam05557 2 AELIESKARL-SQLQNEKKQMELEHKRA------RIELEKKASALKRQLDRESDRNQELqkrirllekreaeaeealreq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 950 ---ARQKKKTDQELSdtkKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSE 1026
Cdd:pfam05557 75 aelNRLKKKYLEALN---KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1027 EDKVNHLEKIRNKL---EQQMDELE-------------ENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEI---TKQKH 1087
Cdd:pfam05557 152 EQLRQNLEKQQSSLaeaEQRIKELEfeiqsqeqdseivKNSKSELARIPELEKELERLREHNKHLNENIENKlllKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1088 DVETTLKRkEEDLHHTNAKLA-ENNSIIAKLQRLIK-----ELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTE 1161
Cdd:pfam05557 232 DLKRKLER-EEKYREEAATLElEKEKLEQELQSWVKlaqdtGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1162 RLEQQGGATAAQ-----LEANKKREAEIAKLRR-EKEEDSLNHEtaISSLRKRHGDSVAELTEQLETLQKLKAKSEAEks 1235
Cdd:pfam05557 311 KARRELEQELAQylkkiEDLNKKLKRHKALVRRlQRRVLLLTKE--RDGYRAILESYDKELTMSNYSPQLLERIEEAE-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1236 klqrDLEESQHATDSEVRSRqdLEKALKTIEVQysELQTKADEQSRQLQdfaalknRLNNENSDLNRSLEEMDnqlnSLH 1315
Cdd:pfam05557 387 ----DMTQKMQAHNEEMEAQ--LSVAEEELGGY--KQQAQTLERELQAL-------RQQESLADPSYSKEEVD----SLR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1316 RLKSTLQSQLDETRRNYDE-ESR-ERQALAATAKNLEHENTILREHLDEEA-ESKADltrQISKLNAEIQQWKARF---- 1388
Cdd:pfam05557 448 RKLETLELERQRLREQKNElEMElERRCLQGDYDPKKTKVLHLSMNPAAEAyQQRKN---QLEKLQAEIERLKRLLkkle 524
|
570 580
....*....|....*....|....*..
gi 127737 1389 -DSEGLNKLEE---IEAAKKALQLKVQ 1411
Cdd:pfam05557 525 dDLEQVLRLPEttsTMNFKEVLDLRKE 551
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
902-1085 |
3.95e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 902 LSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEK 981
Cdd:cd22656 97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 982 QSRDhnIRSLQDEMAN-QDEAVAKLNKEKKhqeesnrKLNEDLQSEEDKVNHLEKIR---NKLEQQMDELEENIDREKRS 1057
Cdd:cd22656 177 ARKE--IKDLQKELEKlNEEYAAKLKAKID-------ELKALIADDEAKLAAALRLIadlTAADTDLDNLLALIGPAIPA 247
|
170 180
....*....|....*....|....*...
gi 127737 1058 RGDIEKAKRKVEGDLKVAQENIDEITKQ 1085
Cdd:cd22656 248 LEKLQGAWQAIATDLDSLKDLLEDDISK 275
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1249-1398 |
4.55e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1249 DSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQdfaALKNRLNNENSDLNRSLEEMDNQLnslhrlkSTLQSQLDET 1328
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLE---EQVERLEAEVEELEAELEEKDERI-------ERLERELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1329 RRNYDEESRERQALaataKNLEHENTILREHLDEEAESKADLTRQISKLNA----EIQQWK------ARFDSEGLNKLEE 1398
Cdd:COG2433 454 RSEERREIRKDREI----SRLDREIERLERELEEERERIEELKRKLERLKElwklEHSGELvpvkvvEKFTKEAIRRLEE 529
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1211-1939 |
5.44e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1211 DSVAELTEQLETLQKLKAKSEAEKS-KLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAAL 1289
Cdd:TIGR00606 160 DSNWPLSEGKALKQKFDEIFSATRYiKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1290 KNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQS----QLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAE 1365
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAlksrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1366 SKADLTRQISKLNAEIQ---QWKARFDSEGLN---KLEEIEAAKKALQLKVQELTDTNE------GLFA----------K 1423
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRllnQEKTELLVEQGRlqlQADRHQEHIRARDSLIQSLATRLEldgferGPFSerqiknfhtlV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1424 IASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDE 1503
Cdd:TIGR00606 400 IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1504 LAEYLDSTRRENKSLAQEVKDLTDQLGEGGRsvAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQiEVSQIRS 1583
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQNEK--ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKS 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1584 EIEKRIQEKEEEFENTRRnhqraLESMQATLEAETKQKEEALRikkKLESDINDLEIALDHANRAYADAQKTIKKYMETV 1663
Cdd:TIGR00606 557 RHSDELTSLLGYFPNKKQ-----LEDWLHSKSKEINQTRDRLA---KLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1664 QELqFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKL 1743
Cdd:TIGR00606 629 FDV-CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLA 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1744 EGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAeNAALKGGKK 1823
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI-MPEEESAKV 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1824 IIAQLEARIRAIEQELDGEQR-RHQDTEKNWRKAERRVKEVEfQVVEEKknEERLTELVDKLQCKLKIFKRQVEEAEEVa 1902
Cdd:TIGR00606 787 CLTDVTIMERFQMELKDVERKiAQQAAKLQGSDLDRTVQQVN-QEKQEK--QHELDTVVSKIELNRKLIQDQQEQIQHL- 862
|
730 740 750
....*....|....*....|....*....|....*..
gi 127737 1903 ASNLNKYKVLTAQFEQAEERADIAENALSKMRNKIRA 1939
Cdd:TIGR00606 863 KSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1438-1670 |
5.72e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1438 LDDAQSDVEKAAAQVAFYEKhrrqfesiiaewKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKS 1517
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1518 LAQEVKDLTDQlgeggRSVAELQKIVRKLEVEKEELQKALDEAEAaleaeeaKVLRAQIEVSQIRSEIEKRIQEKEEEFE 1597
Cdd:COG3206 252 GPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHP-------DVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127737 1598 NTRRNHQRALESMQATLEaetKQKEEALRIKKKlESDINDLEIALDHANRAYADAQktiKKYMETVQELQFQI 1670
Cdd:COG3206 320 AELEALQAREASLQAQLA---QLEARLAELPEL-EAELRRLEREVEVARELYESLL---QRLEEARLAEALTV 385
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1195-1551 |
5.85e-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: 41.58 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1195 SLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESqhatdseVRSRQDLEKALKTIEVQYSELQT 1274
Cdd:pfam05911 501 SGHPSTDASCDYITCKENSSVVEKEGSVSGDDKSSEETSKQSIQQDLSKA-------ISKIIDFVEGLSKEALDDQDTSS 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1275 KADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQ---SQLDETRRNYD-EESRERQALAATAKNLE 1350
Cdd:pfam05911 574 DSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSLLdvsSMEDEIKKHDCiDKVTLSENKVAQVDNGC 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1351 HEntILREHLDEEAESKADLTRQISKLNAEIQQWKarfdsegLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIasQEKv 1430
Cdd:pfam05911 654 SE--IDNLSSDPEIPSDGPLVSGSNDLKTEENKRL-------KEEFEQLKSEKENLEVELASCTENLESTKSQL--QES- 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1431 rfklmqdlddaqsdvekaaaqvafyekhrrqfESIIAEwkkktddLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDS 1510
Cdd:pfam05911 722 --------------------------------EQLIAE-------LRSELASLKESNSLAETQLKCMAESYEDLETRLTE 762
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 127737 1511 TRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKE 1551
Cdd:pfam05911 763 LEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE 803
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1259-1471 |
6.23e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1259 EKALKTIEVQYSELQ---------TKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETR 1329
Cdd:cd22656 83 QNAGGTIDSYYAEILeliddladaTDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1330 RNYDEESRerqalaataknlEHENTILREHLDeeaeskaDLTRQISKLNAEI-QQWKARFDS--EGLNKLEEIEAAKKAL 1406
Cdd:cd22656 163 KALKDLLT------------DEGGAIARKEIK-------DLQKELEKLNEEYaAKLKAKIDElkALIADDEAKLAAALRL 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127737 1407 QLKVQELTDTNEGLFAKIA----SQEKVR--FKLMQ-DLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKK 1471
Cdd:cd22656 224 IADLTAADTDLDNLLALIGpaipALEKLQgaWQAIAtDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNE 295
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
881-1116 |
6.70e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 881 IARSQLESQvADLVEEKNALflsletEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQEL 960
Cdd:PHA02562 192 HIQQQIKTY-NKNIEEQRKK------NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 961 SDTKKHVQDLELSLRKAE---------QEKQSRDHNIRSLQDEManqDEAVAKLNKEKKHQEESNRKLNEDLqseeDKVN 1031
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKL---KELQHSLEKLDTAIDELEEIMDEFN----EQSK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1032 HLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKV---EGDLKVAQENIDEITKQKHDVEttlkrKEEDLHHTNAKLA 1108
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDKIVKTKSELV-----KEKYHRGIVTDLL 412
|
250
....*....|..
gi 127737 1109 ENN----SIIAK 1116
Cdd:PHA02562 413 KDSgikaSIIKK 424
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
880-1121 |
7.00e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 880 EIARSQLESQVA--DLVEEKNALFLS---LETEKANLADAEE-RNEKLNQLKATLESKLSDITGQLEDMQERNE-----D 948
Cdd:pfam03528 48 DLKRQNAVLQEAqvELDALQNQLALAraeMENIKAVATVSENtKQEAIDEVKSQWQEEVASLQAIMKETVREYEvqfhrR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 949 LARQKKKTDQELSDTKKHVQDLELSLRKAEQEKqsrdhnirSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEED 1028
Cdd:pfam03528 128 LEQERAQWNQYRESAEREIADLRRRLSEGQEEE--------NLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAED 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1029 KVNHLEKirnkleQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLA 1108
Cdd:pfam03528 200 KIKELEA------SKMKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQ 273
|
250
....*....|...
gi 127737 1109 ENNSIIAKLQRLI 1121
Cdd:pfam03528 274 KANDQFLESQRLL 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1013-1097 |
7.08e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1013 EESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKrsrgdiEKAKRKVEGDLKVAQENIDEITKQKHDVE-- 1090
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLL------EEAEKEAQQAIKEAKKEADEIIKELRQLQkg 599
|
....*....
gi 127737 1091 --TTLKRKE 1097
Cdd:PRK00409 600 gyASVKAHE 608
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1746-1910 |
7.27e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1746 ELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAEnAALKGGKKI- 1824
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGNVRNNk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1825 --------IAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKK-NEERLTELVDKLQcklKIFKRQV 1895
Cdd:COG1579 90 eyealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAeLDEELAELEAELE---ELEAERE 166
|
170
....*....|....*
gi 127737 1896 EEAEEVAASNLNKYK 1910
Cdd:COG1579 167 ELAAKIPPELLALYE 181
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
887-1314 |
7.53e-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: 41.35 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 887 ESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLE-------DMQERNEDLARQKKKTDQE 959
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDvkerkinVLQKKIENLQEQLRDKDKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 960 LSDTKKHVQdlelslrkaeqekqsrdhnirSLQDEMANQDEAVAKLnkekkhqeesnrklnEDLQSEEDKVnhlekirnk 1039
Cdd:pfam10174 417 LAGLKERVK---------------------SLQTDSSNTDTALTTL---------------EEALSEKERI--------- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1040 leqqMDELEENIDREKRSRGDIEKAKRKvegDLKVAQENIDEITKQKHDVETTLKrkeeDLHHTNAKLAennSIIAKLQR 1119
Cdd:pfam10174 452 ----IERLKEQREREDRERLEELESLKK---ENKDLKEKVSALQPELTEKESSLI----DLKEHASSLA---SSGLKKDS 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1120 LIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKrEAEIAKLR---REKEEDSL 1196
Cdd:pfam10174 518 KLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKA-QAEVERLLgilREVENEKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1197 NHETAISSLRKRhgdSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQdlekalktiEVQYSELqTKA 1276
Cdd:pfam10174 597 DKDKKIAELESL---TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQ---------QLQLEEL-MGA 663
|
410 420 430
....*....|....*....|....*....|....*...
gi 127737 1277 DEQSRQLQDfaALKNRLnnenSDLNRSLEEMDNQLNSL 1314
Cdd:pfam10174 664 LEKTRQELD--ATKARL----SSTQQSLAEKDGHLTNL 695
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1803-1938 |
7.62e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1803 IKEMQIRLDDAEnAALKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVE-EKKNEER----- 1876
Cdd:pfam00261 3 MQQIKEELDEAE-ERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEaEKAADESergrk 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1877 -LTELVDKLQCKLKIFKRQVEEAEEVAASNLNKY-------KVLTAQFEQAEERADIAENALSKMRNKIR 1938
Cdd:pfam00261 82 vLENRALKDEEKMEILEAQLKEAKEIAEEADRKYeevarklVVVEGDLERAEERAELAESKIVELEEELK 151
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1497-1700 |
8.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1497 AKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKaldeaeaaleaeeaKVLRAQI 1576
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------------EIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1577 EVSQIRSEIEKRIQEKEE------------------EFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDL 1638
Cdd:COG3883 80 EIEERREELGERARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127737 1639 EIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDE 1700
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1008-1345 |
8.37e-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: 41.26 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1008 EKKHQEESNRKLNEDL-QSEEDKVNHLEKiRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLkvaqeniDEITKQK 1086
Cdd:pfam17380 286 ERQQQEKFEKMEQERLrQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL-------ERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1087 HDVETTLKRKEEdlhhtnakLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQ 1166
Cdd:pfam17380 358 RKRELERIRQEE--------IAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1167 GGATAAQLEA-NKKREAEIAKLRREKEEdslnHETAISSLRKRHGDSVAELTEqLETLQKLKAKSEAEKSK-LQRDLEES 1244
Cdd:pfam17380 430 EEARQREVRRlEEERAREMERVRLEEQE----RQQQVERLRQQEEERKRKKLE-LEKEKRDRKRAEEQRRKiLEKELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1245 QHATDSEVRSRQDLEKALKTIEVQ-YSELQTKADEQSRQLQDFAALKNRLNNEnsdlNRSLEEMDNQLNSLHRLKstlqs 1323
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQ----MRKATEERSRLEAMERER----- 575
|
330 340
....*....|....*....|..
gi 127737 1324 qldETRRNYDEESRERQALAAT 1345
Cdd:pfam17380 576 ---EMMRQIVESEKARAEYEAT 594
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1189-1350 |
8.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1189 REKEEDSLNHETAIS----SLRKRHGdsvAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALkt 1264
Cdd:PRK09039 51 KDSALDRLNSQIAELadllSLERQGN---QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1265 ievqySELQTKADEQSRQLqdfaalknrlnnenSDLNRSLEEMDNQLNSlhrlkstLQSQLDEtrrnYDEESRERQ---- 1340
Cdd:PRK09039 126 -----DSEKQVSARALAQV--------------ELLNQQIAALRRQLAA-------LEAALDA----SEKRDRESQakia 175
|
170
....*....|....*...
gi 127737 1341 --------ALAATAKNLE 1350
Cdd:PRK09039 176 dlgrrlnvALAQRVQELN 193
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
885-1126 |
9.69e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 885 QLESQVADLVEEKNALflsLETEKANLADAEERNEKLNQLKAT--------------LESKLSDITGQLEDMQERNEDla 950
Cdd:pfam06160 97 DIEEDIKQILEELDEL---LESEEKNREEVEELKDKYRELRKTllanrfsygpaideLEKQLAEIEEEFSQFEELTES-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 951 RQKKKTDQELSDTKKHVQDLELS-------LRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQ--EESNRKLNE 1021
Cdd:pfam06160 172 GDYLEAREVLEKLEEETDALEELmedipplYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKEIQqlEEQLEENLA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127737 1022 DLqsEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLH 1101
Cdd:pfam06160 252 LL--ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELE 329
|
250 260
....*....|....*....|....*
gi 127737 1102 HTNAKLAENNSIIAKLQRLIKELTA 1126
Cdd:pfam06160 330 RVRGLEKQLEELEKRYDEIVERLEE 354
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