|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-765 |
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: 1341.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 500 YQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAI 579
Cdd:cd14909 401 YKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 580 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSL 659
Cdd:cd14909 481 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 660 MTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPKK 739
Cdd:cd14909 561 MTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDPKK 640
|
650 660
....*....|....*....|....*.
gi 24584706 740 CTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14909 641 AAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-765 |
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: 1250.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGAS-KKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASsKKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQ 418
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 419 VTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFGMDLQLCIDLIEKP-MGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaAHF 577
Cdd:cd01377 401 EYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKSE---AHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 578 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGeqakGGRGKKGGGFATVSSAYKEQLN 657
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGG----GKKKKKGGSFRTVSQLHKEQLN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 658 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGI-KGIED 736
Cdd:cd01377 554 KLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIpKGFDD 633
|
650 660
....*....|....*....|....*....
gi 24584706 737 PKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01377 634 GKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-777 |
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: 1017.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 81 NPPKYEKAEDMSNLTYLNDASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 161 GAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKtdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNS 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT------EVGSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 241 SRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLtDNIYDYHIVSQGK-VTV 319
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL-KSPEDYRYLNQGGcLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 320 ASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQA-EQDGEEEGGRVSKLFGCDTAELYKNL 398
Cdd:smart00242 234 DGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 399 LKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCIN 478
Cdd:smart00242 314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 479 FTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHLG 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 558 KSAPFQKPKPPKpgqqaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGgeqakgg 637
Cdd:smart00242 473 HPHFSKPKKKGR-----TEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGS------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 638 rgkkGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYP 717
Cdd:smart00242 541 ----KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 718 DFKMRYQILNPKGIK-GIEDPKKCTKVLIESTELNDDQYRLGNTKVFFRAGVLGQMEEFRD 777
Cdd:smart00242 617 EFLQRYRVLLPDTWPpWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
89-765 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 981.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 89 EDMSNLTYLNDASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLT 168
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 169 NHVNQSMLITGESGAGKTENTKKVIAYFATVGASKktdeAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIR 248
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSG----SAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 249 IHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLtDNIYDYHIVSQ-GKVTVASIDDAEE 327
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 328 FSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGN 407
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 408 EFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 486
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 487 FFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 566 KPPKPgqqaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG---GGEQAKGGRGKKG 642
Cdd:pfam00063 475 RLQGE----THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESaaaNESGKSTPKRTKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 643 GGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMR 722
Cdd:pfam00063 551 KRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 24584706 723 YQILNPKGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:pfam00063 631 YRILAPKTWpKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-765 |
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: 966.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGA------SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 253
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 254 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQ 333
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 334 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 413
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 414 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 573
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 574 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGE--QAKGGRGKKGGGFATVSSA 651
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDpkSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 652 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGI 731
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 24584706 732 --KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14927 641 pdDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-765 |
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: 925.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKtdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK--QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 500 YQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAI 579
Cdd:cd14934 399 YKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPEAHFEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 580 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQakggrgKKGGGFATVSSAYKEQLNSL 659
Cdd:cd14934 479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKKQ------KRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 660 MTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGI-KGIEDPK 738
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIpQGFVDNK 632
|
650 660
....*....|....*....|....*..
gi 24584706 739 KCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14934 633 KASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
101-765 |
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: 922.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGA----SKKTDeaAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 256
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAtgdlAKKKD--SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 257 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFD 336
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 337 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 416
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 497 QEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQaAH 576
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAE-AH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 577 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQaKGGRGKKGGGFATVSSAYKEQL 656
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGK-KKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 657 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGI---KG 733
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIpegQF 637
|
650 660 670
....*....|....*....|....*....|..
gi 24584706 734 IEDPKKCTKvLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14913 638 IDSKKACEK-LLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-765 |
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: 889.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGAskkTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAA---MIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSvPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGK-KELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 500 YQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSApFQKPKPPKPGQQAAHFAI 579
Cdd:cd14929 397 YRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSV-HFQKPKPDKKKFEAHFEL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 580 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAgQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSL 659
Cdd:cd14929 476 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI-STDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 660 MTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE--DP 737
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKfvSS 634
|
650 660
....*....|....*....|....*...
gi 24584706 738 KKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14929 635 RKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
101-765 |
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: 869.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQ 418
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 419 VTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14917 322 VIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQaAHFA 578
Cdd:cd14917 402 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPE-AHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 579 IAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAkGGRGKKGGGFATVSSAYKEQLNS 658
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKG-KGKAKKGSSFQTVSALHRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 659 LMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE--D 736
Cdd:cd14917 560 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQfiD 639
|
650 660
....*....|....*....|....*....
gi 24584706 737 PKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14917 640 SRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
101-765 |
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: 856.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGA---SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 257
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 258 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDI 337
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 417
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 418 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 498 EEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQaAHF 577
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQE-AHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 578 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLN 657
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 658 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE-- 735
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQfi 640
|
650 660 670
....*....|....*....|....*....|
gi 24584706 736 DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-765 |
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: 853.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATV---GASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 257
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIavtGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 258 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDI 337
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 417
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 418 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 498 EEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSaPFQKPKPPKPGQQAAHF 577
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKS-NNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 578 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-QSGGGEQAKGGRGKKGGGFATVSSAYKEQL 656
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGaEAGDSGGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 657 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE- 735
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQf 640
|
650 660 670
....*....|....*....|....*....|.
gi 24584706 736 -DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14923 641 iDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
102-765 |
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: 837.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 102 VLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGES 181
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 182 GAGKTENTKKVIAYFATVGAS--KKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTgeKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 500 YQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQaAHFAI 579
Cdd:cd14918 403 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAE-AHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 580 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAgQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSL 659
Cdd:cd14918 482 IHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA-SAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 660 MTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE--DP 737
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQfiDS 640
|
650 660
....*....|....*....|....*...
gi 24584706 738 KKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
38-1114 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 833.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 38 CWIPDEKEGYLLGEI---KATKGDIVSVG-LQGGETRDLKKDLLQQV--NPPKYEKAEDMSNLTYLNDASVLHNLRQRYY 111
Cdd:COG5022 12 CWIPDEEKGWIWAEIikeAFNKGKVTEEGkKEDGESVSVKKKVLGNDriKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 112 NKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKK 191
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 192 VIAYFATVGASKKTdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKAR 271
Cdd:COG5022 172 IMQYLASVTSSSTV-----EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 272 VISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYHIVSQGKVT-VASIDDAEEFSLTDQAFDILGFTKQEKEDVYR 350
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKL-LLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 351 ITAAVMHMGGMKFKQrGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGV 430
Cdd:COG5022 326 ILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKAL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 431 FDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFI 510
Cdd:COG5022 405 YSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 511 DFgMDLQLCIDLIEK--PMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQqaahFAIAHYAGCVSY 588
Cdd:COG5022 485 DY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRLNKNSNPKFKKSRFRDNK----FVVKHYAGDVEY 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 589 NITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADhagqsgggeqakGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQP 668
Cdd:COG5022 560 DVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFPTLGSRFKESLNSLMSTLNSTQP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 669 HFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGI-----KGIEDPKKCTKV 743
Cdd:COG5022 628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSwtgeyTWKEDTKNAVKS 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 744 LIESTELNDDQYRLGNTKVFFRAGVLGQMEEFRDERLGKIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQRNLRKYLQL 823
Cdd:COG5022 708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 824 RTWPWYKLWQKVKPLLNVSRIEdeiARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSgekgalqdyqeR 903
Cdd:COG5022 788 DYELKWRLFIKLQPLLSLLGSR---KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFG-----------R 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 904 NAKLTAQKNDLENQLRDIQErLTQEEDARNQLfQQKKKADQEISGLK-KDIEDLELNVQKAEQDKatkdhqirnlNDEIA 982
Cdd:COG5022 854 SLKAKKRFSLLKKETIYLQS-AQRVELAERQL-QELKIDVKSISSLKlVNLELESEIIELKKSLS----------SDLIE 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 983 HQDELINKLNKEKKMQGETNQKTGEELQAAE-DKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEG----- 1056
Cdd:COG5022 922 NLEFKTELIARLKKLLNNIDLEEGPSIEYVKlPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNfkkel 1001
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1057 -----DLKLTQEAVADLERNKKELE--QTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARI 1114
Cdd:COG5022 1002 aelskQYGALQESTKQLKELPVEVAelQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARY 1066
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-765 |
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: 831.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGAS--KKTDE--AAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 256
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTgeKKKEEitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 257 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFD 336
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 337 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 416
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 497 QEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQaAH 576
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAE-AH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 577 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF--ADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKE 654
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFsgAQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 655 QLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGI 734
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 24584706 735 E--DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14912 641 QfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
101-765 |
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: 823.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGAS--KKTDE--AAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 256
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTgeKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 257 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFD 336
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 337 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 416
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 497 QEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSaPFQKPKPPKPGQQAAH 576
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKS-NNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 577 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA---GQSGGGEQAkggRGKKGGGFATVSSAYK 653
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAaaeAEEGGGKKG---GKKKGSSFQTVSALFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 654 EQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKG 733
Cdd:cd14910 558 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 24584706 734 IE--DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14910 638 GQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-765 |
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: 816.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGAS--KKTDEA--AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 256
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTgeKKKEEAasGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 257 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFD 336
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 337 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 416
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 497 QEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSaPFQKPKPPKPGQQAAH 576
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKS-NNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 577 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQL 656
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 657 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE- 735
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQf 640
|
650 660 670
....*....|....*....|....*....|.
gi 24584706 736 -DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14915 641 iDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-765 |
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: 809.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRN-EVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASKKTDEAaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSS-SSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKD----ICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQA 334
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREelklELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 335 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREE--QAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQ 412
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 413 GRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQ--HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 490
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 491 HMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPK 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 570 PgqqaaHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKsqnkllieifadhagqsgggeqakggrgkkgggfatvS 649
Cdd:cd00124 479 L-----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS-------------------------------------G 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 650 SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPK 729
Cdd:cd00124 517 SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*..
gi 24584706 730 GIKGIEDPKKCTKV-LIESTELNDDQYRLGNTKVFFR 765
Cdd:cd00124 597 ATEKASDSKKAAVLaLLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-765 |
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: 773.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSK---------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIH 250
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 251 FGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDnIYDYHIVSQGKVTVASIDDAEEFSL 330
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 331 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 410
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 411 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDtQQKRQ--HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 488
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQgaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 489 NHHMFVLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlgksaPFQKPKPP 568
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-----SMHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 569 KPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADhAGQSGGGEQAKGGRG----KKGGG 644
Cdd:cd14911 474 TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD-AEIVGMAQQALTDTQfgarTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 645 FATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQ 724
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 24584706 725 ILNPKGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14911 633 LLTPNVIpKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-765 |
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: 734.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSD-LLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14920 320 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFGMDLQLCIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTnthlGKSAPFQKPKPPKPGQQAA 575
Cdd:cd14920 400 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV----QEQGSHSKFQKPRQLKDKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 576 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQSGGGEQAKGGRGKKGG-GFATV 648
Cdd:cd14920 476 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgLDQVTGMTETAFGSAYKTKKgMFRTV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 649 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNP 728
Cdd:cd14920 556 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 24584706 729 KGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14920 636 NAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-765 |
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: 697.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDE----AAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 255
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKdqssIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 256 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVK-DICLltDNIYDYHIVSQGKVTVASIDDAEEFSLTDQA 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRsELCL--EDYSKYRFLSNGNVTIPGQQDKELFAETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 335 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGR 414
Cdd:cd14932 239 FRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 415 NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNthlgKSAPFQKPKPPKP 570
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQ----EQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 571 GQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH------AGQSGGGEQAKGGRGKKGGG 644
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivglDKVAGMGESLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 645 FATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQ 724
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 24584706 725 ILNPKGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14932 635 ILTPNAIpKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
101-765 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 695.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYN-KLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd01380 2 AVLHNLKVRFCQrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASkktdeaAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS------SSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQ--KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 498 EEYQREGIEWTFIDFgMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQqaahF 577
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHFKKPRFSNTA----F 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 578 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLlieifadhagqsgggeqakggrgkkgggfATVSSAYKEQLN 657
Cdd:cd01380 471 IVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK-----------------------------KTVGSQFRDSLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 658 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDP 737
Cdd:cd01380 522 LLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDK 601
|
650 660
....*....|....*....|....*...
gi 24584706 738 KKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01380 602 KKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-765 |
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: 672.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSD-LLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14921 320 DFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFGMDLQLCIDLIEKPM---GILSILEEESMFPKATDQTFSEKLtnthLGKSAPFQKPKPPKPGQQAA 575
Cdd:cd14921 400 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKL----CTEQGNHPKFQKPKQLKDKT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 576 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAK-------GGRGKKGGGFATV 648
Cdd:cd14921 476 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpSASKTKKGMFRTV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 649 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNP 728
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 24584706 729 KGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14921 636 NAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-765 |
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: 654.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKT----DEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 255
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTkkdqNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 256 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVK-DICLltDNIYDYHIVSQGKVTVASIDDAEEFSLTDQA 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRsELLL--ENYNNYRFLSNGNVTIPGQQDKDLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 335 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGR 414
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 415 NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPM---GILSILEEESMFPKATDQTFSEKLtnthLGKSAPFQKPKPPKP 570
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKV----LQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 571 GQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG-----GGEQAKGGRGKKGGGF 645
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGldkvsGMSEMPGAFKTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 646 ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQI 725
Cdd:cd15896 555 RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 24584706 726 LNPKGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd15896 635 LTPNAIpKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-765 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 649.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSK---KDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKdICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK-TDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14919 237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14919 317 DFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFGMDLQLCIDLIEKPM---GILSILEEESMFPKATDQTFSEKLtnthLGKSAPFQKPKPPKPGQQAA 575
Cdd:cd14919 397 EYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKV----VQEQGTHPKFQKPKQLKDKA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 576 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGR-------GKKGGGFATV 648
Cdd:cd14919 473 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtalpgafKTRKGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 649 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNP 728
Cdd:cd14919 553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 24584706 729 KGI-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14919 633 NSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-765 |
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: 639.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKtdeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNiYDYHIVSQGK-VTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDA-SDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQRGRE--EQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 416
Cdd:cd01381 231 MFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF---IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd01381 311 EQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDFgMDLQLCIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpgq 572
Cdd:cd01381 391 KLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLN--- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 573 qaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFA-DHAGQSGGGEQAkggrgkkgggfATVSSA 651
Cdd:cd01381 467 --TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNeDISMGSETRKKS-----------PTLSSQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 652 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPkGI 731
Cdd:cd01381 534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 24584706 732 KGIE--DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01381 613 PPAHktDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
101-765 |
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: 637.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNevPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLD--SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGASKktdeaakskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 260
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS---------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 261 DIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDnIYDYHIVSQGK-VTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEALDTVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd01383 230 ISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQ-HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd01383 310 IDARDALAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLtNTHLGKSAPFQKPKPPKpgqqaahF 577
Cdd:cd01383 390 EYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGERGGA-------F 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 578 AIAHYAGCVSYNITGWLEKNKDPLNDTVVdQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLN 657
Cdd:cd01383 461 TIRHYAGEVTYDTSGFLEKNRDLLHSDLI-QLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQLF 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 658 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDP 737
Cdd:cd01383 540 KLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDP 619
|
650 660
....*....|....*....|....*...
gi 24584706 738 KKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01383 620 LSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-765 |
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: 634.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKdICLLTDNIYDYHIVSQGKVTVASiDDAEEFSLTDQAFDILG 339
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 499 EYQREGIEWTFIDFGMDLQLCIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNthlgKSAPFQKPKPPKPGQQAA 575
Cdd:cd14930 399 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQ----EQGGHPKFQRPRHLRDQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 576 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGR-----GKKGGGFATVSS 650
Cdd:cd14930 475 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDgppggRPRRGMFRTVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 651 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKG 730
Cdd:cd14930 555 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 24584706 731 I-KGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14930 635 IpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-765 |
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: 612.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGaSKKTdeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 260
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVT-NNHS--------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 261 DIETYLLEKARVISQQSLERSYHIFYQIMSGSV--PGVKDICLLTDnIYDYHIVSQ-GKVTVASIDDAEEFSLTDQAFDI 337
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLGE-PEDYHYLNQsGCIRIDNINDKKDFDHLRLAMNV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAE-QDGEEEGGRVSKLFGCDTAELYKNLLKPRIKV-GNEFVTQGRn 415
Cdd:cd14883 232 LGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVrGNVTEIPLK- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 416 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14883 311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 496 EQEEYQREGIEWTFIDFgMDLQLCIDLIEK-PMGILSILEEESMFPKATDQTFSEKLtNTHLGKSAPFQKPKPPKPGQQa 574
Cdd:cd14883 391 EQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKL-HAAHEKHPYYEKPDRRRWKTE- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 575 ahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFA-------DHAGQSGGGEQAKGGRGKKGggfAT 647
Cdd:cd14883 468 --FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdllalTGLSISLGGDTTSRGTSKGK---PT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 648 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILN 727
Cdd:cd14883 543 VGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLD 622
|
650 660 670
....*....|....*....|....*....|....*....
gi 24584706 728 PKGIKGIED-PKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14883 623 PRARSADHKeTCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-765 |
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: 599.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASKKTDEAakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR-----SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDnIYDYHIVSQGK-VTVASIDDAEEFSLTDQAFDI 337
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFkqrGREEQAEQDG------EEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 411
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEF---SKGEEDDSSVpkdeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 412 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 491
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 492 MFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKL-----TNTHLGKSAPFQKP 565
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLyqtlkDHKRFSKPKLSRTD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 566 kppkpgqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAdhAGQSGGGEQAkggrgkkgGGF 645
Cdd:cd01384 471 -----------FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP--PLPREGTSSS--------SKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 646 ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQI 725
Cdd:cd01384 530 SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 24584706 726 LNPKGIKGIEDPKKCTKVLIESTELNDdqYRLGNTKVFFR 765
Cdd:cd01384 610 LAPEVLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-765 |
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: 596.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATV-GASKKTDEAAKskgsleDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVsGGSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILG 339
Cdd:cd01378 156 GHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 340 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQ---GRNV 416
Cdd:cd01378 236 FTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGRSVyevPLNV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQ-HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHhmFVL 495
Cdd:cd01378 315 EQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 496 --EQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFP-KATDQTFSEKLtnTHLGKSAPFQKPKPPKPG 571
Cdd:cd01378 393 kaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 572 QQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADhagqsgGGEQAKGGRGKkgggfaTVSSA 651
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------GVDLDSKKRPP------TAGTK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 652 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPK-G 730
Cdd:cd01378 538 FKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtW 617
|
650 660 670
....*....|....*....|....*....|....*
gi 24584706 731 IKGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01378 618 PAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
100-765 |
1.40e-179 |
|
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: 559.56 E-value: 1.40e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASkktdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS--------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIydyhivsqgkvtvasIDDAEEFSLTDQAFDIL 338
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREK-LLKDPL---------------LDDVGDFIRMDKAMKKI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFkqrgreeqaEQDGEEEGGR-------------VSKLFGCDTAELYKNLLKpRIKV 405
Cdd:cd01382 217 GLSDEEKLDIFRVVAAVLHLGNIEF---------EENGSDSGGGcnvkpkseqsleyAAELLGLDQDELRVSLTT-RVMQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 406 GNEFVTQGR------NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTqQKRQHFIGVLDIAGFEIFEYNGFEQLCINF 479
Cdd:cd01382 287 TTRGGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPF-ETSSYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 480 TNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHLG- 557
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNh 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 558 -------KSApfqkpkppkpgqQAAH--------FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFA 622
Cdd:cd01382 445 frlsiprKSK------------LKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 623 DHAGQSGGGEQAkggrgKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEG 702
Cdd:cd01382 513 SSTNNNKDSKQK-----AGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 703 IRICRKGFPNRMMYPDFKMRYQILNPKGIKGIeDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01382 588 LDLMQGGFPSRTSFHDLYNMYKKYLPPKLARL-DPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-765 |
9.05e-174 |
|
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: 543.60 E-value: 9.05e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFAtvgaskktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFA---------EVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDniyDYHIVSQGK-VTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLSGcIEVEGVDDVADFEEVVLAMEQL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAE---QDGEEEGGRVSKLFGCDTAELYKNLLKPRIKV--GNEFVTQG 413
Cdd:cd14872 229 GFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkgCDPTRIPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 414 RNVQQVTNSiGALCKGVFDRLFKWLVKKCNETLDTQQ-KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHM 492
Cdd:cd14872 309 TPAQATDAC-DALAKAAYSRLFDWLVKKINESMRPQKgAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 493 FVLEQEEYQREGIEWTFIDFgMDLQLCIDLIEK-PMGILSILEEESMFPKATDQTFSEKLTNTHLGKSapfqKPKPPKPG 571
Cdd:cd14872 388 FKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS----TFVYAEVR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 572 QQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgggeqakggrgkkGGGFATVSSA 651
Cdd:cd14872 463 TSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQ-------------KTSKVTLGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 652 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGI 731
Cdd:cd14872 530 FRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIA 609
|
650 660 670
....*....|....*....|....*....|....*
gi 24584706 732 KGI-EDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14872 610 KRVgPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-765 |
1.45e-172 |
|
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: 540.90 E-value: 1.45e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGaskktdeaakskGSLED----QVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPT 254
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 255 GKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYhivsQGKVTVASID---DAEEFSLT 331
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLF-LDSANECAY----TGANKTIKIEgmsDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 332 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVS--KLFGCDTAELYKNLLKPRIKVGNEF 409
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYatKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 410 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFN 489
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 490 HHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLgksapFQKPKPPK 569
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHK-----DEQDVIEF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 570 PGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF----ADHAGQSGGGEQAKGGRGKKGGGF 645
Cdd:cd14903 458 PRTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekvESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 646 ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQI 725
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 24584706 726 LNPKGIKGIEDPKKCTKVLIESTELND-DQYRLGNTKVFFR 765
Cdd:cd14903 618 FLPEGRNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-765 |
1.40e-170 |
|
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: 535.51 E-value: 1.40e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHV----NQS 174
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVldpsNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 175 MLITGESGAGKTENTKKVIAYFATV------GASKKTDEA----AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFG 244
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARItsgfaqGASGEGEAAseaiEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 245 KFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQgKVTVASIDD 324
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGE-CSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 325 AEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGR-VSKLFGCDTAELYKNLLKPRI 403
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKlAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 404 KVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEK 483
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 484 LQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-----KPmGILSILEE-ESMFPKATDQTFSEKLTNTHLG 557
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDcWRFKGEEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 558 KSAPFQKPKPPKPGQ--------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLiEIfadhagqsg 629
Cdd:cd14890 478 KSGSGGTRRGSSQHPhfvhpkfdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIR-EV--------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 630 ggeqakggrgkkgggfaTVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKG 709
Cdd:cd14890 548 -----------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 710 FPNRMMYPDFKMRYQILNPKGikgiEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14890 611 FALREEHDSFFYDFQVLLPTA----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-765 |
5.89e-167 |
|
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: 525.51 E-value: 5.89e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKkVIAYFATVGASKKTDEAAKSKGS-LEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 257
Cdd:cd14873 81 GESGAGKTESTK-LILKFLSVISQQSLELSLKEKTScVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 258 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNiYDYHIVSQ-GKVTVASIDDAEEFSLTDQAFD 336
Cdd:cd14873 160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTP-ENYHYLNQsGCVEDKTISDQESFREVITAME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 337 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEeegGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 416
Cdd:cd14873 239 VMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTAL---GRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 417 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRqHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14873 316 QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDF-KSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 497 QEEYQREGIEWTFIDFgMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlgksapfQKPKPPKPGQQAAH 576
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-------ANNHFYVKPRVAVN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 577 -FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFaDHAGQSGGGEQAKGGRGKKGggfATVSSAYKEQ 655
Cdd:cd14873 467 nFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF-EHVSSRNNQDTLKCGSKHRR---PTVSSQFKDS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 656 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNpKGIKGIE 735
Cdd:cd14873 543 LHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM-RNLALPE 621
|
650 660 670
....*....|....*....|....*....|
gi 24584706 736 DPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14873 622 DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-763 |
2.69e-161 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 510.10 E-value: 2.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY------RGKRRNEVPPHIFAISDGAYVDMLTNHV-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 172 --NQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 250 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNI-YDYHIVSQGKVTVASIDDAEEF 328
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 329 SLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGR-VSKLFGCDTAELYKNLLKPRIKVGN 407
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRaACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 408 EFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL--DTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQ 485
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 486 QFFNHHMFVLEQEEYQREGIEWTFIDFGMDlQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKL-----TNTHLGKS 559
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYydllaKHASFSVS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 560 APFQKPkppkpgqqaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIeifadhagqsgggeqakggrg 639
Cdd:cd14901 480 KLQQGK---------RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS--------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 640 kkgggfATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDF 719
Cdd:cd14901 530 ------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 24584706 720 KMRYQILNPKG------IKGIEDPKKCTKVLIESTELNDDQYRLGNTKVF 763
Cdd:cd14901 604 VHTYSCLAPDGasdtwkVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
100-765 |
4.38e-161 |
|
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: 509.69 E-value: 4.38e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEV---PPHIFAISDGAYVDMLTNHVN---- 172
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGKGqgtp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 173 QSMLITGESGAGKTENTKKVIAYFATvgASKKTDEAAKSKG------SLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKF 246
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAT--ASKLAKGASTSKGaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 247 IRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKDICLLTDNIYDYHIVSQGK-VTVASIDDA 325
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAG-LDANENAALELTPAESFLFLNQGNcVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 326 EEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQ--AEQDGEEEGGRVSKLFGCDTAELYKNLLKpRI 403
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDvfAQSADGVNVAKAAGLLGVDAAELMFKLVT-QT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 404 KVGnefvTQGRNVQ------QVTNSIGALCKGVFDRLFKWLVKKCN----------ETLDTQQKRQHFIGVLDIAGFEIF 467
Cdd:cd14892 317 TST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkqqtsgvTGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 468 EYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIEK-PMGILSILEEESMFP-KATDQ 545
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 546 TFSEKLTNTHLGKSAPFQKPKPPKPgqqaaHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKsqnkllieifadha 625
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRS-------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 626 gqsgggeqakggrgkkgggfatvSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRI 705
Cdd:cd14892 533 -----------------------SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 706 CRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPKKC----TKVLIEST---ELNDDQYRLGNTKVFFR 765
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNKAGVAASPDACdattARKKCEEIvarALERENFQLGRTKVFLR 656
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
842-1922 |
6.80e-160 |
|
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: 520.89 E-value: 6.80e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDI 921
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 922 QERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGET 1001
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1002 NQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQR 1081
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1082 KDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIE 1161
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1162 LNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEK 1241
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1242 AAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEE 1321
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1322 SRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVArSEELEEAKRKLQARLAEAEE 1401
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1402 TIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELF 1481
Cdd:pfam01576 560 QLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1482 RLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQ 1561
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1562 LELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKN 1641
Cdd:pfam01576 720 VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1642 IKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNAS 1721
Cdd:pfam01576 800 LKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSA 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1722 ISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEA 1801
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1802 NALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQI 1881
Cdd:pfam01576 960 TVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQL 1039
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 24584706 1882 EEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAK 1922
Cdd:pfam01576 1040 EEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
101-765 |
1.22e-157 |
|
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: 499.11 E-value: 1.22e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGASKKtdeaakskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 260
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANN--------RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 261 DIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVK-DICLLTDNIYDYHIVSQGKV--TVASID-DAEEFSLTDQAFD 336
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTvqDIVNNSgNREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 337 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGE----EEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQ 412
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSRisnpEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 413 GRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFN 489
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 490 HHMFVLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNThlgksapFQKPKPPK 569
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNN-------IKSKYYWR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 570 PGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLieifadhagqsgggEQakggrgkkgggfaTVS 649
Cdd:cd01379 467 PKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV--------------RQ-------------TVA 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 650 SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILnpk 729
Cdd:cd01379 520 TYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFL--- 596
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 24584706 730 GIKGIEDPK----KCTKVLIestELNDDQYRLGNTKVFFR 765
Cdd:cd01379 597 AFKWNEEVVanreNCRLILE---RLKLDNWALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-729 |
1.54e-157 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 500.37 E-value: 1.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRgKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASkktDEAAKSKgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF------- 251
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSE---DIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 252 --GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMS--------GSVPGVKDICL----------LTDNIYDYHI 311
Cdd:cd14888 155 msGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntGLSYEENDEKLakgadakpisIDMSSFEPHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 312 VSQgKVTVASI------DDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFK-QRGREEQA--EQDGEEEGGR 382
Cdd:cd14888 235 KFR-YLTKSSChelpdvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAvvSASCTDDLEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 383 VSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDI 461
Cdd:cd14888 314 VASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 462 AGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLI-EKPMGILSILEEESMFP 540
Cdd:cd14888 394 FGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 541 KATDQTFSEKLTNTHLGksapfqKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEI 620
Cdd:cd14888 473 GGKDQGLCNKLCQKHKG------HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 621 FADHAGQSGGGEQakggrgkKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVL 700
Cdd:cd14888 547 FSAYLRRGTDGNT-------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660
....*....|....*....|....*....
gi 24584706 701 EGIRICRKGFPNRMMYPDFKMRYQILNPK 729
Cdd:cd14888 620 QAVQVSRAGYPVRLSHAEFYNDYRILLNG 648
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-765 |
9.21e-156 |
|
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: 495.04 E-value: 9.21e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDeaakskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFgPTGKLAG 259
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL--------VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSG-SVPGVKDICLLTDNIYdYHIVSQGKVTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGlPAQLRQKYGLQEAEKY-FYLNQGGNCEIAGKSDADDFRRLLAAMQVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQRgrEEQAEQDGEEEGGR-----VSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 413
Cdd:cd01387 231 GFSSEEQDSIFRILASVLHLGNVYFHKR--QLRHGQEGVSVGSDaeiqwVAHLLQISPEGLQKALTFKVTETRRERIFTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 414 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd01387 309 LTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDFgMDLQLCIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTHlgksapFQKPKPPKPGQ 572
Cdd:cd01387 389 KLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH------ALNELYSKPRM 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 573 QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQ--AKGGRGKKGGGFATVSS 650
Cdd:cd01387 462 PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPrlGKGRFVTMKPRTPTVAA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 651 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQ-ILNPK 729
Cdd:cd01387 542 RFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRcLVALK 621
|
650 660 670
....*....|....*....|....*....|....*.
gi 24584706 730 GIKGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01387 622 LPRPAPGDMCVSLLSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
100-765 |
1.40e-155 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 495.74 E-value: 1.40e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFatvgaskkTDEAAKSKGS-LEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--------TALSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNiYDYHIVSQGK-VTVASIDDAEEFSLTDQAFDI 337
Cdd:cd01385 153 GAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNQSDcYTLEGEDEKYEFERLKQAMEM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFKQR--GREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 415
Cdd:cd01385 232 VGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 416 VQQVTNSIGALCKGVFDRLFKWLVKKCNETL----DTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 491
Cdd:cd01385 312 LPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 492 MFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHlgksapFQKPKPPKP 570
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH------KDNKYYEKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 571 GQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIE-----------------------IFAD---- 623
Cdd:cd01385 465 QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREligidpvavfrwavlrafframaAFREagrr 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 624 HAGQSGGGE-------QAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTC 696
Cdd:cd01385 545 RAQRTAGHSltlhdrtTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584706 697 NGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPkkcTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKED---IKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
100-765 |
2.49e-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: 479.19 E-value: 2.49e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKR-RNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASKKTDeaakskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD--------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDnIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLED-PDCHRILRDDNRNRPVFNDSEELEYYRQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 -------GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 411
Cdd:cd14897 232 tnimkliGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 412 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF-----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 486
Cdd:cd14897 312 SWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 487 FFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLI-EKPMGILSILEEESMFPKATDQTFSEKLtNTHLGKSAPFQKP 565
Cdd:cd14897 392 YFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 566 KPPKpgqqaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHagqsgggeqakggrgkkgggf 645
Cdd:cd14897 470 PGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY--------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 646 atvssaYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQI 725
Cdd:cd14897 524 ------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 24584706 726 LNPKGIKGIE-DPKKCTKVLieSTELNDDqYRLGNTKVFFR 765
Cdd:cd14897 598 ICDFSNKVRSdDLGKCQKIL--KTAGIKG-YQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
100-727 |
7.89e-142 |
|
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: 457.19 E-value: 7.89e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRN--------EVPPHIFAISDGAYVDMLTNH 170
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 171 VNQSMLITGESGAGKTENTKKVIAYFATVGASK-----------KTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDN 239
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEqnseevltltsSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 240 SSRFGKFIRIHFG-PTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSG-SVPGVKDICLLTDNIYD-YHIVSQGK 316
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGaDQQLLQQLGLKNQLSGDrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 317 -VTVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQR--GREEQAEQDGEEEGGRVSKLFGCDTAE 393
Cdd:cd14907 241 cYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 394 LYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL--------DTQQKRQHFIGVLDIAGFE 465
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 466 IFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTF--IDFgMDLQLCIDLIEK-PMGILSILEEESMFPKA 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 543 TDQTFSEKLTNTHLGKSapfqkPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFA 622
Cdd:cd14907 480 TDEKLLNKIKKQHKNNS-----KLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 623 DHAGQSgggEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEG 702
Cdd:cd14907 555 GEDGSQ---QQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
|
650 660
....*....|....*....|....*
gi 24584706 703 IRICRKGFPNRMMYPDFKMRYQILN 727
Cdd:cd14907 632 IRVRKQGYPYRKSYEDFYKQYSLLK 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-765 |
4.56e-139 |
|
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: 448.97 E-value: 4.56e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 102 VLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDML----TNHVNQSMLI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 178 TGESGAGKTENTKKVIayfatvgasKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFgPTGKL 257
Cdd:cd14889 83 SGESGAGKTESTKLLL---------RQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 258 AGADIETYLLEKARVISQQSLERSYHIFYQIMSG-SVPGVKDICLLTDNIYDY--------HIVSQGKVTVASIDDAeef 328
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDPGKYRYlnngagckREVQYWKKKYDEVCNA--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 329 sltdqaFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRgrEEQAEQDGEEEGGRV---SKLFGCDTAELYKNLLKPRIKV 405
Cdd:cd14889 230 ------MDMVGFTEQEEVDMFTILAGILSLGNITFEMD--DDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 406 GNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNE 482
Cdd:cd14889 302 RGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLapkDDSSVELREIGILDIFGFENFAVNRFEQACINLANE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 483 KLQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDL-IEKPMGILSILEEESMFPKATDQTFSEKLtNTHLGKSAP 561
Cdd:cd14889 382 QLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 562 FQKPKPPKPGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKK 641
Cdd:cd14889 460 YGKSRSKSPK-----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 642 GGGFA-----TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMY 716
Cdd:cd14889 535 SDNFNstrkqSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 24584706 717 PDFKMRYQILNPKgiKGIEDPKKCTKVLIESTELNDdqYRLGNTKVFFR 765
Cdd:cd14889 615 AEFAERYKILLCE--PALPGTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-726 |
4.53e-138 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 445.13 E-value: 4.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMY-----------RGKRRNEVPPHIFAISDGAYVDM-- 166
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 167 --LTNHVNQSMLITGESGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSR 242
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDnnLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 243 FGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVkdiclLTDNIYDyhivsqgKVTvasi 322
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA-----RKRDMYR-------RVM---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 323 ddaeefsltdQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEG-------GRVSKLFGCDTAELY 395
Cdd:cd14900 226 ----------DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 396 KNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQ-----HFIGVLDIAGFEIFEYN 470
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKshgglHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 471 GFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLI-EKPMGILSILEEESMFPKATDQTFSE 549
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 550 KL---TNTHLGKSAPFQKPKPpkpgqqaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFkksqnkllieifadhag 626
Cdd:cd14900 455 KLyraCGSHPRFSASRIQRAR-------GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF----------------- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 627 QSGGgeqakggrgkkgggfatvssAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRIC 706
Cdd:cd14900 511 VYGL--------------------QFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
|
650 660
....*....|....*....|
gi 24584706 707 RKGFPNRMMYPDFKMRYQIL 726
Cdd:cd14900 571 RAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-765 |
1.63e-137 |
|
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: 444.39 E-value: 1.63e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASKKTDEAAKskgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAK--------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSG-SVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDI 337
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEgGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 417
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQL-SQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 418 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 497 QEEYQREGIEWTFIDFgMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlgkSAPFQKPKPPKPGQQAAH 576
Cdd:cd14904 392 EEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNH---QTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 577 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgggEQAKGGRGKKGGGFATVSSAYKEQL 656
Cdd:cd14904 468 FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPS---ETKEGKSGKGTKAPKSLGSQFKTSL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 657 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIED 736
Cdd:cd14904 545 SQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDV 624
|
650 660
....*....|....*....|....*....
gi 24584706 737 PKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14904 625 RRTCSVFMTAIGRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-765 |
8.64e-137 |
|
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: 443.58 E-value: 8.64e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYR--GKRRNE-------VPPHIFAISDGAYVDMLTN- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 170 HVNQSMLITGESGAGKTENTKKVIAYFATVGASKK---TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKF 246
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgapNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 247 IRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIY-------DYHIVSQGKV-T 318
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITgglqlpnEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 319 VASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFK---QRGREEQAEQDGEEEGGRVSKLFGCDTAELY 395
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEskeEDGAAEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 396 KNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL--DTQQKRQHFIGVLDIAGFEIFEYNGFE 473
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 474 QLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLIE-KPMGILSILEEESMFP-KATDQTFSEKL 551
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 552 TNTHLGKSAPFQKPKPPKPGQQAAH----FAIAHYAGCVSYNI-TGWLEKNKDPLNDTVVDQFKKSQNkllieifadhag 626
Cdd:cd14908 480 YETYLPEKNQTHSENTRFEATSIQKtkliFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 627 qsgggeqakggrgkkgggfatvssaYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRIC 706
Cdd:cd14908 548 -------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 707 RKGFPNRMMYPDFKMRYQIL---NPKGIKGI----EDP-----KKCTKVLIEST---------ELNDDQYRLGNTKVFFR 765
Cdd:cd14908 603 RSGYPVRLPHKDFFKRYRMLlplIPEVVLSWsmerLDPqklcvKKMCKDLVKGVlspamvsmkNIPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-765 |
4.58e-135 |
|
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: 437.17 E-value: 4.58e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYY--NKLIYTYSGLFCVAINPYKRYPvytNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTN---HVNQS 174
Cdd:cd14891 1 AGILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGsgrMQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 175 MLITGESGAGKTENTKKVIAYFAT---VGASKKTDEAAKSKG-------SLEDQVVQTNPVLEAFGNAKTVRNDNSSRFG 244
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTravGGKKASGQDIEQSSKkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 245 KFIRIHFGPTG-KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYHIVSQ-GKVTVASI 322
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKE-LLLLSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 323 DDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQR----GREEQAEQDGEEEGGRVSKLFGCDTAELYKNL 398
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEdtseGEAEIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 399 LKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFE-YNGFEQLCI 477
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 478 NFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTHL 556
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTHK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 557 GKSAPFQKPKPPKPGQqaahFAIAHYAGCVSYNITGWLEKNkdplNDTVVDQFkksqnkllieifadhagqsgggeqakg 636
Cdd:cd14891 476 RHPCFPRPHPKDMREM----FIVKHYAGTVSYTIGSFIDKN----NDIIPEDF--------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 637 grgkkgGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMY 716
Cdd:cd14891 521 ------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 24584706 717 PDFKMRYQILNPKGIKGIEDPKKCTkvLIEST----ELNDDQYRLGNTKVFFR 765
Cdd:cd14891 595 AELVDVYKPVLPPSVTRLFAENDRT--LTQAIlwafRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-729 |
2.89e-133 |
|
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: 434.70 E-value: 2.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYR--------GKRRNEVPPHIFAISDGAYVDMLTNH 170
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 171 -VNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGS-LEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIR 248
Cdd:cd14902 81 rRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVeIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 249 IHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYHIVSQ-----GKVTVASID 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDL-LGLQKGGKYELLNSygpsfARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 324 DAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAE---QDGEEEGGRVSKLFGCDTAELYKNLLK 400
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATavtAASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 401 PRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-------TQQKRQHF--IGVLDIAGFEIFEYNG 471
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 472 FEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGMDLQlCIDLIE-KPMGILSILEEESMFPKATDQTFSEK 550
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDdKSNGLFSLLDQECLMPKGSNQALSTK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 551 LTNTHLGKSapfqkpkppkpgqqaaHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-HAGQSG 629
Cdd:cd14902 479 FYRYHGGLG----------------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADeNRDSPG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 630 GGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKG 709
Cdd:cd14902 543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
|
650 660
....*....|....*....|
gi 24584706 710 FPNRMMYPDFKMRYQILNPK 729
Cdd:cd14902 623 YSVRLAHASFIELFSGFKCF 642
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
79-821 |
4.22e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 432.15 E-value: 4.22e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 79 QVNPPKYEkaeDMSNLTYLNDASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYR-GKRRNEVPPHIFA 157
Cdd:PTZ00014 92 QIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 158 ISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATvGASKKTDeaakskGSLEDQVVQTNPVLEAFGNAKTVRN 237
Cdd:PTZ00014 169 TARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGNMD------LKIQNAIMAANPVLEAFGNAKTIRN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 238 DNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTdNIYDYHIVSQGKV 317
Cdd:PTZ00014 242 NNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLK-SLEEYKYINPKCL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 318 TVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQR---GREEQAEQDGEEEG--GRVSKLFGCDTA 392
Cdd:PTZ00014 321 DVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKeegGLTDAAAISDESLEvfNEACELLFLDYE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 393 ELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGF 472
Cdd:PTZ00014 401 SLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 473 EQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLt 552
Cdd:PTZ00014 481 EQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSC- 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 553 NTHLGKSAPFQKPKPPKPGQqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD---HAGQSG 629
Cdd:PTZ00014 560 NTNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGvevEKGKLA 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 630 GGEqakggrgkkgggfaTVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKG 709
Cdd:PTZ00014 636 KGQ--------------LIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLG 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 710 FPNRMMYPDFKMRYQILNpKGI---KGIEDPKKCTKvLIESTELNDDQYRLGNTKVFFRAGVLGQMEEFRDERLGK---I 783
Cdd:PTZ00014 702 FSYRRTFAEFLSQFKYLD-LAVsndSSLDPKEKAEK-LLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepL 779
|
730 740 750
....*....|....*....|....*....|....*...
gi 24584706 784 MSWMQAWARGYLSRkgfKKLQEQRVALKVVQRNLRKYL 821
Cdd:PTZ00014 780 VSVLEALILKIKKK---RKVRKNIKSLVRIQAHLRRHL 814
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-765 |
7.23e-124 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 405.70 E-value: 7.23e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskgsledQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFgPTGKLAG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLR--------QPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDIcLLTDNIYDYHIVSQGKV-TVASIDDAEEFSLTDQAFDIL 338
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQ-LSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQRGRE--EQAEQDGEEEGGRVSKLFgCDTAELYKNLLKPRIKVGN-EFVTQGRN 415
Cdd:cd14896 231 GLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLL-QVPPERLEGAVTHRVTETPyGRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 416 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF--IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDfGMDLQLCIDLI-EKPMGILSILEEESMFPKATDQTFSEKlTNTHLGKSAPFQKPKPPKPGq 572
Cdd:cd14896 390 AQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQK-CHYHHGDHPSYAKPQLPLPV- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 573 qaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAkggrgkkgggfATVSSAY 652
Cdd:cd14896 467 ----FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGK-----------PTLASRF 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 653 KEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIK 732
Cdd:cd14896 532 QQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQE 611
|
650 660 670
....*....|....*....|....*....|...
gi 24584706 733 GIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14896 612 ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
101-765 |
2.44e-123 |
|
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: 406.26 E-value: 2.44e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAkmYRGKRRN--EVPPHIFAISDGAYVDMLT-------NHV 171
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHK--YREEMPGwtALPPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 172 NQSMLITGESGAGKTENTKKVIAYFATVGASKK-TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIH 250
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSKHTTaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRMF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 251 FGP-----TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVK-DICLLTDNIYDYHIVSQGKVTVAS--I 322
Cdd:cd14895 160 FEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKlELQLELLSAQEFQYISGGQCYQRNdgV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 323 DDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDG------------------EEEGGRVS 384
Cdd:cd14895 240 RDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGaasapcrlasaspssltvQQHLDIVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 385 KLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQH---------- 454
Cdd:cd14895 320 KLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaankdtt 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 455 -FIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLIE-KPMGILSI 532
Cdd:cd14895 400 pCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGIFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 533 LEEESMFPKATDQTFSEKL---TNTHLGKSAPFQKPKPPKpgqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQF 609
Cdd:cd14895 479 LDEECVVPKGSDAGFARKLyqrLQEHSNFSASRTDQADVA-------FQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 610 KKSQNKLLIEIFAD-HAGQSGGGEQAKGGRGKKGGGFATVS--SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVD 686
Cdd:cd14895 552 GKTSDAHLRELFEFfKASESAELSLGQPKLRRRSSVLSSVGigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 687 AHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILnpkgikgIEDPKKCTKVLIESTE-LNDDQYRLGNTKVFFR 765
Cdd:cd14895 632 MAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL-------VAAKNASDATASALIEtLKVDHAELGKTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-763 |
7.80e-121 |
|
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: 397.05 E-value: 7.80e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRG-KRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATvGASKKTDeaakskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS-AKSGNMD------LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVP---------GVKDICLLTDNIYDyhivsqgkvtVASIDDAEEFS 329
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSemkskyhllGLKEYKFLNPKCLD----------VPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 330 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKF---KQRGREEQAEQDGEEEG--GRVSKLFGCDTAELYKNLLKPRIK 404
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgkTEQGVDDAAAISNESLEvfKEACSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 405 VGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKL 484
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEML 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 485 QQFFNHHMFVLEQEEYQREGIEWTFIDFGMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLtNTHLGKSAPFQK 564
Cdd:cd14876 384 QKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSAC-VSKLKSNGKFKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 565 PKPPKPGQqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD---HAGQSGGGEqakggrgkk 641
Cdd:cd14876 463 AKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGvvvEKGKIAKGS--------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 642 gggfaTVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 721
Cdd:cd14876 530 -----LIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLY 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 24584706 722 RYQILNPkGI---KGIEDPKKCTKvLIESTELNDDQYRLGNTKVF 763
Cdd:cd14876 605 QFKFLDL-GIandKSLDPKVAALK-LLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-724 |
2.28e-112 |
|
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: 375.20 E-value: 2.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMY----------RGKRRNEVPPHIFAISDGAYVDMLT 168
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 169 NHVNQSMLITGESGAGKTENTKKVIAYFA---------TVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDN 239
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 240 SSRFGKFIRIHF-GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGV----KDICLLTDNIYDYHIVSQ 314
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVskeqKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 315 GKVTVA--SIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQ--RGREEQAEQDGE----------EEG 380
Cdd:cd14899 241 SLCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEArvmssttgafDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 381 GRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL-------------- 446
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 447 -DTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGMDlQLCIDLIE- 524
Cdd:cd14899 401 vDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 525 KPMGILSILEEESMFPKATDQTFSEKLTnTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDT 604
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYY-LEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCES 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 605 VVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFA-------TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPN 677
Cdd:cd14899 559 AAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPN 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 24584706 678 EMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQ 724
Cdd:cd14899 639 DSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
100-763 |
3.72e-111 |
|
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: 369.95 E-value: 3.72e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRR-NEVPPHIFAISDGAY--VDMLTNHVNQSM 175
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYrnVKSLIEPVNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 176 LITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 255
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 256 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIyDYHIVSQGKVTVasidDAEEFSLTDQAF 335
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGA-AFSWLPNPERNL----EEDCFEVTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 336 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQ--DGEEEGGRVSK-LFGCDTAELYKNLLKPRIKVGNE---F 409
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQpmDDTKESVRTSAlLLKLPEDHLLETLQIRTIRAGKQqqvF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 410 VTQGRNVQQVTNSiGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 488
Cdd:cd14880 316 KKPCSRAECDTRR-DCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 489 NHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPKATdqtfSEKLTNTHLGKSAPFQKPKP 567
Cdd:cd14880 395 VAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPS----SAAQLQTRIESALAGNPCLG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 568 PKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKgggfAT 647
Cdd:cd14880 470 HNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPV----LT 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 648 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILN 727
Cdd:cd14880 546 VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 24584706 728 PKGIKGIEDPKKCTKvliesTELNDDQYRLGNTKVF 763
Cdd:cd14880 626 RLRPHTSSGPHSPYP-----AKGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
100-761 |
1.32e-109 |
|
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: 367.38 E-value: 1.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRN-EVPPHIFAISDGAYVDMLTNHVNQSMLI 177
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 178 TGESGAGKTENTKKVIAYFATVGASKKTDEAA--KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPT- 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 255 GKLAGADIETYLLEKARVISQ-QSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASI----------- 322
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 323 ----DDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFK--QRGREEQAEQDGEEEG-GRVSKLFGCDTAELY 395
Cdd:cd14906 241 nnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEedSDFSKYAYQKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 396 KNLLKPRIKVGNEFVTQGR--NVQQVTNSIGALCKGVFDRLFKWLVKKCNETL--DTQQ---------KRQHFIGVLDIA 462
Cdd:cd14906 321 QALLNRNLKAGGRGSVYCRpmEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFnqNTQSndlaggsnkKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 463 GFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIE-KPMGILSILEEESMFPK 541
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 542 ATDQTFSEKLTNTHlgksapFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF 621
Cdd:cd14906 480 GSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 622 ADHagqsgggEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLE 701
Cdd:cd14906 554 QQQ-------ITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLN 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 702 GIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPKKCTKVLI-ESTELNDDQYRLGNTK 761
Cdd:cd14906 627 TIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLIlQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
100-765 |
2.16e-105 |
|
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: 353.35 E-value: 2.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYyNKLIYTYS--GLFCVAINPYKRYPVYTNRCAKMYRGKRRNE-VPPHIFAISDGAYVDMLTNHV-NQSM 175
Cdd:cd14875 1 ATLLHCIKERF-EKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYLALPDPRlLPPHIWQVAHKAFNAIFVQGLgNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 176 LITGESGAGKTENTKKVIAYfatVGASKKTDEAAKSKGSLEDQVVQ----TNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 251
Cdd:cd14875 80 VISGESGSGKTENAKMLIAY---LGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 252 GPT-GKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGK------VTVASIDD 324
Cdd:cd14875 157 DPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNtfvrrgVDGKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 325 AEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQrGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLkprIK 404
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 405 VGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQ--KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNE 482
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 483 KLQQFFNHHMFVLEQEEYQREGIEWTFIDFGmDLQLCIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSap 561
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 562 fqKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgggeqakggrgkk 641
Cdd:cd14875 470 --PYFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 642 gGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 721
Cdd:cd14875 535 -RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 24584706 722 RYQILNPKGIKGIEDPKK----CTKVLIESTEL---NDDQYRLGNTKVFFR 765
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKyseaAKDFLAYYQRLygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
100-765 |
4.50e-105 |
|
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: 351.88 E-value: 4.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRN-----EVPPHIFAISDGAYVDMLTNHVNQ 173
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 174 SMLITGESGAGKTENTKKVIAYFAtVGASKKTDeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 253
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFA-YGHSTSST-------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 254 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTdNIYDYHIVSQGKV-TVASIDDAEEFSLTD 332
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFK-SLESYNFLNASKCyDAPGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 333 QAFDILgFTKQEKEDVYRITAAVMHMGGMKFKQ---RGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 409
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEegdMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 410 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFN 489
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 490 HHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLIEKP-MGILSILEEESMFPKATDQTFSEKlTNTHLgksapfQKPKPP 568
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSS-CKSKI------KNNSFI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 569 KPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGggeqakggrgKKGGGFatV 648
Cdd:cd14886 463 PGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDG----------NMKGKF--L 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 649 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQIL-- 726
Cdd:cd14886 531 GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILis 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 24584706 727 -NPKGIKGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14886 611 hNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
100-765 |
2.18e-102 |
|
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: 345.45 E-value: 2.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVgaskktdeAAKSKGSLEDQVVQ-TNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTA--------AGSVGGVLSVEKLNaALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPG-VKDicLLTDNIYDYHivSQGKVTVASIDD----AEEFSLTDQ 333
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAAlRTE--LHLNQLAESN--SFGIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 334 AFDILGFTKQEKEDVYRITAAVMHM---GGMKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 410
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLgaaGATKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 411 TQGRNVQQVTNS------------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------F 472
Cdd:cd01386 306 TTSSGQESPARSssggpkltgveaLEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGsqrgatF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 473 EQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEwtfIDFGmDLQLC----IDLIEK---------------PMGILSIL 533
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFD-LPELSpgalVALIDQapqqalvrsdlrdedRRGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 534 EEESMFPKATDQTFSEKLTnTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTVVDQFK 610
Cdd:cd01386 462 DEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 611 KSQNKllieiFADHAGQSgggeqakggrgkkgggfatVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGV------ 684
Cdd:cd01386 541 ESQKE-----TAAVKRKS-------------------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDErstssp 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 685 ------VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIE------DPKKCTKVLIESTELND 752
Cdd:cd01386 597 aagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevaDERKAVEELLEELDLEK 676
|
730
....*....|...
gi 24584706 753 DQYRLGNTKVFFR 765
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-765 |
4.35e-99 |
|
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: 334.86 E-value: 4.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYR---GKRRNEVPPHIFAISDGAYVDMLTNHVNQSML 176
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 177 ITGESGAGKTENTKKVIAYFatvgaskkTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 256
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHL--------TCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 257 -LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKDICLLTDNIYDYHIVSQG----KVTVASIDDAEEFSLT 331
Cdd:cd14878 153 hLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDG-LSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLNREKLAVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 332 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 411
Cdd:cd14878 232 KQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 412 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQF 487
Cdd:cd14878 312 RRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 488 FNHHMFVLEQEEYQREGI----------EWTFIDFgmdlqlcidLIEKPMGILSILEEESMFPKATDQTFSEKL------ 551
Cdd:cd14878 392 INEVLFLQEQTECVQEGVtmetayspgnQTGVLDF---------FFQKPSGFLSLLDEESQMIWSVEPNLPKKLqslles 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 552 TNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFadhagQSggg 631
Cdd:cd14878 463 SNTNAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF-----QS--- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 632 eqakggrgkkggGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFP 711
Cdd:cd14878 535 ------------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 712 NRMMYPDFKMRYQILN---PKGIKGIEDPKKCTKVLIESTElndDQYRLGNTKVFFR 765
Cdd:cd14878 603 VRLSFSDFLSRYKPLAdtlLGEKKKQSAEERCRLVLQQCKL---QGWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-728 |
6.44e-93 |
|
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: 314.14 E-value: 6.44e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYtnrCAKMYRGKRRNEVPPHIFAISDGAYVDMLTnHVNQSMLITGE 180
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGA---GAMKAYLKNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFAtvgaskktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFgpTGKLAGA 260
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 261 DIETYLLEKARVISQQSLERSYHIFYQIMSGsvpgvKDICLLTDNIyDYHIVSQGKVTVasIDDAEEFSLTDQAFDILGF 340
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCAS-----KRLNIKNDFI-DTSSTAGNKESI--VQLSEKYKMTCSAMKSLGI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 341 TK-QEKEDvyrITAAVMHMGGMKFKQRGREEQAEQDGEEEggrVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 419
Cdd:cd14898 219 ANfKSIED---CLLGILYLGSIQFVNDGILKLQRNESFTE---FCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 420 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQhfIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14898 293 RTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 500 YQREGIEWTFIDFgMDLQLCIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKppkpgqqaahFAI 579
Cdd:cd14898 371 YKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGFINTKARDK----------IKV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 580 AHYAGCVSYNITGWLEKNKDP------LNDTVVDQFKKSQnklLIEIFadhagqsgggeqakggrgkkgggfatvssayK 653
Cdd:cd14898 440 SHYAGDVEYDLRDFLDKNREKgqllifKNLLINDEGSKED---LVKYF-------------------------------K 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 654 EQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNP 728
Cdd:cd14898 486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-765 |
1.11e-90 |
|
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: 309.64 E-value: 1.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRcakmYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFatVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNT-------LWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKD-ICLLTDNIYDYhiVSQGKVTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNkYKIRSENEYKY--IVNKNVVIPEIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQeKEDVYRITAAVMHMGGMKFK---QRGREEQAEQDGEEEG--GRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 413
Cdd:cd14937 226 NMHDM-KDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNLElvNEISNLLGINYENLKDCLVFTEKTIANQKIEIP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 414 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd14937 305 LSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 494 VLEQEEYQREGIEWTFIDFGMDLQLcIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlgksaPFQKPKPPKPGQQ 573
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTNESI-IDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKF-----SKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 574 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQakggrgkkgggfATVSSAYK 653
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK------------NLITFKYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 654 EQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRIcRKGFPNRMMYPDFKMRYQILNPKGIK- 732
Cdd:cd14937 527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKd 605
|
650 660 670
....*....|....*....|....*....|....
gi 24584706 733 -GIEDPKKCTKVLieSTELNDDQYRLGNTKVFFR 765
Cdd:cd14937 606 sSLTDKEKVSMIL--QNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-765 |
2.52e-90 |
|
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: 311.20 E-value: 2.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRY--------YNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHV 171
Cdd:cd14887 1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 172 NQSMLITGESGAGKTENTKKVIAYFATVGASKKtdeAAKSKGsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRH---GADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 252 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVpgvkdiclltdniydyhiVSQGKVTVASIDDAEEFSL- 330
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAV------------------AAATQKSSAGEGDPESTDLr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 331 -TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDG--------EEEGGRVSKL--FGCDTAEL----- 394
Cdd:cd14887 219 rITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKltsvsvgcEETAADRSHSseVKCLSSGLkvtea 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 395 -YKNLLKPRIKVGNEFVTQGRN-------------------VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQK--- 451
Cdd:cd14887 299 sRKHLKTVARLLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpse 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 452 -----------RQHFIGVLDIAGFEIFE---YNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREG--IEWTFIDFGMD 515
Cdd:cd14887 379 sdsdedtpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 516 LQLCIDLIEKP------------------------MGILSILEEE-SMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKP 570
Cdd:cd14887 459 FPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 571 GQQAA---HFAIAHYAGCVSYNITGWLEKNKDPLNDTvVDQFKKSQNKLLIEIFADHagQSGggeqakggRGKKGGGFAT 647
Cdd:cd14887 539 PALSRenlEFTVSHFACDVTYDARDFCRANREATSDE-LERLFLACSTYTRLVGSKK--NSG--------VRAISSRRST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 648 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILN 727
Cdd:cd14887 608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
|
730 740 750
....*....|....*....|....*....|....*...
gi 24584706 728 PKGIKGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFR 765
Cdd:cd14887 688 PMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
97-764 |
5.59e-84 |
|
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: 290.22 E-value: 5.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 97 LNDASVLHNLRQRYYNKLIYTY---SGLfcVAINPYKRYPV--------YTNRCAKMYRGKRRnEVPPHIFAISDGAYVD 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKE-PLPPHAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 166 MLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKtdeaaksKGS-LEDQVVQTNPVLEAFGNAKTVRNDNSSRFG 244
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSK-------KGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 245 KFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNI-YDYHIVSQGKVTVAS-- 321
Cdd:cd14879 151 RYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSdYALLASYGCHPLPLGpg 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 322 IDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQrgreeqaEQDGEEEG---------GRVSKLFGCDTA 392
Cdd:cd14879 231 SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 393 EL-----YKNLLkprikVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL-DTQQKRQHFIGVLDIAGFEI 466
Cdd:cd14879 304 DLetsltYKTKL-----VRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 467 F---EYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFgMDLQLCIDLI-EKPMGILSILEEE-SMFPK 541
Cdd:cd14879 379 RsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQtRRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 542 ATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAhFAIAHYAGCVSYNITGWLEKNKDPLN-DTVvdqfkksqnKLLiei 620
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFIAVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVLSpDFV---------NLL--- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 621 fadhagqSGGGEQAKGgrgkkgggfatvssaykeqLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVL 700
Cdd:cd14879 525 -------RGATQLNAA-------------------LSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24584706 701 EGIRICRKGFPNRMMYPDFKMRYQILNPkgIKGIEDPKKCtkvLIESTELNDDQYRLGNTKVFF 764
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR--GSAAERIRQC---ARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-714 |
1.23e-73 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 260.99 E-value: 1.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNE-------VPPHIFAISDGAYVDMLTNHV 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 172 NQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEaakskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTE-------RIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 252 ---------GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIV---------- 312
Cdd:cd14884 154 eeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 313 SQGKVTVASID----------DAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQrgreeqaeqdgeeeggr 382
Cdd:cd14884 234 VKGTLRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 383 VSKLFGCDTAELyKNLLKPR-IKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL------------DTQ 449
Cdd:cd14884 297 AAECLQIEEEDL-ENVIKYKnIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 450 QKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIdfgmDLQLCIDLIEKPMGI 529
Cdd:cd14884 376 SINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIFIAKI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 530 LSILEEESMFP----KATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAH-----------FAIAHYAGCVSYNITGWL 594
Cdd:cd14884 452 FRRLDDITKLKnqgqKKTDDHFFRYLLNNERQQQLEGKVSYGFVLNHDADGtakkqnikkniFFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 595 EKNKDPLNDTVVDQFKKSQNKLLIEifADHAGQSGggeqakggrgkkggGFATVSSAYKEQLNSLMTTLRSTQPHFVRCI 674
Cdd:cd14884 532 DKNSDKIETSIETLISCSSNRFLRE--ANNGGNKG--------------NFLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 24584706 675 IPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRM 714
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
101-765 |
1.01e-71 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 255.02 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYrgKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 179
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 180 ESGAGKTENTKKVIAYFATVGASKKTdeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 259
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSK--------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 260 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDnIYDYHIVSQ-GKVTVASIDDAEEFSLTDQAFDIL 338
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGD-INSYHYLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 339 GFTKQEKEDVYRITAAVMHMGGMKFKQR-GREEQAEQDGEEEggrVSKLFGCDTAELYKNLLKPRIKVGNEFVtQGRNvq 417
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKnGKTEVKDRTLIES---LSHNITFDSTKLENILISDRSMPVNEAV-ENRD-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 418 qvtnsigALCKGVFDRLFKWLVKKCNETLDTQQkRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14905 305 -------SLARSLYSALFHWIIDFLNSKLKPTQ-YSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 498 EEYQREGIEW-TFIDFgMDLQLCIDLIEKpmgILSILEEESMFPKATDQTFSEKLTN----THL-GKSAPFqkpkppkpg 571
Cdd:cd14905 377 REYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNflsrHHLfGKKPNK--------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 572 qqaahFAIAHYAGCVSYNITGWLEKNKDP-------------------------LNDTV--VDQFKKSQN---------- 614
Cdd:cd14905 444 -----FGIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVaeLNQMFDAKNtakksplsiv 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 615 KLLIEIFA----------DHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSlmttlrSTQPHFVRCIIPNEMKQPGV 684
Cdd:cd14905 519 KVLLSCGSnnpnnvnnpnNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNS------NCDFHFIRCIKPNSKKTHLT 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 685 VDAHLVMHQLTCNGVLEGIRICRKGFP----NRMMYPDFKMRYQilNPKGIKGIEDPKKCTKVLIESteLNDDQYRLGNT 760
Cdd:cd14905 593 FDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRFSFFFQ--NQRNFQNLFEKLKENDINIDS--ILPPPIQVGNT 668
|
....*
gi 24584706 761 KVFFR 765
Cdd:cd14905 669 KIFLR 673
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
99-764 |
5.61e-69 |
|
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: 245.79 E-value: 5.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 99 DAsVLHNLRQRYYNKLIYTYSGLFCVAINPYkrypvytnrcakMYRGKRRNEVPPHifAISDGAYVDML----------T 168
Cdd:cd14881 1 DA-VMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTR--SSPLAPQLLKVvqeavrqqseT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 169 NHvNQSMLITGESGAGKTENTKKVI-AYFATVGASKKTDeAAKskgsledQVVQTNPVLEAFGNAKTVRNDNSSRFGKFI 247
Cdd:cd14881 66 GY-PQAIILSGTSGSGKTYASMLLLrQLFDVAGGGPETD-AFK-------HLAAAFTVLRSLGSAKTATNSESSRIGHFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 248 RIHFgPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTD-NIYDYHIVSQGKVTVASIDDAE 326
Cdd:cd14881 137 EVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 327 EFSLTDQAFDILG--FTkqekeDVYRITAAVMHMGGMKFKQRGrEEQAEQDGEEEGGRVSKLFGCDTAELYKNLlkprik 404
Cdd:cd14881 216 RFQAWKACLGILGipFL-----DVVRVLAAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGL------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 405 vgnefVTQGRNVQ-QVTNSI----------GALCKGVFDRLFKWLVKKCNE------TLDTQqKRQHFIGVLDIAGFEIF 467
Cdd:cd14881 284 -----TTRTHNARgQLVKSVcdanmsnmtrDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDGFIGILDMFGFEDP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 468 EYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIewtfidfGMDLQL-------CIDLIEK-PMGILSILEEESMf 539
Cdd:cd14881 358 KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGI-------QCEVEVdyvdnvpCIDLISSlRTGLLSMLDVECS- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 540 PKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKsqnkllie 619
Cdd:cd14881 430 PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRM-----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK-------- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 620 ifadHAGQSGggeqakggrgkkgggFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGV 699
Cdd:cd14881 497 ----QNCNFG---------------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQV 557
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 700 LEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPKK--CTKVLIESTELNDDQ--------YRLGNTKVFF 764
Cdd:cd14881 558 LETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKAleDCALILQFLEAQPPSklssvstsWALGKRHIFL 632
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-765 |
1.11e-67 |
|
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: 242.08 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 100 ASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYrgkrrnevppHIFAISDGAYVDMLTNHVNQSMLI-T 178
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 179 GESGAGKTENTKKVIAYFATVGASKKTdeaAKSKGSLEDqvvqtnpVLEAFGNAKTVRNDNSSRFGKFIRIHFgPTGKLA 258
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVT---TKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 259 GADIE-TYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDnIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDI 337
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKG-LQKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 338 LGFTKQEKEDVYRITAAVMHMGGMKFKQRgREEQAEQDGEEEGGR-----VSKLFGCDTAELYkNLLKPRIKVGNEFvtq 412
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMsevkwVAFLLEVDFDQLV-NFLLPKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 413 grNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQkRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHM 492
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 493 FVLEQEEYQREGIEWTF-----IDFGMDLQLcidLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKP 567
Cdd:cd14874 371 FHDQLVDYAKDGISVDYkvpnsIENGKTVEL---LFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNK 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 568 PKPGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgggeqakggrgkkGGGFAT 647
Cdd:cd14874 448 ERLE-----FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNT-------------SDMIVS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 648 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILN 727
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
650 660 670
....*....|....*....|....*....|....*....
gi 24584706 728 PKGIKGIEDPKKCTKVLIESTELN-DDQYRLGNTKVFFR 765
Cdd:cd14874 590 PGDIAMCQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-764 |
5.60e-63 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 230.63 E-value: 5.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 103 LHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRR----------NEVPPHIFAISDGAYVDMLTNHVN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 173 QSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKG----SLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIR 248
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASgvlhPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 249 IHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSV--PGVKDICLLTDNIYDYHIVSQGKVTVASID-DA 325
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 326 EEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKqrgreEQAEQDGEEEGGR---VSKLFGC---DTAEL----- 394
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFV-----PDPEGGKSVGGANsttVSDAQSCalkDPAQIllaak 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 395 --------YKNLLKPR---IKVGNEFVTQGR--NVQQVTNSIGALCKGVFDRLFKWLVKKCNETL----DTQQKRQHFIG 457
Cdd:cd14893 319 llevepvvLDNYFRTRqffSKDGNKTVSSLKvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 458 -----VLDIAGFEIFE--YNGFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYQREG--IEWTFIDFGMDLQLCIDLI 523
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 524 E-KPMGILSILEEESMFPKATDQTFSEKL--TNTHLGKSAPFQKPKPPKPGQQAAH------FAIAHYAGCVSYNITGWL 594
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLfsGNEAVGGLSRPNMGADTTNEYLAPSkdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 595 EKNKDPLNDTVVDQFKKSQNKLLIEIFADH--AGQSGGGEQAKGGRGKKGGGFATVSSAYKE--------------QLNS 658
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaAASSEKAAKQTEERGSTSSKFRKSASSAREsknitdsaatdvynQADA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 659 LMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQilNPKGIKGIEDpk 738
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK--NVCGHRGTLE-- 714
|
730 740
....*....|....*....|....*.
gi 24584706 739 KCTKVLIESTELNDDQYRLGNTKVFF 764
Cdd:cd14893 715 SLLRSLSAIGVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-765 |
6.44e-61 |
|
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: 222.31 E-value: 6.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 180
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 181 SGAGKTENTKKVIAYFATVGaskktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 260
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---------DGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 261 DIETYLLEKARVISQQSLERSYHIFYQIMSG--SVPGVKDICLLTDNIYDYHIVSQG-------KVTVASIDDAEEFSLT 331
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRNYRYLRIPPEvppsklkYRRDDPEGNVERYKEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 332 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREeqAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 411
Cdd:cd14882 233 EEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 412 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQK---RQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 488
Cdd:cd14882 311 RKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 489 NHHMFVLEQEEYQREGIEWTFIDFgMDLQLCID-LIEKPMGILSILEEESMFPKATD---QTFSEKlTNTHLGKSApfqk 564
Cdd:cd14882 391 NQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDDASRSCQDQNyimDRIKEK-HSQFVKKHS---- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 565 pkppkpgqqAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADhagqsgggeqakggrgKKGGG 644
Cdd:cd14882 465 ---------AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN----------------SQVRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 645 FATVSSAYK----EQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 720
Cdd:cd14882 520 MRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFL 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 24584706 721 MRYQILNPKGIKGIEDPK-KCTKVLIestELNDDQYRLGNTKVFFR 765
Cdd:cd14882 600 RRYQFLAFDFDETVEMTKdNCRLLLI---RLKMEGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-249 |
1.54e-51 |
|
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: 179.46 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 122 FCVAINPYKRYPVYTN-RCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVG 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 201 ASKKTD-------EAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 249
Cdd:cd01363 81 FNGINKgetegwvYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-763 |
3.95e-44 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 173.10 E-value: 3.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 101 SVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNE---VPPHIFAISDGAYVDMLTNhvNQSMLI 177
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdlsLNEYHVVHNALKNLNELKR--NQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 178 TGESGAGKTENTKKVIAYFA---------------TVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSR 242
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAyqvkgsrrlptnlndQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 243 FGKFIRIHFgPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTdNIYDYHIVSQGKVTVASI 322
Cdd:cd14938 160 FSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 323 DDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGG-------------MKFKQRGRE----------EQAEQDGEEE 379
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 380 GGR----VSKLFGCDTAELYKNLLKPRIkVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQ-- 453
Cdd:cd14938 318 NVKnlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNINin 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 454 -HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGMD-LQLCIDLIEKPMGILS 531
Cdd:cd14938 397 tNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 532 ILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKK 611
Cdd:cd14938 477 SLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT--FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 612 SQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAY-----------KEQLNSLMTTLRSTQPHFVRCIIPNEMK 680
Cdd:cd14938 555 SENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYdtknqmavsllRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 681 QP-GVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNpkgikgiEDPKKCTKVLIESTELNDDQYRLGN 759
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN-------EDLKEKVEALIKSYQISNYEWMIGN 707
|
....
gi 24584706 760 TKVF 763
Cdd:cd14938 708 NMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
906-1849 |
2.69e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 131.33 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 906 KLTAQKNDLENQLRDIQERLTQEEDARNQLfqqkkkadqeisglKKDIEDLELNVQKAEQDKATKDhQIRNLNDEIahqd 985
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNEL--------------ERQLKSLERQAEKAERYKELKA-ELRELELAL---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 986 eLINKLNKEKkmqgetnqktgEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAV 1065
Cdd:TIGR02168 230 -LVLRLEELR-----------EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1066 ADLERNKKELEQTIQRKDKELSSITAKLEdeqvvvlKHQRQIKELQARIeeleeeveaerqarAKAEKQRADLAreleel 1145
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLE-------ELESKLDELAEEL--------------AELEEKLEELK------ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1146 gerleeaggatsAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKhndaVAEMAEQVDQLNKLKAKAEKekneyyg 1225
Cdd:TIGR02168 351 ------------EELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEA------- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1226 QLNDLRAGVDHITNEKAAQEKiaKQLQHTLNEVQSKLDETNRTLNDFDAskkklsiENSDLLRQLEEAESQVSQLskiki 1305
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQE-------ELERLEEALEELREELEEA----- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1306 slTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAqvwrsKYESdgvARSEEL 1385
Cdd:TIGR02168 474 --EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE-----GYEA---AIEAAL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1386 EEAkrkLQA----RLAEAEETIESLNQKCIG------LEKTKQRLSTEVEDLQLE-VDRANAIANAAEKKQKAFDKIIGE 1454
Cdd:TIGR02168 544 GGR---LQAvvveNLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDREILKnIEGFLGVAKDLVKFDPKLRKALSY 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1455 W---KLKVDDLAAELDASQKECRNYST-----ELFRLKGAYEEGQEQLEAVRRENKNladEVKDLLDQIGEGGRNIHEIE 1526
Cdd:TIGR02168 621 LlggVLVVDDLDNALELAKKLRPGYRIvtldgDLVRPGGVITGGSAKTNSSILERRR---EIEELEEKIEELEEKIAELE 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1527 KARKRLEAEkdelqaaleeaeaaleqeenkvlraQLELSQVRQEIDRRIQEKEEEFENTRKNHQRAldsmQASLEAEAKG 1606
Cdd:TIGR02168 698 KALAELRKE-------------------------LEELEEELEQLRKELEELSRQISALRKDLARL----EAEVEQLEER 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1607 KAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEE 1686
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1687 SRtlleqadRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLAD 1766
Cdd:TIGR02168 829 LE-------RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1767 ELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANalkggkkaIQKLEQRVRELEN-ELDGEQRRHADAQKNLRKSERR 1845
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVR--------IDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRR 973
|
....
gi 24584706 1846 VKEL 1849
Cdd:TIGR02168 974 LKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1165-1889 |
3.15e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.87 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1165 KREAELSKLRRDLEEANIQHESTLANLRKK-HNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAgvdhitnEKAA 1243
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1244 QEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESR 1323
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1324 ERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEE-----------AKRKL 1392
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEieellkkleeaELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1393 QARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKE 1472
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1473 CRNYST--ELFRLKGAYEE-----GQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEE 1545
Cdd:TIGR02168 519 SGILGVlsELISVDEGYEAaieaaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1546 AEAALEQEENKV---LRAQLE--LSQVR------QEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMK 1614
Cdd:TIGR02168 599 GFLGVAKDLVKFdpkLRKALSylLGGVLvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1615 -KKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQ 1693
Cdd:TIGR02168 679 iEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1694 ADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQD 1773
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1774 HAQTQEKLRKALEQQIKELQVRLDEAEANALKgGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQS 1853
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740 750
....*....|....*....|....*....|....*.
gi 24584706 1854 EEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAA 1889
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
840-1714 |
2.67e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.78 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 840 NVSRIED---EIAR----LEEKAKKAEELHAaevkVRKELEALnakllaEKTALLDSLSGEKGALQDYQERNAKLTAQKN 912
Cdd:TIGR02168 187 NLDRLEDilnELERqlksLERQAEKAERYKE----LKAELREL------ELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 913 DLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLN 992
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 993 KEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNK 1072
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1073 KELEQTIQRKDKELSS-----ITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGE 1147
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1148 RLEEAGGATS--AQIELNKKREAELSKLRRDLEEANIQHESTLAN-LRKKHNDAVAEMAEQVDQ---------------- 1208
Cdd:TIGR02168 497 LQENLEGFSEgvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAaLGGRLQAVVVENLNAAKKaiaflkqnelgrvtfl 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1209 ---LNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTL--------NEVQSKLDETNR--TLNDFDAS 1275
Cdd:TIGR02168 577 pldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddldnaLELAKKLRPGYRivTLDGDLVR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1276 KKKLSIENSDllrqlEEAESQVSQLSKIKIsLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEeaegkad 1355
Cdd:TIGR02168 657 PGGVITGGSA-----KTNSSILERRREIEE-LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE------- 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1356 LQRQLSKANAEAQVWRskyesdgvARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRAN 1435
Cdd:TIGR02168 724 LSRQISALRKDLARLE--------AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1436 AIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRREnknladevkdlldqI 1515
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--------------I 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1516 GEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDR------RIQEKEEEFENTRKNH 1589
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNL 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1590 QRALdSMQASLEAEakgkaEALRMKKKLEADINELEIALdhankanaeaqKNIKRYQQQLKDIQTALEEEQRArddareq 1669
Cdd:TIGR02168 942 QERL-SEEYSLTLE-----EAEALENKIEDDEEEARRRL-----------KRLENKIKELGPVNLAAIEEYEE------- 997
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 24584706 1670 lgISERRA--NALQNELEESRTLLEQA-DRGRRQAEQELADAHEQLNE 1714
Cdd:TIGR02168 998 --LKERYDflTAQKEDLTEAKETLEEAiEEIDREARERFKDTFDQVNE 1043
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1318-1883 |
5.02e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.43 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1318 ADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRskyesdgvARSEELEEAKRKLQARLA 1397
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------LELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1398 EAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKafdkiigEWKLKVDDLAAELDASQKECRNYS 1477
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE-------ELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1478 TELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEeaeaaleqeenKV 1557
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-----------EL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1558 LRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIAL----DHANK 1633
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgfleGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1634 ANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADR--GRRQAEQELADAHEQ 1711
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1712 LNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKE 1791
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1792 LQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDL----- 1866
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeeeal 753
|
570 580
....*....|....*....|....*
gi 24584706 1867 --------VDKLQQKIKTYKRQIEE 1883
Cdd:COG1196 754 eelpeppdLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1164-1824 |
1.57e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1164 KKREAELSKLRRDLEEANIQ-HESTLANLRKKHNDAVAEMAE---QVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITN 1239
Cdd:COG1196 223 KELEAELLLLKLRELEAELEeLEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1240 EKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLAD 1319
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1320 EESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQvwrskyesDGVARSEELEEAKRKLQARLAEA 1399
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA--------ELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1400 EETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKecrnysTE 1479
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV------AV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1480 LFRLKGAYEEGQEQLEAVRRENKNLADEvKDLLDQIgeggrnihEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLR 1559
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDD-EVAAAAI--------EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1560 AQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALdsmqaSLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQ 1639
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLE-----AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1640 KNIKRYQQQLKDIQTALEEEQR-ARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQ 1718
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEeALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1719 NASISAAKRKLESELQTLHSDLDELlnEAKNseekakkamvdaarladeLRAEQDHAQTQEKLRkALEQQIKELQvrlde 1798
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEAL--GPVN------------------LLAIEEYEELEERYD-FLSEQREDLE----- 808
|
650 660
....*....|....*....|....*.
gi 24584706 1799 aeanalkggkKAIQKLEQRVRELENE 1824
Cdd:COG1196 809 ----------EARETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
840-1451 |
8.74e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.03 E-value: 8.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 840 NVSRIED---EIAR----LEEKAKKAE---ELHAAEVKVRKELEALNAKLLAEKTALLDSlsgekgALQDYQERNAKLTA 909
Cdd:COG1196 187 NLERLEDilgELERqlepLERQAEKAEryrELKEELKELEAELLLLKLRELEAELEELEA------ELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 910 QKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELIN 989
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 990 KLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLE 1069
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1070 RNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERL 1149
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1150 EEAGGATSAQIELNKKREA-----ELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQ--------------LN 1210
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLrglagAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEylkaakagratflpLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1211 KLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQL 1290
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1291 EEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLS--KANAEAQ 1368
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEaeREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1369 VWRSKYESDGVARSEELEEAKR-KLQARLAEAEETIESL---NQKCIG-LEKTKQR---LSTEVEDLQLEVDR-ANAIAN 1439
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLeELERELERLEREIEALgpvNLLAIEeYEELEERydfLSEQREDLEEARETlEEAIEE 820
|
650
....*....|....*.
gi 24584706 1440 A-AEKKQK---AFDKI 1451
Cdd:COG1196 821 IdRETRERfleTFDAV 836
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1225-1887 |
1.29e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 106.31 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1225 GQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLR-QLEEAESQVSQLSKi 1303
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLER- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1304 kislttQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGvARSE 1383
Cdd:TIGR02169 309 ------SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1384 ELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRA----NAIANAAEKKQKAFDKIigEWKLKv 1459
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIeakiNELEEEKEDKALEIKKQ--EWKLE- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1460 dDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEV---KDLLDQIGEGGRNIH------------- 1523
Cdd:TIGR02169 459 -QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggRAVEEVLKASIQGVHgtvaqlgsvgery 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1524 --EIEKAR-KRLEA---EKDELQAALEEAEAALEQEE------NKVLRAQLELSQVRQE--IDRRIQ--EKEEEFENTRK 1587
Cdd:TIGR02169 538 atAIEVAAgNRLNNvvvEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEDgvIGFAVDlvEFDPKYEPAFK 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1588 NHQR---ALDSMQA-----------SLEAE----------------------AKGKAEALRMKKKLEADINELEIAldha 1631
Cdd:TIGR02169 618 YVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSL---- 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1632 nkanaeaqknikryQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQ 1711
Cdd:TIGR02169 694 --------------QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1712 LNEVSAQNASISAAKRKLESELQTL-----HSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALE 1786
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1787 QQIKELQVRLDE--AEANALKGGKKAIQ----KLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNH 1860
Cdd:TIGR02169 840 EQRIDLKEQIKSieKEIENLNGKKEELEeeleELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
730 740
....*....|....*....|....*..
gi 24584706 1861 ERMQDLVDKLQQKIKTYKRQIEEAEEI 1887
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1003-1883 |
4.69e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.38 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1003 QKTGEELQAAEDKINHLNKVKAKLEQTLDELEDslEREKKVR-GDVEKSKRKVEGDLKLTQeaVADLERNKKELEQTIQR 1081
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRR--EREKAERyQALLKEKREYEGYELLKE--KEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1082 KDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEveaeRQARAKAEKqradlareleelgerleeagGATSAQIE 1161
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE----EQLRVKEKI--------------------GELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1162 LNKKREAELSKLRRDLEEANIQHESTLANLRKKHndavAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEK 1241
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1242 AAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEE 1321
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1322 SRERATLLGKFRNLEHDLDnlreQVEEEAEgkaDLQRQLSKANAEAQVWRSkYESDGVARSEELEEAKR----------K 1391
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYD----RVEKELS---KLQRELAEAEAQARASEE-RVRGGRAVEEVLKASIQgvhgtvaqlgS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1392 LQARLAEAEETI------------ESLNQKCIGLEKTKQ--RLS----TEVEDLQLEVD---RANAIANAA------EKK 1444
Cdd:TIGR02169 533 VGERYATAIEVAagnrlnnvvvedDAVAKEAIELLKRRKagRATflplNKMRDERRDLSilsEDGVIGFAVdlvefdPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1445 QKAFDKIIGEwKLKVDDLAA-----------------------------ELDASQKECRNYSTELFRLKGAYEEGQEQLE 1495
Cdd:TIGR02169 613 EPAFKYVFGD-TLVVEDIEAarrlmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1496 AVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDElqaaleeaeaaleqeenkvLRAQLElsqvrqEIDRRI 1575
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK-------------------LKERLE------ELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1576 QEKEEEFENtrknhqraLDSMQASLEAEAKGKAEALrmkKKLEADINELEIALDHankanaeaqKNIKRYQQQLKDIqta 1655
Cdd:TIGR02169 747 SSLEQEIEN--------VKSELKELEARIEELEEDL---HKLEEALNDLEARLSH---------SRIPEIQAELSKL--- 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1656 leEEQRARDDAreqlgiserRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQT 1735
Cdd:TIGR02169 804 --EEEVSRIEA---------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1736 LHSDLDELLNEAKNSEEKAKkamvdaaRLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANalkggkkaIQKLE 1815
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERD-------ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE--------LSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1816 QRVRELEnELDGEQRRHADAQKNLRKSERRVKEL---SFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEE 1883
Cdd:TIGR02169 938 DPKGEDE-EIPEEELSLEDVQAELQRVEEEIRALepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1572-1932 |
6.76e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1572 DRRIQEKEEEFENTRKNHQRA------LDSMQASLEAEAKgKAE-ALRMKKKL-EADINELEIALDHANKANAEAQKNIK 1643
Cdd:COG1196 171 KERKEEAERKLEATEENLERLedilgeLERQLEPLERQAE-KAErYRELKEELkELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1644 RYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASIS 1723
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1724 AAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAmvdAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEAna 1803
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEA---EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1804 lkggkkAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEE 1883
Cdd:COG1196 405 ------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24584706 1884 AEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGA 1932
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1386-1925 |
7.36e-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: 7.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1386 EEAKRKL---QARLAEAEETIESLNQKCIGLEK------TKQRLSTEVEDLQLEVdRANAIANAAEKKQKAfDKIIGEWK 1456
Cdd:COG1196 175 EEAERKLeatEENLERLEDILGELERQLEPLERqaekaeRYRELKEELKELEAEL-LLLKLRELEAELEEL-EAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1457 LKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEK 1536
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1537 DELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEfentrknhqraldsmQASLEAEAKGKAEALRMKKK 1616
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---------------EEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1617 LEADINELEIALdhankanAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADR 1696
Cdd:COG1196 398 LAAQLEELEEAE-------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1697 GRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQT----LHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQ 1772
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1773 DHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADA---------------QK 1837
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryyvlgdtllgrtlvAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1838 NLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAIS 1917
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
....*...
gi 24584706 1918 KFRAKGRA 1925
Cdd:COG1196 711 EAEEERLE 718
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1105-1886 |
2.11e-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: 95.91 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1105 RQIKELQARIEELEeeveaerqarAKAEKQRADLARELEELGErleeaggatsAQIELNKKREaELSKLRRDLEEAniqh 1184
Cdd:TIGR02169 156 RKIIDEIAGVAEFD----------RKKEKALEELEEVEENIER----------LDLIIDEKRQ-QLERLRREREKA---- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1185 ESTLANLRKKHNDAVAEMAeqvdqlnklkakaekekneyyGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDE 1264
Cdd:TIGR02169 211 ERYQALLKEKREYEGYELL---------------------KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1265 TNRTLNDFDASKKKLSIENSDLLR-QLEEAESQVSQLSKikislttQLEDTKRLADEESRERATLLGKFRNLEHDLDNLR 1343
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLER-------SIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1344 EQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGvARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTE 1423
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1424 VEDLQLEVDRA----NAIANAAEKKQKAFDKIigEWKLKvdDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRR 1499
Cdd:TIGR02169 422 LADLNAAIAGIeakiNELEEEKEDKALEIKKQ--EWKLE--QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1500 ENKNLADEV---KDLLDQIGEGGRNIH---------------EIEKAR-KRLEA---EKDELQAALEEAEAALEQEE--- 1554
Cdd:TIGR02169 498 QARASEERVrggRAVEEVLKASIQGVHgtvaqlgsvgeryatAIEVAAgNRLNNvvvEDDAVAKEAIELLKRRKAGRatf 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1555 ---NKVLRAQLELSQVRQE--IDRRIQ--EKEEEFENTRKNHQRALDSMQaSLEAeAKGKAEALRMkKKLEADINELEIA 1627
Cdd:TIGR02169 578 lplNKMRDERRDLSILSEDgvIGFAVDlvEFDPKYEPAFKYVFGDTLVVE-DIEA-ARRLMGKYRM-VTLEGELFEKSGA 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1628 LDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELAD 1707
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1708 AHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELlnEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQ 1787
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1788 QIKELQVRLdEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLV 1867
Cdd:TIGR02169 813 RLREIEQKL-NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
810
....*....|....*....
gi 24584706 1868 DKLQQKIKTYKRQIEEAEE 1886
Cdd:TIGR02169 892 DELEAQLRELERKIEELEA 910
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
978-1891 |
4.46e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 978 NDEIAHQDELINkLNKEKKMQGETNQKTgeelQAAEDKINHlnkvKAKLEQTLDELEDSLEREKkvrgdVEKSKRKVEgD 1057
Cdd:PTZ00121 1038 NDDVLKEKDIID-EDIDGNHEGKAEAKA----HVGQDEGLK----PSYKDFDFDAKEDNRADEA-----TEEAFGKAE-E 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1058 LKLTQEAVADLERNKKEleqtIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQ-ARIEELEEEVEAERQARAKAEKQRA 1136
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEE----AKKKAEDARKAEEARKAEDARKAEEARKAEDAKrVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1137 DLARELEELGERLEEAGGATSAQIELNKKREAE--LSKLRRDLEEANIQHESTLANLRKKHNDAvaEMAEQVDQLNKLKA 1214
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEErkAEEARKAEDAKKAEAVKKAEEAKKDAEEA--KKAEEERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1215 KAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDEtnrtlndfdaSKKKlsienSDLLRQLEEAE 1294
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE----------AKKK-----AEEAKKADEAK 1321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1295 SQVSQLSKIKISLTTQLEDTKRlADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKY 1374
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKK-AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1375 ESDGvARSEEL---EEAKRKLQARLAEAEETIESLNQKCIGLEKTKqrlSTEVEDLQLEVDRANAIANAAEKKQKAFD-K 1450
Cdd:PTZ00121 1401 EEDK-KKADELkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEAKKAEEAKKKAEEAKKADEaK 1476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1451 IIGEWKLKVDDLAAELDASQKECRnystelfRLKGAYEEGQEQLEAVRRENKNLADEVKDlldqiGEGGRNIHEIEKARK 1530
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKAD-------EAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1531 RLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEA 1610
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1611 LRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRtl 1690
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-- 1702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1691 leQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESE---LQTLHSDLDELLNEAKNSEEKAKKAmvDAARLADE 1767
Cdd:PTZ00121 1703 --KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKA--EEIRKEKE 1778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1768 LRAEQDHAQTQEKLRKALEQQIKELQvrldEAEANALKGGKKAiqklEQRVRELENELDGEQRRHADAQKNLRKSERRVK 1847
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDIF----DNFANIIEGGKEG----NLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 24584706 1848 ELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALN 1891
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
187-707 |
4.29e-18 |
|
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: 91.34 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 187 ENTKKVIAYFATVGASKKTDeaakskgsledQVVQTNPVLEAFGNAKTVRNDNSSRFGKF--IRIHFGPTG---KLAGAD 261
Cdd:cd14894 228 EDEEQLRMYFKNPHAAKKLS-----------IVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCH 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 262 IETYLLEKARVISQQSLER------SYHIFYQIMSG--SVPGVKDIC--LLTDNIYDYHIVSQGKVT------VASID-- 323
Cdd:cd14894 297 ISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGvnAFPFMRLLAkeLHLDGIDCSALTYLGRSDhklagfVSKEDtw 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 324 --DAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQR---GREEQAEQDGEEEGGRVSKLFGCDTAELYKNL 398
Cdd:cd14894 377 kkDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWLGNIELDYRevsGKLVMSSTGALNAPQKVVELLELGSVEKLERM 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 399 LKPR---IKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNE-----TLDTQQKRQH------------FIGV 458
Cdd:cd14894 457 LMTKsvsLQSTSETFEVTLEKGQVNHVRDTLARLLYQLAFNYVVFVMNEatkmsALSTDGNKHQmdsnasapeavsLLKI 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 459 LDIAGFEIFEYNGFEQLCINFTNEKLqqfFNHHMFVLEQEEYQREGIewtfidFGMDLQLCIDLI-EKPMGILSILEEES 537
Cdd:cd14894 537 VDVFGFEDLTHNSLDQLCINYLSEKL---YAREEQVIAVAYSSRPHL------TARDSEKDVLFIyEHPLGVFASLEELT 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 538 MFPKATDQTFSEKLTNTHL------GKSAPFQKPKPPKPGQQAAH---------FAIAHYAGCVSYNITGWLEKNKDPLN 602
Cdd:cd14894 608 ILHQSENMNAQQEEKRNKLfvrniyDRNSSRLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVY 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 603 DTVVDQFKKSQNKLLIEIFaDHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRS----TQPHFVRCIIPNE 678
Cdd:cd14894 688 ANLLVGLKTSNSSHFCRML-NESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSqddkNMPFYFHCIRPNA 766
|
570 580
....*....|....*....|....*....
gi 24584706 679 MKQPGVVDAHLVMHQLTCNGVLEGIRICR 707
Cdd:cd14894 767 KKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
797-1526 |
6.34e-18 |
|
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: 90.90 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 797 RKGFKKLQEQRVAL---KVVQRNLRKYLQlrtwpWYKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAaevKVRKELE 873
Cdd:TIGR02169 197 RQQLERLRREREKAeryQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLEEELEKLTEEIS---ELEKRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 874 ALNAKLLAEKTALLDSLSGEKGALQdyqERNAKLTAQKNDLENQLRDIQERLtqeEDARNQLfqqkKKADQEISGLKKDI 953
Cdd:TIGR02169 269 EIEQLLEELNKKIKDLGEEEQLRVK---EKIGELEAEIASLERSIAEKEREL---EDAEERL----AKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 954 EDLELNVQKAEQDKATKDHQIRNLNDEIahqDELINKLNKEKKMQGETNQKTG---EELQAAEDKINHLNKVKAKLEQTL 1030
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1031 DELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKEL 1110
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1111 QARIEELEEEVEAERQARAKAEKQR-------ADLARELEELGERLEEAGGA------------TSAQIELNKKREA--- 1168
Cdd:TIGR02169 496 EAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNrlnnvvveddavAKEAIELLKRRKAgra 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1169 ---ELSKLRRDLEEANIQHES-------TLANLRKKHNDAVA----------EMAEQVDQLNKLKAKAEKekneyyGQLN 1228
Cdd:TIGR02169 576 tflPLNKMRDERRDLSILSEDgvigfavDLVEFDPKYEPAFKyvfgdtlvveDIEAARRLMGKYRMVTLE------GELF 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1229 D--------LRAGVDHITNEKAAQEKIAkQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQL 1300
Cdd:TIGR02169 650 EksgamtggSRAPRGGILFSRSEPAELQ-RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1301 SKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKanaeaQVWRSKyesdgVA 1380
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-----SRIPEI-----QA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1381 RSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQL-EVDRANAIANAAEKKQKaFDKIIGEWKLKV 1459
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGKKEE-LEEELEELEAAL 877
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1460 DDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIE 1526
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1007-1793 |
1.11e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 90.18 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1007 EELQAAEDKINHLN-KVKAKLEQTLDELEDSLER---EKKVRGDVEKSKRKVEGDLKltqeavADLERNKKELEQTIQRK 1082
Cdd:pfam15921 88 KDLQRRLNESNELHeKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR------NQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1083 DKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEeeveaerQARAKAEKQRADLARELEELGerleeaGGATSaqiEL 1162
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFE-------EASGKKIYEHDSMSTMHFRSL------GSAIS---KI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1163 NKKREAELSKLR-------RDLEEANIQHESTLANLRKKHNDAVAEMAEQ----VDQLNKLKAKAEKEKNEYYGQLNDLR 1231
Cdd:pfam15921 226 LRELDTEISYLKgrifpveDQLEALKSESQNKIELLLQQHQDRIEQLISEheveITGLTEKASSARSQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1232 agvDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLND-FDASKKKLSIENSdllrQLEEAESQVSQLSKIKISLTTQ 1310
Cdd:pfam15921 306 ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANS----ELTEARTERDQFSQESGNLDDQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1311 LEdtKRLADEESRERATLLGKFRN---LEHD------LDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVAR 1381
Cdd:pfam15921 379 LQ--KLLADLHKREKELSLEKEQNkrlWDRDtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1382 SEELEEAKrKLQARLAEAEE----TIESLNQKCIGLEKTKQRLSTEVEDLQlEVDRANAIANAAEKKQKAfdkiigEWKL 1457
Cdd:pfam15921 457 NESLEKVS-SLTAQLESTKEmlrkVVEELTAKKMTLESSERTVSDLTASLQ-EKERAIEATNAEITKLRS------RVDL 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1458 KVDDLAaELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRREnknladeVKDLLDQIGEGGRNIHEIEKARKRLEAEKD 1537
Cdd:pfam15921 529 KLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-------IENMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1538 elqaaleeaeaaleqeeNKVLRAQlELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKL 1617
Cdd:pfam15921 601 -----------------DRRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1618 EADINEL-------EIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTL 1690
Cdd:pfam15921 663 KTSRNELnslsedyEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQ 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1691 LEQADRGRRQAEQELADAH-------EQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAAR 1763
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
810 820 830
....*....|....*....|....*....|..
gi 24584706 1764 LADELRaeqdhAQTQEKLRKALEQ--QIKELQ 1793
Cdd:pfam15921 823 CQDIIQ-----RQEQESVRLKLQHtlDVKELQ 849
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1317-1841 |
1.56e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.59 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1317 LADEESRERA-TLLGKFRNL---EHDLDNLREQVE------------EEAEGKADLQRQLSKAnaeAQVWRSKYESD-GV 1379
Cdd:COG4913 218 LEEPDTFEAAdALVEHFDDLeraHEALEDAREQIEllepirelaeryAAARERLAELEYLRAA---LRLWFAQRRLElLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1380 ARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTE-VEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLK 1458
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1459 VDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNI-HEIEKARKRLEAEKd 1537
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLALRDALAEAL- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1538 elqaaleeaeaaleqeenKVLRAQL----ELSQVRQEiDRRIQ---EK-----------EEEFE-------NTRKNHQRA 1592
Cdd:COG4913 454 ------------------GLDEAELpfvgELIEVRPE-EERWRgaiERvlggfaltllvPPEHYaaalrwvNRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1593 -LDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDH--ANKAN---AEAQKNIKRYQQ------QLKDIQTALEEEQ 1660
Cdd:COG4913 515 vYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcVDSPEELRRHPRaitragQVKGNGTRHEKDD 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1661 RARD--------DAREQLGISERRANALQNELEESRTLLEQAD------RGRRQAEQELADAHEQLNEVSAQNASISAAK 1726
Cdd:COG4913 595 RRRIrsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEaeldalQERREALQRLAEYSWDEIDVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1727 RKLE------SELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADEL-RAEQDHAQTQEKLRKALEQQIKELQVRLDEA 1799
Cdd:COG4913 675 AELErldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 24584706 1800 EANALkggkkaIQKLEQRVRE-LENELDGEQRRHADAQKNLRK 1841
Cdd:COG4913 755 FAAAL------GDAVERELREnLEERIDALRARLNRAEEELER 791
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1606 |
1.92e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 89.36 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 841 VSRIEDEIARLEEKAKKAEELHAaevkVRKELEALNAKLLA-EKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLR 919
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQA----LLKEKREYEGYELLkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 920 DIQERLTQE--------EDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKL 991
Cdd:TIGR02169 269 EIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 992 NKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKS-------KRKVEGDLKLTQEA 1064
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1065 VADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRadlarelee 1144
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA--------- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1145 lGERLEEAGGATSAQIELNKKRE---AELSKLRRDLEEANIQHESTLANLRKK---HNDAVAEMAEQVDQLNKLKAKAEK 1218
Cdd:TIGR02169 500 -RASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEAIELLKRRKAGRATFL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1219 EKNEYYGQLNDLRAG---------VDHITNEKAAQEKIAKQLQHTLneVQSKLDETNRTLND----------FDAS---- 1275
Cdd:TIGR02169 579 PLNKMRDERRDLSILsedgvigfaVDLVEFDPKYEPAFKYVFGDTL--VVEDIEAARRLMGKyrmvtlegelFEKSgamt 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1276 --KKKLSIENSDLLRQLEEAESQVSQLSKIKISLTT---QLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEA 1350
Cdd:TIGR02169 657 ggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqsELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1351 EGKADLQRQLSKANAEAQVWRSKYEsDGVARSEELEEAKRKLQARLAE-----AEETIESLNQKCIGLEKTKQRLSTEVE 1425
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLR 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1426 DLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLA 1505
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1506 DEVKDLLDQIGEGGRnihEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELS-----QVRQEIDRRIQEKE- 1579
Cdd:TIGR02169 896 AQLRELERKIEELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqAELQRVEEEIRALEp 972
|
810 820 830
....*....|....*....|....*....|...
gi 24584706 1580 ------EEFENTRKNhQRALDSMQASLEAEAKG 1606
Cdd:TIGR02169 973 vnmlaiQEYEEVLKR-LDELKEKRAKLEEERKA 1004
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
842-1686 |
2.69e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEELHaAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKltaqKNDLENQLRDI 921
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL----ELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 922 QERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKdhQIRNLNDEIAHQDELINKLNKEKKMQGET 1001
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK--EKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1002 NQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVR---GDVEKSKRKVEGDLKLTQEAVADLERNKKELEQT 1078
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKReaeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1079 IQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSA 1158
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1159 QIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGvdHIT 1238
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV--AIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1239 NEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLA 1318
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1319 D-EESRERATLLGKFRNLEHDLDNLREQVEEEAE--GKADLQRQLSKANAEAQVWRSKYESDgVARSEELEEAKRKLQAR 1395
Cdd:pfam02463 627 GiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEksEVKASLSELTKELLEIQELQEKAESE-LAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1396 LAEAEETIESLNQKCIGLEKTKQRLST--EVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKEC 1473
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDkiNEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1474 RNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQigEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQE 1553
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ--EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1554 ENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMK---KKLEADINELEIALDH 1630
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKeeaEILLKYEEEPEELLLE 943
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1631 ANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEE 1686
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
902-1852 |
3.40e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 88.64 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 902 ERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDlelNVQKAEQDKATKDHQIRNLNDEI 981
Cdd:pfam15921 96 ESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN---TVHELEAAKCLKEDMLEDSNTQI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 982 AHQDELI----NKLNKEKKMQGETNQKTGEELQAAED-KINHLNKVKAKLEQTLDELEDSLEREK----KVRGDVEKSKR 1052
Cdd:pfam15921 173 EQLRKMMlsheGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDTEISYLKgrifPVEDQLEALKS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1053 KVEGDLKLTqeavadLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARieeleeeveaERQARAKAE 1132
Cdd:pfam15921 253 ESQNKIELL------LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1133 KQRADLareleelgerleeaggatsaqielnkkrEAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKL 1212
Cdd:pfam15921 317 RQLSDL----------------------------ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1213 KAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQH---TLNEVQSKLDETNRTLNDFDASKKKLSIE-NSDLLR 1288
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsiTIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1289 QLEEAESQVSQLSKIKiSLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEaegkadlQRQLSKANAEAQ 1368
Cdd:pfam15921 449 QMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1369 VWRSKYEsdgvARSEELEEAKRKlQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAF 1448
Cdd:pfam15921 521 KLRSRVD----LKLQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1449 DKIIGEWKLKVDDLAAELDAS-----QKECRNYSTELFRLKgAYEEGQEQLEAVRrenknladEVKDLLDQIgeggrnIH 1523
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVK-LVNAGSERLRAVK--------DIKQERDQL------LN 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1524 EIEKARKRLEAekdelqaaleeaeaaleqeenkvlraqleLSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEae 1603
Cdd:pfam15921 661 EVKTSRNELNS-----------------------------LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE-- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1604 akgkaealrmkkKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNE 1683
Cdd:pfam15921 710 ------------QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1684 LEESRT-------LLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESE---LQTLHS-DLDELLNEAKNSEE 1752
Cdd:pfam15921 778 LSTVATeknkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvrLKLQHTlDVKELQGPGYTSNS 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1753 KAKKAMVDAA---RLADELRAEQDHAQ-----------TQEKLRKALEQQIKELQVRLDEAEANAL-----KGGKKAIQK 1813
Cdd:pfam15921 858 SMKPRLLQPAsftRTHSNVPSSQSTASflshhsrktnaLKEDPTRDLKQLLQELRSVINEEPTVQLskaedKGRAPSLGA 937
|
970 980 990
....*....|....*....|....*....|....*....
gi 24584706 1814 LEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQ 1852
Cdd:pfam15921 938 LDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1643-1949 |
4.27e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1643 KRYQQqLKDIQTALEEEQRA--RDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNA 1720
Cdd:COG1196 213 ERYRE-LKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1721 SISAAKRKLESELQTLHSDLDEL---LNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLD 1797
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELeerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1798 EAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTY 1877
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1878 KRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPRATSVRPQFDGLA 1949
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1321-1850 |
1.57e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 86.25 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1321 ESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYEsdgvaRSEELEEAKRKLQARLAEAE 1400
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----ELETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1401 ETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTEL 1480
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1481 FRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVlra 1560
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE--- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1561 qLELSQVRQEIDRRIQEKEEEFENTR--KNHQRALDSMQASLEAEAKGKAEALRMK-KKLEADINELEIALDHANKAnAE 1637
Cdd:PRK02224 429 -AELEATLRTARERVEEAEALLEAGKcpECGQPVEGSPHVETIEEDRERVEELEAElEDLEEEVEEVEERLERAEDL-VE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1638 AQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESR----TLLEQADRGRR------QAEQELAD 1707
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKReaaaEAEEEAEEAREevaelnSKLAELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1708 AHEQLNEVSAQNASISAAKRKLEsELQTLHSDLDELLNE------AKNSEEKAKKAMVDAARL----ADELRAEQDHAQT 1777
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIE-RLREKREALAELNDErrerlaEKRERKRELEAEFDEARIeearEDKERAEEYLEQV 665
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1778 QEKLRkALEQQIKELQVRLDEAEA-----NALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKseRRVKELS 1850
Cdd:PRK02224 666 EEKLD-ELREERDDLQAEIGAVENeleelEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQ--RNVETLE 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1761 |
1.59e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.28 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 844 IEDEIARLEE----KAKKAEELHAAEVKVrKELEALnaklLAEKTALLDSLSGEKGALQDYQErnakLTAQKNDLEnqlr 919
Cdd:TIGR02169 158 IIDEIAGVAEfdrkKEKALEELEEVEENI-ERLDLI----IDEKRQQLERLRREREKAERYQA----LLKEKREYE---- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 920 dIQERLTQEEDARnqlfQQKKKADQEISGLKKDIEDLELnvqkaeqdkatkdhQIRNLNDEIAHQDELINKLNKEKKMQG 999
Cdd:TIGR02169 225 -GYELLKEKEALE----RQKEAIERQLASLEEELEKLTE--------------EISELEKRLEEIEQLLEELNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1000 E----TNQKTGEELQAaedkinHLNKVKAKLEQTLDELEDSLEREKK-------VRGDVEKSKRKVE---GDLKLTQEAV 1065
Cdd:TIGR02169 286 EeeqlRVKEKIGELEA------EIASLERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEeerKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1066 ADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEEL 1145
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1146 GERleeaggATSAQIELnKKREAELSKLRRDLEEANIQHESTLANLRkKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYG 1225
Cdd:TIGR02169 440 EEE------KEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYD-RVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1226 QLNDLRAGVDHITN----------------EKAA----------QEKIAKQLQHTLNEVQS------KLDETNRTLNDFD 1273
Cdd:TIGR02169 512 VEEVLKASIQGVHGtvaqlgsvgeryataiEVAAgnrlnnvvveDDAVAKEAIELLKRRKAgratflPLNKMRDERRDLS 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1274 ASKKKLSIENS-DLLRQLEEAESQVSQLskikislttqLEDTKRLADEESRERatLLGKFR--NLEHDLdnlreqveeea 1350
Cdd:TIGR02169 592 ILSEDGVIGFAvDLVEFDPKYEPAFKYV----------FGDTLVVEDIEAARR--LMGKYRmvTLEGEL----------- 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1351 egkadlqrqLSKANAEAQVWRSKYESDGVARSEELEEakRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLE 1430
Cdd:TIGR02169 649 ---------FEKSGAMTGGSRAPRGGILFSRSEPAEL--QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1431 VDRANAIANAAEKKQKAFDKIIgewklkvDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLadEVKD 1510
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARL 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1511 LLDQIGEGGRNIHEIEKARKRLEAekdelqaaleeaeaaleqeenkvlraqlELSQVRQEIDRRIQEKE--EEFENTRKN 1588
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEA----------------------------RLREIEQKLNRLTLEKEylEKEIQELQE 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1589 HQRALDSMQASLEAEakgkAEALRMKK-KLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAR 1667
Cdd:TIGR02169 841 QRIDLKEQIKSIEKE----IENLNGKKeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1668 EQLGISERRANALQNELEE------------SRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRK-LESELQ 1734
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEiedpkgedeeipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDeLKEKRA 996
|
970 980
....*....|....*....|....*..
gi 24584706 1735 TLHSDLDELLNEAKNSEEKAKKAMVDA 1761
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1567-1880 |
1.60e-15 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 83.08 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1567 VRQEIDRRIQEKEE-EFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADineLEIALDHANKANA--EAQKNIK 1643
Cdd:PRK04863 275 MRHANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD---YQAASDHLNLVQTalRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1644 RYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLL--------EQADRG--RRQAEQELADAHE--Q 1711
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldVQQTRAiqYQQAVQALERAKQlcG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1712 LNEVSAQNAS--ISAAKRKLESELQTLhSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQI 1789
Cdd:PRK04863 432 LPDLTADNAEdwLEEFQAKEQEATEEL-LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1790 KELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDK 1869
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
330
....*....|.
gi 24584706 1870 LQQKIKTYKRQ 1880
Cdd:PRK04863 591 LQARIQRLAAR 601
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
801-1471 |
2.47e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 801 KKLQEQRVALKVvqrnlRKYLQLRTWPWYKLWQKVKPLLNVSRIEDeiARLEEKAKKAEELHAAEVKVRKELEALNAKll 880
Cdd:PTZ00121 1176 KKAEAARKAEEV-----RKAEELRKAEDARKAEAARKAEEERKAEE--ARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-- 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 881 aEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNqlfQQKKKADQeisgLKKDIEDlelnV 960
Cdd:PTZ00121 1247 -EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA---EEKKKADE----AKKKAEE----A 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 961 QKAEQDKaTKDHQIRNLNDEIAHQDELINKLNKEKKMQGEtnqKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLERE 1040
Cdd:PTZ00121 1315 KKADEAK-KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE---AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1041 KK---VRGDVEKSKRKVEgDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEEL 1117
Cdd:PTZ00121 1391 KKadeAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1118 EEEVEAERQARakaEKQRADLAreLEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKhnd 1197
Cdd:PTZ00121 1470 KKADEAKKKAE---EAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--- 1541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1198 avAEMAEQVDQLNKLKAKAEKEKNEYYGQLNdlRAGVDHITNEKAAQEkiAKQLQHTLNEVQSKLDETNRTLNDFDASKK 1277
Cdd:PTZ00121 1542 --AEEKKKADELKKAEELKKAEEKKKAEEAK--KAEEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1278 KLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQ 1357
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1358 RQLSKANAEAQVwrskyesdgvaRSEELEEAKRKLQARLAEAEETIeslnqKCIGLEKTKQRLSTEVEDLQLEVDRANAI 1437
Cdd:PTZ00121 1696 KEAEEAKKAEEL-----------KKKEAEEKKKAEELKKAEEENKI-----KAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
650 660 670
....*....|....*....|....*....|....
gi 24584706 1438 ANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQK 1471
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1261-1928 |
4.33e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1261 KLDETNRTLNDFDASKKK----LSIENSDLLRQleEAESQVSQLSKIKISLttqlEDTKRLADEESRERATLLGKFRNLE 1336
Cdd:PTZ00121 1028 KIEELTEYGNNDDVLKEKdiidEDIDGNHEGKA--EAKAHVGQDEGLKPSY----KDFDFDAKEDNRADEATEEAFGKAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1337 HDLDNLREQVEEEAEGKADLQRQLSKANAE----------AQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESL 1406
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEearkaedarkAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1407 nQKCIGLEKTKQRLSTEvEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQK--ECRNYSTELFRLK 1484
Cdd:PTZ00121 1182 -RKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1485 GAYEEGQEQLEAVRRENKNLADEVKDlldqiGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLEL 1564
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKK-----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1565 SQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQAS--LEAEAKGKAEALRMKKKLEADINELEIALDHANKA------NA 1636
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadelkkAA 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1637 EAQKNIKRYQQQLKDIQTALE-----EEQRARDDAREQlGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQ 1711
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEakkkaEEAKKADEAKKK-AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1712 LNEVSAQNASISAAKRKLESELQTlhSDLDELLNEAKNSEEKAKkamVDAARLADELRaEQDHAQTQEKLRKALEQQIKE 1791
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKK---ADEAKKAEEKK-KADELKKAEELKKAEEKKKAE 1567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1792 LQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSfQSEEDRKNHERMQDLVDKLQ 1871
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEK 1646
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1872 QKIKTYKRQIEE----AEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSV 1928
Cdd:PTZ00121 1647 KKAEELKKAEEEnkikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
840-1511 |
5.18e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.83 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 840 NVSRIEDEIARLEEKAKKAEELHAaevKVRKELEALNaKLLAEKTALLDSLSGEKGALQDYQErnaKLTAQKNDLENQLR 919
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNID---KFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELN---LLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 920 DIQerltQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAH-QDELINKLNKEKKMQ 998
Cdd:TIGR04523 191 KIK----NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQLKDEQNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 999 GETNQKTgEELQAAEDKINHLNKVKAKLEQTLDELEDSLERE--KKVRGDVEKSKRK---VEGDLKLTQEAVADLERNKK 1073
Cdd:TIGR04523 267 KQLSEKQ-KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnKELKSELKNQEKKleeIQNQISQNNKIISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1074 ELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLAReleelgerleeag 1153
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE------------- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1154 gatsaQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKhnDAVAEMaeqvdqlnklkakaekekneyygQLNDLRAG 1233
Cdd:TIGR04523 413 -----QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKEL-----------------------IIKNLDNT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1234 VDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLED 1313
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1314 TKRLADEESRERatllgKFRNLEHDLDNLREQVEEEAEGkadlQRQLSKANAEAQVWRSKYESDGVARSEELEE---AKR 1390
Cdd:TIGR04523 543 LEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEkekKIS 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1391 KLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQ 1470
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHY 693
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 24584706 1471 KEC---RNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDL 1511
Cdd:TIGR04523 694 KKYitrMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNF 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1271-1925 |
7.89e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1271 DFDASKKKLSIENSDLLRQLEEAESQVS----QLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQV 1346
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1347 EEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVED 1426
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1427 LQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLAD 1506
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1507 EVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIdRRIQEKEEEFENTR 1586
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-YDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1587 KNHQRALDSMQASLEAEAKGKAEALRMKKKLEADIN------------------ELEIALDHANKA-----NAEAQKNIK 1643
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryatAIEVAAGNRLNNvvvedDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1644 ----------------RYQQQLKDIQTALEE------------EQRAR----------------DDAREQLGISerRANA 1679
Cdd:TIGR02169 566 llkrrkagratflplnKMRDERRDLSILSEDgvigfavdlvefDPKYEpafkyvfgdtlvvediEAARRLMGKY--RMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1680 LQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMV 1759
Cdd:TIGR02169 644 LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1760 DAARLADELRAEQDH-AQTQEKLRK------ALEQQIKELQVRLDEAEAnALKGGKKAIQKLE-----QRVRELENELDG 1827
Cdd:TIGR02169 724 EIEQLEQEEEKLKERlEELEEDLSSleqeieNVKSELKELEARIEELEE-DLHKLEEALNDLEarlshSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1828 EQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAE-EIAALNLAKFRKAQQELEEAE 1906
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgKKEELEEELEELEAALRDLES 882
|
730
....*....|....*....
gi 24584706 1907 ERADLAEQaISKFRAKGRA 1925
Cdd:TIGR02169 883 RLGDLKKE-RDELEAQLRE 900
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1614-1922 |
8.78e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.49 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1614 KKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKdiqtALEEEQRARDDARE-QLGISERRANALQNELEESRTLLE 1692
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAE----KAERYKELKAELRElELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1693 QADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQ 1772
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1773 DHAQTQEKLRKALEQQIKELQVRLDEAEAnALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQ 1852
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEA-ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1853 SEEDRKNHERMQDLVDKLQQK-----IKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAK 1922
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
940-1686 |
1.68e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 79.29 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 940 KKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHL 1019
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1020 NKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDeqvv 1099
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK---- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1100 vLKHQRQIKELQARIEEleeeveaerqarakaekqradlareleelgerleeaggatsAQIELNKKREAELSklrrDLEE 1179
Cdd:TIGR04523 192 -IKNKLLKLELLLSNLK-----------------------------------------KKIQKNKSLESQIS----ELKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1180 ANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNeyygQLNDLragvdhiTNEKAAQEKIAKQLQHTLNEVQ 1259
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK----QLSEK-------QKELEQNNKKIKELEKQLNQLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1260 SKLDETNRTLNDFDASKKKLSIENSDllRQLEEAESQVSQLSKIKISLTTQLEDTKRladeesreratllgKFRNLEHDL 1339
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKK--------------ELTNSESEN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1340 DNLREQVEEEaegkadlQRQLSKANAEAQvwrSKYESdgvarSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQR 1419
Cdd:TIGR04523 359 SEKQRELEEK-------QNEIEKLKKENQ---SYKQE-----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1420 LSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRR 1499
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1500 ENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEenkvlraqlELSQVRQEIDRRIQEKE 1579
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE---------NLEKEIDEKNKEIEELK 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1580 EEFENTRKNhQRALDSMQASLEAEAKGKAEALRMKKKLeadINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEE 1659
Cdd:TIGR04523 575 QTQKSLKKK-QEEKQELIDQKEKEKKDLIKEIEEKEKK---ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
730 740
....*....|....*....|....*..
gi 24584706 1660 QRARDDAREQLGISERRANALQNELEE 1686
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1380-1920 |
3.57e-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: 78.56 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1380 ARSEE----LEEAK--RKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAianAAEKKQKAFDKIIG 1453
Cdd:TIGR02168 152 AKPEErraiFEEAAgiSKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAER---YKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1454 EWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLE 1533
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1534 AEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDR------RIQEKEEEFENTRKNHQRALDSMQASLEAEAKGK 1607
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1608 AEALRMKKKLEADINELEIALDHAnkanaeaQKNIKRYQQQLKDIQTALEEEQRarDDAREQLGISERRANALQNELEES 1687
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1688 RTLLEQADRGRRQAEQELADAHEQLNEVSAQNASIsaakRKLESELQTLHSDLDELLNEAK-------------NSEEKA 1754
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSglsgilgvlseliSVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1755 KKAM---------------VDAARLA-------------------------------------DELRAEQDHAQTQEKLR 1782
Cdd:TIGR02168 536 EAAIeaalggrlqavvvenLNAAKKAiaflkqnelgrvtflpldsikgteiqgndreilknieGFLGVAKDLVKFDPKLR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1783 KALE------------QQIKELQVRLDEAEANALKGG-----------------------KKAIQKLEQRV-------RE 1820
Cdd:TIGR02168 616 KALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGdlvrpggvitggsaktnssilerRREIEELEEKIeeleekiAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1821 LENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQ 1900
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
650 660
....*....|....*....|
gi 24584706 1901 ELEEAEERADLAEQAISKFR 1920
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLK 795
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1156-1855 |
5.41e-14 |
|
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: 78.09 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1156 TSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHndavaEMAEQVDQLNKLKAKAEKEKNEYYGQLN------- 1228
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-----EAQEEQLKKQQLLKQLRARIEELRAQEAvleetqe 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1229 --DLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSiensdllrQLEEAESQVSQLSKIKIS 1306
Cdd:TIGR00618 285 riNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS--------SIEEQRRLLQTLHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1307 LTTQLEDTKRLADEESRERaTLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELE 1386
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1387 EAKRKLQARLAeAEETIESLNQKCIGLEKTKQRLSTEVEDLQlevDRANAIANAAEKKQkafdkIIGEWKLKVDDLAAEL 1466
Cdd:TIGR00618 436 QQRYAELCAAA-ITCTAQCEKLEKIHLQESAQSLKEREQQLQ---TKEQIHLQETRKKA-----VVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1467 dasQKECRNYSTELFRLkGAYEEGQEQLEAVRRENKNLADEVKDLLDQIgeggrniHEIEKARKRLEAEKDelqaaleea 1546
Cdd:TIGR00618 507 ---CGSCIHPNPARQDI-DNPGPLTRRMQRGEQTYAQLETSEEDVYHQL-------TSERKQRASLKEQMQ--------- 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1547 eaaleqeenkvlraqlELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEI 1626
Cdd:TIGR00618 567 ----------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1627 ALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRA-RDDAREQLGISERRANALQNELEE---SRTLLEQADRGRRQAE 1702
Cdd:TIGR00618 631 RLHLQQCSQELALKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQKMQSEKEQltyWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1703 QELADA----HEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQ 1778
Cdd:TIGR00618 711 THIEEYdrefNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1779 EKLRKALEQQIKEL----QVRLDEAEANALKGGKKAIQKLEQRVRELE------NELDGEQRRHADAQKNLRKSERRVKE 1848
Cdd:TIGR00618 791 NRLREEDTHLLKTLeaeiGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksatlGEITHQLLKYEECSKQLAQLTQEQAK 870
|
....*..
gi 24584706 1849 LSFQSEE 1855
Cdd:TIGR00618 871 IIQLSDK 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
908-1131 |
1.61e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 74.42 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 908 TAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDEL 987
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 988 INKLNKEKKMQGETNQKTGE----ELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQE 1063
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1064 AVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKA 1131
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1197-1835 |
1.93e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1197 DAVAEMAEQVDQLnklkakaeKEKNEYYGQLNDLRAGVDHITNEKAAQEkiAKQLQHTLNEVQSKLDETNRTLNDFDASK 1276
Cdd:COG4913 242 EALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1277 KKLSIENSDLLRQLEEAESQVSQLSkikislTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADL 1356
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1357 QRQLSKANAEAQVWRSKYEsdgvARSEELEEAKRKLQARLAEAEETIESL--NQKCI--GLEKTKQRLSTEV----EDLQ 1428
Cdd:COG4913 386 RAEAAALLEALEEELEALE----EALAEAEAALRDLRRELRELEAEIASLerRKSNIpaRLLALRDALAEALgldeAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1429 -----LEVDRANAI-ANAAEK--------------KQKAFDKIIGEWKLKV---------------------DDLAAELD 1467
Cdd:COG4913 462 fvgelIEVRPEEERwRGAIERvlggfaltllvppeHYAAALRWVNRLHLRGrlvyervrtglpdperprldpDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1468 ASQKECRNYSTELFRLKGAYE--EGQEQLEAVRR---------ENKNLADevKDLLDQIGE----GGRNIHEIEKARKRL 1532
Cdd:COG4913 542 FKPHPFRAWLEAELGRRFDYVcvDSPEELRRHPRaitragqvkGNGTRHE--KDDRRRIRSryvlGFDNRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1533 EAEKDELQAALEEAEAaleqeenkvLRAQLELSQVRQEIDRRIQEKEEEFENTRKnHQRALDSMQASLEA--EAKGKAEA 1610
Cdd:COG4913 620 AELEEELAEAEERLEA---------LEAELDALQERREALQRLAEYSWDEIDVAS-AEREIAELEAELERldASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1611 LRMK-KKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEE-EQRARDDAREQLGisERRANALQNELEesR 1688
Cdd:COG4913 690 LEEQlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLE--ERFAAALGDAVE--R 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1689 TLLEQADRGRRQAEQELADAHEQLNEVsaqnasISAAKRKLESELQTLHSDLD------ELLNEAKNS-----EEKAKKA 1757
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLEslpeylALLDRLEEDglpeyEERFKEL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1758 MVDA-----ARLADELRAEQDHAQTQ-EKLRKALEQ-------------------QIKELQVRLDEAEANALKGGKKAIQ 1812
Cdd:COG4913 840 LNENsiefvADLLSKLRRAIREIKERiDPLNDSLKRipfgpgrylrlearprpdpEVREFRQELRAVTSGASLFDEELSE 919
|
730 740
....*....|....*....|...
gi 24584706 1813 KLEQRVRELENELDGEQRRHADA 1835
Cdd:COG4913 920 ARFAALKRLIERLRSEEEESDRR 942
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1245-1756 |
2.05e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1245 EKIAKQLQhTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKiKISLTTQLEDTKRLADEESRE 1324
Cdd:PRK03918 224 EKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1325 RATLLGKFRNLEHDLDNLREQVEEeaegkadLQRQLSKAnaeaqvwrskyeSDGVARSEELEEAKRKLQARLAEAEETIE 1404
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEING-------IEERIKEL------------EEKEERLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1405 SLnQKCIGLEKTKQRLSTEVEDLQLEvDRANAIANAAEKKQKAFDKIigewkLKVDDLAAELDASQKECRNYSTELFRLK 1484
Cdd:PRK03918 363 LY-EEAKAKKEELERLKKRLTGLTPE-KLEKELEELEKAKEEIEEEI-----SKITARIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1485 G---------AYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEaekdelqaaleeAEAALEQEEN 1555
Cdd:PRK03918 436 GkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES------------ELIKLKELAE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1556 KVLRAQLELSQVRQEidrRIQEKEEEFENTR------KNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIAL- 1628
Cdd:PRK03918 504 QLKELEEKLKKYNLE---ELEKKAEEYEKLKekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELe 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1629 -------DHANKANAEAQKNIKRYQQqLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQAdrGRRQA 1701
Cdd:PRK03918 581 elgfesvEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL--EKKYS 657
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1702 EQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKK 1756
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1573-1880 |
2.33e-13 |
|
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: 76.14 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1573 RRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADineLEIALDHANKA-NA-EAQKNIKRYQQQLK 1650
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQD---YQAASDHLNLVqTAlRQQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1651 DIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLeqADRGR------------RQAEQELADAHE--QLNEVS 1716
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL--ADYQQaldvqqtraiqyQQAVQALEKARAlcGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1717 AQNASISAAkrKLESELQTLHSDLDELlnEAKNSEEKAKKAMVDAA-----RLADELRAEQDHAQTQEKLR-----KALE 1786
Cdd:COG3096 436 PENAEDYLA--AFRAKEQQATEEVLEL--EQKLSVADAARRQFEKAyelvcKIAGEVERSQAWQTARELLRryrsqQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1787 QQIKELQVRLDEAEanalkggkkaiQKLE--QRVRELENELDGEQRRHADAQKNL----RKSERRVKELSFQSEEDRKNH 1860
Cdd:COG3096 512 QRLQQLRAQLAELE-----------QRLRqqQNAERLLEEFCQRIGQQLDAAEELeellAELEAQLEELEEQAAEAVEQR 580
|
330 340
....*....|....*....|
gi 24584706 1861 ERMQDLVDKLQQKIKTYKRQ 1880
Cdd:COG3096 581 SELRQQLEQLRARIKELAAR 600
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
847-1857 |
2.40e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 75.85 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 847 EIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTaLLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLT 926
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSRE-IVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 927 QEEDARNQLFQQKKKADQeisGLKKDIEDLELNVQKaeqdkatkdhQIRNLNDEIAHQDELINKLNKEKKmqgETNQKTG 1006
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQ---GTDEQLNDLYHNHQR----------TVREKERELVDCQRELEKLNKERR---LLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1007 E------ELQAAEDKINHLNKVKAKLEQT------LDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKE 1074
Cdd:TIGR00606 344 EllveqgRLQLQADRHQEHIRARDSLIQSlatrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1075 LEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEelgerleeagg 1154
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK----------- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1155 atSAQIELNKKREAELSKLRRDLEEAniqhestlanlRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGV 1234
Cdd:TIGR00606 493 --NSLTETLKKEVKSLQNEKADLDRK-----------LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHS 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1235 DHITNEkAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKikislttQLEDT 1314
Cdd:TIGR00606 560 DELTSL-LGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED-------KLFDV 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1315 KRLADEESreratllgkfrnlehDLDNLREQVEEEAEGKADLQrqlSKANAEAQ-VWRSKYESDGVA--------RSEEL 1385
Cdd:TIGR00606 632 CGSQDEES---------------DLERLKEEIEKSSKQRAMLA---GATAVYSQfITQLTDENQSCCpvcqrvfqTEAEL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1386 EEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRanaianaaekkqkafdkiigewklkvddLAAE 1465
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL----------------------------KEKE 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1466 LDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNladeVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAalee 1545
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES----AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG---- 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1546 aeaaleqeenkvlraqLELSQVRQEIDRRIQEKEEEfentrknhqraLDSMQASLEAEAKGKAEALRMKKKLEADINELE 1625
Cdd:TIGR00606 818 ----------------SDLDRTVQQVNQEKQEKQHE-----------LDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1626 IALDHANKANAEAQKnikrYQQQLKDIQTALEEEQRARDDAREQLGISERranALQNELEESRTLLEQADRGRRQAEQEL 1705
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQ----FEEQLVELSTEVQSLIREIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKV 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1706 ADAHEQLNEVSAQNASI--------SAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAqT 1777
Cdd:TIGR00606 944 NDIKEKVKNIHGYMKDIenkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL-T 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1778 QEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDR 1857
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
953-1534 |
3.94e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 953 IEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEqTLDE 1032
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1033 LEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQR--KDKELSSITAKLEDEQVVVLKHQRQIKEL 1110
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1111 QARIeeleeeveaeRQARAKAEKQRADLAREleelgerleeaggatSAQIELNKKREAELSKLRRDLEEANIQHESTLAN 1190
Cdd:PRK03918 316 LSRL----------EEEINGIEERIKELEEK---------------EERLEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1191 LRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEyygqlndLRAGVDHITNEKAAQEKIAKQLQHTLNEVQS---KLDETNR 1267
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEE-------IEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1268 TLNDFDAS--KKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEEsreraTLLGKFRNLEHDLDNLR-E 1344
Cdd:PRK03918 444 ELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK-----ELAEQLKELEEKLKKYNlE 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1345 QVEEEAEGKADLQRQLSKANAEAQVWRSKYES--DGVARSEELEEAKRKLQARLAEAEETIESLNQKCIG-LEKTKQRLS 1421
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1422 -------------TEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQ-KECRNYSTELFRLKGAY 1487
Cdd:PRK03918 599 pfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGL 678
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 24584706 1488 EEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEA 1534
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
896-1537 |
6.73e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 896 ALQDYQERNAKLTAQKNDLENQLRDIQerlTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNvqkaEQDKATKDHQIR 975
Cdd:TIGR04523 55 ELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND----KEQKNKLEVELN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 976 NLNDEIAHQDELINKLNKEKKmqgetnqKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVE 1055
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIK-------KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1056 GDL----------KLTQEAVADLERNKKELEQTIQRKDKELSSITAKLE--DEQVVVLK--HQRQIKELQARIEELEEEV 1121
Cdd:TIGR04523 201 LLLsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntQTQLNQLKdeQNKIKKQLSEKQKELEQNN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1122 EAERQARAKAEKQRADLAreleelgerleeaggatsaqiELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAE 1201
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEIS---------------------DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1202 MAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSI 1281
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1282 ENSDLLRQLE-------EAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKA 1354
Cdd:TIGR04523 420 EKELLEKEIErlketiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1355 DLQRQLSKANAEAQVWRSKYESdGVARSEELEEAKRKLQARLAEAEETIESLNQ--KCIGLEKTKQRLSTEVEDLQLEVD 1432
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISDLEDELNKDDFelKKENLEKEIDEKNKEIEELKQTQK 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1433 -------RANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLA 1505
Cdd:TIGR04523 579 slkkkqeEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
650 660 670
....*....|....*....|....*....|..
gi 24584706 1506 DEVKDLLDQIGEGGRNIHEIEKARKRLEAEKD 1537
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1236-1884 |
2.68e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1236 HITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFdaskKKLSIENSDLLRQLEEAESQVSQLSKIKISLTtqledtk 1315
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELEELKEEIE------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1316 rladEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLS-----KANAEAQVWRSKYESDGVARSEELEEAKR 1390
Cdd:PRK03918 242 ----ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1391 KLQARLAEAEETIESLNQKCIGLEKTKQRLstevEDLQLEVDRAnaianaaEKKQKAFDKIIgewklkvdDLAAELDASQ 1470
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEEL-------EERHELYEEAK--------AKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1471 KECRNYSTElfRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKAR------KRLEAEKDELqaale 1544
Cdd:PRK03918 379 KRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEEHRK----- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1545 eaeaaleqeeNKVLRAQLELSQVRQEIdRRIQEKEEEFENTRKNhqraldsmqasLEAEAKGKAEALRMKKKLEaDINEL 1624
Cdd:PRK03918 452 ----------ELLEEYTAELKRIEKEL-KEIEEKERKLRKELRE-----------LEKVLKKESELIKLKELAE-QLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1625 EIALdhaNKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLgiserranalqNELEESRTLLEQAdrgRRQAEQE 1704
Cdd:PRK03918 509 EEKL---KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKK---LDELEEE 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1705 LADaheqlnevsaqnasisaakrkLESELQTL-HSDLDEL-------------LNEAKNSEEKAKKAMVDAARLADELRA 1770
Cdd:PRK03918 572 LAE---------------------LLKELEELgFESVEELeerlkelepfyneYLELKDAEKELEREEKELKKLEEELDK 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1771 EQDHAQTQEKLRKALEQQIKELQVRLDEAEanaLKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELS 1850
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEE---YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
650 660 670
....*....|....*....|....*....|....
gi 24584706 1851 fQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEA 1884
Cdd:PRK03918 708 -KAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1413-1886 |
3.21e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1413 LEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKL---KVDDLAAELDASQKECRnystELFRLKGAYEE 1489
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVK----ELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1490 GQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEA--EKDELQAALEEAEAALEQEENKVLRAQLELSQV 1567
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1568 RQEIDRRIQEKE------EEFENTRKNHQRALDSMQASLEA--EAKGKAEALRMKKKLEAD--INELEIALDHANKANAE 1637
Cdd:PRK03918 323 INGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGltPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1638 AQKNIKryqqQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEEsrtllEQADRGRRQAEQELADAHEQLNEVSA 1717
Cdd:PRK03918 403 IEEEIS----KITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE-----EHRKELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1718 QNASISAAKRKLESELQTLH--SDLDELLNEAKNSEEKAKKAMVDAA-----------RLADELRAEQ-------DHAQT 1777
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELekkaeeyeklkEKLIKLKGEIkslkkelEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1778 QEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELE--------------------NELDGEQRRHADAQK 1837
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylelkdaekelereeKELKKLEEELDKAFE 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24584706 1838 NLRKSERRVKELSFQSEEDRKN-----HERMQDLVDKLQQKIKTYKRQIEEAEE 1886
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEK 687
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1386-1922 |
3.73e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1386 EEAKRKLQARLAEAEETIESLNQKciGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAaE 1465
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1466 LDASQKECRNYSTELFRLKgayEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDElqaalee 1545
Cdd:PRK02224 256 LEAEIEDLRETIAETERER---EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE------- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1546 aeaaleqeenkvlrAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRA--LDSMQASLEAEAKGKAEALRmkkKLEADINE 1623
Cdd:PRK02224 326 --------------LRDRLEECRVAAQAHNEEAESLREDADDLEERAeeLREEAAELESELEEAREAVE---DRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1624 LEIALDHANKANAEAQknikryqQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQA--------- 1694
Cdd:PRK02224 389 LEEEIEELRERFGDAP-------VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpv 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1695 -----------DRGRRQA-EQELADAHEQLNEVSAQNASISAAKrKLESELQTLH---SDLDELLNEAKNSEEkakkamv 1759
Cdd:PRK02224 462 egsphvetieeDRERVEElEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEerrEDLEELIAERRETIE------- 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1760 daarlADELRAEQDHAQTQEkLRKALEQQIKELQVRLDEAEANAlkggkKAIQKLEQRVRELENELDGeQRRHADAQKNL 1839
Cdd:PRK02224 534 -----EKRERAEELRERAAE-LEAEAEEKREAAAEAEEEAEEAR-----EEVAELNSKLAELKERIES-LERIRTLLAAI 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1840 RKSERRVKELSFQSEE-DRKNHERMQDLVDKlqqkiKTYKRQIEEAEEIAALNLAKFRKaqqelEEAEERADLAEQAISK 1918
Cdd:PRK02224 602 ADAEDEIERLREKREAlAELNDERRERLAEK-----RERKRELEAEFDEARIEEAREDK-----ERAEEYLEQVEEKLDE 671
|
....
gi 24584706 1919 FRAK 1922
Cdd:PRK02224 672 LREE 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1290-1747 |
4.44e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1290 LEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQV 1369
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1370 WrskyesDGVARSEELEEAKRKLQARLAEAEETIESLNQkcigLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQkafd 1449
Cdd:COG4717 128 L------PLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEE---- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1450 kiigewklkVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVK------------------DL 1511
Cdd:COG4717 194 ---------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1512 LDQIGEGGRNIHEI-------------EKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVR---------- 1568
Cdd:COG4717 265 GGSLLSLILTIAGVlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLspeellelld 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1569 -----QEIDRRIQEKEEEFENTRKNHQRA--LDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKN 1641
Cdd:COG4717 345 rieelQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1642 I--KRYQQQLKDIQTALEEEQRARDDAREQLGiserRANALQNELEESRTLleqadrgrRQAEQELADAHEQLNEVSAQN 1719
Cdd:COG4717 425 LdeEELEEELEELEEELEELEEELEELREELA----ELEAELEQLEEDGEL--------AELLQELEELKAELRELAEEW 492
|
490 500
....*....|....*....|....*....
gi 24584706 1720 ASISAAKRKLESELQTLHSD-LDELLNEA 1747
Cdd:COG4717 493 AALKLALELLEEAREEYREErLPPVLERA 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
883-1511 |
4.46e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 883 KTALLDSLSGEKGALQDYQER-----NAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKAD----------QEIS 947
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQieekeEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 948 GLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKkmqgetnqktgeELQAAEDKInhLNKVKAKLE 1027
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA------------GLDDADAEA--VEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1028 QTLDELEDSLErekKVRGDVEKSKRKVEGdlklTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQvvvlkhqRQI 1107
Cdd:PRK02224 321 DRDEELRDRLE---ECRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRR-------EEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1108 KELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLeeaggatsaqielnKKREAELSKLRRDLEEAniqhEST 1187
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE--------------AELEATLRTARERVEEA----EAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1188 LANLRKKHNDAVAEMAEQVDQLnklkakaekekNEYYGQLNDLRAGVDhitnekaaqekiakQLQHTLNEVQSKLDEtnr 1267
Cdd:PRK02224 449 LEAGKCPECGQPVEGSPHVETI-----------EEDRERVEELEAELE--------------DLEEEVEEVEERLER--- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1268 tlndfdaskkklsiensdlLRQLEEAESQVSQLsKIKISLTTQLEDTKRLADEESRERAtllgkfrnlehdlDNLREQVE 1347
Cdd:PRK02224 501 -------------------AEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERA-------------EELRERAA 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1348 E---EAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELE--EAKRKLQARLAEAEETIESLNQKCIGL----EKTKQ 1418
Cdd:PRK02224 548 EleaEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREALaelnDERRE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1419 RLSTEVE---DLQLEVDrANAIANAAEKKQKAfDKIIGEWKLKVDDLAAELDASQKECrnystelfrlkGAYEEGQEQLE 1495
Cdd:PRK02224 628 RLAEKRErkrELEAEFD-EARIEEAREDKERA-EEYLEQVEEKLDELREERDDLQAEI-----------GAVENELEELE 694
|
650
....*....|....*.
gi 24584706 1496 AVRRENKNLADEVKDL 1511
Cdd:PRK02224 695 ELRERREALENRVEAL 710
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-75 |
9.25e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 61.29 E-value: 9.25e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 24584706 33 DSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGETRDLKKD 75
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKD 43
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1598-1835 |
9.31e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1598 ASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRA 1677
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1678 NALQNELEESRTLLEQ----ADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEK 1753
Cdd:COG4942 93 AELRAELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1754 AKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANAlkggkkaiQKLEQRVRELENELDGEQRRHA 1833
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA--------EELEALIARLEAEAAAAAERTP 244
|
..
gi 24584706 1834 DA 1835
Cdd:COG4942 245 AA 246
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1394-1884 |
9.55e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.64 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1394 ARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDranaiANAAEKKQKaFDKIIGEWKLKVDDLAAELDASQKEC 1473
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-----ETSAELNQL-LRTLDDQWKEKRDELNGELSAADAAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1474 RNYSTELFRL---KGAYEEG--------QEQLEAVRRENKNLADEVKDLLDqigeggrNIHEIEKARKRLEAEKDELQAA 1542
Cdd:pfam12128 318 AKDRSELEALedqHGAFLDAdietaaadQEQLPSWQSELENLEERLKALTG-------KHQDVTAKYNRRRSKIKEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1543 leeaeaaleqeenKVLRAQLELSQVRQEIDRRIQEKEEEFEntrknhqraldsmqaSLEAEAKGKAEAlrmkKKLEADIN 1622
Cdd:pfam12128 391 -------------DIAGIKDKLAKIREARDRQLAVAEDDLQ---------------ALESELREQLEA----GKLEFNEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1623 ELEIALdhaNKANAEAQKNIKRYQQQLKdiqTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAE 1702
Cdd:pfam12128 439 EYRLKS---RLGELKLRLNQATATPELL---LQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1703 ---QELADAHEQLNEV-SAQNASISAAKR-----------KLESELQTLHSDLDELLNEAKNSEE------KAKKAMVDA 1761
Cdd:pfam12128 513 rrlEERQSALDELELQlFPQAGTLLHFLRkeapdweqsigKVISPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDV 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1762 ---ARLADELRAEQDHA----QTQEKLRKALEQQIKELQVRLDEAEAnALKGGKKAIQKLEQRVRELENELDGEQRRHAD 1834
Cdd:pfam12128 593 pewAASEEELRERLDKAeealQSAREKQAAAEEQLVQANGELEKASR-EETFARTALKNARLDLRRLFDEKQSEKDKKNK 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24584706 1835 AqknlRKSERRVKELSFQSEEDRKNHermqdLVDKLQQKIKTYKRQIEEA 1884
Cdd:pfam12128 672 A----LAERKDSANERLNSLEAQLKQ-----LDKKHQAWLEEQKEQKREA 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1030-1610 |
9.82e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1030 LDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIqRKDKELSSITAKLEDEQVVVLKHQRQIKE 1109
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL-REINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1110 LQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREA--ELSKLRRDLEEANIQHEST 1187
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1188 LANLRKKhndaVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLragvdHITNEKAAQEKIAKQLQHTLNEVQSKLdeTNR 1267
Cdd:PRK03918 316 LSRLEEE----INGIEERIKELEEKEERLEELKKKLKELEKRL-----EELEERHELYEEAKAKKEELERLKKRL--TGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1268 TLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTK----------RLADEESRERatLLGKFRnleH 1337
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKE--LLEEYT---A 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1338 DLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVArsEELEEAKRKLQA----RLAEAEETIESLNQKCIGL 1413
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA--EQLKELEEKLKKynleELEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1414 EKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEgqeq 1493
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE---- 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1494 LEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLE-LSQVRQEID 1572
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEeLEKRREEIK 693
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 24584706 1573 RRIQEKEEEFENTRK------NHQRALDSMQASLEAEAKGKAEA 1610
Cdd:PRK03918 694 KTLEKLKEELEEREKakkeleKLEKALERVEELREKVKKYKALL 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1880 |
1.02e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1631 ANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHE 1710
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1711 QLNEVSAQnasisAAKRKLESELQTLHSDLDELLneaknSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIK 1790
Cdd:COG4942 98 ELEAQKEE-----LAELLRALYRLGRQPPLALLL-----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1791 ELQVRLDEAEAnalkggkkAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELsfqseedRKNHERMQDLVDKL 1870
Cdd:COG4942 168 ELEAERAELEA--------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEALIARL 232
|
250
....*....|
gi 24584706 1871 QQKIKTYKRQ 1880
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1069-1888 |
1.31e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.00 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1069 ERNKKELEQTIQRKDKELSSITAKLEdeqvvvLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGER 1148
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEE------LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1149 LeeaggatsaQIELNKKREAELSKLRRDLEEANIQHEStlaNLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLN 1228
Cdd:pfam02463 243 Q---------ELLRDEQEEIESSKQEIEKEEEKLAQVL---KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1229 DLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLT 1308
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1309 TQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEA 1388
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1389 KRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEdlqlevdraNAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDA 1468
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS---------GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1469 SQKECRNYSTELFRLKGAYEEGQEQLEAVRrENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEA 1548
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1549 ALEQEENKVLRAQLELSQVRqeIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIAL 1628
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKES--AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1629 DHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARddareqlgISERRANALQNELEESRTLLEQADRGRRQAEQEladA 1708
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK--------INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK---S 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1709 HEQLNEvsaqnasISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHaqtqeklrkalEQQ 1788
Cdd:pfam02463 768 ELSLKE-------KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ-----------EEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1789 IKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSfQSEEDRKNHERMQdlvd 1868
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESK-EEKEKEEKKELEE---- 904
|
810 820
....*....|....*....|
gi 24584706 1869 KLQQKIKTYKRQIEEAEEIA 1888
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIK 924
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1580-1872 |
1.53e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 69.66 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1580 EEFENTRKNHQRALDSMQASLEAEAKGKAEALRMK-----KKLEADI-NEL-EIALDHANKAN-AEAQKNIKRYQQQLKD 1651
Cdd:COG3206 107 EDPLGEEASREAAIERLRKNLTVEPVKGSNVIEISytspdPELAAAVaNALaEAYLEQNLELRrEEARKALEFLEEQLPE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1652 IQTALEEEQRARDDAREQLGI--SERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASI--SAAKR 1727
Cdd:COG3206 187 LRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1728 KLESELQTLHSDLDELLneaknseekakkamvdaARLADelraeqDHAQTQeklrkALEQQIKELQVRLDEAEANALKGG 1807
Cdd:COG3206 267 QLRAQLAELEAELAELS-----------------ARYTP------NHPDVI-----ALRAQIAALRAQLQQEAQRILASL 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1808 KKAIQKLEQRVRELENELDGEQRRhadaQKNLRKSERRVKELsfqsEEDRKNHERM-QDLVDKLQQ 1872
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEAR----LAELPELEAELRRL----EREVEVARELyESLLQRLEE 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1576-1806 |
2.37e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.87 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1576 QEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTA 1655
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1656 LEEEQRA---RDDAREQLGISERRANALQ----NELEESRTLLEQADRGRRQAEQELAdahEQLNEVSAQNASISAAKRK 1728
Cdd:COG4942 99 LEAQKEElaeLLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELR---ADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1729 LESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKG 1806
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1570-1848 |
3.60e-11 |
|
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: 67.40 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1570 EIDRRIQEKEEEFENTRknhQRALDSMQASLEAEAKGKAEALRMKKKlEADINELEIALDHANKANAEAQKNIKRYQQQL 1649
Cdd:pfam19220 73 GLTRRLSAAEGELEELV---ARLAKLEAALREAEAAKEELRIELRDK-TAQAEALERQLAAETEQNRALEEENKALREEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1650 KDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKL 1729
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1730 ESELQTLHSDL---------------------DELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQ----EKLRKA 1784
Cdd:pfam19220 229 EAQLEEAVEAHraeraslrmklealtaraaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRlaglEADLER 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1785 LEQQIKELQVRLDEAE------ANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKE 1848
Cdd:pfam19220 309 RTQQFQEMQRARAELEeraemlTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKE 378
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
984-1820 |
4.84e-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: 68.46 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 984 QDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQE 1063
Cdd:pfam02463 207 KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1064 AVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELE 1143
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1144 ELGERLE--EAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVA------EMAEQVDQLNKLKAK 1215
Cdd:pfam02463 367 KLEQLEEelLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKkeeleiLEEEEESIELKQGKL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1216 AEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENsdLLRQLEEAES 1295
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA--LIKDGVGGRI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1296 QVSQLSKIKISLTTQLEDTKRladeeSRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEaqvWRSKYE 1375
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAI-----STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLP---LKSIAV 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1376 SDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQkafdkiigew 1455
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA---------- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1456 klKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAE 1535
Cdd:pfam02463 667 --SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1536 KDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKnhqraldsmqasLEAEAKGKAEALRMKK 1615
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL------------KAQEEELRALEEELKE 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1616 KLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQAD 1695
Cdd:pfam02463 813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1696 RGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHA 1775
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 24584706 1776 qTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRE 1820
Cdd:pfam02463 973 -GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1373 |
1.13e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 841 VSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKL----------------LAEKTALLDSLSGE-------KGAL 897
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIreleerieelkkeieeLEEKVKELKELKEKaeeyiklSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 898 QDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKadqeISGLKKDIEDLELNVQKAEQDKATKDhQIRNL 977
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK----LKELEKRLEELEERHELYEEAKAKKE-ELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 978 NDEIAhqDELINKLNKEKkmqgETNQKTGEELqaaEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGD 1057
Cdd:PRK03918 378 KKRLT--GLTPEKLEKEL----EELEKAKEEI---EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1058 LK--LTQEAVADLERNKKELEQTIQRKDK---ELSSITAKLEDEQVVVLKHQ--RQIKELQARIEELEEEVEAERQARAK 1130
Cdd:PRK03918 449 HRkeLLEEYTAELKRIEKELKEIEEKERKlrkELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1131 AEKQRADlareleelgerleeaggatsaqielnkKREAELSKLRRDLEEANiQHESTLANLRKKHNDAVAEMAEQVDQLN 1210
Cdd:PRK03918 529 KLKEKLI---------------------------KLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1211 KLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLS-IENSDLLRQ 1289
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEeLEKKYSEEE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1290 LEEAESQVSQLSKIKISLTTQLEDTKRLADEesreratllgkfrnLEHDLDNLREQVEEEAEGKADLQRqLSKANAEAQV 1369
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREE--------------IKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
....
gi 24584706 1370 WRSK 1373
Cdd:PRK03918 726 LREK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1288-1870 |
1.48e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1288 RQLEEAESQVSQLSKIKiSLTTQLEDTKRLADEESRERATLLGKFRNLEHDL-----DNLREQVEEEAEGKADLQRQLSK 1362
Cdd:COG4913 242 EALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1363 ANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEktkQRLSTEVEDLQLEVDRANAIANAAE 1442
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1443 KKQKAFDKIIGEWKLKVDDLAAELDASQKECRnystELFRLKGAYEEGQEQL-EAVRRENKNLADEVK---DLLdQIGEG 1518
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIA----SLERRKSNIPARLLALrDALAEALGLDEAELPfvgELI-EVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1519 grniHE-----IEKA---------------------------RKRLEAEK-DELQAALEEAEAALEQEENKV-------- 1557
Cdd:COG4913 473 ----EErwrgaIERVlggfaltllvppehyaaalrwvnrlhlRGRLVYERvRTGLPDPERPRLDPDSLAGKLdfkphpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1558 --LRAQL-------------ELSQV---------------RQEIDRRIQEKEEE---FENTRKnhQRALDSMQASLEAEA 1604
Cdd:COG4913 549 awLEAELgrrfdyvcvdspeELRRHpraitragqvkgngtRHEKDDRRRIRSRYvlgFDNRAK--LAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1605 kgkAEALRMKKKLEADINELEIALDHANKA---------NAEAQKNIKRYQQQLKDIQTA----------LEEEQRARDD 1665
Cdd:COG4913 627 ---AEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDASsddlaaleeqLEELEAELEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1666 AREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQtlhSDLDELLN 1745
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE---ERIDALRA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1746 EAKNSEEKAKKAMVDAARL--------------ADELRAEQDHAQT------QEKLRKALEQQIKELQVRLDEAEANALK 1805
Cdd:COG4913 781 RLNRAEEELERAMRAFNREwpaetadldadlesLPEYLALLDRLEEdglpeyEERFKELLNENSIEFVADLLSKLRRAIR 860
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1806 GGKKAIQKLEQRVRELE-NE-----LDGEQRRHADAQKnLRKSERRVKELSFQSEEDRKNH--ERMQDLVDKL 1870
Cdd:COG4913 861 EIKERIDPLNDSLKRIPfGPgrylrLEARPRPDPEVRE-FRQELRAVTSGASLFDEELSEArfAALKRLIERL 932
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
844-1396 |
1.57e-10 |
|
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: 66.68 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 844 IEDEIARLEEKAKKAEELHAAEVKVRkeLEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLEN----QLR 919
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDR--IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 920 DIQERLTQeedARNQLFQQKKKADQEISGLKKDI--EDLELNVQKAEQDKATKDHQirNLNDEIAHQDELINKLNKEKKM 997
Cdd:pfam15921 321 DLESTVSQ---LRSELREAKRMYEDKIEELEKQLvlANSELTEARTERDQFSQESG--NLDDQLQKLLADLHKREKELSL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 998 QGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREK-KVRGDVEKSKRKVEG---DLKLTQEAVADLERNKK 1073
Cdd:pfam15921 396 EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1074 ELEQ----------TIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEEL-------EEEVEAERQARAKAEKQRA 1136
Cdd:pfam15921 476 MLRKvveeltakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKlqelqhlKNEGDHLRNVQTECEALKL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1137 DLARELEELGERLEE---------AGGATSAQIELNKKR-EAELSKLRRDLEEANIqhestlanLRKKHNDAVAEMAEQV 1206
Cdd:pfam15921 556 QMAEKDKVIEILRQQienmtqlvgQHGRTAGAMQVEKAQlEKEINDRRLELQEFKI--------LKDKKDAKIRELEARV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1207 DQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNE-------------------------KAAQEKIAKQLQHTLNEVQSK 1261
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsrnelnslsedyevlkrnfrnkSEEMETTTNKLKMQLKSAQSE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1262 LDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQL-SKIKI---SLTTQLEDTKRLADEE---SRERATLLGKFRN 1334
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALqSKIQFleeAMTNANKEKHFLKEEKnklSQELSTVATEKNK 787
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1335 LEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQvwrskyESDGVARSEELEEAKRKLQARL 1396
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFA------ECQDIIQRQEQESVRLKLQHTL 843
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1419-1914 |
1.98e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1419 RLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIigewkLKVDDLAAELDA--SQKECRNYSTELFRLKGAYEEGQEQLEA 1496
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERL-----AELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1497 VRRENKNLADEVKDLLDQI-GEGGRNIHEIEKARKRLEAEKDelqaaleeaeaaleqeenKVLRAQLELSQVRQEIDRRI 1575
Cdd:COG4913 314 LEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELE------------------ERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1576 QEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEialdhankanaeaqKNIKRYQQQLKDIQta 1655
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE--------------AEIASLERRKSNIP-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1656 lEEEQRARDDAREQLGISERR----ANALQNELEES--RTLLEQADRGRR-------QAEQELADAHEQLN--------E 1714
Cdd:COG4913 440 -ARLLALRDALAEALGLDEAElpfvGELIEVRPEEErwRGAIERVLGGFAltllvppEHYAAALRWVNRLHlrgrlvyeR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1715 VSAQNASISAAK-------RKLESELQTLHSDLDELLNEAKN-----SEE---KAKKAMVDA------------------ 1761
Cdd:COG4913 519 VRTGLPDPERPRldpdslaGKLDFKPHPFRAWLEAELGRRFDyvcvdSPEelrRHPRAITRAgqvkgngtrhekddrrri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1762 --------------ARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANA--------LKGGKKAIQKLEQRVR 1819
Cdd:COG4913 599 rsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidVASAEREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1820 ELEN---ELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQqkiktykRQIEEAEEIAALNL---- 1892
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-------DRLEAAEDLARLELrall 751
|
570 580
....*....|....*....|...
gi 24584706 1893 -AKFRKAQQELEEAEERADLAEQ 1914
Cdd:COG4913 752 eERFAAALGDAVERELRENLEER 774
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
915-1159 |
3.39e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 915 ENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKE 994
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 995 KKMQGETNQKTGEELQA--AEDKINHLNKVKAKLEQTLDELEDslerEKKVRGDVEKSKRKVEGDLKLTQEAVADLERNK 1072
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSesFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1073 KELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEA 1152
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
....*..
gi 24584706 1153 GGATSAQ 1159
Cdd:COG3883 251 AAGAAGA 257
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1440-1894 |
3.74e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1440 AAEKKQKAFDKIIGEWKLKVDDLA------AELDASQKECRNYSTELFRLKGAYEEGQEqLEAVRRENKNLADEVKDLLD 1513
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEeleeelEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1514 QIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRAL 1593
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1594 DSMQASLEAEAKGKAEALRMkkkLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGIS 1673
Cdd:COG4717 234 NELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1674 ERRANALQNELEEsrtLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLEseLQTLHSDLDELLNEAKNSEEK 1753
Cdd:COG4717 311 PALEELEEEELEE---LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1754 AKKAMVDAARLADELRAEQDHAQTQeklrkaLEQQIKELQVRLDEAEANALKggkKAIQKLEQRVRELENELDgeqrrha 1833
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQ------LEELLGELEELLEALDEEELE---EELEELEEELEELEEELE------- 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1834 DAQKNLRKSERRVKELsfqsEEDrknhermqDLVDKLQQKIKTYKRQIEE-AEEIAALNLAK 1894
Cdd:COG4717 450 ELREELAELEAELEQL----EED--------GELAELLQELEELKAELRElAEEWAALKLAL 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
877-1092 |
5.38e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 877 AKLLAEKTALLDSLSGEkgaLQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDL 956
Cdd:COG4942 19 ADAAAEAEAELEQLQQE---IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 957 E--LNVQKAEQDKATKDHQIRNLND------------EIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKV 1022
Cdd:COG4942 96 RaeLEAQKEELAELLRALYRLGRQPplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1023 KAKLEQTLDELEDSLEREKKVRGDVEKskrKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAK 1092
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
749-1134 |
5.49e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 749 ELNDDQYRLGNTKVFFRAGVLGQMEEFRD------ERLGKIMSWMQAWARgylSRKGFKKLQEQrvaLKVVQRNLRKYLQ 822
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNnkevelEELKKILAEDEKLLD---EKKQFEKIAEE---LKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 823 LRTwpwyKLWQKVKPLLNVSRIEDEIARLEEKAKKAEeLHAAEVKvRKELEALNAKLLAEKTALLDSLSGEKGALQDYQE 902
Cdd:pfam05483 447 ARE----KEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-LEKEKLK-NIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 903 RNAKLTAQKNDLENQLRDIQERLTQEED----ARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLN 978
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKEMNLRDelesVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 979 DEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKIN----HLNKVKAKLEQTLD----ELEDSLEREKKVRGDVEKS 1050
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNklelELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVEKA 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1051 KRKVEGDLKLTQ-----------EAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEE 1119
Cdd:pfam05483 681 KAIADEAVKLQKeidkrcqhkiaEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKK 760
|
410
....*....|....*
gi 24584706 1120 EVEAERQARAKAEKQ 1134
Cdd:pfam05483 761 QLEIEKEEKEKLKME 775
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1664-1886 |
5.97e-10 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 64.39 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1664 DDAREQLGISERRANALQNELEESRtlleqadrgrRQAEQELADAHEQLNEVSAQnasisaaKRKLESELQTLHSDLDEL 1743
Cdd:COG1193 503 ERARELLGEESIDVEKLIEELERER----------RELEEEREEAERLREELEKL-------REELEEKLEELEEEKEEI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1744 LNEAKnseEKAKKAMVDAARLAD----ELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANAlkGGKKAIQKLE--QR 1817
Cdd:COG1193 566 LEKAR---EEAEEILREARKEAEelirELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKA--KPAKPPEELKvgDR 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1818 VRELENELDGE-----QRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQI-------EEAE 1885
Cdd:COG1193 641 VRVLSLGQKGEvleipKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSPELdlrgmrvEEAL 720
|
.
gi 24584706 1886 E 1886
Cdd:COG1193 721 P 721
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
782-1433 |
1.42e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 782 KIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQ-RNLRKYLQLRTWPWYKLWQKVKPLLNVSRIEDEIAR-LEEKAKKAE 859
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKkAEEAKKKAD 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 860 ELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDarnqlfqqK 939
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED--------K 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 940 KKADQeisglkkdiedlelnVQKAEQDKATKDhQIRNLNDEIAHQDELinKLNKEKKMQGETNQKTGEELQAAEDKinhl 1019
Cdd:PTZ00121 1405 KKADE---------------LKKAAAAKKKAD-EAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEA---- 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1020 nKVKAKLEQTLDELEDSLEREKKvrgdVEKSKRKVEGDLKLTQEAVADLERNKKELEqtiQRKDKElssitakledeqvv 1099
Cdd:PTZ00121 1463 -KKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADEAKKAAEAKKKADE---AKKAEE-------------- 1520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1100 vlkhQRQIKELQarieeLEEEVEAERQARAKAEKQRADlareleelgerleeaggatsaqiELNKKREAELSKLRRDLEE 1179
Cdd:PTZ00121 1521 ----AKKADEAK-----KAEEAKKADEAKKAEEKKKAD-----------------------ELKKAEELKKAEEKKKAEE 1568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1180 ANIQHESTLANLRKkhndavaemAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQ 1259
Cdd:PTZ00121 1569 AKKAEEDKNMALRK---------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1260 SKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKikislttqledtkrlADEESRERATLLGKFRNLEHDL 1339
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK---------------AEEDEKKAAEALKKEAEEAKKA 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1340 DNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGvARSEEL---EEAKRKLQARLAEAEETIESLNQKCIGLekT 1416
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAV--I 1781
|
650
....*....|....*..
gi 24584706 1417 KQRLSTEVEDLQLEVDR 1433
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDK 1798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1237-1887 |
1.45e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1237 ITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDA-----------SKKKLSIENSDLLRQLEEAESQVSQLSKIK- 1304
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQqikdlndklkkNKDKINKLNSDLSKINSEIKNDKEQKNKLEv 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1305 --ISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYesdgvARS 1382
Cdd:TIGR04523 125 elNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-----LKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1383 EELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDL 1462
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1463 AAELDASQKECRNYSTELFRLKGayEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDelqaa 1542
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT----- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1543 leeaeaaleqeenkvlraqlELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSmqasleaeakgkaealrmKKKLEADIN 1622
Cdd:TIGR04523 353 --------------------NSESENSEKQRELEEKQNEIEKLKKENQSYKQE------------------IKNLESQIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1623 ELEIALDHANKANAEAQKNIKRYQQQ----LKDIQTALEEEQRARD---DAREQLGISERRANALQNELEESRTLLEQAD 1695
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEkellEKEIERLKETIIKNNSeikDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1696 RGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDha 1775
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF-- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1776 qtqEKLRKALEQQIKELQVRLDEAeanalkggKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEE 1855
Cdd:TIGR04523 553 ---ELKKENLEKEIDEKNKEIEEL--------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
650 660 670
....*....|....*....|....*....|..
gi 24584706 1856 DRKNHERMQDLVDKLQQKIKTYKRQIEEAEEI 1887
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1057-1670 |
2.69e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1057 DLKLTQEAVADLERNKKELEQtIQRKDKELSSITAKLE-----DEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKA 1131
Cdd:COG4913 236 DLERAHEALEDAREQIELLEP-IRELAERYAAARERLAeleylRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1132 EKQRADLARELEELGERLEEAGGATSAQIE-----LNKKRE------AELSKLRRDLEEANIQHESTLANLRKKHNDAVA 1200
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1201 EMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEK--------AAQEKIAKQLQHTLNE-------VQSKLDET 1265
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllALRDALAEALGLDEAElpfvgelIEVRPEEE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1266 ------NRTLNDFdaskkKLSiensdLL---RQLEEAESQVSQLsKIKISLTTQ-LEDTKRLADEESRERATLLGKfrnL 1335
Cdd:COG4913 475 rwrgaiERVLGGF-----ALT-----LLvppEHYAAALRWVNRL-HLRGRLVYErVRTGLPDPERPRLDPDSLAGK---L 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1336 EHDLDNLREQVEEEAEGKADL-----QRQLSKAN----AEAQV--WRSKYESDGVARSEEL----EEAKRKLQARLAEAE 1400
Cdd:COG4913 541 DFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPraitRAGQVkgNGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1401 EtieslnqkcigLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIgewklKVDDLAAELDASQKECRNYSTEL 1480
Cdd:COG4913 621 E-----------LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1481 FRLKGAyeegQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEA-------ALEQE 1553
Cdd:COG4913 685 DDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleerfAAALG 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1554 ENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADinELeialdHANK 1633
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED--GL-----PEYE 833
|
650 660 670
....*....|....*....|....*....|....*..
gi 24584706 1634 ANAEAQKNiKRYQQQLKDIQTALEeeqRARDDAREQL 1670
Cdd:COG4913 834 ERFKELLN-ENSIEFVADLLSKLR---RAIREIKERI 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
937-1180 |
2.93e-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: 61.32 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 937 QQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEkkmqgetnqktgeeLQAAEDKI 1016
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE--------------LAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1017 NHLNKVKAKLEQTLDELEDSLereKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDE 1096
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1097 QVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEelgerleeaggATSAQIELNKKREAELSKLRRD 1176
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA-----------ELAAELAELQQEAEELEALIAR 231
|
....
gi 24584706 1177 LEEA 1180
Cdd:COG4942 232 LEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
841-1348 |
4.78e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 841 VSRIEDEIARLEEKAKKAEELHAAEVKVRKELEalnakllaEKTALLDSLsgeKGALQDYQERNAKLTAQKNDLENQLRD 920
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHE--------ERREELETL---EAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 921 IQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGE 1000
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1001 TNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQ 1080
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1081 R--------------KDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQArAKAEKQRADLARELEELG 1146
Cdd:PRK02224 444 EaealleagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1147 ERLEEAggatSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRkkhnDAVAEMAEQVDQLNklkaKAEKEKNEYYGQ 1226
Cdd:PRK02224 523 ELIAER----RETIEEKRERAEELRERAAELEAEAEEKREAAAEAE----EEAEEAREEVAELN----SKLAELKERIES 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1227 LNDLRAGVDHITNEKAAQEkiakqlqhTLNEVQSKLDETNrtlndfDASKKKLSiENSDLLRQLEEA--ESQVSQLSKIK 1304
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIE--------RLREKREALAELN------DERRERLA-EKRERKRELEAEfdEARIEEAREDK 655
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24584706 1305 ISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEE 1348
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
894-1409 |
6.07e-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: 61.28 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 894 KGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISG-------LKKDIEDLELNVQKA--- 963
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEliekkdhLTKELEDIKMSLQRSmst 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 964 ----EQDKATKDHQIRNLNDEIAHQDELINKLNKEKKM---QGETNQKTGEEL-----QAAEDKINHLNKVKAKLEQTLD 1031
Cdd:pfam05483 312 qkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFvvtEFEATTCSLEELlrteqQRLEKNEDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1032 ELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEA------VADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQR 1105
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKkqfekiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1106 QIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEaggaTSAQIELNKKREAELSKLRRDLEEANIQHE 1185
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK----HQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1186 STLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDET 1265
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1266 NRTLNDFDASKKKLSIENSDLLRQLEE-AESQVSQLSKIKIS---LTTQLEDTKRLADEESRER-----------ATLLG 1330
Cdd:pfam05483 628 NKQLNAYEIKVNKLELELASAKQKFEEiIDNYQKEIEDKKISeekLLEEVEKAKAIADEAVKLQkeidkrcqhkiAEMVA 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584706 1331 KFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQK 1409
Cdd:pfam05483 708 LMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1174-1889 |
7.23e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1174 RRDLEEANIQHESTLANLRKKHNDA---VAEMAEQVDQLNKLKAKAEKekneyygqlnDLRAGVDHIT---NEKAAQEKI 1247
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEqyrLVEMARELEELSARESDLEQ----------DYQAASDHLNlvqTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1248 AkQLQHTLNEVQSKLDETNRTLndfdaskKKLSIENSDLLRQLEEAESQVSqlskikiSLTTQLEDTKRLADEESR---- 1323
Cdd:COG3096 350 E-RYQEDLEELTERLEEQEEVV-------EEAAEQLAEAEARLEAAEEEVD-------SLKSQLADYQQALDVQQTraiq 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1324 --------ERA-TLLGK----FRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYE-----SDGVARSEEL 1385
Cdd:COG3096 415 yqqavqalEKArALCGLpdltPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1386 EEAKRKL-----QARLAEAEETIESlnqkciGLEKTKQRLSTEvedlqlevdranaiaNAAEKKQKAFDKIIG---EWKL 1457
Cdd:COG3096 495 QTARELLrryrsQQALAQRLQQLRA------QLAELEQRLRQQ---------------QNAERLLEEFCQRIGqqlDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1458 KVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLA-------DEVKDLLDQIGEGGRNIHEIEKARK 1530
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqDALERLREQSGEALADSQEVTAAMQ 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1531 RLeaekdelqaaleeaeaaleqeenkvLRAQLELSQVRQEIDRRIQEKEEEFENTrknhqraldsMQASLEAEAKGKAEA 1610
Cdd:COG3096 634 QL-------------------------LEREREATVERDELAARKQALESQIERL----------SQPGGAEDPRLLALA 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1611 LRMKKKLEADINElEIALDHAnkANAEAQKNIKRYQQQLKDIQTALEEEQrARDDAREQLGISERRANA-----LQNELE 1685
Cdd:COG3096 679 ERLGGVLLSEIYD-DVTLEDA--PYFSALYGPARHAIVVPDLSAVKEQLA-GLEDCPEDLYLIEGDPDSfddsvFDAEEL 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1686 ESRTLLEQADR-------------GRRQAEQELADAHEQLNEVSAQNASISAAKRKleseLQTLHSDLDELLNE------ 1746
Cdd:COG3096 755 EDAVVVKLSDRqwrysrfpevplfGRAAREKRLEELRAERDELAEQYAKASFDVQK----LQRLHQAFSQFVGGhlavaf 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1747 AKNSEEKAKKAmvdAARLADELRAEQDHAQTQEKLRKALEqQIKELQVRLDE--AEANALkggkkAIQKLEQRVRELENE 1824
Cdd:COG3096 831 APDPEAELAAL---RQRRSELERELAQHRAQEQQLRQQLD-QLKEQLQLLNKllPQANLL-----ADETLADRLEELREE 901
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1825 LDGEQrrhaDAQKNLRKSERRVKELSFQS---EEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAA 1889
Cdd:COG3096 902 LDAAQ----EAQAFIQQHGKALAQLEPLVavlQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQ 965
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1009-1466 |
8.21e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1009 LQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSS 1088
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1089 ITAKLEDEQVvvlkhQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREA 1168
Cdd:COG4717 128 LPLYQELEAL-----EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1169 ELSKLRRDLEEANIQHESTLANLRKKHND-----AVAEMAEQVDQLNKL------------KAKAEKEKNEYYGQLNDLR 1231
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1232 AGVDHI-----TNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKIS 1306
Cdd:COG4717 283 LGLLALlflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1307 LTTQLEDTKRLA---------DEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKyesd 1377
Cdd:COG4717 363 LQLEELEQEIAAllaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE---- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1378 gvARSEELEEAKRKLQARLAEAEETIESLnQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKL 1457
Cdd:COG4717 439 --EELEELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
....*....
gi 24584706 1458 KVDDLAAEL 1466
Cdd:COG4717 516 PVLERASEY 524
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
838-1304 |
8.76e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 838 LLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEAL--------NAKLLAEKTALLDSLSgEKGALQDYQERNAKLTA 909
Cdd:PRK01156 241 LNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELeerhmkiiNDPVYKNRNYINDYFK-YKNDIENKKQILSNIDA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 910 QKNDLEnqlrDIQERLTQEEDARNQlFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELIN 989
Cdd:PRK01156 320 EINKYH----AIIKKLSVLQKDYND-YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 990 KLNKEKKMQGETNQKTGEE----LQAAEDKINHLNKVKAKLEQTLDELEDSL------------------EREKKVRGDV 1047
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNEinvkLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHY 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1048 EKSKRKVEGDLKLTQEAVADLERNKKELeqtIQRKDKELSSITAKLEDEqvvvlkhQRQIKELQARIEELEEEVEAERQA 1127
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDL---KKRKEYLESEEINKSINE-------YNKIESARADLEDIKIKINELKDK 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1128 RAKAEK-----QRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEM 1202
Cdd:PRK01156 545 HDKYEEiknryKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1203 AEQVDQLN---KLKAKAEKEKNEYYGQLNDLR---AGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASK 1276
Cdd:PRK01156 625 ENEANNLNnkyNEIQENKILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
490 500
....*....|....*....|....*...
gi 24584706 1277 KKLSIENSDLLRQLEEAESQVSQLSKIK 1304
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMKKIK 732
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1176-1894 |
1.50e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1176 DLEEANIQHEStlanlrkkHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDhitnekaAQEKIAKQLQHT- 1254
Cdd:PRK04863 356 DLEELEERLEE--------QNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD-------VQQTRAIQYQQAv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1255 --LNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERA-----T 1327
Cdd:PRK04863 421 qaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvarE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1328 LLGKFRNLEHDLDNL--REQVEEEAEGKADLQRQLSKANAEAQvwrsKYESDGVARSEELEEAKRKLQARLAEAEETIES 1405
Cdd:PRK04863 501 LLRRLREQRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFC----KRLGKNLDDEDELEQLQEELEARLESLSESVSE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1406 LNQKCIGLEKTKQRLSTEVEDL----------QLEVDRANAIANAAEKKQKAFDKIIG-------EWKLKVDDLAAELDA 1468
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLaarapawlaaQDALARLREQSGEEFEDSQDVTEYMQqllererELTVERDELAARKQA 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1469 SQKECRNYS----TELFRLKGAYE--------EGQE------------------------QLEAVRRENKNLADEVKDLL 1512
Cdd:PRK04863 657 LDEEIERLSqpggSEDPRLNALAErfggvllsEIYDdvsledapyfsalygparhaivvpDLSDAAEQLAGLEDCPEDLY 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1513 ------DQIGEGGRNIHEIEKArkrleaekdelqaaleeaeaaleqEENKVLRAQLELSQVRQE--IDRRIQEKEEEfen 1584
Cdd:PRK04863 737 liegdpDSFDDSVFSVEELEKA------------------------VVVKIADRQWRYSRFPEVplFGRAAREKRIE--- 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1585 trknhqraldsmqaSLEAEAKGKAEALrmkKKLEADINELEIALDHANK-----------ANAEAQknIKRYQQQLKDIQ 1653
Cdd:PRK04863 790 --------------QLRAEREELAERY---ATLSFDVQKLQRLHQAFSRfigshlavafeADPEAE--LRQLNRRRVELE 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1654 TALEEEQRARDDAREQLGISERRANALqNELEESRTLLEQADRGRR--QAEQELADAHEQLNEVSAQNASISaakrKLES 1731
Cdd:PRK04863 851 RALADHESQEQQQRSQLEQAKEGLSAL-NRLLPRLNLLADETLADRveEIREQLDEAEEAKRFVQQHGNALA----QLEP 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1732 ELQTLHSD-------------LDELLNEAKN---------------SEEKAKKAMVDAARLADELRAEQDHAQTQeklRK 1783
Cdd:PRK04863 926 IVSVLQSDpeqfeqlkqdyqqAQQTQRDAKQqafaltevvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQE---RT 1002
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1784 ALEQQIKELQVRLDEAEAnALKGGKKAIQKLEQRVRELENELD---------GEQR---RHADAQKNLRKSERRVKELSF 1851
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQ-VLASLKSSYDAKRQMLQELKQELQdlgvpadsgAEERaraRRDELHARLSANRSRRNQLEK 1081
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 24584706 1852 QSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEE--IAALNLAK 1894
Cdd:PRK04863 1082 QLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVK 1126
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1634-1855 |
1.97e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1634 ANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLN 1713
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1714 EVSA----QNASISAAKRKLESE-----------LQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDhaqTQ 1778
Cdd:COG3883 90 ERARalyrSGGSVSYLDVLLGSEsfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA---EL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1779 EKLRKALEQQIKELQVRLDEAEANalkggkkaIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEE 1855
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAE--------EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1590-1714 |
2.11e-08 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 58.14 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1590 QRALDSMQASLEAeAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKD--I-QTALEEEQRARDDA 1666
Cdd:COG1566 82 QAALAQAEAQLAA-AEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVsQQELDEARAALDAA 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24584706 1667 REQLGISERRANALQNELEESRTlLEQADRGRRQAEQELADAHEQLNE 1714
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEEE-LAAAQAQVAQAEAALAQAELNLAR 207
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1167-1768 |
2.29e-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: 59.47 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1167 EAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEK 1246
Cdd:pfam12128 257 ELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1247 I----AKQLQHTLNEVQSKLDETNRTLNDFDASKKKlsIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEES 1322
Cdd:pfam12128 337 AdietAAADQEQLPSWQSELENLEERLKALTGKHQD--VTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1323 RERATLLGKFRN-LEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDG-VARSEELEEAKRKLQARLAEA- 1399
Cdd:pfam12128 415 DDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDErIERAREEQEAANAEVERLQSEl 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1400 -------EETIESLNQKCIGLEKTKQRLstevEDLQLEVDRANA-----IANAAEKKQKAFDKIIGEWKLKVDDLAAELD 1467
Cdd:pfam12128 495 rqarkrrDQASEALRQASRRLEERQSAL----DELELQLFPQAGtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1468 ASQK--ECRNYSTELfRLKG----AYEEGQEQLEAVRRENKNLADEVKDLLDQIGEggrnihEIEKARKRLEAEKDELQA 1541
Cdd:pfam12128 571 DGSVggELNLYGVKL-DLKRidvpEWAASEEELRERLDKAEEALQSAREKQAAAEE------QLVQANGELEKASREETF 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1542 ALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFeNTRKNHQRALDSMQASLEAEAKGKAEALRMKK--KLEA 1619
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERL-NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKqaYWQV 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1620 DINELEIALDHANKANAEAQKNIKRYQQQLkdiqtaleEEQRARDDAreQLGISERRANALQNELEESRTLLEQAdrgrR 1699
Cdd:pfam12128 723 VEGALDAQLALLKAAIAARRSGAKAELKAL--------ETWYKRDLA--SLGVDPDVIAKLKREIRTLERKIERI----A 788
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1700 QAEQELADAHEQLNEV-SAQNASISAAKRKLESELQTLHSDLDELLNEAK--NSE-EKAKKAMVDAARLADEL 1768
Cdd:pfam12128 789 VRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTKlrRAKlEMERKASEKQQVRLSEN 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1684-1890 |
3.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1684 LEESRTLlEQADRGRRQAEqELADAHEQLNEVSAQnasisaakRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAAR 1763
Cdd:COG4913 218 LEEPDTF-EAADALVEHFD-DLERAHEALEDAREQ--------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1764 LADEL------RAEQDHAQTQEKLRkALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQK 1837
Cdd:COG4913 288 RRLELleaeleELRAELARLEAELE-RLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1838 NLRK-------SERRVKELSFQSEEDRKN----HERMQDLVDKLQQKIKTYKRQIEEAE-EIAAL 1890
Cdd:COG4913 367 LLAAlglplpaSAEEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELEaEIASL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1502-1942 |
4.08e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1502 KNLADEVKDLLDQIGEGGRNIH--EIEKARKRLEAEKdELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKE 1579
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKK-KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1580 EEFENTRKNHQRaldSMQASLEAEAKGKAEALRMKKkleaDINELEIALDHANKANAEaqkNIKRYQQQLKdiQTALEEE 1659
Cdd:PTZ00121 1165 KAEEARKAEDAK---KAEAARKAEEVRKAEELRKAE----DARKAEAARKAEEERKAE---EARKAEDAKK--AEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1660 QRARDDAREQLGISERRANALQNELEESRtlleQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLEselqtlhsd 1739
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEAR----MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--------- 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1740 ldellnEAKNSEEKAKKAmvDAARLADELRAEQDHAQTQ-EKLRKALEQQIKELQVRLDEAEANAlKGGKKAIQKLEQRV 1818
Cdd:PTZ00121 1300 ------EKKKADEAKKKA--EEAKKADEAKKKAEEAKKKaDAAKKKAEEAKKAAEAAKAEAEAAA-DEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1819 RELEneldgEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKA 1898
Cdd:PTZ00121 1371 KKKE-----EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 24584706 1899 QQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPRATSVR 1942
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1568-1882 |
4.50e-08 |
|
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: 58.21 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1568 RQEIDRRIQEKEE---EFENTRKnHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEialdhankanaeaQKNIKR 1644
Cdd:pfam17380 295 KMEQERLRQEKEEkarEVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR-------------QEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1645 YQQQLKDIQTALEEEqRARDDAREQLGiSERRANALQNELEESRTL-LEQADRGRRQAEQELADAHEQLNEVSAQNASIS 1723
Cdd:pfam17380 361 ELERIRQEEIAMEIS-RMRELERLQME-RQQKNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1724 AAKRKLESELQTLHsdLDELlnEAKNSEEKAKKAMVDAARLADELRAEQ-DHAQTQEKLRKALEQQIKELQVRLDEAEAN 1802
Cdd:pfam17380 439 RLEEERAREMERVR--LEEQ--ERQQQVERLRQQEEERKRKKLELEKEKrDRKRAEEQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1803 alkggKKAIQK-LEQRVRELENEldgEQRRHADAQKNLRKS---ERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYK 1878
Cdd:pfam17380 515 -----RKLLEKeMEERQKAIYEE---ERRREAEEERRKQQEmeeRRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK 586
|
....
gi 24584706 1879 RQIE 1882
Cdd:pfam17380 587 ARAE 590
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1690-1877 |
4.79e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.60 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1690 LLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELlneaknsEEKAKKAMV----DAARLA 1765
Cdd:COG1842 17 LLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------EEKARLALEkgreDLAREA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1766 delrAEQdhaqtqeklRKALEQQIKELQVRLDEAEANALKgGKKAIQKLEQRVRELENELDG--EQRRHADAQKNLRKSE 1843
Cdd:COG1842 90 ----LER---------KAELEAQAEALEAQLAQLEEQVEK-LKEALRQLESKLEELKAKKDTlkARAKAAKAQEKVNEAL 155
|
170 180 190
....*....|....*....|....*....|....
gi 24584706 1844 RrvkelSFQSEEDRKNHERMQDLVDKLQQKIKTY 1877
Cdd:COG1842 156 S-----GIDSDDATSALERMEEKIEEMEARAEAA 184
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
885-1487 |
4.80e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 885 ALLDSLSGEKGALQDYQERNAKLTAQKNDLEnQLRDIQERLTQEEDARNQLFQQKKKAD-----QEISGLKKDIEDLELN 959
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 960 VQKAEQDKATKDHQIRNLNDEIahqDELINKLNKEKkmqgetnqktGEELQAAEDKINHLNKVKAKLEQTLDELEDSLER 1039
Cdd:COG4913 304 LARLEAELERLEARLDALREEL---DELEAQIRGNG----------GDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1040 ekkvrgdvekskrkvegdLKLTQEAVA-DLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELE 1118
Cdd:COG4913 371 ------------------LGLPLPASAeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1119 EeveaeRQAR--AKAEKQRADLAReleelgerleeaggatsaqiELNKKRE-----AELSKLRRDLE--EANIqhESTLA 1189
Cdd:COG4913 433 R-----RKSNipARLLALRDALAE--------------------ALGLDEAelpfvGELIEVRPEEErwRGAI--ERVLG 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1190 NLR------KKHNDAVAEMAEQ-----------VDQLNKLKAKAEKEKNEYYGQL----NDLRAGVDHITNEKAAQEKI- 1247
Cdd:COG4913 486 GFAltllvpPEHYAAALRWVNRlhlrgrlvyerVRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEAELGRRFDYVCVd 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1248 -AKQLQH-----TLnEVQSKLDETNRTLNDFDASKKKLSIeNSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEe 1321
Cdd:COG4913 566 sPEELRRhpraiTR-AGQVKGNGTRHEKDDRRRIRSRYVL-GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1322 SRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRqLSKANAEAqvwrskyesdgvarsEELEEAKRKLQARLAEAEE 1401
Cdd:COG4913 643 LQERREALQRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDL---------------AALEEQLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1402 TIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKK--QKAFDKIIGEWKLK--VDDLAAELDASQKECRNYS 1477
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERelRENLEERIDALRARLNRAE 786
|
650
....*....|
gi 24584706 1478 TELFRLKGAY 1487
Cdd:COG4913 787 EELERAMRAF 796
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1337-1883 |
5.70e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1337 HDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARlaeaEETIESLNqkcIGLEKT 1416
Cdd:pfam05483 60 HYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQ----RKAIQELQ---FENEKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1417 KQRLSTEVEDLQLEVDRANAI-----------ANAAEKKQK------AFDKIIGEWKLKVDDLAAELDASQKECRNYSTE 1479
Cdd:pfam05483 133 SLKLEEEIQENKDLIKENNATrhlcnllketcARSAEKTKKyeyereETRQVYMDLNNNIEKMILAFEELRVQAENARLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1480 L-FRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVL 1558
Cdd:pfam05483 213 MhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1559 RAQLELSQVRQEIDRRIQEK---EEEFENTRKNHQRALDSMQASLEAEAKGKA-----------------EALRM-KKKL 1617
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQkalEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfvvtefeattcsleELLRTeQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1618 EADINELEIALDHANKANAEAQKNIK---RYQQQLKDIQTALEEEQRARDDAREqlgiSERRANALQNELEESRTLLEQA 1694
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKfknNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAR 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1695 DRGRRQAE--------------QELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVD 1760
Cdd:pfam05483 449 EKEIHDLEiqltaiktseehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1761 AARLADEL----RAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANAlKGGKKAIQKLEQRVRELENELDGEQRRHADAQ 1836
Cdd:pfam05483 529 EERMLKQIenleEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 24584706 1837 KNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEE 1883
Cdd:pfam05483 608 KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
817-1325 |
6.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 817 LRKYLQLRTWPWYKLWQKvKPLLNVSRIEDEIARLEEKAKKAEELHAAevkvRKELEALNAKL------LAEKTALLDSL 890
Cdd:COG4717 47 LLERLEKEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELeeleaeLEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 891 SGEKGALQDYQERnAKLTAQKNDLENQLRDIQERLTQEEDARNQLfqqkKKADQEISGLKKDIEDLElnvqkaEQDKATK 970
Cdd:COG4717 122 EKLLQLLPLYQEL-EALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQEELEELL------EQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 971 DHQIRNLNDEIAHQDelinklnkekkmqgetnqktgEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRgdveks 1050
Cdd:COG4717 191 EEELQDLAEELEELQ---------------------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEE------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1051 KRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLedeQVVVLKHQRQIKELQARIEELEEEVEAERQARAK 1130
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL---ALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1131 AEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQheSTLANLRKKHNDAVAEMAEQVDQLN 1210
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA--ALLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1211 KLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEkiAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIEN--SDLLR 1288
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQ 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 24584706 1289 QLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRER 1325
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1288-1859 |
6.16e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.21 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1288 RQLEEAESQVSQLSKiKISLTTQLEDTKRLADEESRerATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKAnaea 1367
Cdd:pfam15921 78 RVLEEYSHQVKDLQR-RLNESNELHEKQKFYLRQSV--IDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNT---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1368 qvwrskyesdgvarSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQlevdranaiaNAAEKKQKA 1447
Cdd:pfam15921 151 --------------VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFE----------EASGKKIYE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1448 FDKIIgewKLKVDDLAAeldASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKN----LADEVKDLLDQ-IGEggrni 1522
Cdd:pfam15921 207 HDSMS---TMHFRSLGS---AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkielLLQQHQDRIEQlISE----- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1523 HEIEKARKRLEAEKdelqaaleeaeaaleqeenkvLRAQLELSQVRQEIdrrIQEKEEEFENTRKNHQRALDSMQASLEA 1602
Cdd:pfam15921 276 HEVEITGLTEKASS---------------------ARSQANSIQSQLEI---IQEQARNQNSMYMRQLSDLESTVSQLRS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1603 EAKgkaEALRMkkkLEADINELEIALDHANKANAEAQKNIKRYQQQ-----------LKDI-----QTALEEEQRAR--- 1663
Cdd:pfam15921 332 ELR---EAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlddqlqklLADLhkrekELSLEKEQNKRlwd 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1664 DDAREQLGISERRANALQNELEESR-TLLEQADRGRRQAEQEladahEQLNEVSAQNAS---ISAAKRKLESELQTLHSD 1739
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRlEALLKAMKSECQGQME-----RQMAAIQGKNESlekVSSLTAQLESTKEMLRKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1740 LDElLNEAKNSEEKAKKAMVD-AARLADELRAEQDHAQTQEKLRKALEQQIKELQ--------VRLDEAEANALK----G 1806
Cdd:pfam15921 481 VEE-LTAKKMTLESSERTVSDlTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegdhLRNVQTECEALKlqmaE 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 24584706 1807 GKKAIQKLEQRVRELeNELDGEQRRHADA----QKNLRK--SERRVKELSFQSEEDRKN 1859
Cdd:pfam15921 560 KDKVIEILRQQIENM-TQLVGQHGRTAGAmqveKAQLEKeiNDRRLELQEFKILKDKKD 617
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1647-1875 |
6.51e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1647 QQLKDIQTALEEEQRARDdAREQLGISERRANALQNELEESRTLLEQAD-----RGRRQAEQELADAHEQLNEVSAQNAS 1721
Cdd:COG4913 235 DDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1722 ISAAKRKLESELQTLHSDLDELLNEAKnseekakkamvdaARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAE- 1800
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRL-------------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAe 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584706 1801 --ANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELsfqseEDRKN--HERMQDLVDKLQQKIK 1875
Cdd:COG4913 381 efAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-----ERRKSniPARLLALRDALAEALG 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1458-1688 |
2.06e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1458 KVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKD 1537
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1538 ELQAALEeaeaaleqeenKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKL 1617
Cdd:COG4942 101 AQKEELA-----------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1618 EADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESR 1688
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
998-1210 |
2.32e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 998 QGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQ 1077
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1078 TIQRKDKELSSITAKL----EDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEelgerleeag 1153
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------- 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1154 gATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKK---HNDAVAEMAEQVDQLN 1210
Cdd:COG4942 168 -ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELE 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1597-1803 |
2.37e-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: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1597 QASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGiseRR 1676
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1677 ANALQNE---LEESRTLLEQADRG----RRQAEQELADAH-EQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAK 1748
Cdd:COG3883 92 ARALYRSggsVSYLDVLLGSESFSdfldRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1749 NSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANA 1803
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1555-1757 |
2.73e-07 |
|
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: 53.78 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1555 NKVLRAQLELsqvrQEIDRRIQEkeeeFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALdhanka 1634
Cdd:COG1579 3 PEDLRALLDL----QELDSELDR----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1635 nAEAQKNIKRYQQQLKDIQTAleeeqrarddareqlgiseRRANALQNEleesrtlLEQADRGRRQAEQELADAHEQLNE 1714
Cdd:COG1579 69 -EEVEARIKKYEEQLGNVRNN-------------------KEYEALQKE-------IESLKRRISDLEDEILELMERIEE 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24584706 1715 VSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKA 1757
Cdd:COG1579 122 LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1172-1886 |
2.89e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1172 KLRRDLEEAniqhESTLANLRKKHNDAVAEMAEQVDQLNKLKAkaekekneyygqlnDLRAGVDH---ITNEKAAQEKIa 1248
Cdd:PRK04863 290 ELRRELYTS----RRQLAAEQYRLVEMARELAELNEAESDLEQ--------------DYQAASDHlnlVQTALRQQEKI- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1249 KQLQHTLNEVQSKLDETNRTLNDFDaskkklsiensdllRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESR----- 1323
Cdd:PRK04863 351 ERYQADLEELEERLEEQNEVVEEAD--------------EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTraiqy 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1324 -------ERA-TLLGK----FRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYES-----DGVARSEELE 1386
Cdd:PRK04863 417 qqavqalERAkQLCGLpdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLvrkiaGEVSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1387 EAKRKLQaRLAEAEETIESLNQKCIGLEKTKQRLSTEvEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLaael 1466
Cdd:PRK04863 497 VARELLR-RLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL---- 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1467 DASQKECRNYSTELfrlkgayEEGQEQLEAVRRENKNLA-------DEVKDLLDQIGEGGRNIHEIEKARKRLeaekdel 1539
Cdd:PRK04863 571 SESVSEARERRMAL-------RQQLEQLQARIQRLAARApawlaaqDALARLREQSGEEFEDSQDVTEYMQQL------- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1540 qaaleeaeaaleqeenkvLRAQLELSQVRQEIDRRIQEKEEEFENtrknhqraLDSMQASLEAEAKGKAEalRMKKKLEA 1619
Cdd:PRK04863 637 ------------------LERERELTVERDELAARKQALDEEIER--------LSQPGGSEDPRLNALAE--RFGGVLLS 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1620 DINElEIALDHANKANAeaqknikRYQQ--------QLKDIQTALEeeqrARDDAREQLGISERRANALQN-----ELEE 1686
Cdd:PRK04863 689 EIYD-DVSLEDAPYFSA-------LYGParhaivvpDLSDAAEQLA----GLEDCPEDLYLIEGDPDSFDDsvfsvEELE 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1687 SRTLLEQADR-------------GRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEK 1753
Cdd:PRK04863 757 KAVVVKIADRqwrysrfpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPE 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1754 AKKAMVDAAR------LADELRAEQDHAQTQEKLRKA------------------LEQQIKELQVRLDEAEANA--LKGG 1807
Cdd:PRK04863 837 AELRQLNRRRveleraLADHESQEQQQRSQLEQAKEGlsalnrllprlnlladetLADRVEEIREQLDEAEEAKrfVQQH 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1808 KKAIQKLEQRV---RELENELDGEQRRHADAQKNLRKSERRVKELS--------FQSEEDRKNHERMQDLVDKLQQKIKT 1876
Cdd:PRK04863 917 GNALAQLEPIVsvlQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTevvqrrahFSYEDAAEMLAKNSDLNEKLRQRLEQ 996
|
810
....*....|
gi 24584706 1877 YKRQIEEAEE 1886
Cdd:PRK04863 997 AEQERTRARE 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1685-1922 |
3.10e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1685 EESRTLLEQA------DRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESElqtlhSDLDELLNEAKNSEEKAKKAM 1758
Cdd:TIGR02168 155 EERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDILNELERQLKSLERQ-----AEKAERYKELKAELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1759 vdaarLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEAnalkggkkAIQKLEQRVRELENELDGEQRRHADAQKN 1838
Cdd:TIGR02168 230 -----LVLRLEELREELEELQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEEIEELQKELYALANE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1839 LRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKR-------QIEEAEEIAALNLAKFRKAQQELEEAEERADL 1911
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEelaeleeKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250
....*....|.
gi 24584706 1912 AEQAISKFRAK 1922
Cdd:TIGR02168 377 LEEQLETLRSK 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1242-1472 |
3.39e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1242 AAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKlsiensdLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEE 1321
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA-------LLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1322 SRERATLLGKFRNLEHDL-DNLREQVEEEAEGKADLqrQLSKANAEAQVWRSKYESdgvARSEELEEAKRKLQARLAEAE 1400
Cdd:COG4942 89 EKEIAELRAELEAQKEELaELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLK---YLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1401 ETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKE 1472
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1631-1885 |
3.80e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.03 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1631 ANKANAEAQKNIKRY-QQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAH 1709
Cdd:pfam05667 226 WNSQGLASRLTPEEYrKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1710 EQLNEVSAQNASISAAKRKLESELQTLH----SDLDELLNEAKNSEEKAKKAMvdaARLADELRAEQDHAQTQEKLRKAL 1785
Cdd:pfam05667 306 LQFTNEAPAATSSPPTKVETEEELQQQReeelEELQEQLEDLESSIQELEKEI---KKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1786 EQQIKeLQVR----LDEAEANALKGgKKAIQKLEQRVRELENE-------LDGEQRRHADAQKNlRKSERRVKelsfqSE 1854
Cdd:pfam05667 383 EKQYK-VKKKtldlLPDAEENIAKL-QALVDASAQRLVELAGQwekhrvpLIEEYRALKEAKSN-KEDESQRK-----LE 454
|
250 260 270
....*....|....*....|....*....|.
gi 24584706 1855 EDRKNHERMQDLVDKLQQKIKTYKRQIEEAE 1885
Cdd:pfam05667 455 EIKELREKIKEVAEEAKQKEELYKQLVAEYE 485
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
897-1058 |
3.81e-07 |
|
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: 53.39 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 897 LQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAE--QDKATKDHQI 974
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 975 RNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLERE-KKVRGDVEKSKRK 1053
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAElEELEAEREELAAK 171
|
....*
gi 24584706 1054 VEGDL 1058
Cdd:COG1579 172 IPPEL 176
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1298-1883 |
4.09e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.14 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1298 SQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQrQLSKANAEAQVWRSKYESd 1377
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAE-GLRAALAGAEMVRKNLEE- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1378 gvARSEELEEAKRKLQARLAEA----EETIESLNQKCIGLEKTKQrlstevedlQLEVDRANAIANAAEKKQKAfdkiig 1453
Cdd:pfam07111 137 --GSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLN---------SLETKRAGEAKQLAEAQKEA------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1454 ewklkvDDLAAELDASQKECRNYSTELFRLKGAYeeGQEQLEAVRRENKNLadEVKDLLDQIgeggrniheiekarKRLE 1533
Cdd:pfam07111 200 ------ELLRKQLSKTQEELEAQVTLVESLRKYV--GEQVPPEVHSQTWEL--ERQELLDTM--------------QHLQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1534 AEKDElqaaleeaeaaleqeenkvLRAQLELSQVR-QEIDRRIQEKEEEFenTRKnhQRALDSmqasLEAEAKGKAEAL- 1611
Cdd:pfam07111 256 EDRAD-------------------LQATVELLQVRvQSLTHMLALQEEEL--TRK--IQPSDS----LEPEFPKKCRSLl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1612 -RMKKKLEAdineLEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQ----RARDDAREQLGISERRANALQNELEe 1686
Cdd:pfam07111 309 nRWREKVFA----LMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailqRALQDKAAEVEVERMSAKGLQMELS- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1687 srtlleQADRGRRQAEQELADAHEQL----NEVSAQNASISAAKRKLESELQTLHSdLDELLNEAKNSEEKAKKAMVDAA 1762
Cdd:pfam07111 384 ------RAQEARRRQQQQTASAEEQLkfvvNAMSSTQIWLETTMTRVEQAVARIPS-LSNRLSYAVRKVHTIKGLMARKV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1763 RLAdELRAEQ------------DHAQTQEKLRKALEQQIKELQV--RLDEAE-ANALKGGKKAIQKLEQRVRELENELDG 1827
Cdd:pfam07111 457 ALA-QLRQEScpppppappvdaDLSLELEQLREERNRLDAELQLsaHLIQQEvGRAREQGEAERQQLSEVAQQLEQELQR 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1828 EQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDK-LQQKIKTYKRQIEE 1883
Cdd:pfam07111 536 AQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQaLQEKVAEVETRLRE 592
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1563-1800 |
4.72e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1563 ELSQVRQEIDRRIqekeEEFENTRKNHQRALDSMQASLEAEAKGKAEA-LRMKKKLEADINELEIALDHANKANAEAQKN 1641
Cdd:COG3096 840 ALRQRRSELEREL----AQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnLLADETLADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1642 IKRYQQqLKDIQTAL-------EEEQRARDDAREQLGISERRANAL---------------QNELEESRTLLEQADRGRR 1699
Cdd:COG3096 916 GKALAQ-LEPLVAVLqsdpeqfEQLQADYLQAKEQQRRLKQQIFALsevvqrrphfsyedaVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1700 QAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLA-DELRAEQDHAQTQ 1778
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRrDELHEELSQNRSR 1074
|
250 260
....*....|....*....|....*.
gi 24584706 1779 ----EKLRKALEQQIKELQVRLDEAE 1800
Cdd:COG3096 1075 rsqlEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1828 |
4.98e-07 |
|
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: 53.00 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1646 QQQLKDIQ---TALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASI 1722
Cdd:COG1579 6 LRALLDLQeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1723 SAAKrklesELQTLHSDLDELLNEAKNSEEKAKKAMvdaarlaDELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEAN 1802
Cdd:COG1579 86 RNNK-----EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....*.
gi 24584706 1803 AlkggKKAIQKLEQRVRELENELDGE 1828
Cdd:COG1579 154 L----EAELEELEAEREELAAKIPPE 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
950-1202 |
5.88e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 950 KKDIEDLeLNVQK-AEQDKATKDhQIRNLNDEIAHQDELIN----KLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKA 1024
Cdd:PHA02562 153 RKLVEDL-LDISVlSEMDKLNKD-KIRELNQQIQTLDMKIDhiqqQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1025 KLEQTLDELEDSLErekkvrgDVEKSKRKVEGDL-KLTQEAV---ADLERNKKELE------------QTIQRKDKELSS 1088
Cdd:PHA02562 231 TIKAEIEELTDELL-------NLVMDIEDPSAALnKLNTAAAkikSKIEQFQKVIKmyekggvcptctQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1089 ITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAqielNKKREA 1168
Cdd:PHA02562 304 IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE----FVDNAE 379
|
250 260 270
....*....|....*....|....*....|....*.
gi 24584706 1169 ELSKLRRDLEEANiqheSTLANLRKK--HNDAVAEM 1202
Cdd:PHA02562 380 ELAKLQDELDKIV----KTKSELVKEkyHRGIVTDL 411
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1381-1885 |
6.08e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1381 RSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLqlevdranaianaaEKKQKAFDKIIGEWKLKVD 1460
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL--------------EQQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1461 DLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQ 1540
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1541 AALEEAEAALEQEENKVLRAQLELSQvrqeidrrIQEKEEEFentrknhqraldsmqasleaeakgkaealrmkKKLEAD 1620
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSN--------LKKKIQKN--------------------------------KSLESQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1621 INELEialdhanKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQ 1700
Cdd:TIGR04523 220 ISELK-------KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1701 AEQELADAHEQ-----LNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHA 1775
Cdd:TIGR04523 293 LKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1776 QTQEKLRKALEQQIKELQVRLDEAEANaLKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEE 1855
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESK-IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
490 500 510
....*....|....*....|....*....|
gi 24584706 1856 DRKNHERMQDLVDKLQQKIKTYKRQIEEAE 1885
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1658-1885 |
6.22e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1658 EEQRARDDAREQLGISERRANALQNELEESR-------TLLEQADRGRRQAEQELADAHEQLNEvsaqnasisaAKRKLE 1730
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRAELLQNRLEECLqeraellQAQEAANRQREKEKERYKRDREQWER----------QRRELE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1731 SELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANalkggkka 1810
Cdd:pfam07888 80 SRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1811 IQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHE-------RMQDLVDKLQQKIKTYKRQIEE 1883
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAqrdtqvlQLQDTITTLTQKLTTAHRKEAE 231
|
..
gi 24584706 1884 AE 1885
Cdd:pfam07888 232 NE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1638 |
9.01e-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: 53.23 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1387 EAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAEL 1466
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1467 DASQKECRNystelfRLKGAYEEGQEQLEAVRRENKNLADEVKDL--LDQIGEGGRN-IHEIEKARKRLEAEKDelqaal 1543
Cdd:COG4942 100 EAQKEELAE------LLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREqAEELRADLAELAALRA------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1544 eeaeaaleqeenKVLRAQLELSQVRQEidrrIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINE 1623
Cdd:COG4942 168 ------------ELEAERAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*
gi 24584706 1624 LEIALDHANKANAEA 1638
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1172-1761 |
1.06e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1172 KLRRDLEEanIQHestlanLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQL 1251
Cdd:pfam05483 216 KLKEDHEK--IQH------LEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1252 QHTLNEVQSKLDET----NRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKIS---LTTQLEDTKRLADEESRE 1324
Cdd:pfam05483 288 IEKKDHLTKELEDIkmslQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfVVTEFEATTCSLEELLRT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1325 RAtllgkfRNLEHDLDNLREQVEEEAEGKADLQRQLS-KANAEAQVWRSKyesDGVARSEELEEAKRKLQarlaEAEETI 1403
Cdd:pfam05483 368 EQ------QRLEKNEDQLKIITMELQKKSSELEEMTKfKNNKEVELEELK---KILAEDEKLLDEKKQFE----KIAEEL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1404 ESLNQKCIGLEKTKQRlstEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRL 1483
Cdd:pfam05483 435 KGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1484 KGAYEEGQEQLEAVRRENKNLADEVKDLlDQIGEGGRNihEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLE 1563
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENL-EEKEMNLRD--ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1564 LSQVRQEIDRRIQEKEEEFENTRKNHQRaldsmqaSLEAEAKGKAEALRMkKKLEADINELEIALDHANKANAEAQKNik 1643
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQE-------NKALKKKGSAENKQL-NAYEIKVNKLELELASAKQKFEEIIDN-- 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1644 rYQQQLKDIQTA----LEEEQRARDDAREQLGISERRANALQNELEESRTLLEqadRGRRQAEQELADAHEQLNEVSAQN 1719
Cdd:pfam05483 659 -YQKEIEDKKISeeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALME---KHKHQYDKIIEERDSELGLYKNKE 734
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 24584706 1720 ASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDA 1761
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1105-1705 |
1.11e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.99 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1105 RQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGG--ATSAQIELNKKREAELSKlrRDLEEANI 1182
Cdd:pfam07111 70 RQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGlrAALAGAEMVRKNLEEGSQ--RELEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1183 QHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNE-KAAQEKIAKQL---------- 1251
Cdd:pfam07111 148 LHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQlSKTQEELEAQVtlveslrkyv 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1252 -QHTLNEVQSKLDETNRtlNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKI----KISLTTQLEDTKRLADEESRERA 1326
Cdd:pfam07111 228 gEQVPPEVHSQTWELER--QELLDTMQHLQEDRADLQATVELLQVRVQSLTHMlalqEEELTRKIQPSDSLEPEFPKKCR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1327 TLLGKFR-------------NLEH---------DLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEE 1384
Cdd:pfam07111 306 SLLNRWRekvfalmvqlkaqDLEHrdsvkqlrgQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1385 lEEAKRKLQARLAEAEE----TIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVD 1460
Cdd:pfam07111 386 -QEARRRQQQQTASAEEqlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1461 DLAAELDASQKECrNYSTELfrlkgayeegqEQLeavrRENKNLADEVKDLLDQIGEggrniHEIEKARKRLEAEKdelq 1540
Cdd:pfam07111 465 SCPPPPPAPPVDA-DLSLEL-----------EQL----REERNRLDAELQLSAHLIQ-----QEVGRAREQGEAER---- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1541 aalEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEalrMKKKLEAD 1620
Cdd:pfam07111 520 ---QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAE---VETRLREQ 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1621 INELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGisERRANALQnELEESRTL----LEQADR 1696
Cdd:pfam07111 594 LSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEG--QRLARRVQ-ELERDKNLmlatLQQEGL 670
|
....*....
gi 24584706 1697 GRRQAEQEL 1705
Cdd:pfam07111 671 LSRYKQQRL 679
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1559-1889 |
1.13e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.36 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1559 RAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDS---MQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKAN 1635
Cdd:pfam07888 66 RDREQWERQRRELESRVAELKEELRQSREKHEELEEKykeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1636 AEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAE-------QELADA 1708
Cdd:pfam07888 146 LERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtittltQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1709 HEQLNEVSAQNASISAAKRKLESELQT---LHSDLDELLNEAKNSEEKAKKAMVDAARLADELraeqdhAQTQEKLRKAL 1785
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKvegLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL------ADASLALREGR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1786 EQQIKELQVRLDEAEANALKGGK--KAIQKLEQRVRELENE---LDGEQRRHADAQK-NLRKSERRVKELSFQSEEDRKN 1859
Cdd:pfam07888 300 ARWAQERETLQQSAEADKDRIEKlsAELQRLEERLQEERMErekLEVELGREKDCNRvQLSESRRELQELKASLRVAQKE 379
|
330 340 350
....*....|....*....|....*....|
gi 24584706 1860 HERMQdlvdKLQQKIKTYKRQIEEAEEIAA 1889
Cdd:pfam07888 380 KEQLQ----AEKQELLEYIRQLEQRLETVA 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1331-1889 |
1.13e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1331 KFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQvwrskyesdgvARSEELEEAKRKLQaRLAEAEETIESLNQKC 1410
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN-----------NAMDDYNNLKSALN-ELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1411 IGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKafDKIIGEWKLKVD--DLAAELDASQKECRNYSTELFRLKGAYE 1488
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNR--NYINDYFKYKNDieNKKQILSNIDAEINKYHAIIKKLSVLQK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1489 EGQEQLEAVRR--ENKNLADEVKDLLDQIGEGGRNIHEIEKarKRLEAEKDELQAALEEAEAALEQEENKVlraqlELSQ 1566
Cdd:PRK01156 337 DYNDYIKKKSRydDLNNQILELEGYEMDYNSYLKSIESLKK--KIEEYSKNIERMSAFISEILKIQEIDPD-----AIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1567 VRQEIDRRIQEKEEEFENTrknhQRALDSMQASLEaEAKGKAEALRMKKKL--------EADINELeiaLDHANKANAEA 1638
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSL----NQRIRALRENLD-ELSRNMEMLNGQSVCpvcgttlgEEKSNHI---INHYNEKKSRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1639 QKNIKRYQQQLKDIqtalEEEQRARDDAREQLGISE-RRANALQNELEESRTLLEQAdrgrRQAEQELADAHEQLNEVSA 1717
Cdd:PRK01156 482 EEKIREIEIEVKDI----DEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDI----KIKINELKDKHDKYEEIKN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1718 QNASIS----AAKRKLESELQTLHSDLDeLLNEAKNSEEKAKKAMVDAARLAD-ELRAEQDHAQTQEKLRKaLEQQIKEL 1792
Cdd:PRK01156 554 RYKSLKledlDSKRTSWLNALAVISLID-IETNRSRSNEIKKQLNDLESRLQEiEIGFPDDKSYIDKSIRE-IENEANNL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1793 QVRLDEAEANalkggKKAIQKLEQRVRELENE---LDGEQRRHA-------DAQKNLRKSERRVKELSFQSEEDRKNHER 1862
Cdd:PRK01156 632 NNKYNEIQEN-----KILIEKLRGKIDNYKKQiaeIDSIIPDLKeitsrinDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
570 580
....*....|....*....|....*..
gi 24584706 1863 MQDLVDKLQQKIKTYKRQIEEAEEIAA 1889
Cdd:PRK01156 707 LRTRINELSDRINDINETLESMKKIKK 733
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
853-1533 |
1.54e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 853 EKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDAR 932
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 933 NQLFQQKKKADQEISGLKkdiedlELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAA 1012
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIE------ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1013 EDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKrkveGDLKLTQEAVADLERNKKELEQ--TIQRKDKELSSIT 1090
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT----SIREISCQQHTLTQHIHTLQQQktTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1091 AKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAEL 1170
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1171 SKLRR--DLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEY-YGQ--LNDLRAGVDHITNEKAAQE 1245
Cdd:TIGR00618 483 LQETRkkAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYaQLEtsEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1246 KIAKQLQHT--------------LNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEaesqvsQLSKIKISLTTQl 1311
Cdd:TIGR00618 563 EQMQEIQQSfsiltqcdnrskedIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP------EQDLQDVRLHLQ- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1312 edtkRLADEESRERATLLGKFRNLEHDldnlrEQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARsEELEEAKRK 1391
Cdd:TIGR00618 636 ----QCSQELALKLTALHALQLTLTQE-----RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK-EMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1392 LQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQ-----LEVDRANAIANAAEKKQKAFDKIIGEWKL--KVDDLAA 1464
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNqslkeLMHQARTVLKARTEAHFNNNEEVTAALQTgaELSHLAA 785
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1465 ELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRR-ENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLE 1533
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
842-1510 |
1.94e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEELHAAEVKVRKELE---ALNAKLLAEKTA------LLD---SLSGEKGALQDYQERNAKLTA 909
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVSLKLEeeiQENKDLIKENNAtrhlcnLLKetcARSAEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 910 Q--KNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGL----KKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAH 983
Cdd:pfam05483 186 MdlNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 984 QDELINKLNKEKKMQGETnqktgeeLQAAEDKINHLNKvkaKLEQTLDELEDSLEREKKVRGDVEKSKRKVegdLKLTQE 1063
Cdd:pfam05483 266 SRDKANQLEEKTKLQDEN-------LKELIEKKDHLTK---ELEDIKMSLQRSMSTQKALEEDLQIATKTI---CQLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1064 AVADLERNKK----------ELEQTIQRKDKELSSITAKLEDEQ----VVVLKHQRQIKELQARIEELEEEVEAERQARA 1129
Cdd:pfam05483 333 KEAQMEELNKakaahsfvvtEFEATTCSLEELLRTEQQRLEKNEdqlkIITMELQKKSSELEEMTKFKNNKEVELEELKK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1130 K-AEKQRadLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVD- 1207
Cdd:pfam05483 413 IlAEDEK--LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1208 --QLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHtlnevqskLDETNRTLNDfdaskkklsiensd 1285
Cdd:pfam05483 491 taHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN--------LEEKEMNLRD-------------- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1286 llrqleEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQ---LSK 1362
Cdd:pfam05483 549 ------ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkaLKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1363 ANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLN---QKCIGLEKTKQRLSTEVEDLQLEVDR--ANAI 1437
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKrcQHKI 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1438 ANAA---EKKQKAFDKIIGE-------WKLKVDDLAAELDASQKECRNYSTELFRLKgayeegqEQLEAVRRENKNLADE 1507
Cdd:pfam05483 703 AEMValmEKHKHQYDKIIEErdselglYKNKEQEQSSAKAALEIELSNIKAELLSLK-------KQLEIEKEEKEKLKME 775
|
...
gi 24584706 1508 VKD 1510
Cdd:pfam05483 776 AKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1042 |
1.99e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 845 EDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALldslsgekGALQDYQERNAKLTAqkndLENQLRDIQER 924
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEIDVAS----AEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 925 LTQEEDARNQLfqqkKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNqk 1004
Cdd:COG4913 677 LERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-- 750
|
170 180 190
....*....|....*....|....*....|....*...
gi 24584706 1005 tGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKK 1042
Cdd:COG4913 751 -LEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
652-676 |
1.99e-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: 50.04 E-value: 1.99e-06
10 20
....*....|....*....|....*
gi 24584706 652 YKEQLNSLMTTLRSTQPHFVRCIIP 676
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1698-1938 |
2.46e-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: 52.07 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1698 RRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQdhaQT 1777
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR---AE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1778 QEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLeqRVRELENELDGEQRRHADAQKnlrkseRRVKELSFQSEEDR 1857
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEELR------ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1858 KNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPR 1937
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 24584706 1938 A 1938
Cdd:COG4942 251 L 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
843-1073 |
2.46e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 843 RIEDEIARLEEKAKKAEELHAAEVKVRKELEALnaKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQK--NDLENQLRD 920
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELL--EPIRELAERYAAARERLAELEYLRAALRLWFAQRrlELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 921 IQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELnvqkaeQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGE 1000
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1001 TNQKTGEELQAAedkinhlnkvKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKK 1073
Cdd:COG4913 374 PLPASAEEFAAL----------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1282-1714 |
3.44e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1282 ENSDLLRQLEEAESQVSQlskikislttQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLS 1361
Cdd:pfam07888 42 ERAELLQAQEAANRQREK----------EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1362 KANAEAQVwrskyesdgvarseeLEEAKRKLQARLAEAEETIESLNQKCIGLEktkqrlsTEVEDLQLEVDRAnaianAA 1441
Cdd:pfam07888 112 ELSEEKDA---------------LLAQRAAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKA-----GA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1442 EKKQKAFDKiigewklkvDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEavrrenkNLADEVKDLLDQIGEGGRN 1521
Cdd:pfam07888 165 QRKEEEAER---------KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-------QLQDTITTLTQKLTTAHRK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1522 IHEIEKARKRLEAEKDELQAALEeaeaaleqeenKVLRAQLELSQVRQEIDRRIQEKeeefentrknHQRALDSMQASL- 1600
Cdd:pfam07888 229 EAENEALLEELRSLQERLNASER-----------KVEGLGEELSSMAAQRDRTQAEL----------HQARLQAAQLTLq 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1601 --EAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERran 1678
Cdd:pfam07888 288 laDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR--- 364
|
410 420 430
....*....|....*....|....*....|....*....
gi 24584706 1679 alqnELEESRTLLEQADRGRRQ---AEQELADAHEQLNE 1714
Cdd:pfam07888 365 ----ELQELKASLRVAQKEKEQlqaEKQELLEYIRQLEQ 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1657-1899 |
3.48e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1657 EEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAE--QELADAHEQLnEVSAqnasISAAKRKLESELQ 1734
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREY-EGYE----LLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1735 TLHSDLDELLNEAKNSEEKAKKamvdaarLADEL-RAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANalkggkkaIQK 1813
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISE-------LEKRLeEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--------IAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1814 LEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLA 1893
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
....*.
gi 24584706 1894 KFRKAQ 1899
Cdd:TIGR02169 386 ELKDYR 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1659-1861 |
3.60e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1659 EQRARDDAREQLGISERRANALQNELEEsrtlLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHS 1738
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1739 DLDelLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRV 1818
Cdd:COG4717 124 LLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24584706 1819 RELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHE 1861
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1605-1915 |
3.73e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1605 KGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNEL 1684
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1685 EESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARL 1764
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1765 ADELRAEQDhAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSER 1844
Cdd:COG4372 170 EQELQALSE-AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1845 RVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQA 1915
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
844-1827 |
4.74e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 844 IEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALldslsGEKGALQDYQERNAKLTAQkndLENQLRDIQE 923
Cdd:PRK04863 302 LAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-----RQQEKIERYQADLEELEER---LEEQNEVVEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 924 RLTQEEDARNQLFQqkkkADQEISGLKKDIEDLE--LNVQkaeQDKATKDHQIRNLNDEiahqdelINKLNKEKKMQGET 1001
Cdd:PRK04863 374 ADEQQEENEARAEA----AEEEVDELKSQLADYQqaLDVQ---QTRAIQYQQAVQALER-------AKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1002 NQKTGEELQAAEDKI-NHLNKVKAKL---EQTLDELEDSLEREKKVRGDVEKSKRKVEGdlkltQEAVADLERNKKELEQ 1077
Cdd:PRK04863 440 AEDWLEEFQAKEQEAtEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVSRSEAWDVA-----RELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1078 TIQRKdKELSSITAKLEDEQVVvlkhQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEeaggATS 1157
Cdd:PRK04863 515 LQQLR-MRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRM----ALR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1158 AQIELNKKREAELSKLRrdleEANIQHESTLANLRKKHNDAVAEmAEQVDQLNKLKAKaekekneyygQLNDLRAGVDHI 1237
Cdd:PRK04863 586 QQLEQLQARIQRLAARA----PAWLAAQDALARLREQSGEEFED-SQDVTEYMQQLLE----------RERELTVERDEL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1238 -TNEKAAQEKIAKQLQHTLNEvqsklDETNRTLND----------FDaskkKLSIEN----SDLLRQLEEAeSQVSQLSK 1302
Cdd:PRK04863 651 aARKQALDEEIERLSQPGGSE-----DPRLNALAErfggvllseiYD----DVSLEDapyfSALYGPARHA-IVVPDLSD 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1303 IKISLTTqLEDtkrladeesreratLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANaeaqvWR-SKYESDGV-- 1379
Cdd:PRK04863 721 AAEQLAG-LED--------------CPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQ-----WRySRFPEVPLfg 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1380 -----ARSEELEEAKRKLQARLAEAE---ETIESLNQKC---IG--------------LEKTKQRLS---TEVEDLQLEV 1431
Cdd:PRK04863 781 raareKRIEQLRAEREELAERYATLSfdvQKLQRLHQAFsrfIGshlavafeadpeaeLRQLNRRRVeleRALADHESQE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1432 DRANAIANAAEKKQKAFDKIIGEWKL--------KVDDLAAELDASQKECR------NYSTELFRLKGAYEEGQEQLEAV 1497
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALNRLLPRLNLladetladRVEEIREQLDEAEEAKRfvqqhgNALAQLEPIVSVLQSDPEQFEQL 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1498 RREnknlADEVKDLLDQIGEGGRNIHEI---------EKARKRLEAEKDelqaaleeaeaaleqeENKVLRAQLELSQV- 1567
Cdd:PRK04863 941 KQD----YQQAQQTQRDAKQQAFALTEVvqrrahfsyEDAAEMLAKNSD----------------LNEKLRQRLEQAEQe 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1568 RQEIDRRIQEKEEEFentRKNHQRaldsmQASLEAEAKGKAEalrMKKKLEADINELEIALDhankANAEAQKNIKRyqq 1647
Cdd:PRK04863 1001 RTRAREQLRQAQAQL---AQYNQV-----LASLKSSYDAKRQ---MLQELKQELQDLGVPAD----SGAEERARARR--- 1062
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1648 qlKDIQTALEEEQRARDDAREQLGISERRANALQNELEES-------RTLLEQAdRGRRQAEQELADAH--------EQL 1712
Cdd:PRK04863 1063 --DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLerdyhemREQVVNA-KAGWCAVLRLVKDNgverrlhrREL 1139
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1713 NEVSAQNA-SISaakRKLESELQTLHSDlDELLNEAKNSEEKAKKA------MVDAARLADElRAEQDHAQTQEKlRKAL 1785
Cdd:PRK04863 1140 AYLSADELrSMS---DKALGALRLAVAD-NEHLRDVLRLSEDPKRPerkvqfYIAVYQHLRE-RIRQDIIRTDDP-VEAI 1213
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1786 EQ---QIKELQVRLDEAE----------ANALkggKKAIQKLEQRVRELENELDG 1827
Cdd:PRK04863 1214 EQmeiELSRLTEELTSREqklaissesvANII---RKTIQREQNRIRMLNQGLQN 1265
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1152-1382 |
5.02e-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: 50.92 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1152 AGGATSAQIELNKKREAELSKLRRDLEEAniqhESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAekekNEYYGQLNDLR 1231
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1232 AGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRT-----------LNDFDASKKKLSIENSDLLRQLEEAESQVSQL 1300
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1301 SKIKISLTTQLEDTKRLADEESRERATL----------LGKfrnLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVW 1370
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALealkaerqklLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|..
gi 24584706 1371 RSKYESDGVARS 1382
Cdd:COG4942 240 AERTPAAGFAAL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1732-1886 |
5.29e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1732 ELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGG---- 1807
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1808 -----------KKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELsfqseedrknHERMQDLVDKLQQKIKT 1876
Cdd:COG1579 91 yealqkeieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAELEE 160
|
170
....*....|
gi 24584706 1877 YKRQIEEAEE 1886
Cdd:COG1579 161 LEAEREELAA 170
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
857-1043 |
5.38e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 857 KAEELHAAEVKVRKELEALNAKLL-AEKtalldslsgekgALQDYQERN---------AKLTAQKNDLENQLRDIQERLT 926
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEeAEA------------ALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 927 QEEDARNQLFQQKKKADQEISGLKKD--IEDLELNVQKAEQDKA------TKDH-QIRNLNDEIAHQDELINKLNKEK-- 995
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAelsaryTPNHpDVIALRAQIAALRAQLQQEAQRIla 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24584706 996 --KMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKV 1043
Cdd:COG3206 317 slEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1561-1792 |
6.13e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.59 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1561 QLELSQVRQEIdrriqekeEEFENTRKNHQ-RALDSMQASLEAEAKGKAEALRMKK---------KLEADINELEIALDH 1630
Cdd:PRK10929 22 APDEKQITQEL--------EQAKAAKTPAQaEIVEALQSALNWLEERKGSLERAKQyqqvidnfpKLSAELRQQLNNERD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1631 ------ANKANAEAQKNIKRYQQQLKDIQTALEEEQ-RARD-------------DAREQLGISERRANALQNeleeSRTL 1690
Cdd:PRK10929 94 eprsvpPNMSTDALEQEILQVSSQLLEKSRQAQQEQdRAREisdslsqlpqqqtEARRQLNEIERRLQTLGT----PNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1691 LEQADRGRRQAEQELADAheQLNEVsaQNASISAAKR----KLESEL-QTLHSDLDELLNEAKNSEEKAKKAMVDAARLA 1765
Cdd:PRK10929 170 LAQAQLTALQAESAALKA--LVDEL--ELAQLSANNRqelaRLRSELaKKRSQQLDAYLQALRNQLNSQRQREAERALES 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 24584706 1766 DELRAEQ---------DHAQTQEKLRKALEQQIKEL 1792
Cdd:PRK10929 246 TELLAEQsgdlpksivAQFKINRELSQALNQQAQRM 281
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1619-1826 |
6.76e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.84 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1619 ADINELEIALDHANKANAEAQKNikRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEEsrtlleqadrgr 1698
Cdd:pfam05622 278 AEIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEE------------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1699 rqaeqeladAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRA-----EQD 1773
Cdd:pfam05622 344 ---------LQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEalrkkDED 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1774 HAQTQEKLRKALEQQ---IKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELD 1826
Cdd:pfam05622 415 MKAMEERYKKYVEKAksvIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1559-1793 |
7.55e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1559 RAQLELSQVRQEIDRRIQEkeeefenTRKNhQRALDSMQASLEAEAKGKAEALRMKKkLEADINELEIALdhankanAEA 1638
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAK-------LRQA-QAELEALKDDNDEETRETLSTLSLRQ-LESRLAQTLDQL-------QNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1639 QKNIKRYQQQLKDIQTALEEEQRARDDAREQLgiseRRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQ 1718
Cdd:PRK11281 141 QNDLAEYNSQLVSLQTQPERAQAALYANSQRL----QQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1719 NASI------------SAAKRKLESELQTLHsdldELLNE--AKNSEEKAKKAMV--DAAR------LADELRAEQDHAQ 1776
Cdd:PRK11281 217 GNTQlqdllqkqrdylTARIQRLEHQLQLLQ----EAINSkrLTLSEKTVQEAQSqdEAARiqanplVAQELEINLQLSQ 292
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24584706 1777 ------------TQEKLR------------KALEQQIKELQ 1793
Cdd:PRK11281 293 rllkateklntlTQQNLRvknwldrltqseRNIKEQISVLK 333
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1770-1890 |
8.58e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1770 AEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKEL 1849
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24584706 1850 SFQSEEDRKNHERMQDLVDKLQQKIKT-YKRQIEEAEEIAAL 1890
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEElIEEQLQELERISGL 150
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1164-1916 |
8.88e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1164 KKREAELSKLRRDLEEANIQ----HESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDL--RAGVDHI 1237
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELlvEQGRLQL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1238 TNEKAAQEKIAKQLQHTLNEVQSKLDETNRtlnDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRL 1317
Cdd:TIGR00606 355 QADRHQEHIRARDSLIQSLATRLELDGFER---GPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEI 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1318 ADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLA 1397
Cdd:TIGR00606 432 RDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1398 EAEETIESLNQKcigLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGE-----WKLKVDD----LAAELDA 1468
Cdd:TIGR00606 512 DLDRKLRKLDQE---MEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQLEDwlhsKSKEINQ 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1469 SQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLL---DQIGEGGRNIHEIEKARKRL------EAEKDEL 1539
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsqDEESDLERLKEEIEKSSKQRamlagaTAVYSQF 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1540 QAALEEAEAALEQEENKVLRAQLELSQVRQEID---RRIQEKEEEFENTRKNHQRALDSMQASLEaeakGKAEALRMKKK 1616
Cdd:TIGR00606 669 ITQLTDENQSCCPVCQRVFQTEAELQEFISDLQsklRLAPDKLKSTESELKKKEKRRDEMLGLAP----GRQSIIDLKEK 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1617 leaDINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDA------REQLGISERRANALQNELEESrtl 1690
Cdd:TIGR00606 745 ---EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGS--- 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1691 leQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAknseekakkamvdaARLADELRA 1770
Cdd:TIGR00606 819 --DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK--------------LQIGTNLQR 882
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1771 EQDHAQTQEKLRKALEQQIKELQVRLDEAEANAlkggkKAIQKLEQRVRELENELDGEQRRHADaqknlrkserrvkELS 1850
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE-----TFLEKDQQEKEELISSKETSNKKAQD-------------KVN 944
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1851 FQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEE--AEEIAALNLAKFRKAQQELEEAEERADLAEQAI 1916
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1715-1944 |
1.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1715 VSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQV 1794
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1795 RLDEAEANALKGGK---------------------KAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQS 1853
Cdd:COG3883 87 ELGERARALYRSGGsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1854 EEDRKNHER----MQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVG 1929
Cdd:COG3883 167 EAAKAELEAqqaeQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|....*
gi 24584706 1930 RGASPAPRATSVRPQ 1944
Cdd:COG3883 247 AGAGAAGAAGAAAGS 261
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1573-1755 |
1.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1573 RRIQEKEEEFENTRKNHQRaLDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHAN--KANAEAQKNIKRYQQQLK 1650
Cdd:COG4717 71 KELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1651 DIQTALEEEQRARDDAREQlgisERRANALQNELEESRTLLEQAdrgrrqAEQELADAHEQLNEVSAQNASISAAKRKLE 1730
Cdd:COG4717 150 ELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 24584706 1731 SELQTLHSDLDELLNEAKNSEEKAK 1755
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
842-1886 |
1.11e-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: 50.82 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEELHAAEVKVRKEleALNAKLLAEKTALLDSLSGE-KGALQDYQERNAKLTAQKNDLEN---Q 917
Cdd:TIGR01612 703 SKIDKEYDKIQNMETATVELHLSNIENKKN--ELLDIIVEIKKHIHGEINKDlNKILEDFKNKEKELSNKINDYAKekdE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 918 LRDIQERL---------------TQEEDARNQLFQQKK-------KADQ------EISGLKKDI---EDLELNVQKAEQD 966
Cdd:TIGR01612 781 LNKYKSKIseiknhyndqinidnIKDEDAKQNYDKSKEyiktisiKEDEifkiinEMKFMKDDFlnkVDKFINFENNCKE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 967 KATKDH-QIRNLNDEIAHQ--DELIN----KLNKEKKMQGETNQKTGEELQaaedKINHLNKVkaklEQTLDELEDSLER 1039
Cdd:TIGR01612 861 KIDSEHeQFAELTNKIKAEisDDKLNdyekKFNDSKSLINEINKSIEEEYQ----NINTLKKV----DEYIKICENTKES 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1040 EKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSI--TAKLEDEQVVVLKHQRQIKELQARIEEL 1117
Cdd:TIGR01612 933 IEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAfkDASLNDYEAKNNELIKYFNDLKANLGKN 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1118 EEEVEAerQARAKAEKQRADLARELEELGERLEEAGGATSAQI-ELNKKREAELSKlrrdleeaNIqhESTLANLRKKHN 1196
Cdd:TIGR01612 1013 KENMLY--HQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIyNIIDEIEKEIGK--------NI--ELLNKEILEEAE 1080
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1197 DAVAEMAEQVDQLNKLKAKAEKEKN--EYYGQLNDLRagvDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDA 1274
Cdd:TIGR01612 1081 INITNFNEIKEKLKHYNFDDFGKEEniKYADEINKIK---DDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED 1157
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1275 SKKKlSIENSDllrqleeaesqVSQLSKIKISLTTQLEDTKRLADEESReratLLGKFRNLEHDLDNLreqveEEAEGka 1354
Cdd:TIGR01612 1158 VADK-AISNDD-----------PEEIEKKIENIVTKIDKKKNIYDEIKK----LLNEIAEIEKDKTSL-----EEVKG-- 1214
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1355 dlqrqlskanaeaqVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQkcigLEKTKQRLSTEV---EDLQLEV 1431
Cdd:TIGR01612 1215 --------------INLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDE----IKEKSPEIENEMgieMDIKAEM 1276
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1432 DRANaIANAAEKK----QKAFDKIIGEWKLK-------------VDDLAAELDASQKECRNYSTELfrlkGAYEEGQEQL 1494
Cdd:TIGR01612 1277 ETFN-ISHDDDKDhhiiSKKHDENISDIREKslkiiedfseesdINDIKKELQKNLLDAQKHNSDI----NLYLNEIANI 1351
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1495 EAVRREN--KNLADEVKDLLDQIGEGGRNIH-EIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEI 1571
Cdd:TIGR01612 1352 YNILKLNkiKKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHI 1431
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1572 DRRIQEKEEEFENTRKNHQRALDSMQaSLEAEAKGKAEALRMKKK-----LEADINELEIALDHANKANAEAQKNIKR-- 1644
Cdd:TIGR01612 1432 LSEESNIDTYFKNADENNENVLLLFK-NIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAie 1510
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1645 -----YQQQLKDIQTALEEEQRArdDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQN 1719
Cdd:TIGR01612 1511 knkelFEQYKKDVTELLNKYSAL--AIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKN 1588
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1720 ASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAmvdaarladelraeqdhaqtqeklrKALEQQIKELQVRLDEA 1799
Cdd:TIGR01612 1589 DKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKET-------------------------ESIEKKISSFSIDSQDT 1643
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1800 EanaLKGGKKAIQKLEQRVRELENeldgEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHErmQDLVDKLQQKIKTYKR 1879
Cdd:TIGR01612 1644 E---LKENGDNLNSLQEFLESLKD----QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE--IGIIEKIKEIAIANKE 1714
|
....*..
gi 24584706 1880 QIEEAEE 1886
Cdd:TIGR01612 1715 EIESIKE 1721
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
841-1433 |
1.48e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 841 VSRIEDEIARLEEKAKK-----AEELHA---AEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNA-KLTAQK 911
Cdd:pfam12128 317 VAKDRSELEALEDQHGAfldadIETAAAdqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 912 NDLENQLRDIQERLTQEEDA--------RNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDhQIRNLNDEIAH 983
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDlqaleselREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLL-QLENFDERIER 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 984 QDELINKLNKEKkmqgETNQKTGEELQAAEDKIN-HLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQ 1062
Cdd:pfam12128 476 AREEQEAANAEV----ERLQSELRQARKRRDQASeALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1063 EAVAD---LERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQ----R 1135
Cdd:pfam12128 552 GKVISpelLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQlvqaN 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1136 ADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHN----DAVAEMAEQVDQLNK 1211
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKRE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1212 LKAKAEKEKNEYYGQLNDLRAGVDhitnekaaQEKIAKQLQHtlnevqskldetnrtlndfDASKKKLSIENSDLLRQLE 1291
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLALLK--------AAIAARRSGA-------------------KAELKALETWYKRDLASLG 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1292 EAESQVSQLSKIKISLTTQLEDTKrladeesRERATLLGKFRNLEHDL----DNLREQVEEEAEGKADLQRQLSKANAEA 1367
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIA-------VRRQEVLRYFDWYQETWlqrrPRLATQLSNIERAISELQQQLARLIADT 837
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1368 QVWRSKYESDGVARSE---ELEEAKRKLQARL---------AEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDR 1433
Cdd:pfam12128 838 KLRRAKLEMERKASEKqqvRLSENLRGLRCEMsklatlkedANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEH 915
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
829-1055 |
2.56e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 829 YKLWQKVKPLLN-----VSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQER 903
Cdd:PRK03918 524 AEEYEKLKEKLIklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 904 NAKLTaqknDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHqiRNLNDEIAH 983
Cdd:PRK03918 604 YLELK----DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY--LELSRELAG 677
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 984 QDELINKLNKEKkmqgETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDV-EKSKRKVE 1055
Cdd:PRK03918 678 LRAELEELEKRR----EEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLkERALSKVG 746
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1486-1849 |
2.93e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1486 AYEEGQEQLEAVRRENKNLADEVKDLLDQIgEGGRNIHEIEKARkrlEAEKDELQAALEEAEAAleqeenkVLRAQLELS 1565
Cdd:pfam17380 283 AVSERQQQEKFEKMEQERLRQEKEEKAREV-ERRRKLEEAEKAR---QAEMDRQAAIYAEQERM-------AMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1566 QVRQEidrriqEKEEEFENTRKNhqraldsmQASLEAEAKGKAEALRMKKKLEADINELEiaLDHANKANAEAQKNIKRY 1645
Cdd:pfam17380 352 RIRQE------ERKRELERIRQE--------EIAMEISRMRELERLQMERQQKNERVRQE--LEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1646 QQQLKDIQTALEEEQRARDdaREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAA 1725
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQ--REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1726 KRKLESELQTlhsdldellNEAKNSEEKAKKAMVDaarlaDELRAEQDHAQTQEKLRKALEQQIKELQVRldeaeanalk 1805
Cdd:pfam17380 494 RKILEKELEE---------RKQAMIEEERKRKLLE-----KEMEERQKAIYEEERRREAEEERRKQQEME---------- 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24584706 1806 gGKKAIQKLEQRVRELENELDGEQRRHaDAQKNLRKSERRVKEL 1849
Cdd:pfam17380 550 -ERRRIQEQMRKATEERSRLEAMERER-EMMRQIVESEKARAEY 591
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1471-1924 |
3.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1471 KECRNYSTELFRLKG----AYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEA 1546
Cdd:COG4717 49 ERLEKEADELFKPQGrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1547 EAALEQEEnkvLRAQLELSQVR-QEIDRRIQEkEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMK-KKLEADINEL 1624
Cdd:COG4717 129 PLYQELEA---LEAELAELPERlEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1625 EIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQ------------LGISERRANALQNELEESRTLLE 1692
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1693 QADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLD---ELLNEAKNSEEKAKKAMVDAARLADELR 1769
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1770 AEQDHAQTQEKLRKALEQQIKELQVRLDEAEAnalkggkkaIQKLEQRVRELENELDGEqrrhadaqknlrkserrvkEL 1849
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEE---------YQELKEELEELEEQLEEL-------------------LG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1850 SFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEA-EEIAALNlakfrkaqQELEEAEERADLAEQAISKFRAKGR 1924
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELEEELEELrEELAELE--------AELEQLEEDGELAELLQELEELKAE 484
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
914-1070 |
3.33e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 914 LENQLRDIQERLTQEEDARNQlfQQKKKADQEISGLKKDIEDLELNVQKAEqdkatkdHQIRNLNDEIAHQDELINKLNK 993
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAE--REKEHEERELTEEEEEIRRLEEQVERLE-------AEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 994 E-KKMQGETNQKTGE--ELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSK----RKVEgdlKLTQEAVA 1066
Cdd:COG2433 449 ElSEARSEERREIRKdrEISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGElvpvKVVE---KFTKEAIR 525
|
....
gi 24584706 1067 DLER 1070
Cdd:COG2433 526 RLEE 529
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
846-1079 |
3.38e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 49.08 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 846 DEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERL 925
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 926 TQEEDAR----NQLFQQKKKADQE------------------ISGLKKDIEDLELNVQKAEQDKATKDHQIRNLndEIAH 983
Cdd:pfam09726 475 KAEQEARasaeKQLAEEKKRKKEEeataaravalaaasrgecTESLKQRKRELESEIKKLTHDIKLKEEQIREL--EIKV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 984 QDelinkLNKEKKMQGETnQKTGEELQAAEDKINHlnkvkakleqtldeLEDSLEREKKVRGDVEKSKRKVEGDLKLTQE 1063
Cdd:pfam09726 553 QE-----LRKYKESEKDT-EVLMSALSAMQDKNQH--------------LENSLSAETRIKLDLFSALGDAKRQLEIAQG 612
|
250
....*....|....*.
gi 24584706 1064 AVADLERNKKELEQTI 1079
Cdd:pfam09726 613 QIYQKDQEIKDLKQKI 628
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1633-1890 |
3.51e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1633 KANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQlgiserranalQNELEESRTLLEQADRGRRQAEQELADAHEQL 1712
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQ-----------KEETEQLKQQLAQAPAKLRQAQAELEALKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1713 NEVSAQ---NASISAAKRKLE---SELQTLHSDLDEL---------------------------LNEAKNSEEKAKKAMV 1759
Cdd:PRK11281 111 DEETREtlsTLSLRQLESRLAqtlDQLQNAQNDLAEYnsqlvslqtqperaqaalyansqrlqqIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1760 DAARlaDELRAEQDHAQTQEKLRKALEQQIKELQV----RLDEAEANalkggkkaIQKLEQRVRELENELDgeqrrhada 1835
Cdd:PRK11281 191 PSQR--VLLQAEQALLNAQNDLQRKSLEGNTQLQDllqkQRDYLTAR--------IQRLEHQLQLLQEAIN--------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1836 QKNLRKSERRVKEL------------SFQSEEDRKNHERMQDLV---DKL----QQKIKTyKRQIEEA--------EEIA 1888
Cdd:PRK11281 252 SKRLTLSEKTVQEAqsqdeaariqanPLVAQELEINLQLSQRLLkatEKLntltQQNLRV-KNWLDRLtqsernikEQIS 330
|
..
gi 24584706 1889 AL 1890
Cdd:PRK11281 331 VL 332
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1602-1873 |
3.62e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.86 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1602 AEAKGKAEALRMK----------KKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQ----------TALEEEQR 1661
Cdd:NF033838 149 EEAEKKAKDQKEEdrrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKakveskkaeaTRLEKIKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1662 ARDDAREQlgiSERRANALQNELEESRTLLEQAD----RGRRQAEQELADAHEQLNEVSAQNASISaakrklESELQTLH 1737
Cdd:NF033838 229 DREKAEEE---AKRRADAKLKEAVEKNVATSEQDkpkrRAKRGVLGEPATPDKKENDAKSSDSSVG------EETLPSPS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1738 SDLDELLNEAKNSEEKAKKAMVDaarladelRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKaiqkleqr 1817
Cdd:NF033838 300 LKPEKKVAEAEKKVEEAKKKAKD--------QKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------- 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1818 vrELENEldgEQRRHADAQKNLRKSE-RRVKELSFQSEEDRKNHERMQDLVDKLQQK 1873
Cdd:NF033838 364 --EPRNE---EKIKQAKAKVESKKAEaTRLEKIKTDRKKAEEEAKRKAAEEDKVKEK 415
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1885 |
3.69e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1639 QKNIKRYQQQLKDIQTaleEEQRARDDAREQLGISERR------ANALQNELEESRTLLEQADRGRRQAEQELADAheQL 1712
Cdd:pfam17380 281 QKAVSERQQQEKFEKM---EQERLRQEKEEKAREVERRrkleeaEKARQAEMDRQAAIYAEQERMAMERERELERI--RQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1713 NEVSAQNASISaaKRKLESELQTLHsDLDELLNEAKNSEEKAKKAMvDAARladelraeQDHAQTQEKLRKALEQQIKEL 1792
Cdd:pfam17380 356 EERKRELERIR--QEEIAMEISRMR-ELERLQMERQQKNERVRQEL-EAAR--------KVKILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1793 QVRLDEAEANalkggKKAIQKLEQ-RVRELENELDGEQRRHADAQKnLRKSERRVKELSFQSEEDRKNHERMQDLVDK-L 1870
Cdd:pfam17380 424 QIRAEQEEAR-----QREVRRLEEeRAREMERVRLEEQERQQQVER-LRQQEEERKRKKLELEKEKRDRKRAEEQRRKiL 497
|
250
....*....|....*
gi 24584706 1871 QQKIKTYKRQIEEAE 1885
Cdd:pfam17380 498 EKELEERKQAMIEEE 512
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1643-1885 |
4.01e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1643 KRYQQQLKDIQTALE-EEQRARDDAREQLGISERRANalqNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNAS 1721
Cdd:pfam02029 70 KREERRQKRLQEALErQKEFDPTIADEKESVAERKEN---NEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1722 ISAA----------KRKLESELQTLHSDLDELLNEAKNSEEKAK----KAMVDAARLADELRAEQDHAQTQEKLRKALEQ 1787
Cdd:pfam02029 147 TEVRqaeeegeeeeDKSEEAEEVPTENFAKEEVKDEKIKKEKKVkyesKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1788 QIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENElDGEQRRHADAQKNL------RKSERRVKELSfqSEEDRKNHE 1861
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESE-EFEKLRQKQQEAELeleelkKKREERRKLLE--EEEQRRKQE 303
|
250 260
....*....|....*....|....*...
gi 24584706 1862 RMQDLV----DKLQQKIKTYKRQIEEAE 1885
Cdd:pfam02029 304 EAERKLreeeEKRRMKEEIERRRAEAAE 331
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
842-1089 |
5.18e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEElhaAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQK---NDLENQL 918
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDE---KIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHdkyEEIKNRY 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 919 RDIQ-ERLTQEEDARNQLFQQKKKADQE-----ISGLKKDIEDLELNVQKAE----QDKATKDHQIRNLNDEIAHQDELI 988
Cdd:PRK01156 556 KSLKlEDLDSKRTSWLNALAVISLIDIEtnrsrSNEIKKQLNDLESRLQEIEigfpDDKSYIDKSIREIENEANNLNNKY 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 989 NKLnKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADL 1068
Cdd:PRK01156 636 NEI-QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
250 260
....*....|....*....|.
gi 24584706 1069 ERNKKELEQTIQRKDKELSSI 1089
Cdd:PRK01156 715 SDRINDINETLESMKKIKKAI 735
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
906-1533 |
5.31e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 906 KLTAQKNDLENQLRDIQERLTQEEDARNQLfqqkKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQD 985
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 986 ELINKLNKekkmQGETNQKTGEELQAAEDKinhlnkvKAKLEQTLDELEDSLEREKKVRGD-VEKSKRKVEGDLKLtqea 1064
Cdd:PRK01156 239 SALNELSS----LEDMKNRYESEIKTAESD-------LSMELEKNNYYKELEERHMKIINDpVYKNRNYINDYFKY---- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1065 VADLErNKKELEQTIQRKDKELSSITAKLEDEQvvvlKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEE 1144
Cdd:PRK01156 304 KNDIE-NKKQILSNIDAEINKYHAIIKKLSVLQ----KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1145 LGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANI---QHESTLANLRKKhndavaemaeqVDQLNKLKAKAEKEKN 1221
Cdd:PRK01156 379 IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVklqDISSKVSSLNQR-----------IRALRENLDELSRNME 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1222 EYYGQLNDLRAGVdHITNEKAaqEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKL-SIENSDLLRQLEEAESQVSQL 1300
Cdd:PRK01156 448 MLNGQSVCPVCGT-TLGEEKS--NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLkKRKEYLESEEINKSINEYNKI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1301 SKIKISLTTQLEDTKRLADEESRERAtLLGKFRNLehDLDNLReqveeeaegkadlQRQLSKANAEAQvwRSKYESDGV- 1379
Cdd:PRK01156 525 ESARADLEDIKIKINELKDKHDKYEE-IKNRYKSL--KLEDLD-------------SKRTSWLNALAV--ISLIDIETNr 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1380 ARSEELEEAKRKLQARLAEAE---ETIESLNQKCIGlektkqrlstEVEDlqlEVDRANAIANAAEKKQKAFDKIIGewk 1456
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEigfPDDKSYIDKSIR----------EIEN---EANNLNNKYNEIQENKILIEKLRG--- 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1457 lKVDDL---AAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLE 1533
Cdd:PRK01156 651 -KIDNYkkqIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1049-1280 |
5.74e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1049 KSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQAR 1128
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1129 AKAEKQRADL---ARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQ 1205
Cdd:COG4942 100 EAQKEELAELlraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1206 VDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTL--NDFDASKKKLS 1280
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTpaAGFAALKGKLP 256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1008-1177 |
6.12e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1008 ELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKltqEAVADLERNKKELEQTiqRKDKELS 1087
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNV--RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1088 SITAKLEdeqvvvlKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIE-LNKKR 1166
Cdd:COG1579 93 ALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEeLEAER 165
|
170
....*....|.
gi 24584706 1167 EAELSKLRRDL 1177
Cdd:COG1579 166 EELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1033-1536 |
6.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1033 LEDSLEREKKVRGDveKSKRKVEGDLKLTQEAVADLERNKKELEQtIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQA 1112
Cdd:COG4717 47 LLERLEKEADELFK--PQGRKPELNLKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1113 RIEELEEeveaeRQARAKAEKQRADLARELEELGerleeaggatsAQIELNKKREAELSKLRRDLEEANIQHESTLANLR 1192
Cdd:COG4717 124 LLQLLPL-----YQELEALEAELAELPERLEELE-----------ERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1193 KKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKiakqlqhtlnevQSKLDETNRTLNDF 1272
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL------------EERLKEARLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1273 DASKKKLSIENSDLLRQLEEAESQ----------VSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNL 1342
Cdd:COG4717 256 AALLALLGLGGSLLSLILTIAGVLflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1343 REQVEEEAEGKADLQRQLSKANAEaqvwrskyesdgvARSEELEEAKRKLQARLAEAE-ETIESLNQKCIGLEKtKQRLS 1421
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEEL-------------EEELQLEELEQEIAALLAEAGvEDEEELRAALEQAEE-YQELK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1422 TEVEDLQLEVDranAIANAAEKKQKAFDKiiGEWKLKVDDLAAELDASQKECRNYSTELFRLK---------GAYEEGQE 1492
Cdd:COG4717 402 EELEELEEQLE---ELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEaeleqleedGELAELLQ 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24584706 1493 QLEAVRRENKNLADE--VKDLLDQIgeggrniheIEKARKRLEAEK 1536
Cdd:COG4717 477 ELEELKAELRELAEEwaALKLALEL---------LEEAREEYREER 513
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1417-1825 |
7.44e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1417 KQRLSTEVEDLQLEVDRANAIANAaEKKQKAFDKIiGEWKLKVDDLAAELDASQKECRNYSTELFRLKG-AYEEGQEQLE 1495
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDL-EQTLALLDKI-DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1496 AvrRENKNLADEVKDLLDQIGEGGRNIHE----IEKARKRLEaekdelqaaleeaeaaleqeenkvlRAQLELS--QVR- 1568
Cdd:PRK11281 120 T--LSLRQLESRLAQTLDQLQNAQNDLAEynsqLVSLQTQPE-------------------------RAQAALYanSQRl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1569 QEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEakgkaeaLRMKKKLEADINELeiaLDHANKANAEAQKNIKRYQQQ 1648
Cdd:PRK11281 173 QQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQ-------NDLQRKSLEGNTQL---QDLLQKQRDYLTARIQRLEHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1649 LKDIQTALEEEQRAR-----DDAREQLGISERRANAL-QNELEESRTLleqadrgrrqaEQELADAHEQLNEVSAQNASI 1722
Cdd:PRK11281 243 LQLLQEAINSKRLTLsektvQEAQSQDEAARIQANPLvAQELEINLQL-----------SQRLLKATEKLNTLTQQNLRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1723 saaKRKLESELQTLHsDLDELLNEAKNS--------EEKAK----KAMVD-AARLADeLRAEQ-DHAQTQEKL------- 1781
Cdd:PRK11281 312 ---KNWLDRLTQSER-NIKEQISVLKGSlllsrilyQQQQAlpsaDLIEGlADRIAD-LRLEQfEINQQRDALfqpdayi 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 24584706 1782 RKALEQQIKElqvrLDEAEANALKGGKKAIQK-LEQRVRELENEL 1825
Cdd:PRK11281 387 DKLEAGHKSE----VTDEVRDALLQLLDERRElLDQLNKQLNNQL 427
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
842-1803 |
9.40e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEElHAAEVKVrkELEALNAKLLAEKTALLDSL---SGEKGALQDYQERNAKLTAQ--KNDLEN 916
Cdd:NF041483 18 SRFEAEMDRLKTEREKAVQ-HAEDLGY--QVEVLRAKLHEARRSLASRPaydGADIGYQAEQLLRNAQIQADqlRADAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 917 QLRDIQ---ERLTQE---EDARNQ------LFQQKKKADQEISGLKKDIED-LELNVQKAEQDKATKDHQIRNLNDEIAH 983
Cdd:NF041483 95 ELRDARaqtQRILQEhaeHQARLQaelhteAVQRRQQLDQELAERRQTVEShVNENVAWAEQLRARTESQARRLLDESRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 984 QDE--LINKLNKEKKMQGETNQKTGEELQAA------------EDKINHLNKVKAKLEQTLDELED-----SLEREKKVR 1044
Cdd:NF041483 175 EAEqaLAAARAEAERLAEEARQRLGSEAESAraeaeailrrarKDAERLLNAASTQAQEATDHAEQlrsstAAESDQARR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1045 GDVEKSK----RKVEGDLKLtQEAVADLERNKKELEQTIQRK------DKELSSITAKLEDEQVVvlkhQRQIKELQAri 1114
Cdd:NF041483 255 QAAELSRaaeqRMQEAEEAL-REARAEAEKVVAEAKEAAAKQlasaesANEQRTRTAKEEIARLV----GEATKEAEA-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1115 eELEEEVEAERQARAKAEKQRADL---ARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEAN-IQHESTLAN 1190
Cdd:NF041483 328 -LKAEAEQALADARAEAEKLVAEAaekARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAErIRREAEAEA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1191 LRKKhndavAEMAEQVDQLNKLKAKAEKEKNEYYGQLND----LRAGVDHITNEKAAQ-EKIAKQLQHtlnEVQSKLDET 1265
Cdd:NF041483 407 DRLR-----GEAADQAEQLKGAAKDDTKEYRAKTVELQEearrLRGEAEQLRAEAVAEgERIRGEARR---EAVQQIEEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1266 NRTLNDFDASKKKlsieNSDLLRQLEEAESQVSQlskikislttqledtkrladEESRERATllgkfrnlehdldNLREQ 1345
Cdd:NF041483 479 ARTAEELLTKAKA----DADELRSTATAESERVR--------------------TEAIERAT-------------TLRRQ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1346 VEEEAE-GKADLQRQLSKANAEAQVWRSKYESdgvARSEELEEAKRKLQARLAEAEETIESLN----QKCIGLEKTKQRL 1420
Cdd:NF041483 522 AEETLErTRAEAERLRAEAEEQAEEVRAAAER---AARELREETERAIAARQAEAAEELTRLHteaeERLTAAEEALADA 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1421 STEVEDLQL----EVDRANaiANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELfRLKGAYE------EG 1490
Cdd:NF041483 599 RAEAERIRReaaeETERLR--TEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRL-RSEAAAEaerlksEA 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1491 QEQLEAVRRE----NKNLADEVKDLLDQIGEggrniheiEKARKRLEAEK----------DELQAALEEAEAALEQEENK 1556
Cdd:NF041483 676 QESADRVRAEaaaaAERVGTEAAEALAAAQE--------EAARRRREAEEtlgsaraeadQERERAREQSEELLASARKR 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1557 VLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQ-------ASLEAEAKGKAEALRMKKKLEAD------INE 1623
Cdd:NF041483 748 VEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQeqaeeeiAGLRSAAEHAAERTRTEAQEEADrvrsdaYAE 827
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1624 LEIALDHANKANAEAQKNIKRYQQQL-KDIQTALEEEQRARDDAREQlgiserrANALQNELEESRTLLEQ-ADRGRRQA 1701
Cdd:NF041483 828 RERASEDANRLRREAQEETEAAKALAeRTVSEAIAEAERLRSDASEY-------AQRVRTEASDTLASAEQdAARTRADA 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1702 EQelaDAHEQLNEVSAQ-NASISAAKRKLESELQTLHSDLDELLNEAK--------NSEEKAKKAMVDAARLADELRAEQ 1772
Cdd:NF041483 901 RE---DANRIRSDAAAQaDRLIGEATSEAERLTAEARAEAERLRDEARaeaervraDAAAQAEQLIAEATGEAERLRAEA 977
|
1050 1060 1070
....*....|....*....|....*....|.
gi 24584706 1773 dhAQTQEKLRKALEQQIKELQVRLDEAEANA 1803
Cdd:NF041483 978 --AETVGSAQQHAERIRTEAERVKAEAAAEA 1006
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
814-1825 |
9.86e-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: 47.64 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 814 QRNLRKYLQLRtwpwyKLWQKVKPLLNvsrieDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALldslsGE 893
Cdd:COG3096 281 RELSERALELR-----RELFGARRQLA-----EEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL-----RQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 894 KGALQDYQ----ERNAKLTAQKNDLEN---QLRDIQERLTQEED----ARNQL----------------FQQ----KKKA 942
Cdd:COG3096 346 QEKIERYQedleELTERLEEQEEVVEEaaeQLAEAEARLEAAEEevdsLKSQLadyqqaldvqqtraiqYQQavqaLEKA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 943 dQEISGLKK-DIEDLELNVQ--KAEQDKATkdHQIRNLNDEIAHQDELINKLNKE----KKMQGETN-----QKTGEELQ 1010
Cdd:COG3096 426 -RALCGLPDlTPENAEDYLAafRAKEQQAT--EEVLELEQKLSVADAARRQFEKAyelvCKIAGEVErsqawQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1011 AAEDKINHLNKVKAkLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLkltqEAVADLERNKKELEQTIQRKDKELSSIT 1090
Cdd:COG3096 503 RYRSQQALAQRLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1091 AKLedeqvvvLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGerleeaggATSAQIELNKKREAEL 1170
Cdd:COG3096 578 EQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ--------EVTAAMQQLLEREREA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1171 SKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNklkakaekekneyyGQLndLRAGVDHITNEKAAQ-EKIAK 1249
Cdd:COG3096 643 TVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLG--------------GVL--LSEIYDDVTLEDAPYfSALYG 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1250 QLQHT-----LNEVQSKLDETNRTLND----------FDAS-KKKLSIENSDLLrQLEEAESQVSQLSKIKislttqled 1313
Cdd:COG3096 707 PARHAivvpdLSAVKEQLAGLEDCPEDlyliegdpdsFDDSvFDAEELEDAVVV-KLSDRQWRYSRFPEVP--------- 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1314 tkrladeesreratLLGKfRNLEHDLDNLREQVEEEAEGKADL---QRQLSKANAE--------AQVWrskYESDGVARS 1382
Cdd:COG3096 777 --------------LFGR-AAREKRLEELRAERDELAEQYAKAsfdVQKLQRLHQAfsqfvgghLAVA---FAPDPEAEL 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1383 EELEEAKRKLQARLAEAEETIESLNQKcigLEKTKQRLST-----------EVEDLQLEVDRANAIANAAEKKQkAFDKI 1451
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQ---LDQLKEQLQLlnkllpqanllADETLADRLEELREELDAAQEAQ-AFIQQ 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1452 IGEWKLKVDDLAAEL--DASQKEcrnystelfRLKGAYEEGQEQLEAVRRENKNLADEVKDLL-----DQIGEGGRNIHE 1524
Cdd:COG3096 915 HGKALAQLEPLVAVLqsDPEQFE---------QLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyeDAVGLLGENSDL 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1525 IEKARKRLEaekdelqaaleeaeaaleqeenkvlRAQLELSQVRQEIdRRIQEKEEEFentrknHQRaldsmQASLEAEA 1604
Cdd:COG3096 986 NEKLRARLE-------------------------QAEEARREAREQL-RQAQAQYSQY------NQV-----LASLKSSR 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1605 KGKAEALRmkkKLEADINELEIALDhankANAEAQKNIKRyqqqlKDIQTALEEEQRARDDAREQLGISERRANALQNEL 1684
Cdd:COG3096 1029 DAKQQTLQ---ELEQELEELGVQAD----AEAEERARIRR-----DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1685 EESRTLLEQAdrgRRQAEQELAdAHEQLNEVSAQNasiSAAKRKLESELQTLHSD-LDELLNEAKNSeekAKKAMVDAAR 1763
Cdd:COG3096 1097 RKAERDYKQE---REQVVQAKA-GWCAVLRLARDN---DVERRLHRRELAYLSADeLRSMSDKALGA---LRLAVADNEH 1166
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1764 LADELRAEQDHAQTQEK----------LRKALEQQIkelqVRLDEAeanalkggKKAIQKLEQRVRELENEL 1825
Cdd:COG3096 1167 LRDALRLSEDPRRPERKvqfyiavyqhLRERIRQDI----IRTDDP--------VEAIEQMEIELARLTEEL 1226
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1241-1859 |
1.01e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1241 KAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEeAESQVSQLSKIKIS----LTTQLED--- 1313
Cdd:NF041483 308 RTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVA-AEDTAAQLAKAARTaeevLTKASEDaka 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1314 -TKRLADEESRERatllgkfRNLEHDLDNLREQVEEEAE---GKA------------DLQRQLSKANAEAQVWRSkyesD 1377
Cdd:NF041483 387 tTRAAAEEAERIR-------REAEAEADRLRGEAADQAEqlkGAAkddtkeyraktvELQEEARRLRGEAEQLRA----E 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1378 GVARSEELE-EAKRKLQARLAEAEETIESLNQKC-IGLEKTKQRLSTEVEDLQLE-VDRANAIANAAEKKqkafdkiige 1454
Cdd:NF041483 456 AVAEGERIRgEARREAVQQIEEAARTAEELLTKAkADADELRSTATAESERVRTEaIERATTLRRQAEET---------- 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1455 wklkvddlaaeLDASQKECRNYSTElfrlkgayeeGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEA 1534
Cdd:NF041483 526 -----------LERTRAEAERLRAE----------AEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEA 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1535 EKdelqaaleeaeaaleqeenKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEakgkAEALRMK 1614
Cdd:NF041483 585 EE-------------------RLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE----AERLRTE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1615 KKLEADINELE---IALDHANKANAEAQKNIKRYQQQLKDIQT-ALEEEQRARDDAREQLGISERRANALQNELEEsrtL 1690
Cdd:NF041483 642 AAADASAARAEgenVAVRLRSEAAAEAERLKSEAQESADRVRAeAAAAAERVGTEAAEALAAAQEEAARRRREAEE---T 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1691 LEQAdrgRRQAEQELADAHEQLNEVSAqnasiSAAKR--KLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADEl 1768
Cdd:NF041483 719 LGSA---RAEADQERERAREQSEELLA-----SARKRveEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQE- 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1769 RAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANAlkggkkaiQKLEQRVRELENELDGEQRRHADAQKNLrkSERRVKE 1848
Cdd:NF041483 790 QAEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDA--------YAERERASEDANRLRREAQEETEAAKAL--AERTVSE 859
|
650
....*....|.
gi 24584706 1849 LSFQSEEDRKN 1859
Cdd:NF041483 860 AIAEAERLRSD 870
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
801-982 |
1.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 801 KKLQEQRVALKVVQRNLRKYLQLR-----------TWPWYKLWQKVKplLNVSRIEDEIARLEEKAKKAEELHAAEVKVR 869
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 870 KELEALNAKLLAEKTALLDSLSGEKGALQ-DYQERNAKLtaqkNDLENQLRDIQERLTQEEDArnqLFQQKKKADQEISG 948
Cdd:COG4913 323 EELDELEAQIRGNGGDRLEQLEREIERLErELEERERRR----ARLEALLAALGLPLPASAEE---FAALRAEAAALLEA 395
|
170 180 190
....*....|....*....|....*....|....
gi 24584706 949 LKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIA 982
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
822-1294 |
1.09e-04 |
|
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: 47.35 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 822 QLRTWPWYKLWQKV--KPLLNVSRIEDEIARLEEKAKKAEELhaaEVKVRKELEALNAKLLAEKTALLDSLSGE--KGAL 897
Cdd:TIGR00606 565 LLGYFPNKKQLEDWlhSKSKEINQTRDRLAKLNKELASLEQN---KNHINNELESKEEQLSSYEDKLFDVCGSQdeESDL 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 898 QDYQERNAKLTAQKNDLENQLRDIQERLTQEEDAR-------NQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATK 970
Cdd:TIGR00606 642 ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 971 DHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINH----LNKVKAKLEQTLDELEDSLEREKkVRGD 1046
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqetlLGTIMPEEESAKVCLTDVTIMER-FQME 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1047 VEKSKRKVEGDLKLTQEAvaDLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQ 1126
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1127 ARAKAEKQRADLARELEELGERLEeaggatsaQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQV 1206
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIR--------EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1207 DQLnklkakaekekneyYGQLNDLRAGV-DHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTL----NDFDASKKKLSI 1281
Cdd:TIGR00606 951 KNI--------------HGYMKDIENKIqDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMrlmrQDIDTQKIQERW 1016
|
490
....*....|...
gi 24584706 1282 ENSDLLRQLEEAE 1294
Cdd:TIGR00606 1017 LQDNLTLRKRENE 1029
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
833-1032 |
1.23e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 833 QKVKPLLNVSRIEDEIARLEekaKKAEELHAAEVKVRKELEALNAKLLAEKTALLDslsgekgalqdyqernakLTAQKN 912
Cdd:COG1579 4 EDLRALLDLQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELED------------------LEKEIK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 913 DLENQLRDIQERLtqeedARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLN 992
Cdd:COG1579 63 RLELEIEEVEARI-----KKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24584706 993 KEKKmqgETNQKTGEELQAAEDKINHLNKVKAKLEQTLDE 1032
Cdd:COG1579 138 AELE---EKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1465-1886 |
1.29e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1465 ELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLL-DQIGEGGRNIH--EIEKARKRLEAEKDELQA 1541
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRRQIQraELELQSTNSELEELQERL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1542 ALEEAEAALEQEENKVLRAQLELSQVR----QEIDRRIQEKEEEFENTRKNHQR-----ALDSMQASLEAEAKGKAEALR 1612
Cdd:pfam05557 142 DLLKAKASEAEQLRQNLEKQQSSLAEAeqriKELEFEIQSQEQDSEIVKNSKSElaripELEKELERLREHNKHLNENIE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1613 MKKKLEADINELEIALDHANKANAEA---QKNIKRYQQQLKD---IQTALEEEQRARDDAREQLGISERRANALQNELEE 1686
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYREEAatlELEKEKLEQELQSwvkLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1687 SRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDEL----------LNEAKNSEEKAKK 1756
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYrailesydkeLTMSNYSPQLLER 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1757 aMVDAARLADELRAE-----------QDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGG----KKAIQKLE---QRV 1818
Cdd:pfam05557 382 -IEEAEDMTQKMQAHneemeaqlsvaEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvdslRRKLETLElerQRL 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1819 RELENELDGEQRRHADAQKNlrkSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEE 1886
Cdd:pfam05557 461 REQKNELEMELERRCLQGDY---DPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLED 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1715-1914 |
1.34e-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: 46.30 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1715 VSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQv 1794
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1795 rldeaeanalkggkKAIQKLEQRVRELENELdgeQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKI 1874
Cdd:COG4942 90 --------------KEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24584706 1875 KTYKRQIEEAEEI-AALNLAKFRKAQQELEEAEERADLAEQ 1914
Cdd:COG4942 153 EELRADLAELAALrAELEAERAELEALLAELEEERAALEAL 193
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1563-1886 |
1.44e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1563 ELSQVRQEIDRRIQEKEEEFENTRKNHQRAldSMQASLEAEAKGKAEALRMKKKLEadinELEIALDHANKANAEAQKNI 1642
Cdd:PLN02939 71 ENGQLENTSLRTVMELPQKSTSSDDDHNRA--SMQRDEAIAAIDNEQQTNSKDGEQ----LSDFQLEDLVGMIQNAEKNI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1643 KRYQQQ----LKDIQTALEEeqrarddaREQLgisERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQ 1718
Cdd:PLN02939 145 LLLNQArlqaLEDLEKILTE--------KEAL---QGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1719 NASISAAKRKLESELQTLHSDLDELLNEAknseeKAKKAMVDAARLADELRAeqdhaqTQEKLRKALEQQIKELQVRLDE 1798
Cdd:PLN02939 214 GATEGLCVHSLSKELDVLKEENMLLKDDI-----QFLKAELIEVAETEERVF------KLEKERSLLDASLRELESKFIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1799 AEANALKGGKKAIQKLEQRVRELENELD--GEQRRHA----DAQKNLRKSERRVKElsfqSEEDRKNHERMQDLVDKLQQ 1872
Cdd:PLN02939 283 AQEDVSKLSPLQYDCWWEKVENLQDLLDraTNQVEKAalvlDQNQDLRDKVDKLEA----SLKEANVSKFSSYKVELLQQ 358
|
330
....*....|....
gi 24584706 1873 KIKTYKRQIEEAEE 1886
Cdd:PLN02939 359 KLKLLEERLQASDH 372
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
843-994 |
1.44e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 843 RIEDEIARLEEKAKKAEELHAAEVKVRKELEALN------------AKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQ 910
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvasaEREIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 911 KNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDI-----EDLELNVQKAEQDKATKDHQiRNLNDEIAHQD 985
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFAAALGDAVERELR-ENLEERIDALR 779
|
....*....
gi 24584706 986 ELINKLNKE 994
Cdd:COG4913 780 ARLNRAEEE 788
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1158-1420 |
1.62e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1158 AQIELNKKR---EAELSKLRRDLEEA-----NIQ-HESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLN 1228
Cdd:PRK11281 43 AQLDALNKQkllEAEDKLVQQDLEQTlalldKIDrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1229 --DLRAGVDHITNEKA-AQEKIAK---QL----------QHTLNEVQSKLDETNRTLNDFDASKKKLSIEnsdlLRQLEE 1292
Cdd:PRK11281 123 lrQLESRLAQTLDQLQnAQNDLAEynsQLvslqtqperaQAALYANSQRLQQIRNLLKGGKVGGKALRPS----QRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1293 AESQVSQLskiKISLTTQ-LEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEE----EAEGKADlQRQLSKANAEA 1367
Cdd:PRK11281 199 AEQALLNA---QNDLQRKsLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSkrltLSEKTVQ-EAQSQDEAARI 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1368 QvwrskyESDGVARseELeEAKRKLQARLAEAEETIESLNQKCIgleKTKQRL 1420
Cdd:PRK11281 275 Q------ANPLVAQ--EL-EINLQLSQRLLKATEKLNTLTQQNL---RVKNWL 315
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1223-1428 |
1.71e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1223 YYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKL-DETNrtlndfdaskKKLSIENS--DLLRQLEEAESQVSQ 1299
Cdd:pfam00038 52 YEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYeDELN----------LRTSAENDlvGLRKDLDEATLARVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1300 LSKIKISLTTQLEDTKRLADEESRE-RATLLGKFRNLEHD----------LDNLREQVEEEAE-GKADLQRQLSKANAEA 1367
Cdd:pfam00038 122 LEAKIESLKEELAFLKKNHEEEVRElQAQVSDTQVNVEMDaarkldltsaLAEIRAQYEEIAAkNREEAEEWYQSKLEEL 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1368 QVWRSKYESDGVARSEELEEAKRKLQARLAEaeetIESLNQKCIGLEK----TKQRLSTEVEDLQ 1428
Cdd:pfam00038 202 QQAAARNGDALRSAKEEITELRRTIQSLEIE----LQSLKKQKASLERqlaeTEERYELQLADYQ 262
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
829-1134 |
1.73e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 829 YKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLT 908
Cdd:COG5185 170 QELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 909 AQKNDLENQLRDIQERLTQEEDARNQLFQQKKkadQEISGLKKDIEDLELNVQKAEQDKATKDHQirNLNDEIAHQDELI 988
Cdd:COG5185 250 QTSDKLEKLVEQNTDLRLEKLGENAESSKRLN---ENANNLIKQFENTKEKIAEYTKSIDIKKAT--ESLEEQLAAAEAE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 989 NKLNKEKKMQGETNQKTGEEL-QAAEDKINHLNKVKAKLEQ--TLDELEDSLEREKKVRGDVEKSKRKVEGD----LKLT 1061
Cdd:COG5185 325 QELEESKRETETGIQNLTAEIeQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTKESLDEIpqnqRGYA 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1062 QEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQ 1134
Cdd:COG5185 405 QEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVR 477
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1664-1819 |
1.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1664 DDAREQLGISERRANALQNELEESRtlleqadrgrRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDEl 1743
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELE----------RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK- 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1744 lnEAKNSEEKAKKAmvdAARLADELRAEQDHAQTQEKLRKALEQQiKELQVRLDEAEANALKGGKKAIQ-KLEQRVR 1819
Cdd:PRK00409 574 --EAQQAIKEAKKE---ADEIIKELRQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKEKQEElKVGDEVK 644
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1078 |
2.79e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 851 LEEKAKKAEELHAAEVKVRKELEALNAKlLAEKTALLDSLsgekgalqdyQERNAKLTAQKNDLENQLRDIQERLTQEED 930
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE-LEELNEEYNEL----------QAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 931 ARNQLFQQKKKADQEISGLK-----KDIEDLeLNvqkaeqdkatkdhQIRNLNDEIAHQDELINKLNKEKKMQGETNQKT 1005
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDvllgsESFSDF-LD-------------RLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1006 GEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQT 1078
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1560-1773 |
2.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1560 AQLELSQVRQEIDRRIQEKEEEfentrknhQRALDSMQASLEaEAKGKAEALRMK-KKLEADINELEIALDhanKANAEA 1638
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAA--------QAELDALQAELE-ELNEEYNELQAElEALQAEIDKLQAEIA---EAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1639 QKNIKRYQQQLKDIQtaleeEQRARDDAREQLGISE------RRANALQNELEESRTLLEQADRGRRQAEQELADAHEQL 1712
Cdd:COG3883 82 EERREELGERARALY-----RSGGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1713 NEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQD 1773
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
876-1095 |
2.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 876 NAKLLAEKTALLDSLsgekgalqdyQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQK--KKADQEISGLKKDI 953
Cdd:COG4913 608 NRAKLAALEAELAEL----------EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 954 EDLELNvqkaeqdkatkdhqirnlNDEIAHQDELINKLNkekkmqgetnqktgEELQAAEDKINHLNKVKAKLEQTLDEL 1033
Cdd:COG4913 678 ERLDAS------------------SDDLAALEEQLEELE--------------AELEELEEELDELKGEIGRLEKELEQA 725
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1034 EDSLEREKKVRGDVEKSKRKV---EGDLKLTQEAVADLERN-KKELEQTIQRKDKELSSITAKLED 1095
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLElraLLEERFAAALGDAVERElRENLEERIDALRARLNRAEEELER 791
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1683-1872 |
3.28e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1683 ELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAknseEKAKKAMVDAA 1762
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEA----EEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1763 RLadeLRAEQDHAQTQEKLRKALEQQIKELQVRLDeaeaNALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKS 1842
Cdd:pfam05557 79 RL---KKKYLEALNKKLNEKESQLADAREVISCLK----NELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190
....*....|....*....|....*....|
gi 24584706 1843 ERRVKELSFQSEEDRKNHERMQDLVDKLQQ 1872
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIKELEFEIQS 181
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1576-1771 |
3.53e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1576 QEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALrmkkkleaDINELEIALDHANKANAEAQKNIKRYQQQLKDIQTA 1655
Cdd:pfam12795 43 QKALDDAPAELRELRQELAALQAKAEAAPKEILASL--------SLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1656 LEEEQRARDDAREQLgiseRRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNAS----ISAAKRKLES 1731
Cdd:pfam12795 115 PERAQQQLSEARQRL----QQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLEQELLSNNnrqdLLKARRDLLT 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24584706 1732 E----LQTLHSDLDELLNEAKNSEekAKKAMVDAARLADELRAE 1771
Cdd:pfam12795 191 LriqrLEQQLQALQELLNEKRLQE--AEQAVAQTEQLAEEAAGD 232
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1637-1849 |
3.84e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1637 EAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLgisERRANALQNELEESRTLLEQADRGRRQAEQ---ELADAHEQLN 1713
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEkykELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1714 E----VSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQI 1789
Cdd:pfam07888 115 EekdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1790 KELQVRLDEAEANALKgGKKAIQKLEQRV-----RELENELDGEQRRhaDAQKNLRKSERRVKEL 1849
Cdd:pfam07888 195 QELRNSLAQRDTQVLQ-LQDTITTLTQKLttahrKEAENEALLEELR--SLQERLNASERKVEGL 256
|
|
| PRK09174 |
PRK09174 |
F0F1 ATP synthase subunit B; |
1671-1771 |
3.96e-04 |
|
F0F1 ATP synthase subunit B;
Pssm-ID: 169692 [Multi-domain] Cd Length: 204 Bit Score: 43.63 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1671 GISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVsAQNASiSAAKRKLESELQTLHSDLDELLNEAKNS 1750
Cdd:PRK09174 80 GIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSI-AQAAR-EAAKAKAEAERAAIEASLEKKLKEAEAR 157
|
90 100
....*....|....*....|..
gi 24584706 1751 EEKAK-KAMVDAARLADELRAE 1771
Cdd:PRK09174 158 IAAIKaKAMADVGSIAEETAAA 179
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1560-1896 |
4.01e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1560 AQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEAL-----RMKKKLEADINE----------- 1623
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLdqelaERRQTVESHVNEnvawaeqlrar 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1624 --------LEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDA--REQLGISERRANALQNELEESRTLLEQ 1693
Cdd:NF041483 161 tesqarrlLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAilRRARKDAERLLNAASTQAQEATDHAEQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1694 --------ADRGRRQ-------AEQELADAHEQLNEVSAQ------NASISAAKRKLESELQ------TLHSDLDELLNE 1746
Cdd:NF041483 241 lrsstaaeSDQARRQaaelsraAEQRMQEAEEALREARAEaekvvaEAKEAAAKQLASAESAneqrtrTAKEEIARLVGE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1747 A-KNSE---EKAKKAMVDAARLADELRA---EQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVR 1819
Cdd:NF041483 321 AtKEAEalkAEAEQALADARAEAEKLVAeaaEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1820 ELENELD---GEQRRHADAQKNLRK---SERRVKELSFQSEEDRKNHERMQDLVDKLQ--QKIKTYKR-----QIEEAEE 1886
Cdd:NF041483 401 EAEAEADrlrGEAADQAEQLKGAAKddtKEYRAKTVELQEEARRLRGEAEQLRAEAVAegERIRGEARreavqQIEEAAR 480
|
410
....*....|
gi 24584706 1887 IAALNLAKFR 1896
Cdd:NF041483 481 TAEELLTKAK 490
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1560-1772 |
4.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1560 AQLELSQVRQEIDRRIQEKEEEFENTRKnhqraldsmqaslEAEAKGKAEALRMKKKLEADINeleialdhankanaEAQ 1639
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKK-------------EALLEAKEEIHKLRNEFEKELR--------------ERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1640 KNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQAdrgRRQAEQELadahEQLNEVSAQN 1719
Cdd:PRK12704 82 NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL---IEEQLQEL----ERISGLTAEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1720 AS---ISAAKRKLESELQTLhsdLDELLNEAK-NSEEKAKKAMVDA-ARLADELRAEQ 1772
Cdd:PRK12704 155 AKeilLEKVEEEARHEAAVL---IKEIEEEAKeEADKKAKEILAQAiQRCAADHVAET 209
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1741-1848 |
4.89e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1741 DELLNEAKN--SEEKAKKAMVDAARLADELRAEQDHAQTQ------EKLRKALEQQIKELQVRLDEAEANALKGGKKAIQ 1812
Cdd:PRK00409 501 ENIIEEAKKliGEDKEKLNELIASLEELERELEQKAEEAEallkeaEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIK 580
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24584706 1813 KLEQ-------RVRELENELDGEQRRHA--DAQKNLRKSERRVKE 1848
Cdd:PRK00409 581 EAKKeadeiikELRQLQKGGYASVKAHEliEARKRLNKANEKKEK 625
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1612-1746 |
4.94e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1612 RMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDiqtALEEEQRARDDAREQlgISERRANALQNELEESRTLL 1691
Cdd:COG0711 24 PILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAE---ARAEAAEIIAEARKE--AEAIAEEAKAEAEAEAERII 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1692 EQAdrgRRQAEQELADAHEQLNEVSAQnASISAAKRKLESEL-QTLHSDL-DELLNE 1746
Cdd:COG0711 99 AQA---EAEIEQERAKALAELRAEVAD-LAVAIAEKILGKELdAAAQAALvDRFIAE 151
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
861-1509 |
5.02e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 861 LHAAEVKVRKELEALNAKLLAektalldslsgeKGALQDYQERNAKL---TAQKNDLENQLRDIQE---RLTQEEDARNQ 934
Cdd:pfam10174 153 LGARDESIKKLLEMLQSKGLP------------KKSGEEDWERTRRIaeaEMQLGHLEVLLDQKEKeniHLREELHRRNQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 935 LFQQKKKA----------DQEISGLKKDIEDLELNVQ--KAEQDKATKDHQ--IRNLNDEIAHQDELINKLNKEKKmqgE 1000
Cdd:pfam10174 221 LQPDPAKTkalqtviemkDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREeeIKQMEVYKSHSKFMKNKIDQLKQ---E 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1001 TNQKTgEELQAAEDKINHLNKVKAKLEQTLDELEDSL----EREKKVRGDVEKSKRKVEGD---LKLTQEAVADLERNK- 1072
Cdd:pfam10174 298 LSKKE-SELLALQTKLETLTNQNSDCKQHIEVLKESLtakeQRAAILQTEVDALRLRLEEKesfLNKKTKQLQDLTEEKs 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1073 ------KELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKaekqradlareleelg 1146
Cdd:pfam10174 377 tlageiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTT---------------- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1147 erleeaggatsaqielnkkreaelsklrrdLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKlkakaekekneyygQ 1226
Cdd:pfam10174 441 ------------------------------LEEALSEKERIIERLKEQREREDRERLEELESLKK--------------E 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1227 LNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEA-ESQVSQLSKIKI 1305
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAhNAEEAVRTNPEI 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1306 SLTTQL--EDTKRLADEESRERAT---LLGKFRNLEHDlDNLREQVEEEAEGKAdlQRQLSKANAEAQVWRSKYESDGVA 1380
Cdd:pfam10174 557 NDRIRLleQEVARYKEESGKAQAEverLLGILREVENE-KNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKK 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1381 RSEELEEAKRKLQARLAEA-----EETIESLNQKCIGLEKTKQRLSTEVEDLQ--------LEVDRANAIANAAEKKQKA 1447
Cdd:pfam10174 634 GAQLLEEARRREDNLADNSqqlqlEELMGALEKTRQELDATKARLSSTQQSLAekdghltnLRAERRKQLEEILEMKQEA 713
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1448 FDKIIGEWKLKVDDLaaELDASQKecrnystelfrlkgayEEGQEQLEAVRRENKNLADEVK 1509
Cdd:pfam10174 714 LLAAISEKDANIALL--ELSSSKK----------------KKTQEEVMALKREKDRLVHQLK 757
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
841-1017 |
5.05e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 841 VSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRD 920
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 921 IQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAhqdELINKLNKEKKMQGE 1000
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTIT---TLTQKLTTAHRKEAE 231
|
170
....*....|....*..
gi 24584706 1001 tNQKTGEELQAAEDKIN 1017
Cdd:pfam07888 232 -NEALLEELRSLQERLN 247
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1643-1861 |
5.17e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.05 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1643 KRYQQQLKDIQTALEEEQRARDDAREQLGiserRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVS---AQN 1719
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESAISSLLAQLP----AVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRkdpFKS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1720 ASISAAKRKLES--ELQTLHSDLDELLNE-AKNSEEKAKKAMVDAAR-LADELRAEQDhaqTQEKLRKALEQQIKELQVR 1795
Cdd:pfam13166 355 IELDSVDAKIESinDLVASINELIAKHNEiTDNFEEEKNKAKKKLRLhLVEEFKSEID---EYKDKYAGLEKAINSLEKE 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1796 LDEAEAnalkggkkAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRvkELSFQSEEDRKNHE 1861
Cdd:pfam13166 432 IKNLEA--------EIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFG--ELELSFNEEGKGYR 487
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
907-1134 |
5.18e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 907 LTAQKNDLENQLRDIQERLTQEEDA-------RNQLFQQKKKADQEIS--------------GLKKDIEDLELNVQKAEQ 965
Cdd:PRK11637 38 FSAHASDNRDQLKSIQQDIAAKEKSvrqqqqqRASLLAQLKKQEEAISqasrklretqntlnQLNKQIDELNASIAKLEQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 966 DKATkdhQIRNLndeiAHQDELINKLNKEKKMQ----GETNQKtGEEL--------QAAEDKINHLNKVKAKLEQTLDEL 1033
Cdd:PRK11637 118 QQAA---QERLL----AAQLDAAFRQGEHTGLQlilsGEESQR-GERIlayfgylnQARQETIAELKQTREELAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1034 EDSLEREKKVRGDVEKSKRKvegdlkltqeavadlernkkeLEQTIQRKDKELSSITAKLEdeqvvvlKHQRQIKELQA- 1112
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQK---------------------LEQARNERKKTLTGLESSLQ-------KDQQQLSELRAn 241
|
250 260
....*....|....*....|..
gi 24584706 1113 RIEELEEEVEAERQARAKAEKQ 1134
Cdd:PRK11637 242 ESRLRDSIARAEREAKARAERE 263
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1318-1562 |
5.19e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1318 ADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQvwrskyesdgvarseELEEAKRKLQARLA 1397
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR---------------ALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1398 EAEETIESLNQKcigLEKTKQRLSTEVEDLQL--EVDRANAIANA-----AEKKQKAFDKIIGEWKLKVDDLAAELDASQ 1470
Cdd:COG4942 87 ELEKEIAELRAE---LEAQKEELAELLRALYRlgRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1471 KECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAAL 1550
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|..
gi 24584706 1551 EQEENKVLRAQL 1562
Cdd:COG4942 244 PAAGFAALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
801-1208 |
5.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 801 KKLQEQRVALKVVQRNLRKYLQLRTwpwyklwQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEvKVRKELEALNAKlL 880
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQE-------ELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAE-L 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 881 AEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDarnqlfQQKKKADQEISGLKKDIEDLELNV 960
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 961 QKAEQDKATKDHQIRNLNDEIAHQDELiNKLNKEKKM----------QGETNQKTGEELQAAE----------DKINHLN 1020
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALE-ERLKEARLLlliaaallalLGLGGSLLSLILTIAGvlflvlgllaLLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1021 KVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVV 1100
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1101 LKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDL--E 1178
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELreE 454
|
410 420 430
....*....|....*....|....*....|....*..
gi 24584706 1179 EANIQHE-------STLANLRKKHNDAVAEMAEQVDQ 1208
Cdd:COG4717 455 LAELEAEleqleedGELAELLQELEELKAELRELAEE 491
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1637-1894 |
5.69e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.02 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1637 EAQKNIKRYQQQLKDIQTAleeeQRARDD----------AREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELA 1706
Cdd:pfam05667 178 KNSKELKEFYSEYLPPVTA----QPSSRAsvvpsllernAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1707 DAHEQLNEVSAQNAS-ISAAKRKLESELQTLHSDLDELLNEAK----NSEEK---AKKAMVDAARLADELRAEQDHAQTQ 1778
Cdd:pfam05667 254 EQLRSAALAGTEATSgASRSAQDLAELLSSFSGSSTTDTGLTKgsrfTHTEKlqfTNEAPAATSSPPTKVETEEELQQQR 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1779 EKLRKALEQQIKELQVRLDEAEANalkggkkaIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELsfqsEEDRK 1858
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKE--------IKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLL----PDAEE 401
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24584706 1859 NHERMQDLVDKLQQKIKTYKRQIEEA-----EEIAALNLAK 1894
Cdd:pfam05667 402 NIAKLQALVDASAQRLVELAGQWEKHrvpliEEYRALKEAK 442
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1556-1883 |
6.00e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1556 KVLRAQLELSQVRQEIDRriQEKEeefentrknHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKAN 1635
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQ--MELE---------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1636 AEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLgiserraNALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEV 1715
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLADAREVI-------SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1716 SAQNASISAAKRKLESELQTLHS------DLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKA----- 1784
Cdd:pfam05557 145 KAKASEAEQLRQNLEKQQSSLAEaeqrikELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENienkl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1785 -LEQQIKELQVRLDEAEanalkGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSE---RRVKEL----------S 1850
Cdd:pfam05557 225 lLKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEdlsRRIEQLqqreivlkeeN 299
|
330 340 350
....*....|....*....|....*....|...
gi 24584706 1851 FQSEEDRKNHERMQDLvdkLQQKIKTYKRQIEE 1883
Cdd:pfam05557 300 SSLTSSARQLEKARRE---LEQELAQYLKKIED 329
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
847-1138 |
6.22e-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: 44.73 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 847 EIARLEEKAKKAEELHAAEVKVRKELEAlnakllAEKTALLDslsgekgalqdyQERNAKLTAQKNDLEnQLRDIQERLT 926
Cdd:pfam17380 373 EISRMRELERLQMERQQKNERVRQELEA------ARKVKILE------------EERQRKIQQQKVEME-QIRAEQEEAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 927 QEEdarnqlfqqkkkadqeisglkkdiedlelnVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTG 1006
Cdd:pfam17380 434 QRE------------------------------VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1007 EELQAAEdkinhlnkvkaklEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQtiQRKDKEL 1086
Cdd:pfam17380 484 RDRKRAE-------------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE--RRKQQEM 548
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1087 ssitakleDEQVVVLKHQRQIKELQARIEELEEEVEAERQARaKAEKQRADL 1138
Cdd:pfam17380 549 --------EERRRIQEQMRKATEERSRLEAMEREREMMRQIV-ESEKARAEY 591
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
833-1081 |
6.48e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 833 QKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNA--------KLLAEKTALLDSLSGEKGA-LQDYQER 903
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedriERLEERREDLEELIAERREtIEEKRER 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 904 NAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLElNVQKAEQDKATKDHQIRNLNDEIAH 983
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREA 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 984 QDElinkLNKEKKMQGETNQKTGEELQAA--EDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLklt 1061
Cdd:PRK02224 618 LAE----LNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL--- 690
|
250 260
....*....|....*....|
gi 24584706 1062 qEAVADLERNKKELEQTIQR 1081
Cdd:PRK02224 691 -EELEELRERREALENRVEA 709
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1311-1446 |
7.72e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 44.36 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1311 LEDTKRLADEESREratllgkFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDgvaRSEELEEAKR 1390
Cdd:COG1193 502 IERARELLGEESID-------VEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEE---KEEILEKARE 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1391 KLQARL----AEAEETIESLNQKCIGLEKTK---QRLSTEVEDLQLEVDRANAIANAAEKKQK 1446
Cdd:COG1193 572 EAEEILrearKEAEELIRELREAQAEEEELKearKKLEELKQELEEKLEKPKKKAKPAKPPEE 634
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
1655-1836 |
7.98e-04 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 44.40 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1655 ALEEEQRARDDAREQLgisERRANALQNELEESRTLLEQADrgrrQAEQELADAHEQLNEVSAQNASISAAKRKLESELQ 1734
Cdd:COG3170 279 AAAEEADALPEAAAEL---AERLAALEAQLAELQRLLALKN----PAPAAAVSAPAAAAAAATVEAAAPAAAAQPAAAAP 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1735 TLHSDLDELLNeAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKL 1814
Cdd:COG3170 352 APALDNPLLLA-GLLRRRKAEADEVDPVAEADVYLAYGRDDQAEEILKEALASEPERLDLRLKLLEIYAARGDRAAFEAL 430
|
170 180
....*....|....*....|..
gi 24584706 1815 EQRVRELENELDGEQRRHADAQ 1836
Cdd:COG3170 431 AAELYALTGGGRALDPDNPLYA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1064-1302 |
8.29e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1064 AVADLERNKKELEQtIQRKDKELSSITAKLEDEQVVVLKhqrQIKELQARIEELEEEVEAERQARAKAEKQRADLARELE 1143
Cdd:COG4942 18 QADAAAEAEAELEQ-LQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1144 elgerleeaggATSAQIElnkKREAELSKLRRDLEEANIQHESTLAnlrkKHNDAVAEMAEQVDQLNKLKAKAEKEKNEY 1223
Cdd:COG4942 94 -----------ELRAELE---AQKEELAELLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584706 1224 YGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSK 1302
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1381-1667 |
8.36e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1381 RSEELEEAKRKLQArLAEA--EETIESLNQKcigLEKTKQRLSTEVEDLQLEVDranaianAAEKKQKAFDKiigewKLK 1458
Cdd:COG3206 143 TSPDPELAAAVANA-LAEAylEQNLELRREE---ARKALEFLEEQLPELRKELE-------EAEAALEEFRQ-----KNG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1459 VDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQigeggRNIHEIEKARKRLEAEKDE 1538
Cdd:COG3206 207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1539 LQAALEEAEAaleqeenKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEaEAKGKAEALrmkKKLE 1618
Cdd:COG3206 282 LSARYTPNHP-------DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA-QLEARLAEL---PELE 350
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24584706 1619 ADINELEialdhankanAEAQKNIKRYQQQLKDIQTALEEEQRARDDAR 1667
Cdd:COG3206 351 AELRRLE----------REVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
927-1536 |
8.57e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 927 QEEDARNQLFQQKKKAdQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDelinklnkEKKMQGETNQKTG 1006
Cdd:pfam10174 114 TEENFRRLQSEHERQA-KELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKG--------LPKKSGEEDWERT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1007 EELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKrKVEGDLKLTQEAVADLERNKKELEQTIQ--RKDK 1084
Cdd:pfam10174 185 RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTK-ALQTVIEMKDTKISSLERNIRDLEDEVQmlKTNG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1085 ELSSITAKLEDEQVVVLKhqrqikelqarieeleeeveaerqARAKAEKQRADlareleelgerleeaggatSAQIELNK 1164
Cdd:pfam10174 264 LLHTEDREEEIKQMEVYK------------------------SHSKFMKNKID-------------------QLKQELSK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1165 KrEAELSKLRRDLEEANIQHESTlanlrKKHNDAVAE-----------MAEQVDQLNKLKAKAEKEKNEYYGQLNDLrag 1233
Cdd:pfam10174 301 K-ESELLALQTKLETLTNQNSDC-----KQHIEVLKEsltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDL--- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1234 vdhiTNEKAAqekiakqLQHTLNEVQSKLDETNRTLNDFdasKKKlsIENsdLLRQLEEAESQVSQLSKIKISLTTQLED 1313
Cdd:pfam10174 372 ----TEEKST-------LAGEIRDLKDMLDVKERKINVL---QKK--IEN--LQEQLRDKDKQLAGLKERVKSLQTDSSN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1314 T------------------KRLADEESRERATLLGKFRNLEHDLDNLREQVE-------EEAEGKADLQRQLSKANAEAQ 1368
Cdd:pfam10174 434 TdtalttleealsekeriiERLKEQREREDRERLEELESLKKENKDLKEKVSalqpeltEKESSLIDLKEHASSLASSGL 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1369 VWRSKYESDGVARSEELEEAKrKLQARL------AEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAE 1442
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECS-KLENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVE 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1443 KKQKAFDKIIGEWKlkvddlaaELDASQKECRNYSTELFRLKGAYE--EGQEQLEAVRRENKNLADEVKDLldQIGEggr 1520
Cdd:pfam10174 593 NEKNDKDKKIAELE--------SLTLRQMKEQNKKVANIKHGQQEMkkKGAQLLEEARRREDNLADNSQQL--QLEE--- 659
|
650
....*....|....*.
gi 24584706 1521 NIHEIEKARKRLEAEK 1536
Cdd:pfam10174 660 LMGALEKTRQELDATK 675
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1569-1886 |
9.33e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.98 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1569 QEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEadINELEIALDHANKANAEAQKNIKRYQQQ 1648
Cdd:pfam09731 88 QVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEA--ISKAESATAVAKEAKDDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1649 LKD-IQTALEEEQRARDDAREQLG-----ISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASI 1722
Cdd:pfam09731 166 LKEaSDTAEISREKATDSALQKAEalaekLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1723 SAAKRKLESELQTLHSDLDELLNEAkNSEEKAkkamvDAARLADELRAEQDHAQTQeklRKALEQQIKELQVRLDEAEAN 1802
Cdd:pfam09731 246 DQYKELVASERIVFQQELVSIFPDI-IPVLKE-----DNLLSNDDLNSLIAHAHRE---IDQLSKKLAELKKREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1803 ALKGGKKAIQKLEQRV-RELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKL-QQKIKTYKRQ 1880
Cdd:pfam09731 317 ALEKQKEELDKLAEELsARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLvEQEIELQREF 396
|
....*.
gi 24584706 1881 IEEAEE 1886
Cdd:pfam09731 397 LQDIKE 402
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
907-1037 |
9.52e-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: 43.69 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 907 LTAQKNDLENQLRdiqERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLElnvqKAEQDKA-------TKDHQiRNL-- 977
Cdd:pfam03148 238 LRAQADAVNFALR---KRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALE----KAIRDKEaplklaqTRLEN-RTYrp 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 978 NDEIAHqDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSL 1037
Cdd:pfam03148 310 NVELCR-DEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSL 368
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1620-1755 |
1.07e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1620 DINELEIALDHANKANAEAQKNIKRYQQQLKDIQT----------ALEEEQRARDDAREQLGISERRANALQNELEESRT 1689
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAleselaisrqDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1690 LLEQADRGRRQ---AEQELADAHEQLNEVSAQNASISAAK----RKLESELQTLHSDLDELLNEAKNSEEKAK 1755
Cdd:pfam00529 132 LAPIGGISRESlvtAGALVAQAQANLLATVAQLDQIYVQItqsaAENQAEVRSELSGAQLQIAEAEAELKLAK 204
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1628-1902 |
1.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1628 LDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQAdrgrRQAEQELAD 1707
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL----EKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1708 AHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAmvdaarlaDELRAEQDHAQTQEKLRKALEQ 1787
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1788 QIKELQVRLD--EAEANALKGGKKAIQKLEQRVRELENELdgeqrrhadaqknlRKSERRVKELsfqsEEDRKNHERMQD 1865
Cdd:PRK03918 308 ELREIEKRLSrlEEEINGIEERIKELEEKEERLEELKKKL--------------KELEKRLEEL----EERHELYEEAKA 369
|
250 260 270
....*....|....*....|....*....|....*..
gi 24584706 1866 LVDKLQQKIKtyKRQIEEAEEIAALnLAKFRKAQQEL 1902
Cdd:PRK03918 370 KKEELERLKK--RLTGLTPEKLEKE-LEELEKAKEEI 403
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1068-1299 |
1.14e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1068 LERNKKELEQTIQRKDKELSSITAKLED--EQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEEL 1145
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEaeAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1146 GERLEEAGGATSAQIElnkkrEAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYG 1225
Cdd:COG3206 246 RAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24584706 1226 QLNDLRAGVDHITNEKAAQEKIAKQlqhtLNEVQSKLDETNRtlnDFDASKKKLsienSDLLRQLEEAESQVSQ 1299
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLER---EVEVARELY----ESLLQRLEEARLAEAL 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1727-1925 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1727 RKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEAnalkg 1806
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1807 gKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKL-QQKIKTYKRQIEEAE 1885
Cdd:COG4717 124 -LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24584706 1886 EIAAlnlaKFRKAQQELEEAEERADLAEQAISKFRAKGRA 1925
Cdd:COG4717 203 ELQQ----RLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1558-1778 |
1.17e-03 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 43.83 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1558 LRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAkGKAEALRMKKKLEADINELEIALDHANKANAE 1637
Cdd:COG3914 8 ALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEA-AAAALLALAAGEAAAAAAALLLLAALLELAAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1638 AQKNIKRYQQQLKDIQTALeEEQRARDDAREQLGISERRanalQNELEESRTLLEQAdrgrRQAEQELADAHEQLNEVSA 1717
Cdd:COG3914 87 LLQALGRYEEALALYRRAL-ALNPDNAEALFNLGNLLLA----LGRLEEALAALRRA----LALNPDFAEAYLNLGEALR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1718 QNASISAAKR------KLESELQTLHSDLDELLNEAKNSEEkakkaMVDAARLADELRAEQDHAQTQ 1778
Cdd:COG3914 158 RLGRLEEAIAalrralELDPDNAEALNNLGNALQDLGRLEE-----AIAAYRRALELDPDNADAHSN 219
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
969-1085 |
1.25e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 43.49 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 969 TKDHQIRNLNDEIAHQDELINKLNKEKKM-------QGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREK 1041
Cdd:smart00435 232 TLQEQLKELTAKDGNVAEKILAYNRANREvailcnhQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKR 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1042 KVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQT--------IQRKDKE 1085
Cdd:smart00435 312 KLKSKFERDNEKLDAEVKEKKKEKKKEEKKKKQIERLeeriekleVQATDKE 363
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1593-1936 |
1.34e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1593 LDSMQASLEAEAKGKAEAL---RMKKKLEADINELEIALDHANKAN-AEAQKNIKRYQQQLKDIQ---TALEEEQRARDD 1665
Cdd:COG5185 185 TLGLLKGISELKKAEPSGTvnsIKESETGNLGSESTLLEKAKEIINiEEALKGFQDPESELEDLAqtsDKLEKLVEQNTD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1666 AR-EQLGISERRANALQNELEESRTLLEQADRGRRQAEQELAD--AHEQLNEVSAQ---NASISAAKRKLESELQTLHSD 1739
Cdd:COG5185 265 LRlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIkkATESLEEQLAAaeaEQELEESKRETETGIQNLTAE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1740 LDELLNEAKNSEEKAKK------AMVDAARLADELRAEQDhaqTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQK 1813
Cdd:COG5185 345 IEQGQESLTENLEAIKEeienivGEVELSKSSEELDSFKD---TIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1814 LEQRVRELE---NELDGEQRRHADAQKNLRKSERRVKELSFQ---------SEEDRKNHERMQDLVDKLQQKIKTYKRQI 1881
Cdd:COG5185 422 IEELQRQIEqatSSNEEVSKLLNELISELNKVMREADEESQSrleeaydeiNRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1882 EEAEEIAALNLAKFR-KAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAP 1936
Cdd:COG5185 502 EKLRAKLERQLEGVRsKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAK 557
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1641-1867 |
1.45e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1641 NIKRYQQQLKDIQTalEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNA 1720
Cdd:pfam05262 195 NFRRDMTDLKERES--QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKED 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1721 SISAAKRKLESELQTLhsdldellnEAKNSEEKAKKAMVDAA-RLADELRAEQDHAQTQE-KLRKALEQQIKELQVRLDE 1798
Cdd:pfam05262 273 KQVAENQKREIEKAQI---------EIKKNDEEALKAKDHKAfDLKQESKASEKEAEDKElEAQKKREPVAEDLQKTKPQ 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584706 1799 AEANALKGGKKAIqkleqrvrelENELDGEQRRHADAQKNLR-------KSERRVKELSFQSEEDRKNHERMQDLV 1867
Cdd:pfam05262 344 VEAQPTSLNEDAI----------DSSNPVYGLKVVDPITNLSelvlidlKTEVRLRESAQQTIRRRGLYEREKDLV 409
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1645-1922 |
1.54e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1645 YQQQLKDIQTALEeeqRARDDAREQL--------GISER----RANALQNELEESRTLLEQADRGRRQAEQELADAHEQL 1712
Cdd:PRK02224 167 YRERASDARLGVE---RVLSDQRGSLdqlkaqieEKEEKdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1713 NEvsaqnasisaaKRKLESELQTLHSDLDELlNEAKNSEEKAKKAmvdaarLADELRaeqDHAQTQEKLRKALEQQIKEL 1792
Cdd:PRK02224 244 EE-----------HEERREELETLEAEIEDL-RETIAETEREREE------LAEEVR---DLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1793 QvrLDEAEANALKggkKAIQKLEQRVRELENELDgEQRRHADAQKNLRKSER-RVKELSFQSEEDRKNHERMQDLVDKLQ 1871
Cdd:PRK02224 303 G--LDDADAEAVE---ARREELEDRDEELRDRLE-ECRVAAQAHNEEAESLReDADDLEERAEELREEAAELESELEEAR 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1872 QKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAK 1922
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1486-1815 |
1.66e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.67 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1486 AYEEGQEQLEAVRRENKNLADEVKDLLDQigeggrniHEIEKARKRLEAEKDELQAALEEAeaaleqeenkvlRAQLE-- 1563
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQDDAAQNALADK--------ERAEADRQRLEQEKQQQLAAISGS------------QSQLEst 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1564 ----LSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQA-SLEAEAKGKAEALRMKKKLEADINE-LEIALDHANKANAE 1637
Cdd:NF012221 1596 dqnaLETNGQAQRDAILEESRAVTKELTTLAQGLDALDSqATYAGESGDQWRNPFAGGLLDRVQEqLDDAKKISGKQLAD 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1638 AQKNIKRYQQQLKDI----QTALEEEQRARDDAreQLGISERRANALQNELEesrtlleqADRGRRQAEQELADAHeqln 1713
Cdd:NF012221 1676 AKQRHVDNQQKVKDAvaksEAGVAQGEQNQANA--EQDIDDAKADAEKRKDD--------ALAKQNEAQQAESDAN---- 1741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1714 evsaqnASISAAKRKLESELQTLHSDLDELLNEAK----NSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQI 1789
Cdd:NF012221 1742 ------AAANDAQSRGEQDASAAENKANQAQADAKgakqDESDKPNRQGAAGSGLSGKAYSVEGVAEPGSHINPDSPAAA 1815
|
330 340
....*....|....*....|....*..
gi 24584706 1790 K-ELQVRLDEAEANALKGGKKAIQKLE 1815
Cdd:NF012221 1816 DgRFSEGLTEQEQEALEGATNAVNRLQ 1842
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1449-1725 |
1.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1449 DKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIgeggrniheiEKA 1528
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1529 RKRLEaekdelqaaleeaeaaleqeenKVLRAQLELSQVRQEIDRRIQEKE-EEFENTRKNHQRALDSMQASLEAEAKGK 1607
Cdd:COG3883 85 REELG----------------------ERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1608 AEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEES 1687
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 24584706 1688 RTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAA 1725
Cdd:COG3883 223 AAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1564-1815 |
1.75e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1564 LSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEadinELEIALDHANKANAEAQKNIK 1643
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE----ELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1644 RYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASIS 1723
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1724 AAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANA 1803
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250
....*....|..
gi 24584706 1804 LKGGKKAIQKLE 1815
Cdd:COG4372 265 LAILVEKDTEEE 276
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
838-1102 |
1.81e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 838 LLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSgekgaLQDYQERNAKLTAQKNDLENQ 917
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLS-----LRQLESRLAQTLDQLQNAQND 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 918 LRDIQERL----TQEEDARNQLFQQKKKAdQEISGLKKDIEDLELNVQKAEQDK-----ATKDHQIRNLNDEIAHQDELI 988
Cdd:PRK11281 144 LAEYNSQLvslqTQPERAQAALYANSQRL-QQIRNLLKGGKVGGKALRPSQRVLlqaeqALLNAQNDLQRKSLEGNTQLQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 989 NKLNKEKKMQGETNQKTGEELQAAEDKINhlNKVKAKLEQTLDELEDSlerekkvrgdvEKSKRKVEGDLkLTQEAVADL 1068
Cdd:PRK11281 223 DLLQKQRDYLTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQSQ-----------DEAARIQANPL-VAQELEINL 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24584706 1069 ERNKKELEQTiqRKDKELS--SITAK--LE---------DEQVVVLK 1102
Cdd:PRK11281 289 QLSQRLLKAT--EKLNTLTqqNLRVKnwLDrltqserniKEQISVLK 333
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1298-1666 |
1.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1298 SQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQvwrskyesD 1377
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE--------Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1378 GVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKL 1457
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1458 KVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKD 1537
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1538 ELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKL 1617
Cdd:COG4372 238 LLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24584706 1618 EADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDA 1666
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1607-1810 |
1.84e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1607 KAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANAlqnelEE 1686
Cdd:TIGR02794 56 QQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ-----AA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1687 SRTLLEQADRGRRQAEqelaDAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAK--------KAM 1758
Cdd:TIGR02794 131 EAKAKAEAEAERKAKE----EAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaeaakaKAA 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24584706 1759 VDAARLADELRAEQDHAQTQeklRKALEQQIKELQVRLDEAEANALKGGKKA 1810
Cdd:TIGR02794 207 AEAAAKAEAEAAAAAAAEAE---RKADEAELGDIFGLASGSNAEKQGGARGA 255
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1644-1813 |
1.88e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1644 RYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRtllEQADRGRRQAEQELADAHE-QLNEVSAQNASI 1722
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---LAAQEQKKQAEEAAKQAALkQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1723 SAAKRKLESELQTLHSDLDELLNEAK--NSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAE 1800
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAAAEAKkkAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
170
....*....|...
gi 24584706 1801 ANALKGGKKAIQK 1813
Cdd:PRK09510 223 AKAAAAKAAAEAK 235
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1620-1854 |
1.98e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1620 DINELEIALDHANKANAeaqknikryqqQLKDIQTALEEEQRARDDAREQLGISERRANALqneLEESRTLLEQADRGRR 1699
Cdd:pfam06008 3 SLNSLTGALPAPYKINY-----------NLENLTKQLQEYLSPENAHKIQIEILEKELSSL---AQETEELQKKATQTLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1700 QAEQELADAHEQLNEVSAQNASISAAKRKLESEL-QTLHSDLdellNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQ 1778
Cdd:pfam06008 69 KAQQVNAESERTLGHAKELAEAIKNLIDNIKEINeKVATLGE----NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1779 ---------EKLRKALEQQIKELQVR---LDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRV 1846
Cdd:pfam06008 145 naeaelkaaQDLLSRIQTWFQSPQEEnkaLANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKK 224
|
....*...
gi 24584706 1847 KELSFQSE 1854
Cdd:pfam06008 225 EEVSEQKN 232
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1488-1746 |
2.28e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1488 EEGQEQLEAVRRENKNLADEVKDLLDQIgEGGRNIHEiEKARKRLEAEKDElqaaleeaeaaleqeenKVLRAQL-ELSQ 1566
Cdd:pfam00038 57 EDLRRQLDTLTVERARLQLELDNLRLAA-EDFRQKYE-DELNLRTSAENDL-----------------VGLRKDLdEATL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1567 VRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALD-HANKANAEAQKNikrY 1645
Cdd:pfam00038 118 ARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEeIAAKNREEAEEW---Y 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1646 QQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQnasisaa 1725
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISE------- 267
|
250 260
....*....|....*....|.
gi 24584706 1726 krkLESELQTLHSDLDELLNE 1746
Cdd:pfam00038 268 ---LEAELQETRQEMARQLRE 285
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1382-1517 |
2.31e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1382 SEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEvdRANAIANAAEKKQKAfdkiIGEWKLKVDD 1461
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE--EDKLLEEAEKEAQQA----IKEAKKEADE 588
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1462 LAAELDASQKEC------RNYSTELFRLKGAYEEGQEQLEAVRRENKNLA--DEVKDL-LDQIGE 1517
Cdd:PRK00409 589 IIKELRQLQKGGyasvkaHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgDEVKYLsLGQKGE 653
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
797-1139 |
2.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 797 RKGFKKLQEQRVALKVVQRNLRKYLQLrtWPWYKLWQKVKPLLN-----VSRIEDEIARLEEKAKKAEELHAAEVKVRKE 871
Cdd:COG4717 101 EEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAelperLEELEERLEELRELEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 872 LEALNAKLLAEKTALLDSLSGEKGALQdyqERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQE------ 945
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQ---QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARllllia 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 946 -----ISGLKKDIEDLELNV--------------------QKAEQDKATKDHQIRNLNDEIAHQ---------------- 984
Cdd:COG4717 256 aallaLLGLGGSLLSLILTIagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEeleellaalglppdls 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 985 -DELINKLNKEKKMQGETNQKTGEELQAAEDKINH-----LNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDL 1058
Cdd:COG4717 336 pEELLELLDRIEELQELLREAEELEEELQLEELEQeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1059 KLTQEAVADLerNKKELEQTIQRKDKELSSITAKLEDeqvvvlkHQRQIKELQARIeELEEEVEAERQARAKAEKQRADL 1138
Cdd:COG4717 416 GELEELLEAL--DEEELEEELEELEEELEELEEELEE-------LREELAELEAEL-EQLEEDGELAELLQELEELKAEL 485
|
.
gi 24584706 1139 A 1139
Cdd:COG4717 486 R 486
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
778-1135 |
2.67e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 778 ERLGKIMSWMQAWARGYLSRK---------GFKKLQEQRVALKVVQRNLRKYLQlrtwpwyKLWQKVKPLLNVSR-IEDE 847
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMERQmaaiqgkneSLEKVSSLTAQLESTKEMLRKVVE-------ELTAKKMTLESSERtVSDL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 848 IARLEEKAKKAEELHAAEVKVRKELEAlnakllaeKTALLDSLSGEKGALQDYQERNAKL---TAQKNDLENQLRDIQER 924
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDL--------KLQELQHLKNEGDHLRNVQTECEALklqMAEKDKVIEILRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 925 LTQ--EEDARNQLFQQKKKADqeisgLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDelinkLNKEKKMQGETn 1002
Cdd:pfam15921 574 MTQlvGQHGRTAGAMQVEKAQ-----LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-----LEKVKLVNAGS- 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1003 qktgEELQAAEDkinhlnkVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRK 1082
Cdd:pfam15921 643 ----ERLRAVKD-------IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24584706 1083 DKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQR 1135
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
1583-1886 |
2.70e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 42.64 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1583 ENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAqknIKRYQQQLKDIQTALEEEQRA 1662
Cdd:PTZ00332 242 EEENKSFSKIHEVQKQANQETSQMKDAKRRLKQRCETDLKHIHDAIQKADLEDAEA---MKRYATNKEKSERFIRENEDR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1663 RDDAREQLGISERRANALQNE-LEESRTLLEQADR-GRRQAEQ----ELADAHEQLNEVSAQNASISAAKRKLESELqtl 1736
Cdd:PTZ00332 319 QEEAWNKIQDLERQLQRLGTErFEEVKRRIEENDReEKRRVEYqqflEVAGQHKKLLELTVYNCDLALRCTGLVEEL--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1737 hsdLDELLNEAKNSEEKAKKAMVDAarladELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANalkggkkaIQKLEQ 1816
Cdd:PTZ00332 396 ---VSEGCAAVKARHDKTNQDLAAL-----RLQVHKEHLEYFRMLYLTLGSLIYKKEKRLEEIDRN--------IRTTHI 459
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1817 RVRELENELDGEQRRHADAQKNLRKSERRV-KELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEE 1886
Cdd:PTZ00332 460 QLEFCVETFDPNAKKHADMKKELYKLRQGVeEELAMLKEKQAQALEMFKESEEALDAAGIEFVHPVDENNE 530
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1615-1890 |
2.71e-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: 42.53 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1615 KKLEADINELEiaLDHANKANAEAQKNIkryqQQLKDIqtaLEEEQRARDDAREQLGISERRANALQNELEESRTLLEQA 1694
Cdd:pfam06160 247 EENLALLENLE--LDEAEEALEEIEERI----DQLYDL---LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1695 DRGRRQAEQELADAheqlnevsaqnasisaakRKLESELQTLHSDLDELLNEAKNSeekakkamvdaarladelraEQDH 1774
Cdd:pfam06160 318 QQSYTLNENELERV------------------RGLEKQLEELEKRYDEIVERLEEK--------------------EVAY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1775 AQTQEKLRKALEQ--QIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRH-----ADAQKNLRKSERRVK 1847
Cdd:pfam06160 360 SELQEELEEILEQleEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIE 439
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24584706 1848 ELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAAL 1890
Cdd:pfam06160 440 DLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATL 482
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1628-1746 |
2.71e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.53 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1628 LDHANKANAEAQKNIKRYQQQLKDiqtALEEEQRARDDARE--QLGISERRANAlqneLEESRTLLEQAdrgRRQAEQEL 1705
Cdd:PRK05759 44 LAAAERAKKELELAQAKYEAQLAE---ARAEAAEIIEQAKKraAQIIEEAKAEA----EAEAARIKAQA---QAEIEQER 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24584706 1706 ADAHEQL-NEVSAqnASISAAKRKLESEL-QTLHSDL-DELLNE 1746
Cdd:PRK05759 114 KRAREELrKQVAD--LAVAGAEKILGRELdAAAQSDLiDKLIAE 155
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1674-1922 |
2.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1674 ERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEK 1753
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1754 AKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEAnALKGGKKAIQKLEQRVRELENELDGEQRRHA 1833
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1834 DAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAE 1913
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
....*....
gi 24584706 1914 QAISKFRAK 1922
Cdd:COG4372 248 KEELLEEVI 256
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1717-1836 |
2.90e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1717 AQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEK---------LRKALEQ 1787
Cdd:cd22656 100 IDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKalkdlltdeGGAIARK 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24584706 1788 QIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQ 1836
Cdd:cd22656 180 EIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| fliD |
PRK08724 |
flagellar filament capping protein FliD; |
1629-1877 |
2.92e-03 |
|
flagellar filament capping protein FliD;
Pssm-ID: 236335 [Multi-domain] Cd Length: 673 Bit Score: 42.55 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1629 DHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGiserranalQNELEESRTLLEQADrgrrqaeqELADA 1708
Cdd:PRK08724 183 DNQIKISVDAEYGNPLKRFEYKTLEDRVRALEKARAAAQQVIA---------PLTPEEQKVAPELSD--------EEGNA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1709 HEQLNEVSAQNASiSAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQ 1788
Cdd:PRK08724 246 IPPADQEVAEEIQ-DAAQIAQQQEATAALAALEEPISAGGATAAAAGQAAIDAAEAKAYLRPEDRIPGWTETASGTLLDS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1789 IKELQVRLDEAEA---------NALKGG---------KKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERrvKELS 1850
Cdd:PRK08724 325 YPEPEEELDEAAIakapdvpgwSNTASGtltdsyvtpKEAQAEIEQKLAQEKAQLDAAVEKGELTPEQAKQIAR--AKLE 402
|
250 260
....*....|....*....|....*..
gi 24584706 1851 FQSEEDRKNHERMQDLVDKLQQKIKTY 1877
Cdd:PRK08724 403 PEERERLEKIDKAQAALKQAQSAFDLY 429
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1615-1713 |
2.95e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.02 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1615 KKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQ-LGISERRANALQNELEESRTLLEQ 1693
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQaLQTAQNNLATAQAALANAEARLAK 336
|
90 100
....*....|....*....|
gi 24584706 1694 ADRGRRQAEQELADAHEQLN 1713
Cdd:TIGR04320 337 AKEALANLNADLAKKQAALD 356
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1627-1730 |
3.15e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1627 ALDHANKANAEAQKNIKRYQQQLKDIQtalEEEQRARDDAREQlgISERRANALQNELEESRTLLEQAdrgRRQAEQELA 1706
Cdd:cd06503 38 SLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKE--AEKIKEEILAEAKEEAERILEQA---KAEIEQEKE 109
|
90 100
....*....|....*....|....*
gi 24584706 1707 DAHEQL-NEVSAQnaSISAAKRKLE 1730
Cdd:cd06503 110 KALAELrKEVADL--AVEAAEKILG 132
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1226-1447 |
3.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1226 QLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQL----- 1300
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1301 -SKIKISLTTQLEDTKRLADeesreratLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSkanaeaqvwrskyesdgv 1379
Cdd:COG3883 97 rSGGSVSYLDVLLGSESFSD--------FLDRLSALSKIADADADLLEELKADKAELEAKKA------------------ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1380 arseELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKA 1447
Cdd:COG3883 151 ----ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1016-1885 |
3.50e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1016 INHLNKVKAKLeQTLDELEDSLEREKKVRGDVEKSKRKV--EGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKL 1093
Cdd:TIGR01612 489 SKQDNTVKLIL-MRMKDFKDIIDFMELYKPDEVPSKNIIgfDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKEL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1094 EDEQVVVLKHQRQIK---------------------ELQARIEELEEEVEAERQA---RAKAEKQRA---DLARELEELG 1146
Cdd:TIGR01612 568 EEENEDSIHLEKEIKdlfdkyleiddeiiyinklklELKEKIKNISDKNEYIKKAidlKKIIENNNAyidELAKISPYQV 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1147 ERLEEAGGATSAQI--ELNKKREAELSKLRRDLeeANIQHESTLANLRKKHNdaVAEMAEQVDqlnklkakaekekNEYY 1224
Cdd:TIGR01612 648 PEHLKNKDKIYSTIksELSKIYEDDIDALYNEL--SSIVKENAIDNTEDKAK--LDDLKSKID-------------KEYD 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1225 GQLNDLRAGVD-HITNEKAAQEKIAKQLQHTLNEVQSKLD-ETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSK 1302
Cdd:TIGR01612 711 KIQNMETATVElHLSNIENKKNELLDIIVEIKKHIHGEINkDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISE 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1303 IKISLTTQL-------EDTKRLADEESR----------ERATLLGKFRNLEHDL-----------DNLREQVEEEAEGKA 1354
Cdd:TIGR01612 791 IKNHYNDQInidnikdEDAKQNYDKSKEyiktisikedEIFKIINEMKFMKDDFlnkvdkfinfeNNCKEKIDSEHEQFA 870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1355 DLQRQLSK-------ANAEAQVWRSKYESDGVARSEELE----EAKRKLQARLAEAEETIESL----NQKCIGLEKTKQR 1419
Cdd:TIGR01612 871 ELTNKIKAeisddklNDYEKKFNDSKSLINEINKSIEEEyqniNTLKKVDEYIKICENTKESIekfhNKQNILKEILNKN 950
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1420 LSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEwkLKVDDLAAELDASQKECRNYSTELFRLKG--AYEEGQEQLEAV 1497
Cdd:TIGR01612 951 IDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKD--ASLNDYEAKNNELIKYFNDLKANLGKNKEnmLYHQFDEKEKAT 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1498 R-------RENKNLAD-------EVKDLLDQI-GEGGRNIHEIEK-ARKRLEA---------EKDELQAALEEAEAALEQ 1552
Cdd:TIGR01612 1029 NdieqkieDANKNIPNieiaihtSIYNIIDEIeKEIGKNIELLNKeILEEAEInitnfneikEKLKHYNFDDFGKEENIK 1108
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1553 EENKVLRAQLELSQVRQEIDRRIQEKEEefenTRKNHQRALDSMQASleaeakgkaealrmkkkleadINELEIALDhan 1632
Cdd:TIGR01612 1109 YADEINKIKDDIKNLDQKIDHHIKALEE----IKKKSENYIDEIKAQ---------------------INDLEDVAD--- 1160
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1633 kaNAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLG-ISERRANalQNELEESRTL------------LEQADRGRR 1699
Cdd:TIGR01612 1161 --KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNeIAEIEKD--KTSLEEVKGInlsygknlgklfLEKIDEEKK 1236
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1700 QAEQELADAH---EQLNEVSAQNASIS---AAKRKLESELQTL---HSDLDELLNEAKNSEEKAKKAMVDAARLADELRA 1770
Cdd:TIGR01612 1237 KSEHMIKAMEayiEDLDEIKEKSPEIEnemGIEMDIKAEMETFnisHDDDKDHHIISKKHDENISDIREKSLKIIEDFSE 1316
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1771 EQDHAQTQEKLRKALEQQIK---ELQVRLDEAEA--NALKGGKkaIQKLEQRVRELENELDGEQRRHADAQKNLRKSERR 1845
Cdd:TIGR01612 1317 ESDINDIKKELQKNLLDAQKhnsDINLYLNEIANiyNILKLNK--IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKK 1394
|
970 980 990 1000
....*....|....*....|....*....|....*....|.
gi 24584706 1846 VKELSFQSEEDRKNHERMQDL-VDKLQQKIKTYKRQIEEAE 1885
Cdd:TIGR01612 1395 IKDDINLEECKSKIESTLDDKdIDECIKKIKELKNHILSEE 1435
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1637-1770 |
3.63e-03 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 40.63 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1637 EAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLgiserraNALQNELEESRTLLEQADRGRRQAEQELADaheqlnevs 1716
Cdd:pfam05335 70 EAEAVVQEESASLQQSQANANAAQRAAQQAQQQL-------EALTAALKAAQANLENAEQVAAGAQQELAE--------- 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24584706 1717 aQNASISAAKRKLESelqtlhsdLDELLNEAKNSEEKAKKAMVDAARLADELRA 1770
Cdd:pfam05335 134 -KTQLLEAAKKRVER--------LQRQLAEARADLEKTKKAAYKAACAAVEAKQ 178
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
897-1450 |
3.71e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 897 LQDYQERNAKLTAQKNDLENQLRDIQ---ERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQ 973
Cdd:PRK01156 192 LKSSNLELENIKKQIADDEKSHSITLkeiERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 974 I---------------------RN-LNDEIAHQDELINKLNKEKKMQGETNQ-----KTGEELQAAEDKINHLNKVKAKL 1026
Cdd:PRK01156 272 NnyykeleerhmkiindpvyknRNyINDYFKYKNDIENKKQILSNIDAEINKyhaiiKKLSVLQKDYNDYIKKKSRYDDL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1027 EQTLDELEDSLEREKKVRGDVEKSKRKVEgdlkltqEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQ 1106
Cdd:PRK01156 352 NNQILELEGYEMDYNSYLKSIESLKKKIE-------EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1107 IKELQARIeeleeeveaeRQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQhes 1186
Cdd:PRK01156 425 VSSLNQRI----------RALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIE--- 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1187 tlanlRKKHNDAVAEMAEQVDQLNKLKAKAEKEkneYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQS----KL 1262
Cdd:PRK01156 492 -----VKDIDEKIVDLKKRKEYLESEEINKSIN---EYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkleDL 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1263 DETNRTLNDFDASKKKLSIENsdLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNL 1342
Cdd:PRK01156 564 DSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1343 REQVEEEAEGKADLQRQLSKANA--EAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKcigLEKTKQRL 1420
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSiiPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR---INELSDRI 718
|
570 580 590
....*....|....*....|....*....|
gi 24584706 1421 STEVEDLQLEVDRANAIANAAEKKQkAFDK 1450
Cdd:PRK01156 719 NDINETLESMKKIKKAIGDLKRLRE-AFDK 747
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
865-1095 |
4.07e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 865 EVKVRKELEALNAKLLAEKTALLDSLSGEKGALQ-------DYQERNAKLTAQKNDlenqlrDIQERLTQEEDARNQLFQ 937
Cdd:PHA02562 161 DISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQqqiktynKNIEEQRKKNGENIA------RKQNKYDELVEEAKTIKA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 938 QKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDE----------------IAHQDELINKL-NKEKKMQGE 1000
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptctqqISEGPDRITKIkDKLKELQHS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1001 TNQ--KTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQT 1078
Cdd:PHA02562 315 LEKldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
250 260
....*....|....*....|
gi 24584706 1079 IQRKDKE---LSSITAKLED 1095
Cdd:PHA02562 395 KSELVKEkyhRGIVTDLLKD 414
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
1676-1790 |
4.07e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 40.11 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1676 RANALQNELEESRTLLEQAD-------RGRRQAEQELADAheqlnevsaqnasISAAKRKLESELQTLHSDLDELL-NEA 1747
Cdd:PRK09173 34 RADRIKNELAEARRLREEAQqllaeyqRKRKEAEKEAADI-------------VAAAEREAEALTAEAKRKTEEYVaRRN 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 1748 KNSEEKAKKAMVDAARL------------ADELRAEQDHAQTQEKLRKALEQQIK 1790
Cdd:PRK09173 101 KLAEQKIAQAETDAINAvrssavdlaiaaAEKLLAEKVDAKAASELFKDALAQVK 155
|
|
| V_Alix_like_1 |
cd09238 |
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ... |
1557-1877 |
5.11e-03 |
|
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This domain family is comprised of uncharacterized plant proteins. It belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), (His-Domain) type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_Rim20_Bro1_like superfamily also have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members of the V_Alix_like superfamily also have a proline-rich region (PRR).
Pssm-ID: 185751 Cd Length: 339 Bit Score: 41.30 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1557 VLRAQLELSQVRQEIdRRIQEKEEEFENTrknhQRALD-SMQASLEAEAKGKAEALRMKKKLEADINELEiALDHANKAN 1635
Cdd:cd09238 18 LIRTEADRLAAASDE-ARVALREMELPET----LIALDgGASLPGDLGLDEEVEAVQISGGLAALEGELP-RLRELRRVC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1636 aeaqknikryQQQLKDIQTALEEEQRARDDAREQLGISERRANA------LQNELEESRTLLEQADRGRRQAEQELADAH 1709
Cdd:cd09238 92 ----------TELLAAAQESLEAEATEDSAARTQYGTAWTRPPSatltknLWERLNRFRVNLEQAGDSDESLRRRIEDAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1710 ---EQLNEVSAQNA----------------SISAAKRKLESELQTLHSD---LDELLNEAKNSEEKAKKAMVDAARLADE 1767
Cdd:cd09238 162 dgmLILDDEPAAAAaptlrapmlstdeddaSIVGTLRSNLEELEALGNEragIEDMMKALKRNDNILAKVMATTGSYDAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1768 LRAEqdhAQTQEKLRKALEQQIkelqvrldEAEANALKggkkAIQKLEQRVRELENeLDGEQRRHADAQKNLRKSERRVK 1847
Cdd:cd09238 242 FKEE---LKKYDSVREAVSKNI--------SSQDDLLS----RLRALNEKFSQIFD-VEGWRAATESHATQIRAAVAKYR 305
|
330 340 350
....*....|....*....|....*....|
gi 24584706 1848 ELSFQSEEDRKNHERMQDLVDKLQQKIKTY 1877
Cdd:cd09238 306 ELREGMEEGLRFYSGFQEAVRRLKQECEDF 335
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
842-1204 |
5.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 842 SRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDI 921
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 922 QERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGET 1001
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1002 NQKTGEELQAAEdkinhlnkvKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQR 1081
Cdd:COG4372 166 LAALEQELQALS---------EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1082 KDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIE 1161
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24584706 1162 LNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAE 1204
Cdd:COG4372 317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
875-1200 |
5.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 875 LNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIE 954
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 955 DLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQK-------TGEELQAAEDKINHLNKVKAKLE 1027
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleaqiaeLQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1028 QTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQI 1107
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1108 KELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHEST 1187
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|...
gi 24584706 1188 LANLRKKHNDAVA 1200
Cdd:COG4372 324 LAKKLELALAILL 336
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
898-1070 |
5.40e-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: 41.20 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 898 QDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQL--FQQKKKADQEisglkkdiedlELNVQKAEQDKATKDHQIR 975
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLtdFENQTEKDQT-----------ALETLEKALKDLLTDEGGA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 976 NLNDEIahqDELINKLNKEKKmqgetnqktgEELQAAEDKINhlnkvkaKLEQTLDELEDSLEREKKVRGDVEKSKRKVE 1055
Cdd:cd22656 176 IARKEI---KDLQKELEKLNE----------EYAAKLKAKID-------ELKALIADDEAKLAAALRLIADLTAADTDLD 235
|
170
....*....|....*
gi 24584706 1056 GDLKLTQEAVADLER 1070
Cdd:cd22656 236 NLLALIGPAIPALEK 250
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
839-1051 |
5.49e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 839 LNVSRIE---DEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKgalQDYQERNAKLTAQKNDLE 915
Cdd:PHA02562 171 LNKDKIRelnQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 916 NQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKK---------DIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDE 986
Cdd:PHA02562 248 MDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584706 987 LINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQT----------LDELEDSLEREKKVRGDVEKSK 1051
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvdnaeeLAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
985-1111 |
5.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 985 DELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREkkVRGDVEKSKRKVEGDLKLTQEa 1064
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE--AQQAIKEAKKEADEIIKELRQ- 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24584706 1065 vadlernkKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQ 1111
Cdd:PRK00409 596 --------LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1670-1841 |
5.77e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1670 LGISERRANALQNELEESrtLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKR---------KLESELQTLHSDL 1740
Cdd:COG3524 160 LAESEELVNQLSERARED--AVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATaeallqliaTLEGQLAELEAEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1741 DELLNEAKNseekakkamvDAARLaDELRAEQDhaqtqeklrkALEQQIKELQVRLdeaeanALKGGKKAIQKLEQRVRE 1820
Cdd:COG3524 238 AALRSYLSP----------NSPQV-RQLRRRIA----------ALEKQIAAERARL------TGASGGDSLASLLAEYER 290
|
170 180
....*....|....*....|.
gi 24584706 1821 LENELDGEQRRHADAQKNLRK 1841
Cdd:COG3524 291 LELEREFAEKAYTSALAALEQ 311
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1344-1451 |
5.84e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.54 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1344 EQVEEEAEGKADLQRQLSKANAEAQvwRSKY----------ESDGVARSEELEEAKrklqARLAEAEETIESLNQKC--- 1410
Cdd:PTZ00491 673 ELLEQEARGRLERQKMHDKAKAEEQ--RTKLlelqaesaavESSGQSRAEALAEAE----ARLIEAEAEVEQAELRAkal 746
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24584706 1411 -----IGLEKTKQRLSTEVEDLQ----LEVDRANAIANA-AEKKQKAFDKI 1451
Cdd:PTZ00491 747 rieaeAELEKLRKRQELELEYEQaqneLEIAKAKELADIeATKFERIVEAL 797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1026 |
5.90e-03 |
|
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: 41.58 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 833 QKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTAL---LDSLSGEKGALQDY----QERNA 905
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRREleelREKLA 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 906 KLTAQKNDLENQLRDIQERLTQEEDARNQLFQQK--------KKADQEISGLKKDIEDL-ELNV------QKAEQDKATK 970
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLENKIKELgPVNLaaieeyEELKERYDFL 1005
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 971 DHQIRNLNDEIAHQDELINKLNKEKKmqgetnqktgEELQAAEDKIN-HLNKVKAKL 1026
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREAR----------ERFKDTFDQVNeNFQRVFPKL 1052
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1703-1892 |
5.99e-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: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1703 QELADAHEQLNeVSAQNASISAAKRKLESELQTLHSDLDELlnEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQeklR 1782
Cdd:COG3206 155 NALAEAYLEQN-LELRREEARKALEFLEEQLPELRKELEEA--EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQ---L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1783 KALEQQIKELQVRLDEAEANALKGGKKA--------IQKLEQRVRELENELDGEQRRHADaqknlrkserrvkelsfqse 1854
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALpellqspvIQQLRAQLAELEAELAELSARYTP-------------------- 288
|
170 180 190
....*....|....*....|....*....|....*...
gi 24584706 1855 edrkNHERMQdlvdKLQQKIKTYKRQIEEAEEIAALNL 1892
Cdd:COG3206 289 ----NHPDVI----ALRAQIAALRAQLQQEAQRILASL 318
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1522-1687 |
7.24e-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: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1522 IHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIdRRIQEKEEEFENTRKNHQRALDSMQASLE 1601
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-KRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1602 AEAKGKAEAlrmkkKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQ 1681
Cdd:COG1579 91 YEALQKEIE-----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*.
gi 24584706 1682 NELEES 1687
Cdd:COG1579 166 EELAAK 171
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1772-1893 |
7.39e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1772 QDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSF 1851
Cdd:pfam08614 13 LDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEK 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24584706 1852 QSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAE--------EIAALNLA 1893
Cdd:pfam08614 93 KLREDERRLAALEAERAQLEEKLKDREEELREKRklnqdlqdELVALQLQ 142
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1399-1529 |
7.47e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.48 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1399 AEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDR---ANAIANAAEKKQKAFDKIIgEWKLKVDDLAAELDASQKECRN 1475
Cdd:COG4026 75 AEKFFEELKGMVGHVERMKLPLGHDVEYVDVELVRkeiKNAIIRAGLKSLQNIPEYN-ELREELLELKEKIDEIAKEKEK 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24584706 1476 YSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKAR 1529
Cdd:COG4026 154 LTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKR 207
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
839-994 |
7.85e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 839 LNVSRIEDEIA---------RLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLsgekgaLQDYQERNAkLTA 909
Cdd:PRK11281 234 ARIQRLEHQLQllqeainskRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRL------LKATEKLNT-LTQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 910 QKNDLENQLrdiqERLTQEEdaRN---Q-------------LFQQKKK--ADQEISGLKKDIEDL-----ELN------- 959
Cdd:PRK11281 307 QNLRVKNWL----DRLTQSE--RNikeQisvlkgslllsriLYQQQQAlpSADLIEGLADRIADLrleqfEINqqrdalf 380
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24584706 960 -----VQKAEQD-KATKDHQIRN-LNDEIAHQDELINKLNKE 994
Cdd:PRK11281 381 qpdayIDKLEAGhKSEVTDEVRDaLLQLLDERRELLDQLNKQ 422
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1614-1890 |
8.26e-03 |
|
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: 41.16 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1614 KKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALeeeqrarDDAREQLGISERRANALQNELEESRTLLEQ 1693
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY-------NDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1694 ADRGRRQAEQELADAHEQLNEVSAQNASISAAKRK---LESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRA 1770
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1771 EQDHAQTQEKLRKALEQQIKELQVRL----DEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRV 1846
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEIsdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24584706 1847 KELSFQSEEDRKNHERMQDLVDKLQQKIKTYK--------------RQIEEAEEIAAL 1890
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKqeiknlesqindleSKIQNQEKLNQQ 409
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1557-1793 |
8.50e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1557 VLRAQlELSQVRQEIDRRIQEKEEEFENTRKNHQRAlDSMQASLEAEAKGKAEALRMKKkleadineleialdhankana 1636
Cdd:pfam15709 337 RLRAE-RAEMRRLEVERKRREQEEQRRLQQEQLERA-EKMREELELEQQRRFEEIRLRK--------------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1637 eaqknikryqQQLKDIQTALEEEQRARddaREQLGISERRANALQnelEESRTLLEQADRGRRQAEQELADAHEQlnevs 1716
Cdd:pfam15709 394 ----------QRLEEERQRQEEEERKQ---RLQLQAAQERARQQQ---EEFRRKLQELQRKKQQEEAERAEAEKQ----- 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584706 1717 aqnasisaAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARladeLRAEQDHAQTQEKLRKALEQQIKELQ 1793
Cdd:pfam15709 453 --------RQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKAR----LEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1336-1511 |
9.14e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1336 EHDLDNLREQVEE-------EAEGKADLQRQLSKANAEAqvwrskyeSDGVARSEELEEAKRKLQARLAEAEETIESLNQ 1408
Cdd:PRK09039 52 DSALDRLNSQIAEladllslERQGNQDLQDSVANLRASL--------SAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1409 KCIGLEKTKQRLSTEVEDLQLEVdranaianAAEKKQKAfdkiigewklkvdDLAAELDASQKECRnystelfrlkgaye 1488
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQI--------AALRRQLA-------------ALEAALDASEKRDR-------------- 168
|
170 180
....*....|....*....|....
gi 24584706 1489 EGQEQLEAV-RRENKNLADEVKDL 1511
Cdd:PRK09039 169 ESQAKIADLgRRLNVALAQRVQEL 192
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1783-1889 |
9.53e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584706 1783 KALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHaDAQKNLRKSERRVKELSFQSEEDRKNHER 1862
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARW-EAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100
....*....|....*....|....*..
gi 24584706 1863 MQDLVDKLQQKIKTYKRQIEEAEEIAA 1889
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| |
