|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
575-1305 |
0e+00 |
|
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: 1031.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDShPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKA 814
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNS-FGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 815 VRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAAF-----GLTQPNAPNGGLSPSKSP 889
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATK--AASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFkhhlsGGPQQSTTSSGQESPARS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 890 TSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGQQVGATLADLRHNYLQERL 969
Cdd:cd01386 318 SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 970 QMLFHHTTLVAPRDRYAQELVEIEMDLASEChPGPLISLIDKAPQNHVVRSsqrDLREHDRRGMLWLLDEEAIYPNSNDD 1049
Cdd:cd01386 398 QLLFHERTFVAPLERYKQENVEVDFDLPELS-PGALVALIDQAPQQALVRS---DLRDEDRRGLLWLLDEEALYPGSSDD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1050 TFLERLFSHYGDREH---HSLLRKCAGPRQFVLHHLQGTNPVLYAVDGWVRHSREHPGIRNAVSLLQDSSREeinrlyig 1126
Cdd:cd01386 474 TFLERLFSHYGDKEGgkgHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE-------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1127 sltrgsgamvfcgsfaglegtqslrrvssirrsftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCYLLQHNAGKHT 1206
Cdd:cd01386 546 -----------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDE 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1207 KYTANGspssaagqvSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLAS---------NK 1277
Cdd:cd01386 591 RSTSSP---------AAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKklglnsevaDE 661
|
730 740
....*....|....*....|....*...
gi 116008016 1278 DVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01386 662 RKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
575-1305 |
3.84e-112 |
|
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: 371.92 E-value: 3.84e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKT-EDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLA-LAAGAYNNFINA-----EKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAaLSGSGSSKSSSSassieQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPFISLSQKL--EDRHRAANDFMRTVQAF 805
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSGCdrIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSP 885
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEA---LTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 886 SKSPTSDTghewAWECLEALVIGLYSEALAAVVALINRQIC--TSSHTIASIMLIDTPGFQNPASCG-QQvgatladLRH 962
Cdd:cd00124 318 TKPLTVEQ----AEDARDALAKALYSRLFDWLVNRINAALSptDAAESTSFIGILDIFGFENFEVNSfEQ-------LCI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 963 NYLQERLQMLFHHTTLVAPRDRYAQELVEIEMdlasechpgplISLIDKAPqnhVVrssqrDLREHDRRGMLWLLDEEAI 1042
Cdd:cd00124 387 NYANEKLQQFFNQHVFKLEQEEYEEEGIDWSF-----------IDFPDNQD---CL-----DLIEGKPLGILSLLDEECL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1043 YPNSNDDTFLERLFSHYGDReHHSLLRKCAGPRQFVLHHLQGtnPVLYAVDGWVrhsrehpgIRNavsllQDSSREEINR 1122
Cdd:cd00124 448 FPKGTDATFLEKLYSAHGSH-PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFL--------EKN-----KDTLPPDLVD 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1123 LyigsltrgsgamvfcgsfaglegtqsLRRVSSIRRSfttagvkrnsimlqvkftVDGIIDTLRRTGTHFVHCylLQHNA 1202
Cdd:cd00124 512 L--------------------------LRSGSQFRSQ------------------LDALMDTLNSTQPHFVRC--IKPND 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1203 GKhtkytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLAS----NKD 1278
Cdd:cd00124 546 EK--------KPG-----------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEkasdSKK 606
|
730 740
....*....|....*....|....*..
gi 116008016 1279 VSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd00124 607 AAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
556-1317 |
3.45e-109 |
|
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: 364.94 E-value: 3.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 556 NSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQ 635
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 636 TAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFINA--EKVNALCTILEAFGNTKTCLNSNATRMTQ 713
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA-SVSGSNTEVGSveDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 714 LLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLeniTSEDSHPFISLSQKLE---- 789
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL---KSPEDYRYLNQGGCLTvdgi 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 790 -DrhraANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlGTGSTARTQFANPTAARKASGLLGVNLEDLSS 868
Cdd:smart00242 237 dD----AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEE-GRNDNAASTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 869 AafgLTqpnapngglspskSPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLID 939
Cdd:smart00242 312 A---LT-------------KRKIKTGGEVitkplnveqALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 940 TPGFQNpascgqqvgatladLRH--------NYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDK 1011
Cdd:smart00242 376 IYGFEI--------------FEVnsfeqlciNYANEKLQQFFNQHVFKLEQEEYERE--GIDWTFIDFFDNQDCIDLIEK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1012 APQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSlLRKCAGPRQFVLHHLQGTnpVLYA 1091
Cdd:smart00242 440 KPP-----------------GILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS-KPKKKGRTEFIIKHYAGD--VTYD 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1092 VDGWVRHSREhPGIRNAVSLLQDSSreeiNRLyIGSLtrgsgamvfcgsFAGLEGTQSlrrvSSIRrsFTTAGVK-RNSi 1170
Cdd:smart00242 500 VTGFLEKNKD-TLSDDLIELLQSSK----NPL-IASL------------FPSGVSNAG----SKKR--FQTVGSQfKEQ- 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1171 mLQVkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSeeemvnvPLLRSQLRGSQVLEAARLHR 1250
Cdd:smart00242 555 -LNE------LMDTLNSTNPHFIRC--IKPNEEK------------KPGDFDS-------SLVLHQLRYLGVLENIRIRR 606
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 1251 LGFPESVPLLEFVRRFGLLAGDLASNKDV----SVEQILAVNELDVASYRIGPSQILFRSGVLSELEAKRD 1317
Cdd:smart00242 607 AGFPYRLPFDEFLQRYRVLLPDTWPPWGGdakkACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
563-1305 |
2.10e-99 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 336.56 E-value: 2.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 563 VEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV 642
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 643 ETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAG--AYNNFINAEKV----NAlctILEAFGNTKTCLNSNATRMTQLLS 716
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGsgSAGNVGRLEEQilqsNP---ILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 717 LDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSedshpFISLSQKLEDRHRAAN 796
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKD-----YHYLSQSGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 797 D---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTArtQFANPTAARKASGLLGVNLEDLSSAafgL 873
Cdd:pfam00063 233 DseeFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA--VPDDTENLQKAASLLGIDSTELEKA---L 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 874 TqpnapngglspskSPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGF 943
Cdd:pfam00063 308 C-------------KRRIKTGRETvskpqnveqANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASfIGVLDIYGF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 944 Q----NpaSCGQqvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDKAPqnhvvr 1019
Cdd:pfam00063 375 EifekN--SFEQ--------LCINYVNEKLQQFFNHHMFKLEQEEYVRE--GIEWTFIDFGDNQPCIDLIEKKP------ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1020 ssqrdlrehdrRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLRKcagPRQ-----FVLHHLQGTnpVLYAVDG 1094
Cdd:pfam00063 437 -----------LGILSLLDEECLFPKATDQTFLDKLYSTFSK---HPHFQK---PRLqgethFIIKHYAGD--VEYNVEG 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1095 WVRHSREhPGIRNAVSLLQDSSREEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSlrrvssirrSFTTAGVK-RNSIMLq 1173
Cdd:pfam00063 498 FLEKNKD-PLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPKRTKKK---------RFITVGSQfKESLGE- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1174 vkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSeeemvnvPLLRSQLRGSQVLEAARLHRLGF 1253
Cdd:pfam00063 567 -------LMKTLNSTNPHYIRC--IKPNEKK------------RAGVFDN-------SLVLHQLRCNGVLEGIRIRRAGF 618
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 1254 PESVPLLEFVRRFGLLAGDLASNKDVS----VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:pfam00063 619 PNRITFQEFVQRYRILAPKTWPKWKGDakkgCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
541-2019 |
9.40e-98 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 348.99 E-value: 9.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 541 NGEQLTVDEDDVE--KQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMF 618
Cdd:COG5022 44 DGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 619 RGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA--EKVNALCTILEA 696
Cdd:COG5022 124 SGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSieKQILATNPILEA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 697 FGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSE 776
Cdd:COG5022 204 FGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN--PK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 777 DSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGStarTQFANPTAARKAS 856
Cdd:COG5022 282 DYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGA---AIFSDNSVLDKAC 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 857 GLLGVNLEDLSSAafgLTQpnapngglspsksPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICT 927
Cdd:COG5022 359 YLLGIDPSLFVKW---LVK-------------RQIKTGGEWivvplnleqALAIRDSLAKALYSNLFDWIVDRINKSLDH 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 928 SSHTIASIMLIDTPGFQ----NpascgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLAsECHPG 1003
Cdd:COG5022 423 SAAASNFIGVLDIYGFEifekN----------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE--GIEWSFI-DYFDN 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1004 -PLISLIDKApqnhvvrssqrdlrehDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYgdREHHSLLRKCAGPRQ--FVLH 1080
Cdd:COG5022 490 qPCIDLIEKK----------------NPLGILSLLDEECVMPHATDESFTSKLAQRL--NKNSNPKFKKSRFRDnkFVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1081 HLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREEINRLyigsltrgsgamvfcgsFAGLEGTQSLRRvssirrsF 1160
Cdd:COG5022 552 HYAGD--VEYDVEGFLDKNKD-PLNDDLLELLKASTNEFVSTL-----------------FDDEENIESKGR-------F 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1161 TTAGVKRNSIMLQvkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssaagqvssEEEMVNVPLLRSQLRGS 1240
Cdd:COG5022 605 PTLGSRFKESLNS-------LMSTLNSTQPHYIRC--IKPNEEK-------------------SPWTFDNQMVLSQLRCC 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1241 QVLEAARLHRLGFPESVPLLEFVRRFGLL------AGDLASNKDV--SVEQILAVNELDVASYRIGPSQILFRSGVLSEL 1312
Cdd:COG5022 657 GVLETIRISRAGFPSRWTFDEFVQRYRILspskswTGEYTWKEDTknAVKSILEELVIDSSKYQIGNTKVFFKAGVLAAL 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1313 EAKRDVLLSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTAN 1392
Cdd:COG5022 737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYL 816
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1393 EELLMLRAKLeKIECDRSEvkAENQKLEAKlSELTVDLAEERSTAHIATERLE-----AETAERLKLEK----ELGDQTN 1463
Cdd:COG5022 817 ACIIKLQKTI-KREKKLRE--TEEVEFSLK-AEVLIQKFGRSLKAKKRFSLLKketiyLQSAQRVELAErqlqELKIDVK 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLngiSEDEDAENEdgvgggvykLKYERVAReLEFTKRrlhtqhEHDLEQLVALKKHLe 1543
Cdd:COG5022 893 SISSLKLVNLELESEIIELKKSL---SSDLIENLE---------FKTELIAR-LKKLLN------NIDLEEGPSIEYVK- 952
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 mklsdaYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFdAECQSLQDAV-RQERQAKERYGRE 1622
Cdd:COG5022 953 ------LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALqESTKQLKELPVEV 1025
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAEKFTLEQTLADTRL----DLEFK-EEKLASLQRELEEM------TFGGGTEEEFAQLRRSK----NETERRAKE 1687
Cdd:COG5022 1026 AELQSASKIISSESTELSILkplqKLKGLlLLENNQLQARYKALklrrenSLLDDKQLYQLESTENLlktiNVKDLEVTN 1105
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1688 QEEELDEMAGQIQLLEQAKLRLEmtletmrkearresQQRDEELEEVRGN-GYKKIKALECQLETEHEERTLLLREKHEL 1766
Cdd:COG5022 1106 RNLVKPANVLQFIVAQMIKLNLL--------------QEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWEANLEALPSP 1171
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1767 ERRLSSMEDRDRvdrdaEEALnqklrrdlrkYKALLKDAQTQLERLKADTpgKTLIRQLRNqledaESARSLAMKARQTA 1846
Cdd:COG5022 1172 PPFAALSEKRLY-----QSAL----------YDEKSKLSSSEVNDLKNEL--IALFSKIFS-----GWPRGDKLKKLISE 1229
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEqINVSEAE---FKLNEM 1923
Cdd:COG5022 1230 GWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQY-INVGLFNalrTKASSL 1308
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1924 EAERNNLKEQVAEL------QHRLDNV-ENLgdPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKL-- 1994
Cdd:COG5022 1309 RWKSATEVNYNSEElddwcrEFEISDVdEEL--EELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPAdk 1386
|
1530 1540
....*....|....*....|....*
gi 116008016 1995 QNEVTQSKMREMQAQDVIKKSQKSL 2019
Cdd:COG5022 1387 ENNLPKEILKKIEALLIKQELQLSL 1411
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
575-1305 |
4.02e-91 |
|
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: 311.71 E-value: 4.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNfiNAEKVNALCT----------ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQ 724
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKK--KKESGKKKGTledqilqanpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 725 IASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQK----LEDrhraANDFMR 800
Cdd:cd01377 159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTG--DPSYYFFLSQGELtidgVDD----AEEFKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 801 TVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARtqFANPTAARKASGLLGVNLEDLSSAafgLTQPNapn 880
Cdd:cd01377 233 TDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAE--LDGTEEADKAAHLLGVNSSDLLKA---LLKPR--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 881 gglspSKsptsdTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----Npa 947
Cdd:cd01377 305 -----IK-----VGREWvtkgqnkeqVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 948 SCGQqvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIE-------MDLAsechpgPLISLIDKAPQnhvvrs 1020
Cdd:cd01377 373 SFEQ--------LCINYTNEKLQQFFNHHMFVLEQEEYKKE--GIEwtfidfgLDLQ------PTIDLIEKPNM------ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1021 sqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFS-HYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHS 1099
Cdd:cd01377 431 -----------GILSILDEECVFPKATDKTFVEKLYSnHLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWLEKN 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1100 REhPGIRNAVSLLQDSSREEINRL---YIGSLTRGSGAMVFCGSFaglegtqslRRVSSI-RRSFttagvkrNSIMlqvk 1175
Cdd:cd01377 498 KD-PLNENVVALLKKSSDPLVASLfkdYEESGGGGGKKKKKGGSF---------RTVSQLhKEQL-------NKLM---- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1176 ftvdgiiDTLRRTGTHFVHCYLLQHN--AGKhtkytangspssaagqvsseeemVNVPLLRSQLRGSQVLEAARLHRLGF 1253
Cdd:cd01377 557 -------TTLRSTHPHFVRCIIPNEEkkPGK-----------------------IDAPLVLHQLRCNGVLEGIRICRKGF 606
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 1254 PESVPLLEFVRRFGLLAGDLASNKDVS----VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01377 607 PNRIIFAEFKQRYSILAPNAIPKGFDDgkaaCEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
575-1305 |
3.50e-83 |
|
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: 289.22 E-value: 3.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPGELERQLLQanpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFISLSQKLEDRHRAANDFMRTVQAFET 807
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGF---NNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 808 LNIDAKAVRGIWSILAAIYHLGiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSK 887
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFG--NISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA---ILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 888 SPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ----NpascgqqvgaTLADLRH 962
Cdd:cd14920 313 AQTK----EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEifelN----------SFEQLCI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 963 NYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEchpgPLISLIDKaPQNhvvrssqrdlrehdRRGMLWLLDE 1039
Cdd:cd14920 379 NYTNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGLDLQ----PCIDLIER-PAN--------------PPGVLALLDE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1040 EAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREE 1119
Cdd:cd14920 440 ECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGK--VDYKADEWLMKNMD-PLNDNVATLLHQSSDRF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1120 INRLYigsltrgsgamvfcgsfAGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLQV-----KFTVDGIIDTLRRTGTHFVH 1194
Cdd:cd14920 517 VAELW-----------------KDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTvgqlyKESLTKLMATLRNTNPNFVR 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1195 CYLLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD-- 1272
Cdd:cd14920 580 CIIPNH--------------EKRAGKLDPH-------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNai 638
|
730 740 750
....*....|....*....|....*....|....*.
gi 116008016 1273 ---LASNKDVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14920 639 pkgFMDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
575-1305 |
6.28e-81 |
|
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: 282.64 E-value: 6.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAA-------------GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLD 718
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkgsgavphpAVNPAVLIGELEQQLLQanpILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 719 FDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedSHPFISLSQKLEDRHRAANDF 798
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVK---SYAFLSNGSLPVPGVDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 799 MRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTArtQFANPTAARKASGLLGVNLEDLSSAafgLTQPNA 878
Cdd:cd14911 238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQA--TLPDNTVAQKIAHLLGLSVTDMTRA---FLTPRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 879 PNGGLSPSKSPTSDTgHEWAwecLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ----Npascgqqv 953
Cdd:cd14911 313 KVGRDFVTKAQTKEQ-VEFA---VEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFEifelN-------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 954 gaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKApqnhvvrssqrdlrehdrRG 1032
Cdd:cd14911 381 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKfIDFGLDLQ--PTIDLIDKP------------------GG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1033 MLWLLDEEAIYPNSNDDTFLERLFSHYGdrEHHSLLRK-CAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSL 1111
Cdd:cd14911 439 IMALLDEECWFPKATDKTFVDKLVSAHS--MHPKFMKTdFRGVADFAIVHYAGR--VDYSAAKWLMKNMD-PLNENIVSL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1112 LQDSSREEINRLYIGSLTRGSGAmvfcgsfAGLEGTQSLRRvssirrsfTTAGVKRNSIMLqVKFTVDGIIDTLRRTGTH 1191
Cdd:cd14911 514 LQGSQDPFVVNIWKDAEIVGMAQ-------QALTDTQFGAR--------TRKGMFRTVSHL-YKEQLAKLMDTLRNTNPN 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1192 FVHCYLLQHN--AGKhtkytangspssaagqvsseeemVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL 1269
Cdd:cd14911 578 FVRCIIPNHEkrAGK-----------------------IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 116008016 1270 AGDLAS----NKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14911 635 TPNVIPkgfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
575-1305 |
5.23e-78 |
|
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: 273.83 E-value: 5.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNfiNAEKVNALCT-------------ILEAFGNTKTCLNSNATRMTQLLSLDFDQ 721
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKT--KKDQSSIALShgelekqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 722 TGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedSHPFISLSQKLEDRHRAANDFMRT 801
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS---KYRFLSNGNVTIPGQQDKELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 802 VQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNG 881
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKK--ERNSDQASMPDDTAAQKVCHLLGMNVTDFTRA---ILSPRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 882 GLSPSKSPTsdtgHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ----NpascgqqvgaT 956
Cdd:cd14932 311 RDYVQKAQT----QEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFEifelN----------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 957 LADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKApqnhvvrssqrdlreHDRRGMLW 1035
Cdd:cd14932 377 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSfIDFGLDLQ--PCIELIEKP---------------NGPPGILA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1036 LLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDS 1115
Cdd:cd14932 440 LLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDADFCIIHYAGK--VDYKANEWLMKNMD-PLNENVATLLNQS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1116 SREeinrlYIGSLTRGSGAMVFCGSFAGLEgtqslrrvSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHC 1195
Cdd:cd14932 517 TDK-----FVSELWKDVDRIVGLDKVAGMG--------ESLHGAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRC 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1196 YLLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD--- 1272
Cdd:cd14932 584 IIPNH--------------EKKAGKLAHH-------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNaip 642
|
730 740 750
....*....|....*....|....*....|....*
gi 116008016 1273 --LASNKDVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14932 643 kgFMDGKQACVLMVKAL-ELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
575-1305 |
8.50e-75 |
|
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: 264.57 E-value: 8.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSED--SHPFISLSQKLEDRHraandFMRTVQAF 805
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTflSNGFVPIPAAQDDEM-----FQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSP 885
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLMGINVTDFTRS---ILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 886 SKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIM-LIDTPGFQNPAScgqqvgATLADLRHNY 964
Cdd:cd14921 311 QKAQTK----EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEV------NSFEQLCINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 965 LQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDkapqnhvvrssqrdlREHDRRGMLWLLDEEAIY 1043
Cdd:cd14921 381 TNEKLQQLFNHTMFILEQEEYQREGIEWNfIDFGLDLQ--PCIELIE---------------RPNNPPGVLALLDEECWF 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1044 PNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREeinrl 1123
Cdd:cd14921 444 PKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSIIHYAGK--VDYNASAWLTKNMD-PLNDNVTSLLNASSDK----- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1124 YIGSLTRGSGAMVfcgsfaGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLqVKFTVDGIIDTLRRTGTHFVHCYLLQHnag 1203
Cdd:cd14921 516 FVADLWKDVDRIV------GLDQMAKMTESSLPSASKTKKGMFRTVGQL-YKEQLGKLMTTLRNTTPNFVRCIIPNH--- 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1204 khtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD-----LASNKD 1278
Cdd:cd14921 586 -----------EKRSGKLDAF-------LVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANaipkgFMDGKQ 647
|
730 740
....*....|....*....|....*..
gi 116008016 1279 VSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14921 648 ACILMIKAL-ELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
576-1305 |
2.80e-73 |
|
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: 259.17 E-value: 2.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRgcKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLAlAAGAYNNFINAEKVNALCtILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLP 735
Cdd:cd01383 80 SGAGKTETAKIAMQYLA-ALGGGSSGIENEILQTNP-ILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 736 ERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhleNITSEDSHPFISLSQKLE-DRHRAANDFMRTVQAFETLNIDAKA 814
Cdd:cd01383 158 EKSRVVQLANGERSYHIFYQLCAGASPALREKL---NLKSASEYKYLNQSNCLTiDGVDDAKKFHELKEALDTVGISKED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 815 VRGIWSILAAIYHLGiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTsdtg 894
Cdd:cd01383 235 QEHIFQMLAAVLWLG--NISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLA---LSTRKIQAGGDKIVKKLT---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 895 HEWAWECLEALVIGLYSEALAAVVALINRQICTSSH-TIASIMLIDTPGFQ----NpascgqqvgaTLADLRHNYLQERL 969
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFEsfqkN----------SFEQLCINYANERL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 970 QMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNS 1046
Cdd:cd01383 376 QQHFNRHLFKLEQEEYELDGIDwtkVDFEDNQEC-----LDLIEKKPL-----------------GLISLLDEESNFPKA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1047 NDDTFLERLFSH-------YGDREhhsllrkcagpRQFVLHHLQGTnpVLYAVDGWVRHSRE--HPGIrnaVSLLQDSSr 1117
Cdd:cd01383 434 TDLTFANKLKQHlksnscfKGERG-----------GAFTIRHYAGE--VTYDTSGFLEKNRDllHSDL---IQLLSSCS- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1118 eeinrlyiGSLTRgsgamvfcgSFAGLEGTQSLRRVSSIRRSftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCyl 1197
Cdd:cd01383 497 --------CQLPQ---------LFASKMLDASRKALPLTKAS--GSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRC-- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1198 lqhnagkhTKYTANGSPSsaagqvSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNK 1277
Cdd:cd01383 556 --------IKPNNKQLPG------VFDQDLV-----LQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
730 740 750
....*....|....*....|....*....|....
gi 116008016 1278 D------VSVEQILAVNEldvASYRIGPSQILFR 1305
Cdd:cd01383 617 QdplstsVAILQQFNILP---EMYQVGYTKLFFR 647
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
575-1305 |
3.53e-73 |
|
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: 259.64 E-value: 3.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALC----TILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASL 730
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqanPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 731 QVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNI 810
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE---PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 811 DAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSaafGLTQPNAPNGGLSPSKSPT 890
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTR---GILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 891 SdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQnpascgqqvgatLADLRH------N 963
Cdd:cd14919 313 K----EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------------IFDLNSfeqlciN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 964 YLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKAPqnhvvrssqrdlrehDRRGMLWLLDEEAI 1042
Cdd:cd14919 377 YTNEKLQQLFNHTMFILEQEEYQREGIEWNfIDFGLDLQ--PCIDLIEKPA---------------GPPGILALLDEECW 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1043 YPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREeinr 1122
Cdd:cd14919 440 FPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGK--VDYKADEWLMKNMD-PLNDNIATLLHQSSDK---- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1123 lYIGSLTRGSGAMVFCGSFAGLEGTQSLRRVSSIRRSFTTAGvkrnsimLQVKFTVDGIIDTLRRTGTHFVHCYLLQHna 1202
Cdd:cd14919 513 -FVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVG-------QLYKEQLAKLMATLRNTNPNFVRCIIPNH-- 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1203 gkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD-----LASNK 1277
Cdd:cd14919 583 ------------EKKAGKLDPH-------LVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNsipkgFMDGK 643
|
730 740
....*....|....*....|....*...
gi 116008016 1278 DVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14919 644 QACVLMIKAL-ELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
575-1305 |
1.30e-70 |
|
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: 251.91 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAY------NNFINA-----EKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHktkkdqNSLALShgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFISLSQKLEDRHRAANDFMRTVQ 803
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENY---NNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 804 AFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGL 883
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKK--ERHTDQASMPDNTAAQKVCHLMGMNVTDFTRA---ILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 884 SPSKSPTsdtgHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQNPAScgqqvgATLADLRH 962
Cdd:cd15896 313 YVQKAQT----QEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFEIFEL------NSFEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 963 NYLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKAPQNhvvrssqrdlrehdrRGMLWLLDEEA 1041
Cdd:cd15896 383 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSfIDFGLDLQ--PCIDLIEKPASP---------------PGILALLDEEC 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1042 IYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREEIN 1121
Cdd:cd15896 446 WFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEADFCIIHYAGK--VDYKADEWLMKNMD-PLNDNVATLLNQSTDKFVS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1122 RLY-----IGSLTRGSGAMVFCGSFAGLEGTqslrrvssirrsFTTAGvkrnsimLQVKFTVDGIIDTLRRTGTHFVHCY 1196
Cdd:cd15896 523 ELWkdvdrIVGLDKVSGMSEMPGAFKTRKGM------------FRTVG-------QLYKEQLSKLMATLRNTNPNFVRCI 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1197 LLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD---- 1272
Cdd:cd15896 584 IPNH--------------EKKAGKLDPH-------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNaipk 642
|
730 740 750
....*....|....*....|....*....|....
gi 116008016 1273 -LASNKDVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd15896 643 gFMDGKQACVLMIKSL-ELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
575-1305 |
8.67e-66 |
|
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: 237.69 E-value: 8.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVAsspkGRKEPGVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSE---DSHPFISLSQKLEdrhraanDFMRTVQA 804
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYrflTNGPSSSPGQERE-------LFQETLES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 805 FETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLS 884
Cdd:cd14930 234 LRVLGFSHEEITSMLRMVSAVLQFGNIVLKR--ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRA---LLTPRIKVGRDY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 885 PSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIM-LIDTPGFQNpascgQQVGaTLADLRHN 963
Cdd:cd14930 309 VQKAQTK----EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEI-----FQLN-SFEQLCIN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 964 YLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLAsechpgPLISLIDkapqnhvvrssqrdlREHDRRGMLWLLD 1038
Cdd:cd14930 379 YTNEKLQQLFNHTMFVLEQEEYQREgipwtFLDFGLDLQ------PCIDLIE---------------RPANPPGLLALLD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSRE 1118
Cdd:cd14930 438 EECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGK--VDYKANEWLMKNMD-PLNDNVAALLHQSTDR 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1119 EINRLYigsltrgsgamvfcgsfAGLEGTQSLRRVSSIRRSfTTAGVKRNSIMLQV----KFTVDGIIDTLRRTGTHFVH 1194
Cdd:cd14930 515 LTAEIW-----------------KDVEGIVGLEQVSSLGDG-PPGGRPRRGMFRTVgqlyKESLSRLMATLSNTNPSFVR 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1195 CYLLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLA 1274
Cdd:cd14930 577 CIVPNH--------------EKRAGKLEPR-------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 635
|
730 740 750
....*....|....*....|....*....|....*
gi 116008016 1275 S----NKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14930 636 PkgfmDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
575-1305 |
2.31e-63 |
|
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: 229.66 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFinAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNGV--EQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 735 PERQRAGRRLGHEHSFHIMTRLLAGAAGllqkeLHLENITSEDSHPFISLSQKLEDRH-RAANDFMRTVQAFETLNIDAK 813
Cdd:cd14872 159 LEKSRVVYQIKGERNFHIFYQLLASPDP-----ASRGGWGSSAAYGYLSLSGCIEVEGvDDVADFEEVVLAMEQLGFDDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 814 AVRGIWSILAAIYHLGIAGVTKLGTGSTARTQ-FANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTSD 892
Cdd:cd14872 234 DINNVMSLIAAILKLGNIEFASGGGKSLVSGStVANRDVLKEVATLLGVDAATLEEA---LTSRLMEIKGCDPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 893 tghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ--NPASCGQqvgatladLRHNYLQERL 969
Cdd:cd14872 311 ---AQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifEKNSFEQ--------LCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 970 QMLFHHTTLVAPRDRYAQELVEIEmdlasecHpgplISLIDKAPqnhVVrssqrDLREHDRRGMLWLLDEEAIYPNSNDD 1049
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFE-------H----IDFIDNQP---VL-----DLIEKKQPGLMLALDDQVKIPKGSDA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1050 TFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRhsrehpgiRNAVSLLQDssreeinrLYIgsLT 1129
Cdd:cd14872 441 TFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLE--------KNKDTLQKD--------LYV--LL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1130 RGSGAMVFCGSFAGLEGTQSLRRVssirrsfTTAGvkrnsimlQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHtkyt 1209
Cdd:cd14872 501 SSSKNKLIAVLFPPSEGDQKTSKV-------TLGG--------QFRKQLSALMTALNATEPHYIRC--VKPNQEKR---- 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1210 angsPSSAAGQVSSEeemvnvpllrsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL----AGDLASNKDVSVEQIL 1285
Cdd:cd14872 560 ----ARLFDGFMSLE-----------QLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvktiAKRVGPDDRQRCDLLL 624
|
730 740
....*....|....*....|
gi 116008016 1286 AVNELDVASYRIGPSQILFR 1305
Cdd:cd14872 625 KSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
576-1305 |
2.35e-63 |
|
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: 230.32 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLALAAgAYNNFINAEKVNALCT----------ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIA-ATGDLAKKKDSKMKGTledqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLI--TTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPNGG 882
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKTAYLMGLNSSDLLKA---LCFPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 883 LSPSKSPTSDTGHewawECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14913 311 EYVTKGQTVDQVH----HAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEifeyN----------SLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASeChpgplISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14913 377 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLAA-C-----IELIEKP------------------MGI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14913 433 FSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAEahFSLIHYAGT--VDYSVSGWLEKNKD-PLNETVVG 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYigsltrgsgamvfcGSFAGLEGTQSLRRVSSIR-RSF-TTAGVKRNSImlqvkftvDGIIDTLRRT 1188
Cdd:cd14913 510 LYQKSSNRLLAHLY--------------ATFATADADSGKKKVAKKKgSSFqTVSALFRENL--------NKLMSNLRTT 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCYLlqhnagkhtkytANGSPSSAAgqvsseeemVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd14913 568 HPHFVRCII------------PNETKTPGA---------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 116008016 1269 L------AGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14913 627 LnasaipEGQFIDSKK-ACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
575-1305 |
3.64e-60 |
|
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: 220.62 E-value: 3.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNF----INAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASL 730
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 731 QVLLPERQRAGRRLGHEHSFHIMTRLLAGaagllQKELHLENITSEDSHPFISLS------QKLEDrhraANDFMRTVQA 804
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSG-----KKELRDLLLVSANPSDFHFCScgavavESLDD----AEELLATEQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 805 FETLNIDAKAVRGIWSILAAIYHLgiaGVTKLGTGSTARTQFANPTA-ARKASGLLGVNLEDLSSaafGLTQPNAPNGGL 883
Cdd:cd14929 232 MDILGFLPDEKYGCYKLTGAIMHF---GNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVK---GLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 884 SPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLAD 959
Cdd:cd14929 306 YVTRSQNI----EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEildyN----------SLEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 960 LRHNYLQERLQMLFHHTTLVAPRDRYAQELVE-IEMDLASECHpgPLISLIDKApqnhvvrssqrdlrehdrRGMLWLLD 1038
Cdd:cd14929 372 LCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDwVSIDFGLDLQ--ACIDLIEKP------------------MGIFSILE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLF-SHYGDREHhslLRKCAGPRQ-----FVLHHLQGTNPvlYAVDGWVRHSRehpGIRN--AVS 1110
Cdd:cd14929 432 EECMFPKATDLTFKTKLFdNHFGKSVH---FQKPKPDKKkfeahFELVHYAGVVP--YNISGWLEKNK---DLLNetVVA 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYIGSLTRGSgAMVFcGSFAGLEGTqSLRRVSSIRrsfttagvkrnsimlqvKFTVDGIIDTLRRTGT 1190
Cdd:cd14929 504 VFQKSSNRLLASLFENYISTDS-AIQF-GEKKRKKGA-SFQTVASLH-----------------KENLNKLMTNLKSTAP 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1191 HFVHCYllqhNAGKhtkytaNGSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL- 1269
Cdd:cd14929 564 HFVRCI----NPNV------NKIPG-----------VLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILn 622
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 116008016 1270 -----AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14929 623 prtfpKSKFVSSRKAA-EELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
575-1277 |
1.21e-59 |
|
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: 218.89 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMF------RGCKTEDMPPHVYSLAQTAYRSLVETRR-- 646
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 647 --DQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA-------EKVNALCTILEAFGNTKTCLNSNATRMTQLLSL 717
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNAterenvrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 718 DFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAgllQKELHLENITSEDSHPFISLSQKLeDRHRAAND 797
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGAS---SDELHALGLTHVEEYKYLNSSQCY-DRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 798 ---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTarTQFANPTAARKASGLLGVNLEDLSSaafGL 873
Cdd:cd14901 237 svqYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGnLCFVKKDGEGGT--FSMSSLANVRAACDLLGLDMDVLEK---TL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 874 TQPNAPNGG------LSPSKSPTSDtghewaweclEALVIGLYSEALAAVVALINRQICTSSHTIAS--IMLIDTPGFQN 945
Cdd:cd14901 312 CTREIRAGGeyitmpLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAYSESTGASrfIGIVDIFGFEI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 946 PAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVeiemdlasechPGPLISLidkaPQNHVVRSsqrdL 1025
Cdd:cd14901 382 FAT------NSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAI-----------PWTFVEY----PNNDACVA----M 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1026 REHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREHPGi 1105
Cdd:cd14901 437 FEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGA--VCYATDGFCDKNKDHVH- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1106 RNAVSLLQDSSREeinrlYIGSltrgsgamvfcgsfaglegtqslrrvssirrsfttagvkrnSIMLQVKFTVDGIIDTL 1185
Cdd:cd14901 514 SEALALLRTSSNA-----FLSS-----------------------------------------TVVAKFKVQLSSLLEVL 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1186 RRTGTHFVHCYllqhnagkhtkytangSPSSAAgqvsSEEEMvNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRR 1265
Cdd:cd14901 548 NATEPHFIRCI----------------KPNDVL----SPSEF-DAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
730
....*....|..
gi 116008016 1266 FGLLAGDLASNK 1277
Cdd:cd14901 607 YSCLAPDGASDT 618
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
576-1305 |
2.79e-57 |
|
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: 212.28 E-value: 2.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLA------------LAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14912 82 SGAGKTVNTKRVIQYFAtiavtgekkkeeITSGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQ 803
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLI--TTNPYDYPFVSQGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 804 AFETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPN 880
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREEQAEPDGtevADKAAYLQSLNSADLLKA---LCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 881 GGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaT 956
Cdd:cd14912 311 GNEYVTKGQTV----EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEifdfN----------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 957 LADLRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASechpgpLISLIDKApqnhvvrssqrdlrehdrR 1031
Cdd:cd14912 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLAA------CIELIEKP------------------M 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1032 GMLWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNA 1108
Cdd:cd14912 433 GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKAEahFSLIHYAGV--VDYNITGWLDKNKD-PLNETV 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSSREEINRLYIGSLT-RGSGAmvfcGSFA---GLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDT 1184
Cdd:cd14912 510 VGLYQKSAMKTLAYLFSGAQTaEGASA----GGGAkkgGKKKGSSFQTVSALFRE-----------------NLNKLMTN 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1185 LRRTGTHFVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVR 1264
Cdd:cd14912 569 LRSTHPHFVRCII----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILYADFKQ 627
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 116008016 1265 RFGLL------AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14912 628 RYKVLnasaipEGQFIDSKKAS-EKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
575-1305 |
1.74e-56 |
|
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: 210.20 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCT-------------ILEAFGNTKTCLNSNATRMTQLLSLDFDQ 721
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 722 TGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhLENITSEDSHpFISLSQKLEDRHRAANDFMRT 801
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LVSMNPYDYH-FCSQGVTTVDNMDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 802 VQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQfaNPTAARKASGLLGVNLEDLSSaafGLTQPNAPNG 881
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAD--GTESADKAAYLMGVSSADLLK---GLLHPRVKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 882 GLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTL 957
Cdd:cd14927 314 NEYVTKGQSV----EQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEifefN----------SF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 958 ADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEchpgPLISLIDKApqnhvvrssqrdlrehdrRGML 1034
Cdd:cd14927 380 EQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEwvfIDFGLDLQ----ACIDLIEKP------------------LGIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1035 WLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLH----HLQGTNPvlYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14927 438 SILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHfevvHYAGVVP--YNIVGWLDKNKD-PLNETVVA 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRL---YIGSLTRGSGAmvfcgsfaglEGTQSLRRVSSirrSFTTAGvkrnsimlQV-KFTVDGIIDTLR 1186
Cdd:cd14927 515 IFQKSQNKLLATLyenYVGSDSTEDPK----------SGVKEKRKKAA---SFQTVS--------QLhKENLNKLMTNLR 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1187 RTGTHFVHCYLLQHNAgkhtkytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRF 1266
Cdd:cd14927 574 ATQPHFVRCIIPNETK----------TPG-----------VMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 116008016 1267 GLL-----AGDLASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14927 633 RILnpsaiPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
576-1305 |
3.75e-56 |
|
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: 208.82 E-value: 3.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLA------------LAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14910 82 SGAGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQ 803
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLI--TTNPYDYAFVSQGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 804 AFETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPN 880
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAAYLQNLNSADLLKA---LCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 881 GGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaT 956
Cdd:cd14910 311 GNEYVTKGQTV----QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 957 LADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdlrehdrR 1031
Cdd:cd14910 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLAA------CIELIEKP------------------M 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1032 GMLWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNA 1108
Cdd:cd14910 433 GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKGKVEahFSLIHYAGT--VDYNIAGWLDKNKD-PLNETV 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSSREEINRLYIGSltRGSGAMVFCGSFAGLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDTLRRT 1188
Cdd:cd14910 510 VGLYQKSSMKTLALLFSGA--AAAEAEEGGGKKGGKKKGSSFQTVSALFRE-----------------NLNKLMTNLRST 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd14910 571 HPHFVRCII----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 116008016 1269 L------AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14910 630 LnasaipEGQFIDSKKAS-EKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
576-1305 |
3.98e-56 |
|
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: 208.77 E-value: 3.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCT----------ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTledqiiqanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEniTSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIS--TNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSaafGLTQPNAPNGg 882
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAGYLMGLNSAEMLK---GLCCPRVKVG- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 883 lspSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14923 311 ---NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLAA------CIELIEKP------------------MGI 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14923 434 FSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKAEahFSLVHYAGT--VDYNIAGWLDKNKD-PLNETVVG 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYigsltrgsgamvfcGSFAGLEGTQSlrrvSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGT 1190
Cdd:cd14923 511 LYQKSSLKLLSFLF--------------SNYAGAEAGDS----GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHP 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1191 HFVHCYLlqhnaGKHTKytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL- 1269
Cdd:cd14923 573 HFVRCLI-----PNETK-----TPG-----------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILn 631
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 116008016 1270 -----AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14923 632 asaipEGQFIDSKNAS-EKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
575-1305 |
6.33e-56 |
|
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: 207.96 E-value: 6.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINA-----EKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASAS 729
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGkgsleDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 730 LQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLN 809
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 810 IDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFAN---PTAARKASGLLGVNLEDLSSaafGLTQPNAPNGGLSPS 886
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFG-----NMKFKQKPREEQAEvdtTEVADKVAHLMGLNSGELQK---GITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 887 KSPTSDTGHewawECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLADLRH 962
Cdd:cd14934 311 KGQNMEQCN----NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEifefN----------SFEQLCI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 963 NYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASeChpgplISLIDKApqnhvvrssqrdlrehdrRGMLWLL 1037
Cdd:cd14934 377 NFTNEKLQQFFNHHMFVLEQEEYKREgiewvFIDFGLDLQA-C-----IDLLEKP------------------MGIFSIL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1038 DEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCA---GPR-QFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQ 1113
Cdd:cd14934 433 EEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGkgkGPEaHFELVHYAGT--VGYNITGWLEKNKD-PLNETVVGLFQ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1114 DSSreeinrLYIGSLtrgsgamvFCGSFAGLEGTQSLRRVSSIrrsFTTAGVKRNSImlqvkftvDGIIDTLRRTGTHFV 1193
Cdd:cd14934 510 KSS------LGLLAL--------LFKEEEAPAGSKKQKRGSSF---MTVSNFYREQL--------NKLMTTLHSTAPHFV 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1194 HCYLlqhnagkHTKYTANGspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDL 1273
Cdd:cd14934 565 RCIV-------PNEFKQSG--------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
|
730 740 750
....*....|....*....|....*....|....*..
gi 116008016 1274 -----ASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14934 624 ipqgfVDNKKAS-ELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
576-1305 |
6.66e-56 |
|
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: 208.43 E-value: 6.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLALAA------------GAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhlenITSEDSHPFISLSQ------KLEDRHraanD 797
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEML----LITTNPYDFAFVSQgeitvpSIDDQE----E 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 798 FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLT 874
Cdd:cd14915 233 LMATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAAYLTSLNSADLLKA---LC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 875 QPNAPNGGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----Npascg 950
Cdd:cd14915 305 YPRVKVGNEYVTKGQTV----QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 951 qqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdl 1025
Cdd:cd14915 376 -----SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLAA------CIELIEKP------------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1026 rehdrRGMLWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREh 1102
Cdd:cd14915 432 -----MGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKGKAEahFSLVHYAGT--VDYNIAGWLDKNKD- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1103 PGIRNAVSLLQDSSREEINRLYIG---SLTRGSGamvfcGSFAGLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVD 1179
Cdd:cd14915 504 PLNETVVGLYQKSGMKTLAFLFSGgqtAEAEGGG-----GKKGGKKKGSSFQTVSALFRE-----------------NLN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1180 GIIDTLRRTGTHFVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPL 1259
Cdd:cd14915 562 KLMTNLRSTHPHFVRCLI----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILY 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 116008016 1260 LEFVRRFGLL------AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14915 621 ADFKQRYKVLnasaipEGQFIDSKKAS-EKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
581-1305 |
4.28e-55 |
|
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: 205.64 E-value: 4.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 581 LRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGK 660
Cdd:cd14883 7 LKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 661 STSFKHALNYLAlAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRA 740
Cdd:cd14883 87 TETTKLILQYLC-AVTNNHSWVEQQILEA-NTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 741 GRRLGHEHSFHIMTRLLAGAAGL--LQKELHLENItsEDSHpFISLSQ--KLEDRHRAaNDFMRTVQAFETLNIDAKAVR 816
Cdd:cd14883 165 TFQAPGERNYHVFYQLLAGAKHSkeLKEKLKLGEP--EDYH-YLNQSGciRIDNINDK-KDFDHLRLAMNVLGIPEEMQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 817 GIWSILAAIYHLGIAGVTKLgTGSTARTQFANPTAARKASGLLGVNLEDLSSAaFGLTQPNAP-NGGLSPSKsptsdtgH 895
Cdd:cd14883 241 GIFSVLSAILHLGNLTFEDI-DGETGALTVEDKEILKIVAKLLGVDPDKLKKA-LTIRQINVRgNVTEIPLK-------V 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 896 EWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHH 975
Cdd:cd14883 312 QEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKV------NSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 976 TTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPqnhvvrssqrdlrehdrRGMLWLLDEEAIYPNSNDDTFL 1052
Cdd:cd14883 386 YVFKLEQEEYEKEGINwshIVFTDNQEC-----LDLIEKPP-----------------LGILKLLDEECRFPKGTDLTYL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1053 ERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSRE-HPgiRNAVSLLQDSSREEINRLYigsltrg 1131
Cdd:cd14883 444 EKLHAAHEKHPYYEKPDRRRWKTEFGVKHYAGE--VTYTVQGFLDKNKDtQQ--DDLFDLMSRSKNKFVKELF------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1132 sgamVFCGSFAGLEGTQSLRRVSSIRRSfttaGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKhtkytan 1211
Cdd:cd14883 513 ----TYPDLLALTGLSISLGGDTTSRGT----SKGKPTVGDTFKHQLQSLVDVLSATQPWYVRC--IKPNSLK------- 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1212 gspssaagqvssEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLA-----GDLASNKDvSVEQILA 1286
Cdd:cd14883 576 ------------EPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDprarsADHKETCG-AVRALMG 642
|
730
....*....|....*....
gi 116008016 1287 VNELDVASYRIGPSQILFR 1305
Cdd:cd14883 643 LGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
577-1305 |
7.32e-55 |
|
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: 204.97 E-value: 7.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 577 VLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRS 656
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 657 GSGKSTSFKHALNYLALAA----------GAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIA 726
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 727 SASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFE 806
Cdd:cd14918 162 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLI--TTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 807 TLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPNGGL 883
Cdd:cd14918 240 ILGFTPEEKVSIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAAYLQSLNSADLLKA---LCYPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 884 SPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLAD 959
Cdd:cd14918 312 YVTKGQTV----QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----------SLEQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 960 LRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGML 1034
Cdd:cd14918 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLAA------CIELIEKP------------------LGIF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1035 WLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSL 1111
Cdd:cd14918 434 SILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEahFSLIHYAGT--VDYNITGWLDKNKD-PLNDTVVGL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1112 LQDSSREEINRLYigsltrgsgamvfcGSFAGLEGTqslrrvSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTH 1191
Cdd:cd14918 511 YQKSAMKTLASLF--------------STYASAEAD------SGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPH 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1192 FVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL-- 1269
Cdd:cd14918 571 FVRCII----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLna 629
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 116008016 1270 ----AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14918 630 saipEGQFIDSKKAS-EKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
575-1305 |
1.83e-54 |
|
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: 203.29 E-value: 1.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAGAYNNFINA--EKV---NALctiLEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASA 728
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSveQQVlesNPL---LEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 729 SLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ----KLEDRHRaANDFMRTVQA 804
Cdd:cd01384 158 AIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-----KDPKQFHYLNQskcfELDGVDD-AEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 805 FETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPN--APNG 881
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGnIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDA---LCKRVivTPDG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 882 GLSPSKSPTSdtghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpaSCGQqvgatl 957
Cdd:cd01384 309 IITKPLDPDA------ATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFEsfktN--SFEQ------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 958 adLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDlasechpgpLISLIDkapqNHVVrssqRDLREHDRRGMLWLL 1037
Cdd:cd01384 375 --FCINLANEKLQQHFNQHVFKMEQEEYTKE--EIDWS---------YIEFVD----NQDV----LDLIEKKPGGIIALL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1038 DEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKcaGPRQFVLHHLQGtnPVLYAVDGWVRHSR-----EHpgirnaVSLL 1112
Cdd:cd01384 434 DEACMFPRSTHETFAQKLYQTLKDHKRFSKPKL--SRTDFTIDHYAG--DVTYQTDLFLDKNKdyvvaEH------QALL 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1113 QDSSREEINRLYIGSLTRGsgamvfcgsfaglegtqslrrvssirrsfTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHF 1192
Cdd:cd01384 504 NASKCPFVAGLFPPLPREG-----------------------------TSSSSKFSSIGSRFKQQLQELMETLNTTEPHY 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1193 VHCylLQHNagkhtkytangspssaagQVSSEEEMVNVPLLRsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD 1272
Cdd:cd01384 555 IRC--IKPN------------------NLLKPGIFENANVLQ-QLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPE 613
|
730 740 750
....*....|....*....|....*....|....*.
gi 116008016 1273 LASNKD---VSVEQILAVNELDvaSYRIGPSQILFR 1305
Cdd:cd01384 614 VLKGSDdekAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
576-1305 |
5.97e-54 |
|
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: 202.26 E-value: 5.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLALAAgAYNNFINAEKVNALCTI----------LEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIA-AIGDRSKKDQTPGKGTLedqiiqanpaLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN--NPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSaafGLTQPNAPNGg 882
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFG-----NMKFKQKQREEQAEPDGteeADKSAYLMGLNSADLLK---GLCHPRVKVG- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 883 lspSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14917 310 ---NEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEifdfN----------SFE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14917 377 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLQA------CIDLIEKP------------------MGI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14917 433 MSILEEECMFPKATDMTFKAKLFdNHLGKSNNFQKPRNIKGKPEahFSLIHYAGT--VDYNIIGWLQKNKD-PLNETVVG 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYIGslTRGSGAMVFCGSFAGLEGTqSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDTLRRTGT 1190
Cdd:cd14917 510 LYQKSSLKLLSNLFAN--YAGADAPIEKGKGKAKKGS-SFQTVSALHRE-----------------NLNKLMTNLRSTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1191 HFVHCYLlqhnaGKHTKytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL- 1269
Cdd:cd14917 570 HFVRCII-----PNETK-----SPG-----------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILn 628
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 116008016 1270 -----AGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14917 629 paaipEGQFIDSRK-GAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
575-1279 |
3.79e-53 |
|
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: 199.64 E-value: 3.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAL-------CTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIA 726
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVeqailesSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 727 SASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAgllQKELHLENITSEDSHPFISLSQKLEDRH-RAANDFMRTVQAF 805
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLE---HEEREEFYLSTPENYHYLNQSGCVEDKTiSDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGtgstarTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGG-- 882
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGnIEFITAGG------AQVSFKTALGRSAELLGLDPTQLTDA---LTQRSMFLRGee 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 883 -LSPSKSptsdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHtIASIMLIDTPGFQNpascgQQVGaTLADLR 961
Cdd:cd14873 309 iLTPLNV-------QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFEN-----FEVN-HFEQFN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 962 HNYLQERLQMLFHHTTLVAPRDRYAQELVEIE----MDLAsEChpgplISLIDKapqnhvvrssqrdlrehdRRGMLWLL 1037
Cdd:cd14873 375 INYANEKLQEYFNKHIFSLEQLEYSREGLVWEdidwIDNG-EC-----LDLIEK------------------KLGLLALI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1038 DEEAIYPNSNDDTFLERLfsHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhpGIRNAV-SLLQDSS 1116
Cdd:cd14873 431 NEESHFPQATDSTLLEKL--HSQHANNHFYVKPRVAVNNFGVKHYAGE--VQYDVRGILEKNRD--TFRDDLlNLLRESR 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 REEINRLYIGSLTRGSGAMVFCGSfaglegtqslrrvssirrsfttaGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCy 1196
Cdd:cd14873 505 FDFIYDLFEHVSSRNNQDTLKCGS-----------------------KHRRPTVSSQFKDSLHSLMATLSSSNPFFVRC- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1197 lLQHNAGKHTkytangspssaagqvsseeEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASN 1276
Cdd:cd14873 561 -IKPNMQKMP-------------------DQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
...
gi 116008016 1277 KDV 1279
Cdd:cd14873 621 EDV 623
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
576-1305 |
4.38e-53 |
|
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: 198.92 E-value: 4.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYA-SNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINAE-KVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ-------KLEDrhraANDFMRTVQAFE 806
Cdd:cd01380 162 LLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL-----GSAEDFFYTNQggspvidGVDD----AAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 807 TLNIDAKAVRGIWSILAAIYHLGiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPS 886
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLG--NVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKW---LCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 887 KSPTsdtgHEWAWECLEALVIGLYSEALAAVVALINRQICTS-SHTIAS-IMLIDTPGFQnpascgqqvgatladlrH-- 962
Cdd:cd01380 308 KPLT----LQQAIVARDALAKHIYAQLFDWIVDRINKALASPvKEKQHSfIGVLDIYGFE-----------------Tfe 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 963 ---------NYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDkapqnhvvrssqrdlrehDRRGM 1033
Cdd:cd01380 367 vnsfeqfciNYANEKLQQQFNQHVFKLEQEEYVKE--EIEWSFIDFYDNQPCIDLIE------------------GKLGI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSR-----EHpgirna 1108
Cdd:cd01380 427 LDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHFKKPRFSNTAFIVKHFADD--VEYQVEGFLEKNRdtvseEH------ 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSsreEINRLYIGSLTRgsgamvfcgsfaglegtQSLrrvssirrsfttagvkrNSIMlqvkftvdgiiDTLRRT 1188
Cdd:cd01380 499 LNVLKAS---KNRKKTVGSQFR-----------------DSL-----------------ILLM-----------ETLNST 530
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCyllqhnagkhTKytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd01380 531 TPHYVRC----------IK------PNDEKLPFTFDPKRV-----VQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRV 589
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 116008016 1269 LAG---DLASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01380 590 LLPskeWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
575-1305 |
8.76e-53 |
|
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: 198.47 E-value: 8.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYL-ALAAGAYNNfiNAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFdQTGQIASASLQVL 733
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLsSLYQDQTED--RLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFISLSQKLEDRHRA-ANDFMRTVQAFETLNIDA 812
Cdd:cd14896 158 LLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ---GPETYYYLNQGGACRLQGKEdAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 813 KAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQ--PNAPNGGLSPSKSPt 890
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGA---VTHrvTETPYGRVSRPLPV- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 891 sdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSH--TIASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQER 968
Cdd:cd14896 311 -----EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEaeSDATIGVVDAYGFEALRVNG------LEQLCINLASER 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 969 LQMLFHHTTLVAPRDRYAQELVeiemdlasECHPGPLislidkapqnhVVRSSQRDLREHDRRGMLWLLDEEAIYPNSND 1048
Cdd:cd14896 380 LQLFSSQTLLAQEEEECQRELL--------PWVPIPQ-----------PPRESCLDLLVDQPHSLLSILDDQTWLSQATD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1049 DTFLERLFSHYGDrehHSLLRKCAGPRQ-FVLHHLQGtnPVLYAVDGWVRHSREHpgIRNAVSLLQDSSReeinrlyigs 1127
Cdd:cd14896 441 HTFLQKCHYHHGD---HPSYAKPQLPLPvFTVRHYAG--TVTYQVHKFLNRNRDQ--LDPAVVEMLAQSQ---------- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1128 ltrgsgamvfcgsfaglegtqsLRRVSSI-RRSFTTAGVKRNSIMLQVKF--TVDGIIDTLRRTGTHFVHCylLQHNAGK 1204
Cdd:cd14896 504 ----------------------LQLVGSLfQEAEPQYGLGQGKPTLASRFqqSLGDLTARLGRSHVYFIHC--LNPNPGK 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1205 HTKytangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDlaSNKDVSVEQI 1284
Cdd:cd14896 560 LPG-------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSE--RQEALSDRER 618
|
730 740
....*....|....*....|....*.
gi 116008016 1285 LAVNELDVAS-----YRIGPSQILFR 1305
Cdd:cd14896 619 CGAILSQVLGaesplYHLGATKVLLK 644
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
575-1270 |
1.65e-52 |
|
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: 197.67 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMA--PLsLYSEKVVSMFRgcKTEDM----PPHVYSLAQTAYRSL----VET 644
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKsiPL-LYDVPGFDSQR--KEEATasspPPHVFSIAERAYRAMkgvgKGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 645 RRDQSLIFMGRSGSGKSTSFKHALNYLA----LAAGAYNNFINA---EKVNAlC-----TILEAFGNTKTCLNSNATRMT 712
Cdd:cd14892 78 GTPQSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAAnahESIEE-CvllsnLILEAFGNAKTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 713 QLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLlqKELHLENITSEDSHpFISLSQKLE-DR 791
Cdd:cd14892 157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDAN--ENAALELTPAESFL-FLNQGNCVEvDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 792 HRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAF 871
Cdd:cd14892 234 VDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 872 GLTQPNAPNGGLSPSKSPtsdtghEWAWECLEALVIGLYSEALAAVVALINRqiCTSSHTIASIMLIDTPGFQNPASC-- 949
Cdd:cd14892 314 TQTTSTARGSVLEIKLTA------REAKNALDALCKYLYGELFDWLISRINA--CHKQQTSGVTGGAASPTFSPFIGIld 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 950 --GQQVGAT--LADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQnhvvrssq 1022
Cdd:cd14892 386 ifGFEIMPTnsFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDC-----LDLIQKKPL-------- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1023 rdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFsHYGDREHHSLLRKcagPR----QFVLHHLQGTnpVLYAVDGWVrh 1098
Cdd:cd14892 453 ---------GLLPLLEEQMLLKRKTTDKQLLTIY-HQTHLDKHPHYAK---PRfecdEFVLRHYAGD--VTYDVHGFL-- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1099 srehpgIRNAVSLLQDssreeinrlyigsltrgsgamvfcgsfaglegtqsLRRVSSIRRSFTTagvkrnsimlqvkfTV 1178
Cdd:cd14892 516 ------AKNNDNLHDD-----------------------------------LRDLLRSSSKFRT--------------QL 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1179 DGIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVP 1258
Cdd:cd14892 541 AELMEVLWSTTPSYIKC--IKPNNLK------------FPGGFSCE-------LVRDQLIYSGVLEVVRIRREGFPIRRQ 599
|
730
....*....|..
gi 116008016 1259 LLEFVRRFGLLA 1270
Cdd:cd14892 600 FEEFYEKFWPLA 611
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
576-1305 |
2.38e-52 |
|
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: 197.59 E-value: 2.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLALAAG----AYNNFINAEKVNALCTI------LEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrSKKENPNANKGTLEDQIiqanpaLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTN--NPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSaafGLTQPNAPNGG 882
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYG-----NMKFKQKQREEQAEPDGtedADKSAYLMGLNSADLLK---GLCHPRVKVGN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 883 LSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14916 312 EYVTKGQSV----QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEifdfN----------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLQA------CIDLIEKP------------------MGI 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14916 434 MSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRNVKGKQEahFSLVHYAGT--VDYNILGWLEKNKD-PLNETVVG 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRL---YIGSLTRGSGAmvfcgSFAGLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDTLRR 1187
Cdd:cd14916 511 LYQKSSLKLMATLfstYASADTGDSGK-----GKGGKKKGSSFQTVSALHRE-----------------NLNKLMTNLKT 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1188 TGTHFVHCYLlqhnagkhtkytangsPSSaagqvSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFG 1267
Cdd:cd14916 569 THPHFVRCII----------------PNE-----RKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 627
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 116008016 1268 LL------AGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14916 628 ILnpaaipEGQFIDSRK-GAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
572-1096 |
2.85e-52 |
|
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: 196.62 E-value: 2.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 572 LNEASVLHCLRQRYASNLIHTKAGPT-LLVVNPMAPLSLYSEKV----VSMFRGC---KTEDMPPHVYSLAQTAYRSLVE 643
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASlgeyGSEYYDTtsgSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 644 TRRDQSLIFMGRSGSGKSTSFKHALN-YLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQT 722
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRqLLRLSSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 723 GQIASA-SLQVLLpERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSE-----------DSHPFISLSQKLED 790
Cdd:cd14879 161 GRLIGAkVLDYRL-ERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYallasygchplPLGPGSDDAEGFQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 791 rhraandfMRTvqAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAa 870
Cdd:cd14879 240 --------LKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETS- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 871 fgLTqpnapngglspSKspTSDTGHEWAWECLEA---------LVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDT 940
Cdd:cd14879 309 --LT-----------YK--TKLVRKELCTVFLDPegaaaqrdeLARTLYSLLFAWVVETINQKLCAPEDDFATfISLLDF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 941 PGFQNPASCGqqvGATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE----MDlASEC------HPGPLISLID 1010
Cdd:cd14879 374 PGFQNRSSTG---GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPatsyFD-NSDCvrllrgKPGGLLGILD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1011 KAPqnhvvrssqrdlrehdRRgmlwlldeeaiYPNSNDDTFLERLFSHYGDreHHSLLRKCA-----GPRQFVLHHLQGt 1085
Cdd:cd14879 450 DQT----------------RR-----------MPKKTDEQMLEALRKRFGN--HSSFIAVGNfatrsGSASFTVNHYAG- 499
|
570
....*....|.
gi 116008016 1086 nPVLYAVDGWV 1096
Cdd:cd14879 500 -EVTYSVEGFL 509
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
575-1305 |
4.36e-52 |
|
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: 196.06 E-value: 4.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDM-PPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDLL-DKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENI-------TSEDSHPFISLSQKLEDRHRAANDF---MRTVq 803
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPdchrilrDDNRNRPVFNDSEELEYYRQMFHDLtniMKLI- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 804 AFETLNIDAkavrgIWSILAAIYHlgIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFGLTQpnapnggL 883
Cdd:cd14897 239 GFSEEDISV-----IFTILAAILH--LTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVN-------T 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 884 SPSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIA-----SIMLIDTPGFQNPASCGqqvgatLA 958
Cdd:cd14897 305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQImtrgpSIGILDMSGFENFKINS------FD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEmDLASECHpGPLISLIDKAPQnhvvrssqrdlrehdrrGMLWLLD 1038
Cdd:cd14897 379 QLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDN-DDVLELFFKKPL-----------------GILPLLD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHH--SLLRKCAgprqFVLHHLQGTnpVLYAVDGWVRHSREHPGIrNAVSLLQDSS 1116
Cdd:cd14897 440 EESTFPQSTDSSLVQKLNKYCGESPRYvaSPGNRVA----FGIRHYAEQ--VTYDADGFLEKNRDNLSS-DIVGCLLNSN 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 REEINRLYIGSLTRgsgamvfcgSFAGLegtqsLRRVSSIRRSFTTAgVKRNSIMLQVKFTVDgiidtlrrtgthfvhcy 1196
Cdd:cd14897 513 NEFISDLFTSYFKR---------SLSDL-----MTKLNSADPLFVRC-IKPNNFLRPNKFDDE----------------- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1197 llqhnagkhtkytangspssaagqvsseeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDlaSN 1276
Cdd:cd14897 561 -----------------------------------LVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF--SN 603
|
730 740 750
....*....|....*....|....*....|..
gi 116008016 1277 KDVSVEQILAVNELDVAS---YRIGPSQILFR 1305
Cdd:cd14897 604 KVRSDDLGKCQKILKTAGikgYQFGKTKVFLK 635
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
575-1305 |
5.71e-52 |
|
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: 196.15 E-value: 5.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAGAYNNFInAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDST-IKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLagAAGLLQKELHLENiTSEDSHPFISLSQKLEDRHRAANdFMRTVQAFETLNIDAK 813
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDS-ANECAYTGANKTIKIEGMSDRKH-FARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 814 AVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFGLTQPNAPNGGLSPSKSptsdt 893
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK----- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 894 ghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNpascgqqvgatladLRH--------NYL 965
Cdd:cd14903 311 --DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEH--------------FKHnsfeqfciNYA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 966 QERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDkapqnhvvrssqrdlrehDRRGMLWLLDEEAIYPN 1045
Cdd:cd14903 375 NEKLQQKFTQDVFKTVQIEYEEE--GIRWAHIDFADNQDVLAVIE------------------DRLGIISLLNDEVMRPK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1046 SNDDTFLERLFSHYGDREHHSLLRKCAgPRQFVLHHLQGtnPVLYAVDGWVRHSREhpgirnavSLLQDSSreeinrlyi 1125
Cdd:cd14903 435 GNEESFVSKLSSIHKDEQDVIEFPRTS-RTQFTIKHYAG--PVTYESLGFLEKHKD--------ALLPDLS--------- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1126 gSLTRGSG----AMVFCGSFAGLEGTQSLRRVSSIRRSFTTAGVKrnSIMLQVKFTVDGIIDTLRRTGTHFVHCyllqhn 1201
Cdd:cd14903 495 -DLMRGSSkpflRMLFKEKVESPAAASTSLARGARRRRGGALTTT--TVGTQFKDSLNELMTTIRSTNVHYVRC------ 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1202 agkhTKYTANGSPSSAagqvssEEEMVNvpllrSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAgDLASNKDVSV 1281
Cdd:cd14903 566 ----IKPNSIKSPTEL------DHLMVV-----SQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL-PEGRNTDVPV 629
|
730 740
....*....|....*....|....*....
gi 116008016 1282 ----EQILAVNELDV-ASYRIGPSQILFR 1305
Cdd:cd14903 630 aercEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
576-1270 |
2.00e-51 |
|
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: 194.03 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLALAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLP 735
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 736 ERQRAGRRLGHEHSFHIMTRLLAGAA--GLLQKELHLENITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAK 813
Cdd:cd01379 161 EKSRVVHQAIGERNFHIFYYIYAGLAedKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 814 AVRGIWSILAAIYHLGIAGVTKLGTG--STARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTS 891
Cdd:cd01379 241 EVDSVYSILAAILHIGDIEFTEVESNhqTDKSSRISNPEALNNVAKLLGIEADELQEA---LTSHSVVTRGETIIRNNTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 892 DTghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIA---SIMLIDTPGFQN-PASCGQQVGATLADlrhnylqE 967
Cdd:cd01379 318 EE----ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDeplSIGILDIFGFENfQKNSFEQLCINIAN-------E 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 968 RLQMLFHHTTLVAPRDRYAQELVeiemdlasechPGPLISLIDKAPqnhVVrssqrDLREHDRRGMLWLLDEEAIYPNSN 1047
Cdd:cd01379 387 QIQYYFNQHIFAWEQQEYLNEGI-----------DVDLIEYEDNRP---LL-----DMFLQKPMGLLALLDEESRFPKAT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1048 DDTFLERLfsHYGDREHHSLLRKCAGPrQFVLHHLQGTnpVLYAVDGWVRHSREH--PGIrnaVSLLQDSSReeinrlyi 1125
Cdd:cd01379 448 DQTLVEKF--HNNIKSKYYWRPKSNAL-SFGIHHYAGK--VLYDASGFLEKNRDTlpPDV---VQLLRSSEN-------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1126 gsltrgsgamvfcgsfaglegtqslrrvSSIRRsfTTAGVKRNSIM-LQVKFTVdgiidtlrrtGT-HFVHCylLQHNAG 1203
Cdd:cd01379 512 ----------------------------PLVRQ--TVATYFRYSLMdLLSKMVV----------GQpHFVRC--IKPNDS 549
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1204 KhtkytangspssAAGQVSSEEEMVnvpllrsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLA 1270
Cdd:cd01379 550 R------------QAGKFDREKVLK-------QLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA 597
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
575-1269 |
1.90e-50 |
|
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: 191.31 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYnNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH-SWIE-QQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ----KLEDRHRAAnDFMRTVQAFETLNI 810
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-----GDASDYYYLTQgnclTCEGRDDAA-EFADIRSAMKVLMF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 811 DAKAVRGIWSILAAIYHLG----IAGVTKlgtgSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGlsps 886
Cdd:cd01381 233 TDEEIWDIFKLLAAILHLGnikfEATVVD----NLDASEVRDPPNLERAAKLLEVPKQDLVDA---LTTRTIFTRG---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 887 KSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIA---SIMLIDTPGFQNPA--SCGQqvgatladLR 961
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSsrtSIGVLDIFGFENFEvnSFEQ--------LC 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 962 HNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQNhvvrssqrdlrehdrrgMLWLLD 1038
Cdd:cd01381 374 INFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDV-----LDLIALKPMN-----------------IMSLID 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHHsLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSRE--HPGIRNavsLLQDSS 1116
Cdd:cd01381 432 EESKFPKGTDQTMLEKLHSTHGNNKNY-LKPKSDLNTSFGINHFAGV--VFYDTRGFLEKNRDtfSADLLQ---LVQSSK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 REEINRLYIGSLTRGSgamvfcgsfaglegtqslrrvSSIRRSFTTAGVKRNSImlqvkftvDGIIDTLRRTGTHFVHCy 1196
Cdd:cd01381 506 NKFLKQLFNEDISMGS---------------------ETRKKSPTLSSQFRKSL--------DQLMKTLSACQPFFVRC- 555
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1197 lLQHNAGKHTKYTangspssaagqvssEEEMVnvplLRsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL 1269
Cdd:cd01381 556 -IKPNEYKKPMLF--------------DRELC----VR-QLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL 608
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
581-1094 |
3.23e-50 |
|
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: 190.83 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 581 LRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGK 660
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 661 STSFKHALNYLALAAGAYNNFINAEKVNALCT--ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQ 738
Cdd:cd01378 87 TEASKRIMQYIAAVSGGSESEVERVKDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 739 RAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFISLSQKLE-DRHRAANDFMRTVQAFETLNIDAKAVRG 817
Cdd:cd01378 167 RVVGQIKGERNFHIFYQLLKGASQEYLQELGLQ---RPEQYYYYSKSGCFDvDGIDDAADFKEVLNAMKVIGFTEEEQDS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 818 IWSILAAIYHLG-IAGVTKLGTGSTARTQFANPTAARkasgLLGVNLEDLSSAafgLT--QPNAPNGGLSPSKSPTSDTG 894
Cdd:cd01378 244 IFRILAAILHLGnIQFAEDEEGNAAISDTSVLDFVAY----LLGVDPDQLEKA---LThrTIETGGGGRSVYEVPLNVEQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 895 hewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIM-LIDTPGF----QNpaSCGQqvgatladLRHNYLQERL 969
Cdd:cd01378 317 ---AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN--SFEQ--------FCINYVNEKL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 970 QMLFHHTTLVAPRDRYAQELVEIEmdlasechPgplISLIDkapqNHVVrssqRDLREHDRRGMLWLLDEE-AIYPNSND 1048
Cdd:cd01378 384 QQIFIELTLKAEQEEYVREGIEWT--------P---IKYFN----NKII----CDLIEEKPPGIFAILDDAcLTAGDATD 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 116008016 1049 DTFLERLFSHYGDREHHS--LLRKCAGPRQFVLHHLQGtnPVLYAVDG 1094
Cdd:cd01378 445 QTFLQKLNQLFSNHPHFEcpSGHFELRRGEFRIKHYAG--DVTYNVEG 490
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
575-1305 |
4.52e-50 |
|
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: 190.37 E-value: 4.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV----ETRRDQS 649
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIpDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 650 LIFMGRSGSGKSTSFKHALNYLALAAGaYNNFINAEKVNALCT------------------ILEAFGNTKTCLNSNATRM 711
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITS-GFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 712 TQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEniTSEDShpFISLSQKLEDR 791
Cdd:cd14890 160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ--TPVEY--FYLRGECSSIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 792 HRA-ANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG-----IAGVTKLGTGSTARtqfanPTaARKASGLLGVNLED 865
Cdd:cd14890 236 SCDdAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfeSENDTTVLEDATTL-----QS-LKLAAELLGVNEDA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 866 LSSAAfgLTQPNAPNGglspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQn 945
Cdd:cd14890 310 LEKAL--LTRQLFVGG-----KTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFE- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 946 pasCGQQvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEC----------HPGPLISLIDka 1012
Cdd:cd14890 382 ---KFEW--NTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACleliegkvngKPGIFITLDD-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1013 pqNHVVRSSQRDLR----EHDRRGmlwlldeeaiyPNSNDDTflerlFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpV 1088
Cdd:cd14890 455 --CWRFKGEEANKKfvsqLHASFG-----------RKSGSGG-----TRRGSSQHPHFVHPKFDADKQFGIKHYAGD--V 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1089 LYAVDGWVRHSREHpgirnavslLQDSSREEINrlyigsltrgsgamvfcgsfaglEGTQSLRRVssirrsfttagvkrn 1168
Cdd:cd14890 515 IYDASGFNEKNNET---------LNAEMKELIK-----------------------QSRRSIREV--------------- 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1169 SIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNagkhtkytangsPSSAAGQVSSEEemvnvpLLRsQLRGSQVLEAARL 1248
Cdd:cd14890 548 SVGAQFRTQLQELMAKISLTNPRYVRC--IKPN------------ETKAPGKFDGLD------CLR-QLKYSGMMEAIQI 606
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1249 HRLGFPESVPLLEFVRRFGLLAGDlASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14890 607 RQQGFALREEHDSFFYDFQVLLPT-AENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
575-1269 |
1.78e-49 |
|
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: 189.72 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKT--------EDMPPHVYSLAQTAYRSLV-ET 644
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLpDLYSESQLNAYKASMTstspvsqlSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 645 RRDQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFINAEKVNA-------LCT--ILEAFGNTKTCLNSNATRMTQLL 715
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLT-SVGRDQSSTEQEGSDAveigkriLQTnpILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 716 SLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQKLEDRHRAA 795
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQK--GGKYELLNSYGPSFARKRAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 796 ND----FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGtGSTARTQFANPTAAR--KASGLLGVNLEDLSSA 869
Cdd:cd14902 238 DKyaqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEN-GQEDATAVTAASRFHlaKCAELMGVDVDKLETL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 870 afgLTQPNAPNGG------LSPsksptsdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTI---------AS 934
Cdd:cd14902 317 ---LSSREIKAGVevmvlkLTP----------EQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVsisdedeelAT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 935 IMLIDTPGFQNPASCGqqvgatLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDK 1011
Cdd:cd14902 384 IGILDIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC-----LALFDD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1012 APQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREhhsllrkcagprQFVLHHLQGTnpVLYA 1091
Cdd:cd14902 453 KSN-----------------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG------------QFVVHHFAGR--VCYN 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1092 VDGWVRHSREH-PGirNAVSLLQDSSREEInrLYIGSLTRgsgamvfCGSFAGLEGTQSLRRVSSIRRSfttagvkrnSI 1170
Cdd:cd14902 502 VEQFVEKNTDAlPA--DASDILSSSSNEVV--VAIGADEN-------RDSPGADNGAAGRRRYSMLRAP---------SV 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1171 MLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHTKYTangspssaagqvsSEEEMVnvpllrSQLRGSQVLEAARLHR 1250
Cdd:cd14902 562 SAQFKSQLDRLIVQIGRTEAHYVRC--LKPNEVKKPGIF-------------DRERMV------EQMRSVGVLEAVRIAR 620
|
730
....*....|....*....
gi 116008016 1251 LGFPESVPLLEFVRRFGLL 1269
Cdd:cd14902 621 HGYSVRLAHASFIELFSGF 639
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
575-1305 |
9.94e-49 |
|
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: 186.58 E-value: 9.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAL-------CTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLedqvvqtNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEdsHPFISLSQKLEDRHRAANDFMRTVQAFET 807
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYD--YYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 808 LNIDAKAVRGIWSILAAIYHLGIAGVTKLGtgstaRTQFANPTAAR---KASGLLGVNLEDLSSAafgLTQPNAPNGGLS 884
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRG-----REEQAEQDGEEeggRVSKLFGCDTAELYKN---LLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 885 PSKSPTSDTghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGqqvgatLADLRHNY 964
Cdd:cd14909 311 VTQGRNVQQ----VTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCINF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 965 LQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASeChpgplISLIDKApqnhvvrssqrdlrehdrRGMLWLLDE 1039
Cdd:cd14909 381 TNEKLQQFFNHHMFVLEQEEYKREgidwaFIDFGMDLLA-C-----IDLIEKP------------------MGILSILEE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1040 EAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQ----FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDS 1115
Cdd:cd14909 437 ESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQqaahFAIAHYAGC--VSYNITGWLEKNKD-PLNDTVVDQFKKS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1116 SreeiNRLYIGSLTRGSGAMvfcgsfAGLEGTQSLRRvssirrsftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHC 1195
Cdd:cd14909 514 Q----NKLLIEIFADHAGQS------GGGEQAKGGRG---------KKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRC 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1196 YLlqHNAGKHTKytangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLA- 1274
Cdd:cd14909 575 II--PNEMKQPG-------------------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIq 633
|
730 740 750
....*....|....*....|....*....|...
gi 116008016 1275 --SNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14909 634 geEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
575-1305 |
4.54e-46 |
|
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: 178.41 E-value: 4.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFInAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQtGQIASASLQVLL 734
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV-TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQKLEDR---HRAANDFMRTVQAFETLNID 811
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-----QEAEKYFYLNQGGNCEiagKSDADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 812 AKAVRGIWSILAAIYHLG---------IAGVTKLGTGSTARTQFanptaarkASGLLGVNLEDLSSA-AFGLTQPNAPNg 881
Cdd:cd01387 234 SEEQDSIFRILASVLHLGnvyfhkrqlRHGQEGVSVGSDAEIQW--------VAHLLQISPEGLQKAlTFKVTETRRER- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 882 glspSKSPTSDtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPAScgqqvgATLADLR 961
Cdd:cd01387 305 ----IFTPLTI---DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSE------NSFEQLC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 962 HNYLQERLQMLFHHTTLVAPRDRYAQELVE-IEMDLASEChpgPLISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEE 1040
Cdd:cd01387 372 INYANENLQYYFNKHVFKLEQEEYIREQIDwTEIAFADNQ---PVINLISKKPV-----------------GILHILDDE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1041 AIYPNSNDDTFLERLFSHYGDREHHSllRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSRehpgirnavsllqDSSREEI 1120
Cdd:cd01387 432 CNFPQATDHSFLEKCHYHHALNELYS--KPRMPLPEFTIKHYAGQ--VWYQVHGFLDKNR-------------DQLRQDV 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1121 NRLYIGSLTRGSGAMvfcgsFAGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQH 1200
Cdd:cd01387 495 LELLVSSRTRVVAHL-----FSSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRC--LKP 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1201 NAGKHTKytangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRF-GLLAGDLASNKDV 1279
Cdd:cd01387 568 NHKKEPM-------------------LFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYrCLVALKLPRPAPG 628
|
730 740
....*....|....*....|....*....
gi 116008016 1280 SVEQILAVNELDVAS---YRIGPSQILFR 1305
Cdd:cd01387 629 DMCVSLLSRLCTVTPkdmYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
575-1305 |
3.40e-45 |
|
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: 176.03 E-value: 3.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYL-ALAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd01385 81 ESGSGKTESTNFLLHHLtALSQKGYGSGVEQTILGA-GPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEniTSEDSHpFISLSQ-KLEDRHRAANDFMRTVQAFETLNIDA 812
Cdd:cd01385 160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK--QPEDYH-YLNQSDcYTLEGEDEKYEFERLKQAMEMVGFLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 813 KAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGG---LSPSKSP 889
Cdd:cd01385 237 ETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEA---LTTKKTVTVGetlILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 890 TSDTGHEWAWECLEALV---IGLYSEAlaavvALINRQIcTSSHTIASIMLIDTPGFQNpascgqqVGA-TLADLRHNYL 965
Cdd:cd01385 314 EAIATRDAMAKCLYSALfdwIVLRINH-----ALLNKKD-LEEAKGLSIGVLDIFGFED-------FGNnSFEQFCINYA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 966 QERLQMLFHHTTLVAPRDRYAQE---LVEIEMDLASEChpgplISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAI 1042
Cdd:cd01385 381 NEHLQYYFNQHIFKLEQEEYKKEgisWHNIEYTDNTGC-----LQLISKKPT-----------------GLLCLLDEESN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1043 YPNSNDDTFLERLFSHYGDREHHSL--LRKCAgprqFVLHHLQGTnpVLYAVDGWVRHSREH--PGIrnaVSLLQDSS-- 1116
Cdd:cd01385 439 FPGATNQTLLAKFKQQHKDNKYYEKpqVMEPA----FIIAHYAGK--VKYQIKDFREKNLDLmrPDI---VAVLRSSSsa 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 --REEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSLRRVSSI------RRSFTTAGVKRN-----SIMLQVKFTVDGIID 1183
Cdd:cd01385 510 fvRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGhsltlhDRTTKSLLHLHKkkkppSVSAQFQTSLSKLME 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1184 TLRRTGTHFVHCylLQHNAGKhtkytangspssaaGQVSSEEEMVnvplLRsQLRGSQVLEAARLHRLGFPESVPLLEFV 1263
Cdd:cd01385 590 TLGQAEPFFIRC--IKSNAEK--------------KPLRFDDELV----LR-QLRYTGMLETVRIRRSGYSVRYTFQEFI 648
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 116008016 1264 RRFG-LLAGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01385 649 TQFQvLLPKGLISSKE-DIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
575-1195 |
1.07e-44 |
|
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: 173.97 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAGPIEQRILEA-NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhLENITSEDshpfislsqkledrhraANDFMRTVQAFETLNIDAK 813
Cdd:cd01382 160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPLLDD-----------------VGDFIRMDKAMKKIGLSDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 814 AVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPT--AARKASGLLGVNLEDLSSAafgLTQP--NAPNGGLS----- 884
Cdd:cd01382 222 EKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSeqSLEYAAELLGLDQDELRVS---LTTRvmQTTRGGAKgtvik 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 885 -PSKSptsdtgHEwAWECLEALVIGLYSEALAAVVALINRQI--CTSSHTIAsimLIDTPGFQNpascgqqvgatladLR 961
Cdd:cd01382 299 vPLKV------EE-ANNARDALAKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEY--------------FE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 962 H--------NYLQERLQMLFHHTTLvaprdRYAQELVEIEmdlasechpG---PLISLIDKapQNHVvrssqrDLREHDR 1030
Cdd:cd01382 355 VnsfeqfciNYCNEKLQQFFNERIL-----KEEQELYEKE---------GlgvKEVEYVDN--QDCI------DLIEAKL 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1031 RGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLrkcAGPRQ--------------FVLHHLQGTnpVLYAVDGWV 1096
Cdd:cd01382 413 VGILDLLDEESKLPKPSDQHFTSAVHQKHKN---HFRL---SIPRKsklkihrnlrddegFLIRHFAGA--VCYETAQFI 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1097 R------H-SREhpgirnavSLLQDSSREEINRLYIGSLTRGSGamvfcgsfaglegtqslRRVSSIRRSFTTAGVKRNS 1169
Cdd:cd01382 485 EknndalHaSLE--------SLICESKDKFIRSLFESSTNNNKD-----------------SKQKAGKLSFISVGNKFKT 539
|
650 660
....*....|....*....|....*.
gi 116008016 1170 IMLQvkftvdgIIDTLRRTGTHFVHC 1195
Cdd:cd01382 540 QLNL-------LMDKLRSTGTSFIRC 558
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
576-1270 |
3.70e-44 |
|
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: 173.22 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSekvVSMFRgcktEDMP------PHVYSLAQTAYRSL------- 641
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYR----EEMPgwtalpPHVFSIAEGAYRSLrrrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 642 VETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCT--------ILEAFGNTKTCLNSNATRMTQ 713
Cdd:cd14895 75 GASKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 714 LLSLDF-----DQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHpFISLSQ-- 786
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQ-YISGGQcy 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 787 KLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG--IAGVTKLGTGSTARTQFANPTAARKA--------- 855
Cdd:cd14895 234 QRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvLFVASSEDEGEEDNGAASAPCRLASAspssltvqq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 856 -----SGLLGVNLEDLSSAafgLTQPNAPNGGlspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALIN-----RQI 925
Cdd:cd14895 314 hldivSKLFAVDQDELVSA---LTTRKISVGG----ETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 926 CTSSHTIAS------IMLIDTPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDL 996
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFEEFEV------NQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwnaVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 997 ASEChpgplISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQ 1076
Cdd:cd14895 461 NSVC-----LEMLEQRPS-----------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1077 FVLHHLQGTnpVLYAVDGWVRHSREHPGiRNAVSLLQDSSREEINRLyigsltrgsgamvfCGSFAGLEGTQ-SLRRVSS 1155
Cdd:cd14895 519 FQIHHYAGA--VRYQAEGFCEKNKDQPN-AELFSVLGKTSDAHLREL--------------FEFFKASESAElSLGQPKL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1156 IRRSFTTAGVKRNSimlQVKFTVDGIIDTLRRTGTHFVHCYllqhnagkhtkytangSPSSAagqvsSEEEMVNVPLLRS 1235
Cdd:cd14895 582 RRRSSVLSSVGIGS---QFKQQLASLLDVVQQTQTHYIRCI----------------KPNDE-----SASDQFDMAKVSS 637
|
730 740 750
....*....|....*....|....*....|....*
gi 116008016 1236 QLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLA 1270
Cdd:cd14895 638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
575-1270 |
2.34e-42 |
|
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: 167.18 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGcKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIpGLYSDEMLLKFIQ-PSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLAlAAGAYN----NFINAE--KVNALctiLEAFGNTKTCLNSNATRMTQLLSLDFDQT----- 722
Cdd:cd14888 80 GESGAGKTESTKYVMKFLA-CAGSEDikkrSLVEAQvlESNPL---LEAFGNARTLRNDNSSRFGKFIELQFSKLkskrm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 723 ----GQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLE-----------------NITSEDSHP- 780
Cdd:cd14888 156 sgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEendeklakgadakpisiDMSSFEPHLk 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 781 FISLSQKLEDRHRAAND---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTARTQFANPTAARKAS 856
Cdd:cd14888 236 FRYLTKSSCHELPDVDDleeFESTLYAMQTVGISPEEQNQIFSIVAAILYLGnILFENNEACSEGAVVSASCTDDLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 857 GLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTSDTghewAWECLEALVIGLYSEALAAVVALINRQIC-TSSHTIASI 935
Cdd:cd14888 316 SLLGVDAEDLLNA---LCYRTIKTAHEFYTKPLRVDE----AEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 936 MLIDTPGFQN-PASCGQQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDlasechpgPLislidKAPQ 1014
Cdd:cd14888 389 GVLDIFGFECfQLNSFEQ-------LCINFTNERLQQFFNNFVFKCEEKLYIEE--GISWN--------PL-----DFPD 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1015 NhvvrSSQRDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKcaGPRQFVLHHLQGtnPVLYAVDG 1094
Cdd:cd14888 447 N----QDCVDLLQEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAG--PVKYCSDG 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1095 WVRHSREHPGIrNAVSLLQDSSREEINRLYIGSLTRGSgamvfcgsfaglEGTQSLRRVSSIRRSFttagvkRNSImlqv 1174
Cdd:cd14888 519 FLEKNKDQLSV-DAQEVIKNSKNPFISNLFSAYLRRGT------------DGNTKKKKFVTVSSEF------RNQL---- 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1175 kftvDGIIDTLRRTGTHFVHCyllqhnagkhTKYTANGSPssaagqvsSEEEMVNVpllRSQLRGSQVLEAARLHRLGFP 1254
Cdd:cd14888 576 ----DVLMETIDKTEPHFIRC----------IKPNSQNVP--------DLFDRISV---NEQLKYGGVLQAVQVSRAGYP 630
|
730
....*....|....*.
gi 116008016 1255 ESVPLLEFVRRFGLLA 1270
Cdd:cd14888 631 VRLSHAEFYNDYRILL 646
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
575-1305 |
2.31e-41 |
|
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: 163.96 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIdNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAGAYNNFINAeKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFI--SLSQKLEDRHRAANDFMRTVQAFETLNID 811
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLD---PNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 812 AKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDlssaAFGLTQPNAPNGGLSPSKSPTS 891
Cdd:cd14904 237 NDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAKMLGLPTTRIEE----ALCNRSVVTRNESVTVPLAPVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 892 dtghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTI-ASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQERLQ 970
Cdd:cd14904 313 ------AEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIkGQIGVLDIFGFEDFAHNG------FEQFCINYANEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 971 MLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDkapqnhvvrssqrdlrehDRRGMLWLLDEEAIYPNSNDDT 1050
Cdd:cd14904 381 QKFTTDVFKTVEEEYIRE--GLQWDHIEYQDNQGIVEVID------------------GKMGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1051 FLERLFSHYGDREHHSLLRKCAGPR-QFVLHHLQGtnPVLYAVDGWVRHSREHPGiRNAVSLLQDSSREEINRLYIGSLT 1129
Cdd:cd14904 441 LVNKIRTNHQTKKDNESIDFPKVKRtQFIINHYAG--PVTYETVGFMEKHRDTLQ-NDLLDLVLLSSLDLLTELFGSSEA 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1130 RGSGAMvfcgsfaglegtqslrrvsSIRRSFTTAgvkRNSIMLQVKFTVDGIIDTLRRTGTHFVHCyllqhnagkhTKYT 1209
Cdd:cd14904 518 PSETKE-------------------GKSGKGTKA---PKSLGSQFKTSLSQLMDNIKTTNTHYVRC----------IKPN 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1210 ANGSPSSAAGQVSSEeemvnvpllrsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDV---SVEQILA 1286
Cdd:cd14904 566 ANKSPTEFDKRMVVE-----------QLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDVrrtCSVFMTA 634
|
730
....*....|....*....
gi 116008016 1287 VNELDVASYRIGPSQILFR 1305
Cdd:cd14904 635 IGRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
575-1094 |
5.72e-40 |
|
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: 159.81 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTE--------DMPPHVYSLAQTAYRSLVETR 645
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 646 RDQSLIFMGRSGSGKSTSFKHALNYLalaAGAYNNFINAEKVNALCT---------------------ILEAFGNTKTCL 704
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFL---TQLSQQEQNSEEVLTLTSsiratskstksieqkilscnpILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 705 NSNATRMTQLLSLDFD-QTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPFIS 783
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 784 LSQKLEdrHRAAND---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLG 860
Cdd:cd14907 238 KSNCYE--VDTINDeklFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 861 VNLEDLSSAAfgLTQPNAPNGGL--SPSKSPtsdtghewawEC---LEALVIGLYSEALAAVVALINRQI--------CT 927
Cdd:cd14907 316 IDEEELKEAL--TTKIRKVGNQVitSPLSKK----------ECinnRDSLSKELYDRLFNWLVERLNDTImpkdekdqQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 928 SSHTIASIMLIDTPGFQNPASCG-QQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASECHPGPLI 1006
Cdd:cd14907 384 FQNKYLSIGLLDIFGFEVFQNNSfEQ-------LCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLNQLSYTDNQDVI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1007 SLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRqFVLHHLQGtn 1086
Cdd:cd14907 457 DLLDKPPI-----------------GIFNLLDDSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAK-- 516
|
....*...
gi 116008016 1087 PVLYAVDG 1094
Cdd:cd14907 517 EVEYNIEG 524
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
541-867 |
8.98e-40 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 160.97 E-value: 8.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 541 NGEQLTVDEDDVEKQNSPA-LDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR 619
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQIdPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 620 GCK-TEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFG 698
Cdd:PTZ00014 155 DAKdSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 699 NTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedS 778
Cdd:PTZ00014 235 NAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLE---E 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 779 HPFISLS----QKLEDrhraANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTA 851
Cdd:PTZ00014 312 YKYINPKcldvPGIDD----VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGnveIEGKEEGGLTDAAAISDESLEV 387
|
330
....*....|....*.
gi 116008016 852 ARKASGLLGVNLEDLS 867
Cdd:PTZ00014 388 FNEACELLFLDYESLK 403
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
577-1305 |
5.51e-39 |
|
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: 156.61 E-value: 5.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 577 VLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV----ETRRDQSLIF 652
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 653 MGRSGSGKSTSFKHALNYL-ALAAGAYNNFINAEKVNALctiLEAFGNTKTCLNSNATRMTQLLSLDFdQTGQIASASLQ 731
Cdd:cd14889 83 SGESGAGKTESTKLLLRQImELCRGNSQLEQQILQVNPL---LEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 732 VLLPERQRAGRRLGHEHSFHIMTRLLAGAAgLLQKELHleNITSEDSHPFISlsqkledrHRAANDfmRTVQAFETLN-- 809
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGIS-AEDRENY--GLLDPGKYRYLN--------NGAGCK--REVQYWKKKYde 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 810 -IDAKAVRG--------IWSILAAIYHLGiaGVTKLGTGSTA-RTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAP 879
Cdd:cd14889 226 vCNAMDMVGfteqeevdMFTILAGILSLG--NITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKT---LTCTVTF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 880 NGGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQIC---TSSHTIASIMLIDTPGFQNPA-SCGQQVGA 955
Cdd:cd14889 301 TRGEQIQRHHTK----QQAEDARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFENFAvNRFEQACI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 956 TLADlrhnylqERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDKAPQnhvvrssqrdlrehdrrGMLW 1035
Cdd:cd14889 377 NLAN-------EQLQYFFNHHIFLMEQKEYKKE--GIDWKEITYKDNKPILDLFLNKPI-----------------GILS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1036 LLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAgpRQFVLHHLQGTnpVLYAVDGWVRHSREH--PGIRnavSLLQ 1113
Cdd:cd14889 431 LLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKS--PKFTVNHYAGK--VTYNASGFLEKNRDTipASIR---TLFI 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1114 DSSREEINRLYIGSLTRgsgamvfcgsfaglEGTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFV 1193
Cdd:cd14889 504 NSATPLLSVLFTATRSR--------------TGTLMPRAKLPQAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFV 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1194 HCYLLQHNagkhtkytangspsSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFG--LLAG 1271
Cdd:cd14889 570 RCIKPNHV--------------KVPGQLDSK-------YIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKilLCEP 628
|
730 740 750
....*....|....*....|....*....|....
gi 116008016 1272 DLASNKDvSVEQILavNELDVASYRIGPSQILFR 1305
Cdd:cd14889 629 ALPGTKQ-SCLRIL--KATKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
575-1289 |
4.49e-38 |
|
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: 154.75 E-value: 4.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKT-EDMPPHVYSLAQTAYRSLVETRRDQSLIF 652
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 653 MGRSGSGKSTSFKHALNYLALAAGAY----------NNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQT 722
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNqqqnnnnnnnNNSIEKDILTS-NPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 723 -GQIASASLQVLLPERQRAGRRLGHEH-SFHIMTRLLAGAAGLLQKELHLENITSEDSH---------PFISLSQKLEDR 791
Cdd:cd14906 160 dGKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYldarddvisSFKSQSSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 792 HRAAND----FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAA-RKASGLLGVNLEDL 866
Cdd:cd14906 240 HNNKTEsiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASlESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 867 SSAafgLTQPNAPNGGLSPSKSPTSDTGHewAWECLEALVIGLYSEALAAVVALINR-----------QICTSSHTIASI 935
Cdd:cd14906 320 KQA---LLNRNLKAGGRGSVYCRPMEVAQ--SEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 936 MLIDTPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVeiemdlasechPGPLISLIDKapqn 1015
Cdd:cd14906 395 GVLDIFGFENLSS------NSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI-----------PWSNSNFIDN---- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1016 hvvrSSQRDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYgdREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGW 1095
Cdd:cd14906 454 ----KECIELIEKKSDGILSLLDDECIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGD--VTYQTDGW 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1096 VRHSRehpgirnavsllqDSSREEINRLyigsLTRGSGAMVfcgsfAGLEGTQSLRRVSSIRRSfttagVKRNSIMLQVK 1175
Cdd:cd14906 526 LEKNR-------------DSLYSDVEDL----LLASSNFLK-----KSLFQQQITSTTNTTKKQ-----TQSNTVSGQFL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1176 FTVDGIIDTLRRTGTHFVHCylLQHNagkhtkytangspssaagqVSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPE 1255
Cdd:cd14906 579 EQLNQLIQTINSTSVHYIRC--IKPN-------------------QTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSY 637
|
730 740 750
....*....|....*....|....*....|....
gi 116008016 1256 SVPLLEFVRRFGLLAGDLasNKDVSVEQILAVNE 1289
Cdd:cd14906 638 RRDFNQFFSRYKCIVDMY--NRKNNNNPKLASQL 669
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
575-1305 |
9.17e-37 |
|
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: 150.57 E-value: 9.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYAS--------NLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRR 646
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 647 DQSLIFMGRSGSGKSTSFKHALNYLALAA---GAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLL-AGAAGLLQKELHLEnitsEDSHPFislsqkledrhraanDFMRTV 802
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCnAAVAAATQKSSAGE----GDPEST---------------DLRRIT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 803 QAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTA------ARKASGLLGVnlEDLSSaafGLTQP 876
Cdd:cd14887 222 AAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSvgceetAADRSHSSEV--KCLSS---GLKVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 877 NAPNGGL-SPSKSPTSDTGHEWAWECLEALVI------------------------GLYSEALAAVVALINRQICTSSHT 931
Cdd:cd14887 297 EASRKHLkTVARLLGLPPGVEGEEMLRLALVSrsvretrsffdldgaaaardaackNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 932 IAS--------------IMLIDTPGFQNPASCGQQvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLA 997
Cdd:cd14887 377 SESdsdedtpsttgtqtIGILDLFGFEDLRNHSKN---RLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 998 SECHPGPLISLIDKAPQNHV-------VRSSQRDLREHDRRGMLWLL-DEEAIYPNSNDDTFLERLFSHYGDREHHSLLR 1069
Cdd:cd14887 454 AFPFSFPLASTLTSSPSSTSpfsptpsFRSSSAFATSPSLPSSLSSLsSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1070 KCAGPR-------QFVLHHLQGTnpVLYAVDGWVRHSRehpgirnavsllqDSSREEINRLYIGsltrgsgamvfCGSFA 1142
Cdd:cd14887 534 YKNITPalsrenlEFTVSHFACD--VTYDARDFCRANR-------------EATSDELERLFLA-----------CSTYT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1143 GLEGTQSLRRVSSIRRsfttagvKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHTKytangspssaagqvs 1222
Cdd:cd14887 588 RLVGSKKNSGVRAISS-------RRSTLSAQFASQLQQVLKALQETSCHFIRC--VKPNRVQEAG--------------- 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1223 seeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRF-GLLAGDL--ASNKDVSVEQILAVNELDVASYRIGP 1299
Cdd:cd14887 644 ----IFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYeTKLPMALreALTPKMFCKIVLMFLEINSNSYTFGK 719
|
....*.
gi 116008016 1300 SQILFR 1305
Cdd:cd14887 720 TKIFFR 725
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
575-1305 |
3.92e-35 |
|
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: 144.80 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIH--TKAGPTLLVVNPMAPLSlysEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETR---RDQS 649
Cdd:cd14891 1 AGILHNLEERSKLDNQRpyTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 650 LIFMGRSGSGKSTSFKHALNYL--------ALAAGAYNNFINAEKVNALCT---------ILEAFGNTKTCLNSNATRMT 712
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLttravggkKASGQDIEQSSKKRKLSVTSLderlmdtnpILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 713 QLLSLDF-DQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedshPFISLSQ----K 787
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPE-----DFIYLNQsgcvS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 788 LEDRHRAANdFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGT--GSTARTQFANPTAARKASGLLGVNLED 865
Cdd:cd14891 233 DDNIDDAAN-FDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTseGEAEIASESDKEALATAAELLGVDEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 866 LSSAafgLTQP-------------NAPNGGLSPsksptsdtghewaweclEALVIGLYSEALAAVVALINRQICTSSHTI 932
Cdd:cd14891 312 LEKV---ITQReivtrgetftikrNAREAVYSR-----------------DAIAKSIYERLFLWIVQQINTSLGHDPDPL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 933 ASIMLIDTPGFQN--PASCGQQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLAS---EChpgplIS 1007
Cdd:cd14891 372 PYIGVLDIFGFESfeTKNDFEQ-------LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPdnrEC-----LD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1008 LIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGD-----REHHSLLRKCagprqFVLHHL 1082
Cdd:cd14891 440 LIASKPN-----------------GILPLLDNEARNPNPSDAKLNETLHKTHKRhpcfpRPHPKDMREM-----FIVKHY 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1083 QGTnpVLYAVDGWVRhsrehpgiRNAVSLLQDssreeinrlyIGSLTRGSGAmvFCGSFAGLEGTQSLRRVSSIRrsftt 1162
Cdd:cd14891 498 AGT--VSYTIGSFID--------KNNDIIPED----------FEDLLASSAK--FSDQMQELVDTLEATRCNFIR----- 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1163 aGVKRNSIMlqvkftvdgiidtlrRTGtHFVHCYLLQhnagkhtkytangspssaagqvsseeemvnvpllrsQLRGSQV 1242
Cdd:cd14891 551 -CIKPNAAM---------------KVG-VFDNRYVVD------------------------------------QLRCSGI 577
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1243 LEAARLHRLGFPESVPLLEFVRRFGLLAGD----LASNKDVS-VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14891 578 LQTCEVLKVGLPTRVTYAELVDVYKPVLPPsvtrLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1380-2067 |
9.84e-35 |
|
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: 145.70 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1380 NVHRTEEQLKTANEELlmlRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahiaTERLEAETAERL-KLEKEL 1458
Cdd:pfam01576 374 NLEKAKQALESENAEL---QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--------SERQRAELAEKLsKLQSEL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 GDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggvyKLKYERVARELEFTKRRLHTQHEHDLEQLVAL 1538
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ-------KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1539 KKH---LEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQ- 1614
Cdd:pfam01576 516 ERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQl 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1615 --AKERYGREKDVLQAEKFTLEQTLADTRLDLEF----KEEKLASLQRELEEMTfggGTEEEFA---------------- 1672
Cdd:pfam01576 596 vsNLEKKQKKFDQMLAEEKAISARYAEERDRAEAeareKETRALSLARALEEAL---EAKEELErtnkqlraemedlvss 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 ---------QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIK 1743
Cdd:pfam01576 673 kddvgknvhELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVR 752
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHEERTLLLREKHELERRLSSMEDR-DRVDRDAEEALNQklrrdLRKYKALLKDAQTQLERLKADTpgktli 1822
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQiDAANKGREEAVKQ-----LKKLQAQMKDLQRELEEARASR------ 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1823 RQLRNQLEDAEsarslamKARQTAEAELTEVQAMFDESHRARNDAEEranaahrDRAELQAQIEENEeelgelmKKYSAT 1902
Cdd:pfam01576 822 DEILAQSKESE-------KKLKNLEAELLQLQEDLAASERARRQAQQ-------ERDELADEIASGA-------SGKSAL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1903 VKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLD--NVENLGDPSMAMMS----KRLELRTKELESRL-ELEQA 1975
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEqlTTELAAERSTSQKSesarQQLERQNKELKAKLqEMEGT 960
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1976 TRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDM-----REEFHAVSSREQ--ESLTRRKDLEKKVE 2048
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqveDERRHADQYKDQaeKGNSRMKQLKRQLE 1040
|
730
....*....|....*....
gi 116008016 2049 QMESEgAALKNDLRLALQR 2067
Cdd:pfam01576 1041 EAEEE-ASRANAARRKLQR 1058
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
575-1269 |
4.88e-34 |
|
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: 141.58 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR--GC-------KTEDMPPHVYSLAQTAYRSLV-ET 644
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLlrsqgieSPQALGPHVFAIADRSYRQMMsEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 645 RRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA----------EKVNALCTILEAFGNTKTCLNSNATRMTQL 714
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 715 LSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQK--ELHLENITSEDSHPFISLS------- 785
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyEFHDGITGGLQLPNEFHYTgqggapd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 786 -QKLEDRhraaNDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTArtQFANPTAARKASGLLGV 861
Cdd:cd14908 241 lREFTDE----DGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqleFESKEEDGAAEIA--EEGNEKCLARVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 862 NLEDLSSAafgLTQPNAPNGGlspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQI-CTSSHTI-ASIMLID 939
Cdd:cd14908 315 DVDKLLRA---LTSKIIVVRG----KEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInWENDKDIrSSVGVLD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 940 TPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplislidkapqnh 1016
Cdd:cd14908 388 IFGFECFAH------NSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEwafIEFPDNQDC---------------- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1017 vvrssqRDLREHDRRGMLWLLDEEAIYP-NSNDDTFLERLFSHY---GDREHHSLLRKCAGPRQ-----FVLHHlqgtnp 1087
Cdd:cd14908 446 ------LDTIQAKKKGILTMLDDECRLGiRGSDANYASRLYETYlpeKNQTHSENTRFEATSIQktkliFAVRH------ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1088 vlYAvdGWVRHSREhpgirnavSLLQDSSREEInrlyigSLTRGSgamvfcgSFAglEGTqslrrvssirrsfttagvkr 1167
Cdd:cd14908 514 --FA--GQVQYTVE--------TTFCEKNKDEI------PLTADS-------LFE--SGQ-------------------- 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1168 nsimlQVKFTVDGIIDTLRRTGTHFVHCYllqhnagkhtkytangSPSSAAgqvssEEEMVNVPLLRSQLRGSQVLEAAR 1247
Cdd:cd14908 547 -----QFKAQLHSLIEMIEDTDPHYIRCI----------------KPNDAA-----KPDLVTRKRVTEQLRYGGVLEAVR 600
|
730 740
....*....|....*....|..
gi 116008016 1248 LHRLGFPESVPLLEFVRRFGLL 1269
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRML 622
|
|
| PDZ_MYO18-like |
cd06747 |
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ... |
337-426 |
2.35e-33 |
|
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467229 [Multi-domain] Cd Length: 90 Bit Score: 124.35 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 337 QLVIRRQksPRQDFGFSLRKAICLDRTESLTSPIFRPVIFAEPGAGGGATGL--LPGDRLIKVNGTPVGELPREIIIEMI 414
Cdd:cd06747 1 EITLKRQ--PTGDFGFSLRRGTIVERGPDDGQELKRTVHFAEPGAGTKNLATglLPGDRLIEVNGVNVENASRDEIIEMI 78
|
90
....*....|..
gi 116008016 415 RNSGEAVTVEVQ 426
Cdd:cd06747 79 RKSGDTVTLKVQ 90
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
575-866 |
5.48e-32 |
|
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: 135.12 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGC-KTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDApDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAA-GAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQV 732
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKsGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 733 LLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFISLS----QKLEDRhraaNDFMRTVQAFETL 808
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGL---KEYKFLNPKcldvPGIDDV----ADFEEVLESLKSM 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 809 NIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDL 866
Cdd:cd14876 233 GLTEEQIDTVFSIVSGVLLLGnvkITGKTEQGVDDAAAISNESLEVFKEACSLLFLDPEAL 293
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
576-1280 |
8.28e-32 |
|
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: 134.28 E-value: 8.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYS----EKVVSMF--RGCKTED-----MPPHVYSLAQTAYRSLVE 643
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLpGLYSsdtmAKYLLSFeaRSSSTRNkgsdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 644 TRR----DQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFIN----------AEKVNALCTILEAFGNTKTCLNSNAT 709
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYLA-QAGDNNLAASvsmgkstsgiAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 710 RMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAgllqkelhlenitsedshpfislsqkle 789
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGAS---------------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 790 DRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG--IAGVTKLGTGSTARTQFANPT--AARKASG-LLGVNLE 864
Cdd:cd14900 213 EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGnlTFEHDENSDRLGQLKSDLAPSsiWSRDAAAtLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 865 DLSSAafgLTQPNAPNGGLSPSKSPTSDTghewAWECLEALVIGLYSEALAAVVALINR-----QICTSSHTIASIMLID 939
Cdd:cd14900 293 KLEKA---LSVRRIRAGTDFVSMKLSAAQ----ANNARDALAKALYGRLFDWLVGKMNAflkmdDSSKSHGGLHFIGILD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 940 TPGFQN-PASCGQQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQn 1015
Cdd:cd14900 366 IFGFEVfPKNSFEQ-------LCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQDC-----VNLISQRPT- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1016 hvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGW 1095
Cdd:cd14900 433 ----------------GILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGH--VEYSTDGF 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1096 VRHSRehpgirnavsllqDSSREEINRLYigsltrgsgamVFCGSFaglegtqslrrvssirrsfttagvkrnsimlqvK 1175
Cdd:cd14900 495 LEKNK-------------DVLHQEAVDLF-----------VYGLQF---------------------------------K 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1176 FTVDGIIDTLRRTGTHFVHCylLQHNagkhtkytangspSSAAGQVSSEEEMVNvpllrsQLRGSQVLEAARLHRLGFPE 1255
Cdd:cd14900 518 EQLTTLLETLQQTNPHYVRC--LKPN-------------DLCKAGIYERERVLN------QLRCNGVMEAVRVARAGFPI 576
|
730 740
....*....|....*....|....*
gi 116008016 1256 SVPLLEFVRRFGLLAGDLASNKDVS 1280
Cdd:cd14900 577 RLLHDEFVARYFSLARAKNRLLAKK 601
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
575-869 |
2.42e-31 |
|
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: 133.02 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR---GCKTEDMPPHVYSLAQTAYRSLVETRRDQSLI 651
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 652 FMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCtILEAFGNTKTCLNSNATRMTQLLSLDF-DQTGQIASASL 730
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNC-ILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 731 QVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedSHPFisLSQKL-EDRHRAANDFMRT-----VQA 804
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLC---AHRY--LNQTMrEDVSTAERSLNREklavlKQA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 805 FETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTqfANPTAARKASGLLGVNLEDLSSA 869
Cdd:cd14878 235 LNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFV--SDLQLLEQVAGMLQVSTDELASA 297
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
575-1270 |
2.71e-31 |
|
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: 133.05 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGC-KTEDMPPHVYSLAQTAYR---SLVETRrDQS 649
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRnvkSLIEPV-NQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 650 LIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAL-------CTILEAFGNTKTCLNSNATRMTQLLSLDFDQT 722
Cdd:cd14880 80 IVVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIeqrilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 723 GQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPfiSLSQKLEDrhraaNDFMRTV 802
Cdd:cd14880 160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLP--NPERNLEE-----DCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 803 QAFETLNIDAKAVRGIWSILAAIYHLGiagvtklgtgstaRTQFANPTAARKASGLLGVNLEDLSSAAFGLTQPNAP--- 879
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLG-------------NIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHlle 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 880 ---------NGGLSPSKSPTSDTGHEWAWECLEALViglYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQN-PAS 948
Cdd:cd14880 300 tlqirtiraGKQQQVFKKPCSRAECDTRRDCLAKLI---YARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESfPEN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 949 cgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEmdlasechpgpLISLIDKapQNHVvrssqrDLREH 1028
Cdd:cd14880 377 -------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWS-----------FINYQDN--QTCL------DLIEG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1029 DRRGMLWLLDEEAIYPNSND----DTFLERLFSHYGDREHHSLLRKcagpRQFVLHHLQGtnPVLYAVDGWVRHSREhPG 1104
Cdd:cd14880 431 SPISICSLINEECRLNRPSSaaqlQTRIESALAGNPCLGHNKLSRE----PSFIVVHYAG--PVRYHTAGLVEKNKD-PV 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1105 IRNAVSLLQDSSREEINRLyigsltrgsgamvfcgsFAGLEGTQSLRRVSSIRRSfttAGVkrnSIMLQVKFTVDGIIDT 1184
Cdd:cd14880 504 PPELTRLLQQSQDPLLQKL-----------------FPANPEEKTQEEPSGQSRA---PVL---TVVSKFKASLEQLLQV 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1185 LRRTGTHFVHCylLQHNAGkhtkytangspssAAGQVSSEEEMVnvpllrSQLRGSQVLEAARLHRLGFPESVPLLEFVR 1264
Cdd:cd14880 561 LHSTTPHYIRC--IKPNSQ-------------CQAQTFLQEEVL------SQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
....*.
gi 116008016 1265 RFGLLA 1270
Cdd:cd14880 620 RYKLLR 625
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
575-1305 |
9.41e-30 |
|
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: 127.82 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYsekvVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLaLAAGAYNNFINaekvNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQ 731
Cdd:cd14937 77 ESGSGKTEASKLVIKYY-LSGVKEDNEIS----NTLWDsnfILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 732 VLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhleNITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNI- 810
Cdd:cd14937 152 IFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKY---KIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMh 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 811 DAKavRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDL---------SSAAFGLTQPNA 878
Cdd:cd14937 229 DMK--DDLFLTLSGLLLLGnveYQEIEKGGKTNCSELDKNNLELVNEISNLLGINYENLkdclvftekTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 879 PNGGLSPSKSPTSDtghewaweclealvigLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQnpascgQQVGATLA 958
Cdd:cd14937 307 VEESVSICKSISKD----------------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKNSLE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQElveiemdlasechpGPLISLIDKAPQNHVVrssqrDLREhDRRGMLWLLD 1038
Cdd:cd14937 365 QLLINIANEEIHSIYLYIVYEKETELYKAE--------------DILIESVKYTTNESII-----DLLR-GKTSIISILE 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGpRQFVLHHLqgTNPVLYAVDGWVRHSREHPGiRNAVSLLQDSSRE 1118
Cdd:cd14937 425 DSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDIN-KNFVIKHT--VSDVTYTITNFISKNKDILP-SNIVRLLKVSNNK 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1119 EINRLYigsltrgsgamvfcgsfAGLEGTQSLRRvssirrsfttagvkRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylL 1198
Cdd:cd14937 501 LVRSLY-----------------EDVEVSESLGR--------------KNLITFKYLKNLNNIISYLKSTNIYFIKC--I 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1199 QHNAGKhtkytangspssaagqvssEEEMVNVPLLRSQLRGSQVLEAARLhRLGFPESVPLLEFVRRFGLLagDLASNKD 1278
Cdd:cd14937 548 KPNENK-------------------EKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYL--DYSTSKD 605
|
730 740 750
....*....|....*....|....*....|..
gi 116008016 1279 VSVEQ-----ILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14937 606 SSLTDkekvsMILQNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
575-1305 |
7.91e-27 |
|
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: 118.84 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTE-----DMPPHVYSLAQTAYRSLVETRRDQ 648
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 649 SLIFMGRSGSGKSTSFKHALNYLalaagAYNNFINAEKVNALC----TILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQ 724
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFF-----AYGHSTSSTDVQSLIlgsnPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 725 IASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITS---------------EDSHPFISLSQKLE 789
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESynflnaskcydapgiDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 790 D--RHRAANDFMRTVQAFETL-NIDAKAvrgiwsilaaiyhlgiagVTKLGTGSTARtqFANPTAARKASGLLGVNLEDL 866
Cdd:cd14886 236 KlfSKNEIDSFYKCISGILLAgNIEFSE------------------EGDMGVINAAK--ISNDEDFGKMCELLGIESSKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 867 SSAAfgLTQPNAPNGglspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ-- 944
Cdd:cd14886 296 AQAI--ITKVVVINN-----ETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEff 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 945 --NpascgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASEchPGPLISLIDKAPQnhvvrssq 1022
Cdd:cd14886 369 erN----------TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTD--NSNVLAVFDKPNL-------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1023 rdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSReH 1102
Cdd:cd14886 429 ---------SIFSFLEEQCLIQTGSSEKFTSSCKSKIKN---NSFIPGKGSQCNFTIVHTAAT--VTYNTEEFVDKNK-H 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1103 PGIRNAVSLLQDSsreeinrlyigsltrgsgamvfcgsfaglegTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGII 1182
Cdd:cd14886 494 KLSVDILELLMGS-------------------------------TNPIVNKAFSDIPNEDGNMKGKFLGSTFQLSIDQLM 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1183 DTLRRTGTHFVHCylLQHNAGKHTKYTANGSpssaagqvsseeemvnvplLRSQLRGSQVLEAAR-LHRlGFPESVPLLE 1261
Cdd:cd14886 543 KTLSATKSHFIRC--IKTNQDKVPNKYETKS-------------------VYNQLISLSIFESIQtIHR-GFAYNDTFEE 600
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 116008016 1262 FVRRFGLL------AGDLASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14886 601 FFHRNKILishnssSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
578-1195 |
1.40e-24 |
|
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: 111.99 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 578 LHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLY----------SEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRD 647
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 648 QSLIFMGRSGSGKSTSFKHALNYL------------ALAAGAYNNFINAEKVNALcTILEAFGNTKTCLNSNATRMTQLL 715
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLceigdeteprpdSEGASGVLHPIGQQILHAF-TILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 716 SLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAG--LLQKELHLENITSEdshpFISLSQKLEDRHR 793
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNKCVNE----FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 794 ---AANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG--------IAGVTKLGTGSTARTQFANPTAARKASGLLGVN 862
Cdd:cd14893 239 falDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdpEGGKSVGGANSTTVSDAQSCALKDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 863 LEDLSSAA----FGLTQPNAPNGGLSPSkSPTSDTGHEwAWECLEALVIGLYS-------EALAAVVALINRQICTSSHT 931
Cdd:cd14893 319 LLEVEPVVldnyFRTRQFFSKDGNKTVS-SLKVVTVHQ-ARKARDTFVRSLYEslfnflvETLNGILGGIFDRYEKSNIV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 932 IAS--IMLIDTPGFQNPAScgQQVGatLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASEchpgpliSLI 1009
Cdd:cd14893 397 INSqgVHVLDMVGFENLTP--SQNS--FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTVN-------SNV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1010 D-KAPQNHVVrssqrDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFShyGDREHHSLLRKCAG----------PRQ-- 1076
Cdd:cd14893 466 DiTSEQEKCL-----QLFEDKPFGIFDLLTENCKVRLPNDEDFVNKLFS--GNEAVGGLSRPNMGadttneylapSKDwr 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1077 --FVLHHLQGTnpVLYAVDGWvrHSREHPGIRNAVSLLQDSSREEINRlyigslTRGSGAMVFCGSFAGLEGTQSLRRVS 1154
Cdd:cd14893 539 llFIVQHHCGK--VTYNGKGL--SSKNMLSISSTCAAIMQSSKNAVLH------AVGAAQMAAASSEKAAKQTEERGSTS 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116008016 1155 S-IRRSFTTAGVKRN---SIMLQVKFTVDGIIDTLRRTGTHFVHC 1195
Cdd:cd14893 609 SkFRKSASSARESKNitdSAATDVYNQADALLHALNHTGKNFLVC 653
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
576-829 |
3.24e-24 |
|
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: 110.70 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKT-EDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALC------------------TILEAFGNTKTCLNSNATRMT 712
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrRLPTNLNDQEEDNIHNeentdyqfnmsemlkhvnVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 713 QLLSLDFDQTgQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSedshpfISLSQKLEDRH 792
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN------YSMLNNEKGFE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 116008016 793 RAANDFMRTVQAFETLNI---DAKAVRGIWSILAAIYHLG 829
Cdd:cd14938 235 KFSDYSGKILELLKSLNYifdDDKEIDFIFSVLSALLLLG 274
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
575-1269 |
3.25e-24 |
|
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: 110.67 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYAS-NLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDM-PPHVYSLAQTAYRSL-VETRRDQSLI 651
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 652 FMGRSGSGKSTSFKHALNYLA-LAAGAYNNFIN---AEKVNALCT----ILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGqLSYMHSSNTSQrsiADKIDENLKwsnpVMESFGNARTVRNDNSSRFGKYIKLYFDPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 724 QIASASLQV-LLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKEL-HLEniTSED------SHPFISL---SQKLEDrh 792
Cdd:cd14875 161 GVMVGGQTVtYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLK--TAQDykclngGNTFVRRgvdGKTLDD-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 793 raANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLgiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFG 872
Cdd:cd14875 237 --AHEFQNVRHALSMIGVELETQNSIFRVLASILHL---MEVEFESDQNDKAQIADETPFLTACRLLQLDPAKLRECFLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 873 LTQPNApnggLSPSKSPTSDTGHEWAWeClEALVIGLYSEALAAVVALINRQI-CTSSHTIAsimLIDTPGFQNPASCGq 951
Cdd:cd14875 312 KSKTSL----VTILANKTEAEGFRNAF-C-KAIYVGLFDRLVEFVNASITPQGdCSGCKYIG---LLDIFGFENFTRNS- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 952 qvgatLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKApqnhvvrssqrdlreh 1028
Cdd:cd14875 382 -----FEQLCINYANESLQNHYNKYTFINDEEECRREGIQipkIEFPDNSEC-----VNMFDQK---------------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1029 dRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhpGIRNA 1108
Cdd:cd14875 436 -RTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPKSTIPNQFGVNHYAAF--VNYNTDEWLEKNTD--ALKED 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSSREEinrlYIGSLTrgsgamvfcgsfaglegtqSLRRVSSiRRSFTTAgvkrnsIMLQVKFTvdGIIDTLRRT 1188
Cdd:cd14875 511 MYECVSNSTDE----FIRTLL-------------------STEKGLA-RRKQTVA------IRFQRQLT--DLRTELEST 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCyllqhnagkhTKYTANGSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd14875 559 ETQFIRC----------IKPNMEASPS-----------FLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYL 617
|
.
gi 116008016 1269 L 1269
Cdd:cd14875 618 I 618
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1387-2073 |
1.11e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.76 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1387 QLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVK 1466
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1467 NLQETTEKLEMELICAKSDLNgISEDEDAENEDgvgggvyklKYERVARELEftkrrlhtQHEHDLEQLVALKKHLEMKL 1546
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLD-ELAEELAELEE---------KLEELKEELE--------SLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1547 SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKdvL 1626
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE--L 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1627 QAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAK 1706
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1707 LRLEMTLETM-----------RKEARRESQQRDEELE-------EVRGNGYKKIKALECQLETEHEERTLLLRE----KH 1764
Cdd:TIGR02168 533 EGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvkfDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1765 ELERRLSSMEDRDRVDRDAEEALNQ--KLRRDLR---------------------------KYKALLKDAQTQLERLKAD 1815
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELakKLRPGYRivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1816 -TPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGE 1894
Cdd:TIGR02168 693 iAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1895 LMKKYSATVKQLNT--EQINVSEAEFK-----LNEMEAERNNLKEQVAELQHRLDNVENlgdpSMAMMSKRLElrtkELE 1967
Cdd:TIGR02168 773 AEEELAEAEAEIEEleAQIEQLKEELKalreaLDELRAELTLLNEEAANLRERLESLER----RIAATERRLE----DLE 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1968 SRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKV 2047
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740
....*....|....*....|....*.
gi 116008016 2048 EQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
576-1281 |
2.03e-23 |
|
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: 107.29 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEdmpPHVYSLAQTAYRSLVeTRRDQSLIFMGR 655
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE---PHVYDVAEASVQDLL-VHGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 656 SGSGKSTSFKHALNYLaLAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDqtGQIASASLQVLLP 735
Cdd:cd14898 78 SGSGKTENAKLVIKYL-VERTASTTSIE-KLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 736 ERQRAGRRLGHEHSFHIMTRLLAgaagllQKELHLENitseDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIdaKAV 815
Cdd:cd14898 154 EKSRVTHHEKGERNFHIFYQFCA------SKRLNIKN----DFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGI--ANF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 816 RGIWSILAAIYHLGI-----AGVTKLgTGSTARTQFANptaarkasgLLGVNLEDLSSAAFgltqpnapnGGLSPSKSPT 890
Cdd:cd14898 222 KSIEDCLLGILYLGSiqfvnDGILKL-QRNESFTEFCK---------LHNIQEEDFEESLV---------KFSIQVKGET 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 891 SDTGH--EWAWECLEALVIGLYSEALAAVVALINRqiCTSSHTIASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQER 968
Cdd:cd14898 283 IEVFNtlKQARTIRNSMARLLYSNVFNYITASINN--CLEGSGERSISVLDIFGFEIFESNG------LDQLCINWTNEK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 969 LQMLFHHTTLVAPRDRYAQELVEiemdlasechpgplISLIDKAPQNHVVRSSQRDLrehdrrGMLWLLDEEAIYPNSND 1048
Cdd:cd14898 355 IQNDFIKKMFRAKQGMYKEEGIE--------------WPDVEFFDNNQCIRDFEKPC------GLMDLISEESFNAWGNV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1049 DTFLERLFSHYGDRehhslLRKCAGPRQFVLHHlqgTNPVLYAVDGWVrhsrehpgirnavsllqDSSREEINRLYIGSL 1128
Cdd:cd14898 415 KNLLVKIKKYLNGF-----INTKARDKIKVSHY---AGDVEYDLRDFL-----------------DKNREKGQLLIFKNL 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1129 trgsgamvfcgsfaGLEGTQSlrrvssirrsfttagvkRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHTKy 1208
Cdd:cd14898 470 --------------LINDEGS-----------------KEDLVKYFKDSMNKLLNSINETQAKYIKC--IRPNEECRPW- 515
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1209 tangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDVSV 1281
Cdd:cd14898 516 ------------------CFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFEVVDYRK 570
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
575-1274 |
5.66e-23 |
|
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: 106.49 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFrgcktedmppHVYSLAQTAYRSLVE-TRRDQSLIFM 653
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSmSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 654 GRSGSGKSTSFKHALNYLALAAgayNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFdQTGQIASASLQVL 733
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQP---KSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 734 LP-ERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ--KLEDRHRAANDFMRTVQAFETLNI 810
Cdd:cd14874 147 VPlEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI-----KGLQKFFYINQgnSTENIQSDVNHFKHLEDALHVLGF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 811 DAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTART-QFANPTAARKASGLLGVNLEDLSSAafgltqpnapnggLSPSKS 888
Cdd:cd14874 222 SDDHCISIYKIISTILHIGnIYFRTKRNPNVEQDVvEIGNMSEVKWVAFLLEVDFDQLVNF-------------LLPKSE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 889 PTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTiASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQER 968
Cdd:cd14874 289 DGTTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEFLINSVNER 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 969 LQMLFHHTTLVAPRDRYAQELVEIEMDLASECHPGPLISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSND 1048
Cdd:cd14874 362 IENLFVKHSFHDQLVDYAKDGISVDYKVPNSIENGKTVELLFKKPY-----------------GLLPLLTDECKFPKGSH 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1049 DTFLERLFSHYGDREHHSLLRkcAGPR-QFVLHHLQGTnpVLYAVDGWVRHSREHPGIrNAVSLLQDSSREEINRLYigs 1127
Cdd:cd14874 425 ESYLEHCNLNHTDRSSYGKAR--NKERlEFGVRHCIGT--TWYNVTDFFSRNKRIISL-SAVQLLRSSKNPIIGLLF--- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1128 ltrgsgamvfcgsfaglegtqslrrvssirRSFTtaGVKRNSIMLQVKFTVDG---IIDTLRRTGTHFVHCyLLQHNAGK 1204
Cdd:cd14874 497 ------------------------------ESYS--SNTSDMIVSQAQFILRGaqeIADKINGSHAHFVRC-IKSNNERQ 543
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 1205 HTKYtangspssaagqvsseeemvNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFG-LLAGDLA 1274
Cdd:cd14874 544 PKKF--------------------DIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRcLLPGDIA 594
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
575-1096 |
1.47e-22 |
|
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: 105.37 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKT-------EDMPPHVYSLAQTAYRSLVETRR 646
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLkELYDQDVMNVYLHKKSnsaasaaPFPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 647 DQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQ----- 721
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 722 ----TGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAA----------------GLLQ--KELHLENITSEDSH 779
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSdedlarrnlvrncgvyGLLNpdESHQKRSVKGTLRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 780 PFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGiagvtklgtgstartqfanPTAARKASGLL 859
Cdd:cd14884 241 GSDSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG-------------------NRAYKAAAECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 860 GVNLEDLSSaafgLTQPNAPNGGLSPSKSPTSDtghEWAWECLEALVIGLYSEALAAVVALINR--------------QI 925
Cdd:cd14884 302 QIEEEDLEN----VIKYKNIRVSHEVIRTERRK---ENATSTRDTLIKFIYKKLFNKIIEDINRnvlkckekdesdneDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 926 CTSSHTIASIMliDTPGFQNPAscgqqvGATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASECHpgPL 1005
Cdd:cd14884 375 YSINEAIISIL--DIYGFEELS------GNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYS--DT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1006 ISLIDKAPQN--HVVRSSQRDLREHDRRGMLWLLDEEAIYpnsnddtFLERLFShYG-----DREHHSLLRKCAgPRQFV 1078
Cdd:cd14884 445 LIFIAKIFRRldDITKLKNQGQKKTDDHFFRYLLNNERQQ-------QLEGKVS-YGfvlnhDADGTAKKQNIK-KNIFF 515
|
570
....*....|....*...
gi 116008016 1079 LHHLQGtnPVLYAVDGWV 1096
Cdd:cd14884 516 IRHYAG--LVTYRINNWI 531
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1385-2053 |
2.24e-22 |
|
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: 105.64 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEellmLRAKLEKIecdRSEVKAENQKLEAKLSELT--VDLAEERSTA----------HIA--TERLEAETAE 1450
Cdd:pfam01576 46 QEQLQAETE----LCAEAEEM---RARLAARKQELEEILHELEsrLEEEEERSQQlqnekkkmqqHIQdlEEQLDEEEAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1451 RLKLEKELGDQTNKVKNLQETT-------EKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRR 1523
Cdd:pfam01576 119 RQKLQLEKVTTEAKIKKLEEDIllledqnSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1524 lhtqHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQ 1603
Cdd:pfam01576 199 ----EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1604 SLQDAVRQERQAKERYGREK----DVLQAEKFTLEQTLADTRLDLEFK---EEKLASLQRELEEMTfgGGTEEEFAQLRR 1676
Cdd:pfam01576 275 ELQEDLESERAARNKAEKQRrdlgEELEALKTELEDTLDTTAAQQELRskrEQEVTELKKALEEET--RSHEAQLQEMRQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1677 SKNETerrakeqeeeLDEMAGQIQLLEQAKLRLEMTLETMRKEaRRESQQRDEELEEVRGNGYKKIKALECQLETEHEER 1756
Cdd:pfam01576 353 KHTQA----------LEELTEQLEQAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1757 TLLLREKHELERRLSSMEDR-DRVDRDAEEALNQ--KLRRDLRKYKALLKDAQTQL-ERLKADTPGKTLIRQ-------L 1825
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSElESVSSLLNEAEGKniKLSKDVSSLESQLQDTQELLqEETRQKLNLSTRLRQledernsL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1826 RNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYS----- 1900
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNrlqqe 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1901 ---ATVKQLNTEQI--NVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRT---KELE----- 1967
Cdd:pfam01576 582 lddLLVDLDHQRQLvsNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALeakEELErtnkq 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1968 -----------------SRLELEQATRArLEVQVNRHKEALEKLQNEVTqskmremQAQDVIKKSQKSLRDMREEF-HAV 2029
Cdd:pfam01576 662 lraemedlvsskddvgkNVHELERSKRA-LEQQVEEMKTQLEELEDELQ-------ATEDAKLRLEVNMQALKAQFeRDL 733
|
730 740
....*....|....*....|....
gi 116008016 2030 SSREQESLTRRKDLEKKVEQMESE 2053
Cdd:pfam01576 734 QARDEQGEEKRRQLVKQVRELEAE 757
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
576-1101 |
3.01e-22 |
|
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: 104.40 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRgcKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSKYLR-DYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFI----SLSQKLEDRHRAandFMRTVQAFETLNI 810
Cdd:cd14905 159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDI---NSYHYLnqggSISVESIDDNRV---FDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 811 DAKAVRGIWSILAAIYHLGIAGVTKlgtgSTARTQFANPTAarkasgllgvnLEDLS-SAAFGLTQpnAPNGGLSPSKSP 889
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQ----KNGKTEVKDRTL-----------IESLShNITFDSTK--LENILISDRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 890 TSDtghewAWECLEALVIGLYSEALAAVVALINRQICTS--SHTIAsimLIDTPGFQNPASCGQQvgatlaDLRHNYLQE 967
Cdd:cd14905 296 VNE-----AVENRDSLARSLYSALFHWIIDFLNSKLKPTqySHTLG---ILDLFGQESSQLNGYE------QFSINFLEE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 968 RLQMLFHHTTLVAPRDRYAQELVeiemdlasechpgPLISLIDKAPQNHVVRSSQRdlrehdrrgMLWLLDEEAIYPNSN 1047
Cdd:cd14905 362 RLQQIYLQTVLKQEQREYQTERI-------------PWMTPISFKDNEESVEMMEK---------IINLLDQESKNINSS 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 116008016 1048 DDTFLERLfSHYGDReHHSLLRKcagPRQFVLHHLQGTnpVLYAVDGWVRHSRE 1101
Cdd:cd14905 420 DQIFLEKL-QNFLSR-HHLFGKK---PNKFGIEHYFGQ--FYYDVRGFIIKNRD 466
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
576-1280 |
6.62e-22 |
|
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: 102.90 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRgCKTE-DMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYR-CKSRsDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 655 RSGSGKSTSFKHALNYLALAAGAYNNfiNAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLGDGNRG--ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 735 PERQRAGRRLGHEHSFHIMTRLLAG--AAGLLqKELHLEN------ITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFE 806
Cdd:cd14882 159 LEKLRVSTTDGNQSNFHIFYYFYDFieAQNRL-KEYNLKAgrnyryLRIPPEVPPSKLKYRRDDPEGNVERYKEFEEILK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 807 TLNIDAKAVRGIWSILAAIYHLGIAGVTKlGTGStarTQFANPTAARKASGLLGVnleDLSSAAFGLTQPNAPNGGLSPS 886
Cdd:cd14882 238 DLDFNEEQLETVRKVLAAILNLGEIRFRQ-NGGY---AELENTEIASRVAELLRL---DEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 887 KSPTSDTghewAWECLEALVIGLYSEALAAVVALIN------RQICTSSHtiaSIMLIDTPGFQnpasCGQQVGatLADL 960
Cdd:cd14882 311 RKHTTEE----ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKY---SISIHDMFGFE----CFHRNR--LEQL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 961 RHNYLQErlQMLFHhttlvaprdrYAQELVEIEMdLASECHPGPLISLidkapqNHVVRSSQRDLREHDRRGMLWLLDeE 1040
Cdd:cd14882 378 MVNTLNE--QMQYH----------YNQRIFISEM-LEMEEEDIPTINL------RFYDNKTAVDQLMTKPDGLFYIID-D 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1041 AIYPNSNDDTFLERLfshygdREHHSLLRKCAGPRQFVLHHLQGTnpVLYavdgwvrHSREhpgirnavslLQDSSREEI 1120
Cdd:cd14882 438 ASRSCQDQNYIMDRI------KEKHSQFVKKHSAHEFSVAHYTGR--IIY-------DARE----------FADKNRDFV 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1121 NRLYIGSLTRGSGAMVfcgsfaglegtQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIidtlRRTGTHFVHCYLlqh 1200
Cdd:cd14882 493 PPEMIETMRSSLDESV-----------KLMFTNSQVRNMRTLAATFRATSLELLKMLSIGA----NSGGTHFVRCIR--- 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1201 nagKHTKYTANGSPSsaagqvsseeEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDVS 1280
Cdd:cd14882 555 ---SDLEYKPRGFHS----------EVV-----RQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT 616
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1563-2104 |
7.52e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1563 WKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRL 1642
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1643 DLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARR 1722
Cdd:COG1196 310 RRRELEERLEELEEELAE------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1723 ESQQRDEELEEVRgNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALL 1802
Cdd:COG1196 384 LAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1803 KDAQTQLERLKAdtpGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRAR----------------ND 1866
Cdd:COG1196 463 ELLAELLEEAAL---LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1867 AEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNT-EQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVE 1945
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1946 NLgdpsmammSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREE 2025
Cdd:COG1196 620 DT--------LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2026 FHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLR 2104
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1387-2045 |
9.87e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1387 QLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVK 1466
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1467 NLQETTEKLEMELicaksdlngisededaenedgvgggvyklkyervareleftkrrlhTQHEHDLEQLVALKKHLEMKL 1546
Cdd:COG1196 313 ELEERLEELEEEL----------------------------------------------AELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1547 SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVL 1626
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1627 QAEKFTLEQTLADTRLDLEFKEEKLASLQRELEemtfgggteeefaQLRRSKNETERRAKEQEEELDEMAGQIQlleqak 1706
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEE-------------ALLELLAELLEEAALLEAALAELLEELA------ 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1707 lrlemtletmRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKhelerrlssmedrdRVDRDAEEA 1786
Cdd:COG1196 488 ----------EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA--------------AYEAALEAA 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1787 LNQKLRRDLRkykALLKDAQTQLERLKADTPGK----TLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAM---FDE 1859
Cdd:COG1196 544 LAAALQNIVV---EDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1860 SHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEfklNEMEAERNNLKEQVAELQH 1939
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE---AELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1940 RLDNVENLgdpsmAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSL 2019
Cdd:COG1196 698 ALLAEEEE-----ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
650 660 670
....*....|....*....|....*....|....*..
gi 116008016 2020 RDMR-----------EEFHAVSSREQESLTRRKDLEK 2045
Cdd:COG1196 773 EREIealgpvnllaiEEYEELEERYDFLSEQREDLEE 809
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1507-2057 |
1.02e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1507 KLKYERVARELEFTKRRLHtQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQvvgqwkrKAQKMTNEMNDLRMLLEEQNA 1586
Cdd:COG1196 217 ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1587 RNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfggg 1666
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE------ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1667 TEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALE 1746
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1747 CQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKykALLKDAQTQLERLKADTPGKTLIRQLR 1826
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1827 NQL------------------EDAESARSLAMKARQTAEAELTEVQAMFDESHRA--------RNDAEERANAAHRDRAE 1880
Cdd:COG1196 517 AGLrglagavavligveaayeAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1881 LQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMS---- 1956
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalle 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1957 --KRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQ 2034
Cdd:COG1196 677 aeAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580
....*....|....*....|...
gi 116008016 2035 ESLTRRKDLEKKVEQMESEGAAL 2057
Cdd:COG1196 757 PEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1400-2062 |
2.37e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.99 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1400 AKLEKIECDRSEVKAENQKLEAKLSELTVDLaeERstahIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEmel 1479
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQL--ER----LRREREKAERYQALLKEKREYEGYELLKEKEALERQKE--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1480 icaksdlNGISEDEDAENEdgvgggVYKLKYERVARELEftkrrlhtqhehdLEQLVALKKHLEMKLSDAYEEvvEQRQV 1559
Cdd:TIGR02169 241 -------AIERQLASLEEE------LEKLTEEISELEKR-------------LEEIEQLLEELNKKIKDLGEE--EQLRV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1560 vgqwKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLAD 1639
Cdd:TIGR02169 293 ----KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1640 TRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETER-------RAKEQEEELDEMAGQIQLLEQAKLRLEMT 1712
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDY------REKLEKLKREINELKReldrlqeELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1713 LETMRKEARrESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLR 1792
Cdd:TIGR02169 443 KEDKALEIK-KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1793 ------RDLRKYK------------ALLK--------DAQTQLERLKADTPGK------TLIRQLRNQL----------- 1829
Cdd:TIGR02169 522 gvhgtvAQLGSVGeryataievaagNRLNnvvveddaVAKEAIELLKRRKAGRatflplNKMRDERRDLsilsedgvigf 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1830 -------------------------EDAESARSLAMKAR----------------------------------------- 1843
Cdd:TIGR02169 602 avdlvefdpkyepafkyvfgdtlvvEDIEAARRLMGKYRmvtlegelfeksgamtggsraprggilfsrsepaelqrlre 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1844 ---------QTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVS 1914
Cdd:TIGR02169 682 rleglkrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1915 EAEFKLNEMEAERNNLKEQVAEL-----QHRLDNVENLGDpSMAMMSKRLELRTKELESRLELEQATRARLEvqvnrhkE 1989
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELS-KLEEEVSRIEARLREIEQKLNRLTLEKEYLE-------K 833
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1990 ALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLR 2062
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
576-1271 |
1.18e-19 |
|
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: 95.95 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 576 SVLHCLRQRYASNLIHTKAGPTLLVVNPM----APLSLYSEKVVSMFrgcktedmpPHVYSLAQTAYRSLVETRRDQSLI 651
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYrdvgNPLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 652 FMGRSGSGKSTSFKHALNYL-ALAAG-----AYNNfinaekVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQtGQI 725
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLfDVAGGgpetdAFKH------LAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHpFISLSQKLEDRHRAANDFmrtvQAF 805
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLR-YLSHGDTRQNEAEDAARF----QAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 806 ETlnidAKAVRGI-----WSILAAIYHLGiagvtklgtgstaRTQFANP----------TAARKASGLLGVnledlSSAA 870
Cdd:cd14881 221 KA----CLGILGIpfldvVRVLAAVLLLG-------------NVQFIDGgglevdvkgeTELKSVAALLGV-----SGAA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 871 F--GLTQPNAPNGGlSPSKSPTSDtghEWAWECLEALVIGLYSEALAAVVALIN--RQICTSSHTIA---SIMLIDTPGF 943
Cdd:cd14881 279 LfrGLTTRTHNARG-QLVKSVCDA---NMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 944 QNPAScgqqvgATLADLRHNYLQERLQMlFHHT-----TLVAPRDRYAQelVEIEMDLASEChpgPLISLIdkapqnhvv 1018
Cdd:cd14881 355 EDPKP------SQLEHLCINLCAETMQH-FYNThifksSIESCRDEGIQ--CEVEVDYVDNV---PCIDLI--------- 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1019 rSSQRDlrehdrrGMLWLLDEEAiYPNSNDDTFLERLFSHYgdREHHSLLR-KCAGPRQFVLHHLQGTnpVLYavdgwvr 1097
Cdd:cd14881 414 -SSLRT-------GLLSMLDVEC-SPRGTAESYVAKIKVQH--RQNPRLFEaKPQDDRMFGIRHFAGR--VVY------- 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1098 hsrehpgirNAVSLLqDSSREEINRLYIGSLTRGSgamvfCgSFAGLEGTQslrrvssirrSFTTagvkrnsimlqvkfT 1177
Cdd:cd14881 474 ---------DASDFL-DTNRDVVPDDLVAVFYKQN-----C-NFGFATHTQ----------DFHT--------------R 513
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1178 VDGIIDTLRRTGTHFVHCyllqhnagkhTKYTANGSPSSAAGQVSSEeemvnvpllrsQLRGSQVLEAARLHRLGFPESV 1257
Cdd:cd14881 514 LDNLLRTLVHARPHFVRC----------IRSNTTETPNHFDRGTVVR-----------QIRSLQVLETVNLMAGGYPHRM 572
|
730
....*....|....
gi 116008016 1258 PLLEFVRRFGLLAG 1271
Cdd:cd14881 573 RFKAFNARYRLLAP 586
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1385-2103 |
3.10e-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: 95.52 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEA------KLSELTVDLAEERSTAHIAteRLEAETAERLKLEKEL 1458
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEKREYEGYELLK--EKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 GDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGG-----GVYKLKYERVARELEFTKRRLHtQHEHDLE 1533
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekiGELEAEIASLERSIAEKERELE-DAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1534 QLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQnarnnllekkqrkfDAECQSLQDAVRQER 1613
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV--------------DKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1614 QAKERYGREK-------DVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggTEEEFAQLRRSKNETERRAK 1686
Cdd:TIGR02169 392 EKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-----ALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1687 EQEEELDEMAGQIQL-LEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLeTEHEERTLLLREKhE 1765
Cdd:TIGR02169 467 YEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL-GSVGERYATAIEV-A 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1766 LERRLSSMEDRDrvDRDAEEALNQKLRRDLRKYKAL----LKDAQTQLERLKADTPGKTLI------RQLRNQ------- 1828
Cdd:TIGR02169 545 AGNRLNNVVVED--DAVAKEAIELLKRRKAGRATFLplnkMRDERRDLSILSEDGVIGFAVdlvefdPKYEPAfkyvfgd 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1829 ---LEDAESARSLAMKARQ-TAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVK 1904
Cdd:TIGR02169 623 tlvVEDIEAARRLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVE-NLGDPSMAMMSKRLELrtKELESRLEleqatraRLEVQ 1983
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEeDLSSLEQEIENVKSEL--KELEARIE-------ELEED 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1984 VNRHKEALEKLQNEVTQSKmremqaqdvIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRL 2063
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 116008016 2064 ALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRL 2103
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1511-2075 |
1.47e-17 |
|
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: 89.73 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1511 ERVARELEFTKRRLHTQHE-----HDL-EQLVALKKHLE-MKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEE 1583
Cdd:TIGR02168 192 EDILNELERQLKSLERQAEkaeryKELkAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEKKQRKFDAECQSLQ----DAVRQERQAKER---YGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQR 1656
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALAneisRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1657 ELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRG 1736
Cdd:TIGR02168 352 ELESL------EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1737 NGYK----KIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVdrdAEEALnQKLRRDLRKYKALLKDAQTQLERL 1812
Cdd:TIGR02168 426 LLKKleeaELKELQAELEELEEELEELQEELERLEEALEELREELEE---AEQAL-DAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1813 KADTPGKTLIRQLRNQL--------------EDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERA------- 1871
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLsgilgvlselisvdEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsi 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1872 -----NAAHRDRAELQAQIEENEEELGELMKKYSATV--------------------KQLNTEQINVS------------ 1914
Cdd:TIGR02168 582 kgteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnalelaKKLRPGYRIVTldgdlvrpggvi 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1915 -------------------EAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGD-------------PSMAMMSKRLELR 1962
Cdd:TIGR02168 662 tggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleelsrqiSALRKDLARLEAE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1963 TKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKD 2042
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670
....*....|....*....|....*....|...
gi 116008016 2043 LEKKVEQMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-2069 |
1.87e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAK--ERYgrekDVLQAEKFTLEQTLAdtRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQE 1689
Cdd:COG1196 206 ERQAEkaERY----RELKEELKELEAELL--LLKLRELEAELEELEAELEE------LEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 EELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQR---DEELEEVRgngyKKIKALECQLETEHEERTLLLREKHEL 1766
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRrelEERLEELE----EELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1767 ERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADtpgKTLIRQLRNQLEDAESARSLAMKARQTA 1846
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEeneeelgelmkkysATVKQLNTEQINVSEAEFKLNEMEAE 1926
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--------------ELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1927 RNNLKEQVAELQHRLDNV-ENLGDPSMAMMSKRL-ELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMR 2004
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 2005 EMQAQ--DVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIA 2069
Cdd:COG1196 573 RATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1576-1949 |
5.23e-17 |
|
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: 88.19 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1576 DLRMLLEEQ------NARNNLLEKKQRKFDAECQSLQDAVRQ--------ERQAK--ERYgREkdvLQAEKFTLEQTLAD 1639
Cdd:TIGR02168 156 ERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDILNElerqlkslERQAEkaERY-KE---LKAELRELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1640 TRLD-----LEFKEEKLASLQRELEEMTFG-GGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLemtl 1713
Cdd:TIGR02168 232 LRLEelreeLEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1714 etmrkearresQQRDEELEevrgngyKKIKALECQLETEHEERTLLLREKHELERRLSSMEdrdrVDRDAEEALNQKLRR 1793
Cdd:TIGR02168 308 -----------RERLANLE-------RQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1794 DLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEdaesarsLAMKARQTAEAELTEVQAMFDESHRARNDAEERANA 1873
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSK------VAQLELQIA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 1874 AhrDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGD 1949
Cdd:TIGR02168 433 A--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1533-2075 |
6.27e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1533 EQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMT---NEMNDLRMLLEEqnarnnlLEKKQRKFDAECQSLqDAV 1609
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEevlREINEISSELPE-------LREELEKLEKEVKEL-EEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNET-------E 1682
Cdd:PRK03918 237 KEEIEELEK---ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYldelreiE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTletmrKEARRESQQRDEELEEvRGNGYKKIKALECQLETEHEERTLLlrE 1762
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEEL-----KKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGL--T 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 KHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADTP----------GKTLIRQLRNQLEDA 1832
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCPvcgrelteehRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1833 ESARSLAMKARQTAEAELTEVQAMFDESHRAR---------NDAEERANAAHRDRAELQAQIEENEEELGELMKKysaTV 1903
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG---EI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1904 KQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLdnvENLGDPSMAMMSKRLE---------LRTKELESRLELEQ 1974
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKelepfyneyLELKDAEKELEREE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1975 ATRARLEVQVnrhKEALEKLQNEVTQSKMREMQAQDVIKK-SQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:PRK03918 619 KELKKLEEEL---DKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570 580
....*....|....*....|....*
gi 116008016 2054 GAALKNDL---RLALQRIADLQQAM 2075
Cdd:PRK03918 696 LEKLKEELeerEKAKKELEKLEKAL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1385-2053 |
1.44e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELtvdlaEERStahiatERLEAETAERLKLEKELGDQTNK 1464
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-----EELK------EEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 VKNLQETTEKLEMELICAKSDLNGISEDEDaenedgvgggvYKLKYERVARELEFTKRRLHtQHEHDLEQLVALKKHLEM 1544
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKE-----------KAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1545 KLSDAyeevveqrqvvgqwkrkaQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDaecQSLQDAVRQERQAKERYGREKD 1624
Cdd:PRK03918 329 RIKEL------------------EEKEERLEELKKKLKELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1625 VLqaekftleqtladtrldlefkEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAG------- 1697
Cdd:PRK03918 388 KL---------------------EKELEELEKAKEEI------EEEISKITARIGELKKEIKELKKAIEELKKakgkcpv 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1698 -QIQLLEQAKLRL--EMTLETmrKEARRESQQRDEELEEVRgngyKKIKALECQLETEHEERTL--LLREKHELERRLSS 1772
Cdd:PRK03918 441 cGRELTEEHRKELleEYTAEL--KRIEKELKEIEEKERKLR----KELRELEKVLKKESELIKLkeLAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MeDRDRVDRDAEEAlnQKLRRDLRKYKALLKDAQTQLERLKadtPGKTLIRQLRNQLEDAESARS-LAMKARQTAEAELT 1851
Cdd:PRK03918 515 Y-NLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKLE---ELKKKLAELEKKLDELEEELAeLLKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1852 EVQAMFDESHRARNDAEERANAAHRDRAELqaqieeneeelgelmkkysatvKQLNTEQINVSEAEFKLNEMEAERNNLK 1931
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREE----------------------KELKKLEEELDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1932 EQVAELQHRLDNVENlgdpsmammsKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDv 2011
Cdd:PRK03918 647 KELEELEKKYSEEEY----------EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK- 715
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 116008016 2012 IKKSQKSLRDMREEFhavssREQESLTRRKDLeKKVEQMESE 2053
Cdd:PRK03918 716 LEKALERVEELREKV-----KKYKALLKERAL-SKVGEIASE 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1451-1811 |
2.45e-16 |
|
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: 85.88 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1451 RLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLngisedEDAENEdgvgggvyklkyERVARELEFTKRRLHTQHEH 1530
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKEL------EELEEE------------LEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1531 DL-------EQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQ 1603
Cdd:TIGR02168 734 DLarleaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1604 SLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETER 1683
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL------ESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1684 RAKEQEEELDEMAGQIQlleqaklrlemTLETMRKEARRESQQRDEELEEVRgNGYKKIKALECQLE---TEHEERTLLL 1760
Cdd:TIGR02168 888 ALALLRSELEELSEELR-----------ELESKRSELRRELEELREKLAQLE-LRLEGLEVRIDNLQerlSEEYSLTLEE 955
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 1761 REKHELERRLSSMEDRDRVDR-------------DAEEAL-NQKLRRD-LRKYKALLKDAQTQLER 1811
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRlenkikelgpvnlAAIEEYeELKERYDfLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1761-2073 |
8.46e-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: 83.96 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1761 REKHELERRLSSMEDRDRVDRDAEEALNQkLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAE-SARSLA 1839
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEE-VEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEgYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1840 MKA----RQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKK--YSATVKQLNTEQI-- 1911
Cdd:TIGR02169 232 KEAlerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkiGELEAEIASLERSia 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1912 ----NVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRtKELESRLELEQATRARLEVQVNRH 1987
Cdd:TIGR02169 312 ekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1988 KEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQR 2067
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
....*.
gi 116008016 2068 IADLQQ 2073
Cdd:TIGR02169 471 LYDLKE 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1432-2062 |
1.84e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1432 EERSTAHIATERLEAETAERL-KLEKELGDQtnKVKNLQETTEKLEMELicakSDLngiseDEDAENedgvgggvYKLKY 1510
Cdd:PRK02224 169 ERASDARLGVERVLSDQRGSLdQLKAQIEEK--EEKDLHERLNGLESEL----AEL-----DEEIER--------YEEQR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1511 ERVARELEFTKRRLhTQHEHDLEQLVALK---KHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNAR 1587
Cdd:PRK02224 230 EQARETRDEADEVL-EEHEERREELETLEaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVL--------------QAEKFTLEQTLADTRLDLEFKEEKLAS 1653
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLredaddleeraeelREEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1654 LQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQlleqaklRLEMTLETMRKearresqqRDEELEE 1733
Cdd:PRK02224 389 LEEEIEEL------RERFGDAPVDLGNAEDFLEELREERDELREREA-------ELEATLRTARE--------RVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1734 VRGNGykkiKALECQLETEHEERTLLLREKHE----LERRLSSMEDRdrvdrdaEEALNQKLRRdlrkyKALLKDAQTQL 1809
Cdd:PRK02224 448 LLEAG----KCPECGQPVEGSPHVETIEEDRErveeLEAELEDLEEE-------VEEVEERLER-----AEDLVEAEDRI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1810 ERL--KADTPGKtLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIee 1887
Cdd:PRK02224 512 ERLeeRREDLEE-LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-- 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1888 neeelgelmkkysatvkqlntEQINvseaefKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLElRTKELE 1967
Cdd:PRK02224 589 ---------------------ESLE------RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE-RKRELE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1968 SRLELEQATRARLEVQvnRHKEALEKLQNEVTQSKMREMQAQDVI---KKSQKSLRDMREEFHAVSSREQesltRRKDLE 2044
Cdd:PRK02224 641 AEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIgavENELEELEELRERREALENRVE----ALEALY 714
|
650
....*....|....*...
gi 116008016 2045 KKVEQMESEGAALKNDLR 2062
Cdd:PRK02224 715 DEAEELESMYGDLRAELR 732
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1336-2057 |
1.91e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1336 ARKKMSQRRVQEL----AVRCIQ-----RNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTANEEllMLRAKLEKIE 1406
Cdd:PTZ00121 1181 ARKAEEVRKAEELrkaeDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE--RNNEEIRKFE 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1407 CDRSEVKAENQ---KLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELIcak 1483
Cdd:PTZ00121 1259 EARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK--- 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1484 sdlngiSEDEDAENEDGVGggvyKLKYERVARELEFTKRRlhtqhehdlEQLVALKKHLEMKLSDAYEEVVEQRQVVGQW 1563
Cdd:PTZ00121 1336 ------KKAEEAKKAAEAA----KAEAEAAADEAEAAEEK---------AEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1564 KRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcqSLQDAVRQERQAKERYGREKDVLQAEKFtleqtladtrld 1643
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEEA------------ 1462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1644 lefkeEKLASLQRELEEMtfgggteEEFAQLRRSKNETERRAKEQEEELDEMAGQiqllEQAKLRLEmtlETMRKEARRE 1723
Cdd:PTZ00121 1463 -----KKKAEEAKKADEA-------KKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKAD---EAKKAEEAKK 1523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1724 SQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLK 1803
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1804 DAQTQLERLKADTPGKTLIRQLRNqledAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDraelqa 1883
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------ 1673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1884 qieeneeelgelmKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDnvenlgdpsmammskrlELRT 1963
Cdd:PTZ00121 1674 -------------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-----------------ELKK 1723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1964 KELESRLELEQATRARLEvqvnrHKEALEKLQNEVTQSKmremQAQDVIKKSQKSLRDMREEFHAVSSRE--QESLTRRK 2041
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEEldEEDEKRRM 1794
|
730
....*....|....*.
gi 116008016 2042 DLEKKVEQMESEGAAL 2057
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1678-2026 |
2.77e-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: 82.41 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1678 KNETERRAKEQEEELD-------EMAGQIQLLE-QAKL------------RLEMTLETMR-KEARRESQQRDEELEEVRg 1736
Cdd:TIGR02168 174 RKETERKLERTRENLDrledilnELERQLKSLErQAEKaerykelkaelrELELALLVLRlEELREELEELQEELKEAE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1737 ngyKKIKALECQLETEHEERTLLLREKHELERRLssmedrdrvdrdaeealnQKLRRDLRKYKALLKDAQTQLERLKADt 1816
Cdd:TIGR02168 253 ---EELEELTAELQELEEKLEELRLEVSELEEEI------------------EELQKELYALANEISRLEQQKQILRER- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 pgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM 1896
Cdd:TIGR02168 311 -----LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1897 KKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDnvenlgdpsmammskrlELRTKELESRLELEQAT 1976
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-----------------EAELKELQAELEELEEE 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1977 RARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQ---KSLRDMREEF 2026
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1584-2073 |
3.04e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEKKqRKFDAECQSLQDAVRQERQAKERYGREKDvlqaEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTf 1663
Cdd:PRK03918 161 ENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKEK----ELEEVLREINEISSELPELREELEKLEKEVKELE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1664 ggGTEEEFAQLRRSKNETERRAKEQEEELDEmagqiqlleqaklrlemtLETMRKEARRESqqrdEELEEVRGNgYKKIK 1743
Cdd:PRK03918 235 --ELKEEIEELEKELESLEGSKRKLEEKIRE------------------LEERIEELKKEI----EELEEKVKE-LKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADTPGKTLIR 1823
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYEEAK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1824 QLRNQLEDAESarSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEE---------------N 1888
Cdd:PRK03918 369 AKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1889 EEELGELMKKYSATVKQLNTEQINVSEAEFKLN----EMEAERNN---------LKEQVAELQHRLD--NVENLGDPS-- 1951
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRkelrELEKVLKKeseliklkeLAEQLKELEEKLKkyNLEELEKKAee 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1952 ---MAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHA 2028
Cdd:PRK03918 527 yekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE 606
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 116008016 2029 VSSREQE---SLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:PRK03918 607 LKDAEKElerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1379-1937 |
5.24e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1379 LNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKEL 1458
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 gdqtnkvKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggvyklKYERVARELEFTKRRLHTQHEhdLEQLVAL 1538
Cdd:COG1196 354 -------EEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------LLEALRAAAELAAQLEELEEA--EEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1539 KKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcqsLQDAVRQERQAKER 1618
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA---LAELLEELAEAAAR 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1619 YGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEqeeeldemagQ 1698
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA----------A 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1699 IQLLEQAKLRlEMTLETMRKEARRESQQRDEELEEVrgngykkikalecqleteHEERTLLLREKHELERRLSSMEDRDR 1778
Cdd:COG1196 563 IEYLKAAKAG-RATFLPLDKIRARAALAAALARGAI------------------GAAVDLVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1779 VDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADtpGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFD 1858
Cdd:COG1196 624 GRTLVAARLEAALRR-AVTLAGRLREVTLEGEGGSAG--GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1859 ESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAEL 1937
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
598-710 |
5.50e-15 |
|
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: 74.69 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 598 LLVVNPMAPLSLYSEKVV-SMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAG 676
Cdd:cd01363 2 LVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 116008016 677 AYNNfINAEKVNALCT---------------ILEAFGNTKTCLNSNATR 710
Cdd:cd01363 82 NGIN-KGETEGWVYLTeitvtledqilqanpILEAFGNAKTTRNENSSR 129
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1384-2063 |
6.72e-15 |
|
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: 80.92 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVD----LAEERSTAHIATERLE--AETAERLKLEKE 1457
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlIKENNATRHLCNLLKEtcARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 LGDQTNKV-KNLQETTEKLemelICAKSDLNGISEDEDAENEdgvgggvYKLK--YERVARELEFTKRRLH--------- 1525
Cdd:pfam05483 177 EREETRQVyMDLNNNIEKM----ILAFEELRVQAENARLEMH-------FKLKedHEKIQHLEEEYKKEINdkekqvsll 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1526 ----TQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKK-QRKFDA 1600
Cdd:pfam05483 246 liqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1601 ECQSLQDA---VRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLA----SLQR---ELEEMT-FGGGTEE 1669
Cdd:pfam05483 326 ICQLTEEKeaqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKkssELEEMTkFKNNKEV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1670 EFAQLRRSKNETERRAKEQEEeLDEMAGQIQLLEQaklRLEMTLETmrkearRESQQRDEELE----EVRGNGY-KKIKA 1744
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQ-FEKIAEELKGKEQ---ELIFLLQA------REKEIHDLEIQltaiKTSEEHYlKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1745 LECQLETEHEERTLLLREKHELerrlsSMEDRDRVDRDAEEALnqklrrDLRKYKALLKDAQTQLERLkadtpgktlIRQ 1824
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKL-----LLENKELTQEASDMTL------ELKKHQEDIINCKKQEERM---------LKQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1825 LRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQ--------------IEENEE 1890
Cdd:pfam05483 536 IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnlkkqienknknIEELHQ 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1891 ELGELMKKYSATVKQLNTEQInvseaefKLNEMEAERNNLKEQVAELqhrLDNVENlgdpsmammskrlELRTKELESRL 1970
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAYEI-------KVNKLELELASAKQKFEEI---IDNYQK-------------EIEDKKISEEK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1971 ELEQATRARLEVQvnrhkEALeKLQNEV---TQSKMREMQAQDVIKKSQ--KSLRDMREEFHAVSSREQESLTRRKDLEK 2045
Cdd:pfam05483 673 LLEEVEKAKAIAD-----EAV-KLQKEIdkrCQHKIAEMVALMEKHKHQydKIIEERDSELGLYKNKEQEQSSAKAALEI 746
|
730
....*....|....*...
gi 116008016 2046 KVEQMESEGAALKNDLRL 2063
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEI 764
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1383-1803 |
1.00e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEV---KAENQKLEAKLSELtvdlaEERstaHIATERLEAETAERLKLEKELG 1459
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLeelKKKLKELEKRLEEL-----EER---HELYEEAKAKKEELERLKKRLT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1460 DQT-----NKVKNLQETTEKLEME---LICAKSDLNGISED-EDAENEDGVGGGVYKLkyerVAREL-EFTKRRLHTQHE 1529
Cdd:PRK03918 383 GLTpekleKELEELEKAKEEIEEEiskITARIGELKKEIKElKKAIEELKKAKGKCPV----CGRELtEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1530 HDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKR--KAQKMTNEMNDLRMLLEEQNARNnlLEKKQRKFDaECQSLQD 1607
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEE--LEKKAEEYE-KLKEKLI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1608 AVRQERQAKERYGREKDVLQAEKFTLEQTLADtrldlefKEEKLASLQRELEEMTFGGGTE------------EEFAQLR 1675
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDE-------LEEELAELLKELEELGFESVEEleerlkelepfyNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1676 RSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEE 1755
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 116008016 1756 RTLLLREKHELERRLSSMEDRDRVDRDAEEALN--QKLRRDLRKYKALLK 1803
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELEKLEKALErvEELREKVKKYKALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1383-1981 |
1.42e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIEcdrSEVKaENQKLEAKLSELTVDLAEERSTAHIATERLEaETAERLK-LEKELGDQ 1461
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLE---KEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIR-ELEERIEeLKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1462 TNKVKNLQETTEKLE--MELICAKSDLNgiseDEDAENEDGVGGGVYKLK-YERVARELEFTKRRLhtqhEHDLEQLVAL 1538
Cdd:PRK03918 279 EEKVKELKELKEKAEeyIKLSEFYEEYL----DELREIEKRLSRLEEEINgIEERIKELEEKEERL----EELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1539 KKHLEmKLSDAYEEVVEQRQVVGQWKR-KAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQdavrqerqaKE 1617
Cdd:PRK03918 351 EKRLE-ELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---------KE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1618 RYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAG 1697
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRI------EKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1698 QIQLLEQAKL--RLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHE---ERTLLLREKHELERRLSS 1772
Cdd:PRK03918 495 LIKLKELAEQlkELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MEDR-DRVDRDAEEALNQKLRRDLRKYKAL--LKDAQTQLERLkadtpgKTLIRQLRNQLEDAESARSLAMKARQTAEAE 1849
Cdd:PRK03918 575 LLKElEELGFESVEELEERLKELEPFYNEYleLKDAEKELERE------EKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1850 LTEVQAMFDES--HRARNDAEERANAAHRDRAELQaqieeneeelgelmkkysatvkqlnteqinvsEAEFKLNEMEAER 1927
Cdd:PRK03918 649 LEELEKKYSEEeyEELREEYLELSRELAGLRAELE--------------------------------ELEKRREEIKKTL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 116008016 1928 NNLKEQVAELQHRLDNVENLGdpsmAMMSKRLELRTKELESRLELEQATRARLE 1981
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLE----KALERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1382-2075 |
4.86e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1382 HRTEEQLKTANEELlmlrAKLEKIecdRSEVKAENQKLE--AKLSELTVDLAEERSTAHIA--TERLEAETAERLKLEKE 1457
Cdd:TIGR02168 175 KETERKLERTRENL----DRLEDI---LNELERQLKSLErqAEKAERYKELKAELRELELAllVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 LGDQTNKVKNLQETTEKLEMELicakSDLNG-ISEDEDAENEdgvgggvYKLKYERVARELEftkrRLhtqhEHDLEQLV 1536
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKL----EELRLeVSELEEEIEE-------LQKELYALANEIS----RL----EQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1537 ALKKHLEMKLsdayEEVVEQRQvvgQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAK 1616
Cdd:TIGR02168 309 ERLANLERQL----EELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1617 ERygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERraKEQEEELDEMA 1696
Cdd:TIGR02168 382 ET-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRER------LQQEIEELLKKLEEAEL--KELQAELEELE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1697 GQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVR--GNGYKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAqlQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1775 DRDRVDRDAEEALNQKLRRDLRKYkaLLKDAQTQLERLKADTP---GKTLIRQL------------RNQLEDAESARSLA 1839
Cdd:TIGR02168 527 ELISVDEGYEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQnelGRVTFLPLdsikgteiqgndREILKNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1840 MKARQTAEAELTEVQAMFDESH-----------RARNDAEER------------------ANAAHRDRAELQAQIEENEE 1890
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVLvvddldnalelAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1891 ELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDpSMAMMSKRLELRTKELESRL 1970
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1971 ELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQM 2050
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
730 740
....*....|....*....|....*
gi 116008016 2051 ESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELI 868
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1394-2062 |
6.12e-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: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1394 ELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTvdlAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTE 1473
Cdd:TIGR00618 167 ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT---LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1474 KLEMELicaksdlngisedeDAENEdgvgggvyKLKYERVARELEFTKRRLHTQhehdLEQLVALKKHLEmkLSDAYEEV 1553
Cdd:TIGR00618 244 YLTQKR--------------EAQEE--------QLKKQQLLKQLRARIEELRAQ----EAVLEETQERIN--RARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1554 VEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQE---RQAKERYGREKDVLQAEK 1630
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEihiRDAHEVATSIREISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1631 fTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrlE 1710
Cdd:TIGR00618 376 -TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC----T 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1711 MTLETMRKEARRESQQRDEELEEVRGNgYKKIKALECQLETEHEERTLLLREKH-ELERRLSSMEDRdRVDRDAEEALNQ 1789
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPA-RQDIDNPGPLTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1790 KLRRDLRKYKALLK-------DAQTQLERLKADTPGKTLIRQ-------LRNQL-EDAESARSLAMKARQTAEAELTEVQ 1854
Cdd:TIGR00618 529 RMQRGEQTYAQLETseedvyhQLTSERKQRASLKEQMQEIQQsfsiltqCDNRSkEDIPNLQNITVRLQDLTEKLSEAED 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1855 AMFDESHRARNDAEERANaaHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKlnEMEAERNNLKEQv 1934
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLALQ- 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1935 aELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQ------ATRARLEVQVNRHKEALEKLQNE----------- 1997
Cdd:TIGR00618 684 -KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassSLGSDLAAREDALNQSLKELMHQartvlkartea 762
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 1998 -------VTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKD----LEKKVEQMESEGAALKNDLR 2062
Cdd:TIGR00618 763 hfnnneeVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdediLNLQCETLVQEEEQFLSRLE 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1383-2000 |
6.17e-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: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANE--ELLMLRAKLEKI--ECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETaERLKLEKEL 1458
Cdd:TIGR00618 184 MEFAKKKSLHGkaELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 GDQTNKVKNLQETTEKLE-----MELICAKSDLNGISEdEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLE 1533
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEetqerINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1534 QLVALKKHL---EMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRkfDAECQSLQDAVR 1610
Cdd:TIGR00618 342 EQRRLLQTLhsqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1611 QERQAKERYGREKDVLQAEKFTL-EQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFA-QLRRSKNETERRAKEQ 1688
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELcAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlQETRKKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1689 EEELDEMAGQ--------------------IQLLEQAKLRLEMTLETMRKEARRESQQR---DEELEEVRGNGYK---KI 1742
Cdd:TIGR00618 500 QEEPCPLCGScihpnparqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRaslKEQMQEIQQSFSIltqCD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1743 KALECQL--------------ETEHEERTLLLREKHELERRLSSMEDRDRV---DRDAEEALNQKLRRDLRKYKALLKDA 1805
Cdd:TIGR00618 580 NRSKEDIpnlqnitvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTLTQER 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1806 QTQLERLKADTPgKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQI 1885
Cdd:TIGR00618 660 VREHALSIRVLP-KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1886 EENEEELGELMKKYSATVKQLNTEQINVSEAEF-------KLNEMEAERNNLKEQVAELQHRLdnvenlgdpsmAMMSKR 1958
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEAHFNNNEEVTaalqtgaELSHLAAEIQFFNRLREEDTHLL-----------KTLEAE 807
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 116008016 1959 LELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQ 2000
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1545-1993 |
6.48e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.50 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1545 KLSDAYEEVVEQRQVVGQWKRKaqkmTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQsLQDAVRQERQAKERYGREKD 1624
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1625 VLQAEKFTLEQtLADTRLDLEFKEEKLASLQRELEE--MTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLL 1702
Cdd:COG4717 147 RLEELEERLEE-LRELEEELEELEAELAELQEELEEllEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1703 EQAKLRLEMTLETMRKEARRESQQR-----------DEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLS 1771
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1772 SMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKAdtpgktlIRQLRNQLEDAESARSLAmKARQTAEAELT 1851
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-------LQELLREAEELEEELQLE-ELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1852 EVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATvkQLNTEqinVSEAEFKLNEMEAERNNLK 1931
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEE---LEELEEELEELEEELEELR 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1932 EQVAELQHRLDNVENLGDPSMAmmskRLELRTKELESRLELEQATRARLEVQV-NRHKEALEK 1993
Cdd:COG4717 453 EELAELEAELEQLEEDGELAEL----LQELEELKAELRELAEEWAALKLALELlEEAREEYRE 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1380-2052 |
1.10e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1380 NVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERstahiaterLEAETAERLKLEKELG 1459
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE---------LEELEEELEELQEELE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1460 DQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDA-----ENEDGVGGGVYKLKYERVARELEF--TKRRLHTQHEHDL 1532
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSlerlqENLEGFSEGVKALLKNQSGLSGILgvLSELISVDEGYEA 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1533 EQLVALKKHLEMKLSDAYEEVVeqRQVVGQWKRKAQKMT-----------NEMNDLRMLLEEQNARNNLLEkkQRKFDAE 1601
Cdd:TIGR02168 538 AIEAALGGRLQAVVVENLNAAK--KAIAFLKQNELGRVTflpldsikgteIQGNDREILKNIEGFLGVAKD--LVKFDPK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1602 --------------CQSLQDAVRQERQAKERY------------------GREKDVL-----QAEKFTLEQTLADTRLDL 1644
Cdd:TIGR02168 614 lrkalsyllggvlvVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSsilerRREIEELEEKIEELEEKI 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1645 EFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLEtmrkearres 1724
Cdd:TIGR02168 694 AELEKALAELRKELEEL------EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT---------- 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1725 qqrdeELEEvrgngykKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKD 1804
Cdd:TIGR02168 758 -----ELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRE 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1805 AQTQLERLKADTpgKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQ 1884
Cdd:TIGR02168 825 RLESLERRIAAT--ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1885 IEeneeelgelmkkysatvkqlnteqinvsEAEFKLNEMEAERNNLKEQVAELQHRLDnvenlgdpsmammskRLELRTK 1964
Cdd:TIGR02168 903 LR----------------------------ELESKRSELRRELEELREKLAQLELRLE---------------GLEVRID 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1965 ELESRL-ELEQATRARLEVQVNRHKEALEKLQNEVTQskmremqaqdvIKKSQKSLRDMR----EEFHAVSSREQESLTR 2039
Cdd:TIGR02168 940 NLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR-----------LENKIKELGPVNlaaiEEYEELKERYDFLTAQ 1008
|
730
....*....|...
gi 116008016 2040 RKDLEKKVEQMES 2052
Cdd:TIGR02168 1009 KEDLTEAKETLEE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1381-1884 |
2.24e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1381 VHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1461 QTNKVKNLQETTEKLEMELICAKSDLNGIsEDEDAENEDGVGGGVYKLkyERVARELEftkrrlhtQHEHDLEQLVALKK 1540
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEEL-EEEIEELRERFGDAPVDL--GNAEDFLE--------ELREERDELREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1541 HLEMKLSDAYEEVVEQRQVVGQWK-------RKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQER 1613
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1614 QAKERYGREKDVlqaekftlEQTLADTRLDLEFKEEKLASLQRELEEmtfgggteeefaqLRRSKNETERRAKEQEEELD 1693
Cdd:PRK02224 510 RIERLEERREDL--------EELIAERRETIEEKRERAEELRERAAE-------------LEAEAEEKREAAAEAEEEAE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1694 EMAGQIQLLEQAKLRLEMTLETMRKeaRRESQQRDEELEEVRGNGYKKIKALEcQLETEHEERtllLREKHELERRLSSM 1773
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLER--IRTLLAAIADAEDEIERLREKREALA-ELNDERRER---LAEKRERKRELEAE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 EDRDRVdrdaEEALNQKLRRDlrKYKALLKDAQTQLERLKADTPGKtlIRQLRNQLEDAESARslamKARQTAEAELTEV 1853
Cdd:PRK02224 643 FDEARI----EEAREDKERAE--EYLEQVEEKLDELREERDDLQAE--IGAVENELEELEELR----ERREALENRVEAL 710
|
490 500 510
....*....|....*....|....*....|.
gi 116008016 1854 QAMFDEshrarndAEERANAAHRDRAELQAQ 1884
Cdd:PRK02224 711 EALYDE-------AEELESMYGDLRAELRQR 734
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1490-2075 |
3.62e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.39 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1490 SEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKlSDAYEEVVEQRQ--VVGQWKRKA 1567
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-KKALEYYQLKEKleLEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1568 QKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLE-- 1645
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKE-EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErr 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1646 ---------FKEEKLASLQRELEEMTFGGG---TEEEFAQLRRSKNETERRAKEQEEELDE------MAGQIQLLEQAKL 1707
Cdd:pfam02463 309 kvddeeklkESEKEKKKAEKELKKEKEEIEeleKELKELEIKREAEEEEEEELEKLQEKLEqleeelLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1708 RLEMTLETMRKEARRESQQRDE-ELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELER----RLSSMEDRDRVDRD 1782
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLlELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKeeleKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1783 AEEALNQKLR-RDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQ------A 1855
Cdd:pfam02463 469 KSEDLLKETQlVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvaistA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1856 MFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVK----QLNTEQINVSEAEFKLNEMEAERNNLK 1931
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1932 EQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDV 2011
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 2012 IKKSQKSLRDMREEFHAVSSREQE-SLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1574-2070 |
5.47e-13 |
|
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: 74.87 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1574 MNDLR-MLLEEQNARNNLLEKKQRKFDAECQSLQDavRQERQAKERYGREKDVLQAEKFTLEQTLAD-TRLDLEFKEEKL 1651
Cdd:pfam12128 195 FRDVKsMIVAILEDDGVVPPKSRLNRQQVEHWIRD--IQAIAGIMKIRPEFTKLQQEFNTLESAELRlSHLHFGYKSDET 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1652 ASLQRELEEMTFGGGTEEEFAQLR----RSKNETERRAKEQEEELDEMAGQIQLLE-QAKLRLEMTLETMRKEARRESQQ 1726
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDdqwkEKRDELNGELSAADAAVAKDRSELEALEdQHGAFLDADIETAAADQEQLPSW 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEeLEEVRgngyKKIKALE-CQLETEHEERTLLLREKHELERRLSSMED--------RDR---VDRDAEEALNQKLRRD 1794
Cdd:pfam12128 353 QSE-LENLE----ERLKALTgKHQDVTAKYNRRRSKIKEQNNRDIAGIKDklakireaRDRqlaVAEDDLQALESELREQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1795 LRKYKALLKDAQTQLE--------RLKADTPGKTLIRQLRN---QLEDAESARSLAMKARQTAEAELTEVQAMFDESHRA 1863
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQLENfdeRIERAREEQEAANAEVERLQSELRQARKRRDQASEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1864 RNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQ-----LNTEQINVSEAEFKLNEMEAERNNlkeQVAELQ 1938
Cdd:pfam12128 508 LRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQsigkvISPELLHRTDLDPEVWDGSVGGEL---NLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1939 HRLDNVENlgdPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTqskmremQAQDVIKKSQKS 2018
Cdd:pfam12128 585 LDLKRIDV---PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET-------FARTALKNARLD 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 116008016 2019 LRDMREEFHAVSSREQESLTRRKDL-EKKVEQMESEGAALKNDLRLALQRIAD 2070
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLKQLDKKHQAWLEEQKE 707
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1385-1995 |
6.59e-13 |
|
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: 74.77 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEK-IECDRSEVKAENQKLEAKLSELtvdlaeERSTAHIATERLEAETaERLKLEKELGDQTN 1463
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLEStVSQLRSELREAKRMYEDKIEEL------EKQLVLANSELTEART-ERDQFSQESGNLDD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDlNGISEDEDAENEdgvgggvykLKYERVARELEftKRRLHTQhehdleQLVALKKHLE 1543
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNS---------ITIDHLRRELD--DRNMEVQ------RLEALLKAMK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 MKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND----LRMLLEEQNARNNLLEKKQRKFDAECQSLQDavrqerqaKERy 1619
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEKVSSLTAQLEStkemLRKVVEELTAKKMTLESSERTVSDLTASLQE--------KER- 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1620 grekdvlQAEKFTLEQTLADTRLDLEFKEekLASLQRELEEMTfGGGTEEEFAQLRRS-KNETERRAKEQEEELDEMAGQ 1698
Cdd:pfam15921 511 -------AIEATNAEITKLRSRVDLKLQE--LQHLKNEGDHLR-NVQTECEALKLQMAeKDKVIEILRQQIENMTQLVGQ 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1699 ------IQLLEQAKLRLEMTLETM----------RKEAR-RESQQR--DEELEEVR--GNGYKKIKALEcqleTEHEERT 1757
Cdd:pfam15921 581 hgrtagAMQVEKAQLEKEINDRRLelqefkilkdKKDAKiRELEARvsDLELEKVKlvNAGSERLRAVK----DIKQERD 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1758 LLLREKHELERRLSSM-EDRDRVDRDAEEAlNQKLRRDLRKYKALLKDAQTQLErlkadtpgktlirQLRNQLEDAESAR 1836
Cdd:pfam15921 657 QLLNEVKTSRNELNSLsEDYEVLKRNFRNK-SEEMETTTNKLKMQLKSAQSELE-------------QTRNTLKSMEGSD 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1837 SLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQieeneeelgelMKKYSATVKQLNTEQinvsea 1916
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE-----------KNKLSQELSTVATEK------ 785
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1917 efklNEMEAERNNLKEQVAELQHRLDNVENLGDpsmammskRLELRTKELESRLELEQATRARLEVQvnrHKEALEKLQ 1995
Cdd:pfam15921 786 ----NKMAGELEVLRSQERRLKEKVANMEVALD--------KASLQFAECQDIIQRQEQESVRLKLQ---HTLDVKELQ 849
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1385-2061 |
7.23e-13 |
|
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: 74.38 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRsEVKAENQKLEAKLSEltvDLAEE-RSTAHiaterlEAETAERLKlEKELGDQTN 1463
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMER-DAMADIRRRESQSQE---DLRNQlQNTVH------ELEAAKCLK-EDMLEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQE---TTEKLEMELICAKSDLNGISEDEDAENED-------GVGGGVYKLKYErVARELEFTKRRLHTQHEhdle 1533
Cdd:pfam15921 171 QIEQLRKmmlSHEGVLQEIRSILVDFEEASGKKIYEHDSmstmhfrSLGSAISKILRE-LDTEISYLKGRIFPVED---- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1534 QLVALKKHLEMKL-------SDAYEEVVEQRQV-VGQWKRKAQKMTNEMNDLRMLLE--EQNARN-NLLEKKQRkfdAEC 1602
Cdd:pfam15921 246 QLEALKSESQNKIelllqqhQDRIEQLISEHEVeITGLTEKASSARSQANSIQSQLEiiQEQARNqNSMYMRQL---SDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1603 QSLQDAVRQE-RQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNET 1681
Cdd:pfam15921 323 ESTVSQLRSElREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1682 --ERRAKEQ------EEELDEMAGQIQlleqaklRLEMTLETMRKEARresQQRDEELEEVRGN--GYKKIKALECQLET 1751
Cdd:pfam15921 403 lwDRDTGNSitidhlRRELDDRNMEVQ-------RLEALLKAMKSECQ---GQMERQMAAIQGKneSLEKVSSLTAQLES 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1752 EHEertLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLR-----------------------RDLRKYKALLKDAQTQ 1808
Cdd:pfam15921 473 TKE---MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaieatnaeitklrsrvdlklqelQHLKNEGDHLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1809 LERLKADTPGK-TLIRQLRNQLEDAESarsLAMKARQTAEAELTEvQAMFDESHRARndaeeranaahrdRAELQaQIEE 1887
Cdd:pfam15921 550 CEALKLQMAEKdKVIEILRQQIENMTQ---LVGQHGRTAGAMQVE-KAQLEKEINDR-------------RLELQ-EFKI 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1888 NEEELGELMKKYSATVKQLNTEQINV----SEAEFKLNEMEAERNNLKEQVAELQHRLDNvenlgdpsmamMSKRLELRT 1963
Cdd:pfam15921 612 LKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNS-----------LSEDYEVLK 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1964 KELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQ---ESLTRR 2040
Cdd:pfam15921 681 RNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleEAMTNA 760
|
730 740
....*....|....*....|....*...
gi 116008016 2041 -------KDLEKKVEQMESEGAALKNDL 2061
Cdd:pfam15921 761 nkekhflKEEKNKLSQELSTVATEKNKM 788
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1378-2026 |
1.08e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 73.78 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1378 LLNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEaklsELTVDLAEERSTAHIATERLEAETAERLKLEKE 1457
Cdd:PRK01156 158 ILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKSHSITLKEIERLSIEYNNAMDD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 ---LGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEdgvgggvYKLKYERVARELEFTKRRLHTQHEHDLEQ 1534
Cdd:PRK01156 234 ynnLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE-------LEERHMKIINDPVYKNRNYINDYFKYKND 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1535 LVALKKHLEMKLSD--AYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEqnarnnlLEKKQRKFdaecQSLQDAVRQE 1612
Cdd:PRK01156 307 IENKKQILSNIDAEinKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE-------LEGYEMDY----NSYLKSIESL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1613 RQAKERYGREKDVLQAEkftLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKneteRRAKEQEEEL 1692
Cdd:PRK01156 376 KKKIEEYSKNIERMSAF---ISEILKIQEIDPDAIKKELNEINVKLQDI------SSKVSSLNQRI----RALRENLDEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1693 DEmagqiqlleqaklRLEMtLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSS 1772
Cdd:PRK01156 443 SR-------------NMEM-LNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEY 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MEDRDRVDRDAEEALNQKLRRDLRKYK---ALLKDAQTQLERLKADtpgktlIRQLRnqLEDAESARSLAMKA-RQTAEA 1848
Cdd:PRK01156 509 LESEEINKSINEYNKIESARADLEDIKikiNELKDKHDKYEEIKNR------YKSLK--LEDLDSKRTSWLNAlAVISLI 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1849 ELTEVQAMFDESHRARNDAEERANaahrdraELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERN 1928
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQ-------EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1929 NLKEQVAELQHRldnvenlgDPSMAMMSKRL---ELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKmRE 2005
Cdd:PRK01156 654 NYKKQIAEIDSI--------IPDLKEITSRIndiEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN-ET 724
|
650 660
....*....|....*....|.
gi 116008016 2006 MQAQDVIKKSQKSLRDMREEF 2026
Cdd:PRK01156 725 LESMKKIKKAIGDLKRLREAF 745
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1381-1811 |
2.72e-12 |
|
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: 72.46 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1381 VHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1461 QTNKVknlqettEKLEMELICAKSDLNGISEDEDAenedGVGGGVYKL-KYERVARELEFTKRRLHTQhehdLEQLVALK 1539
Cdd:pfam15921 424 RNMEV-------QRLEALLKAMKSECQGQMERQMA----AIQGKNESLeKVSSLTAQLESTKEMLRKV----VEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLEmklsdAYEEVVEQRQVVGQWKRKAQKMTN-EMNDLR-----MLLEEQNARNNllEKKQRKFDAECQSLQ------- 1606
Cdd:pfam15921 489 MTLE-----SSERTVSDLTASLQEKERAIEATNaEITKLRsrvdlKLQELQHLKNE--GDHLRNVQTECEALKlqmaekd 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1607 ---DAVRQE----RQAKERYGREKDVLQAEKFTLEQTLADTRLDL-EFK--EEKLASLQRELEEMTfgGGTEEEFAQLRR 1676
Cdd:pfam15921 562 kviEILRQQienmTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELqEFKilKDKKDAKIRELEARV--SDLELEKVKLVN 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1677 SKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESqqrdEELEEVRGNGYKKIKALECQLE-TEHEE 1755
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS----EEMETTTNKLKMQLKSAQSELEqTRNTL 715
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116008016 1756 RTLLLREKHELERRLsSMEDRDRVDRDAEEALNQKLR------RDLRKYKALLKDAQTQLER 1811
Cdd:pfam15921 716 KSMEGSDGHAMKVAM-GMQKQITAKRGQIDALQSKIQfleeamTNANKEKHFLKEEKNKLSQ 776
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1387-2047 |
3.26e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.98 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1387 QLKTANEELLMLRAKLEKIEcdrSEVKAENQ---KLEAKLSELTVDLAEerstahiaTERLEAETAERL-KLEKELGDQT 1462
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKIN---SEIKNDKEqknKLEVELNKLEKQKKE--------NKKNIDKFLTEIkKKEKELEKLN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1463 NKVKNLQETTEKLEMELICAKSDLNGISEDEDaenedgvgggvyKLKYERVARELEFTkrrlhtqhehDLEQLVALKKHL 1542
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNID------------KIKNKLLKLELLLS----------NLKKKIQKNKSL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1543 EMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND----LRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKEr 1618
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1619 ygrEKDVLQAEKftLEQTLADTRLDLEFKEEKLASLQRELEEMTFG-GGTEEEFAQLRRSKNETERRAKEQEEELDEMAG 1697
Cdd:TIGR04523 296 ---EISDLNNQK--EQDWNKELKSELKNQEKKLEEIQNQISQNNKIiSQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1698 QIQLLE---QAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:TIGR04523 371 EIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKD----EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1775 DRDRVdrdaeealnqkLRRDLRKYKALLKDAQTQLERLKAdtpgktLIRQLRNQLEDAESarslamkarqtaeaELTEVQ 1854
Cdd:TIGR04523 447 NQDSV-----------KELIIKNLDNTRESLETQLKVLSR------SINKIKQNLEQKQK--------------ELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1855 AMFDESHRARNDAEERANAAHRDRAELQAQIeeneeelgelmKKYSATVKQLNTEqinVSEAEFKLNEMEAE--RNNLKE 1932
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKI-----------EKLESEKKEKESK---ISDLEDELNKDDFElkKENLEK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1933 QVAELQHRLDNVENLGDPSMAMMS------KRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEvtqskmrEM 2006
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEekqeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI-------IK 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 116008016 2007 QAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKV 2047
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1532-1885 |
4.71e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEmndlrmlLEEQNARNNLLEKKQRKFDAECQSLQDAVRQ 1611
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKERYGREKDVLQAEkftleqtladtrldLEFKEEKLASLQRELEEMtfgggteeeFAQLRRSK-NETERRAKEQEE 1690
Cdd:TIGR02169 749 LEQEIENVKSELKELEAR--------------IEELEEDLHKLEEALNDL---------EARLSHSRiPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1691 ELDEMAGQIQLLEQAKLRLEMTLETMRKEaRRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRL 1770
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1771 SSME-DRDRVDRDAEEALN--QKLRRDLRKYKALLKDAQTQLERLKADTpgKTLIRQLRNQLEDAESARSLAmKARQTAE 1847
Cdd:TIGR02169 885 GDLKkERDELEAQLRELERkiEELEAQIEKKRKRLSELKAKLEALEEEL--SEIEDPKGEDEEIPEEELSLE-DVQAELQ 961
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 116008016 1848 AELTEVQAM----------FDESHRARNDAEERANAAHRDRAELQAQI 1885
Cdd:TIGR02169 962 RVEEEIRALepvnmlaiqeYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1379-1842 |
6.10e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1379 LNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahIATERLEAETAERLKLEKEL 1458
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG------NGGDRLEQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 GDQTNKVKNLQETTEKLEMELI-----------CAKSDLNGISEDEDA--ENEDGVGGGVYKLK--YERVARELEFTKRR 1523
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPasaeefaalraEAAALLEALEEELEAleEALAEAEAALRDLRreLRELEAEIASLERR 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1524 LHTQHEHDLEQLVALKKHLEMKLSD------------------------------------AYE----EVVEQR------ 1557
Cdd:COG4913 435 KSNIPARLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllvppEHYaaalRWVNRLhlrgrl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1558 --QVVGQWKRKAQKMTNEMNDL--RMLLEEQNARNNLLEKKQRKFDAEC----QSLQD---AVRQERQAKERYGR-EKDV 1625
Cdd:COG4913 515 vyERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFDYVCvdspEELRRhprAITRAGQVKGNGTRhEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1626 lqaekftleQTLADTRLDLEFK-EEKLASLQRELeemtfgggteeefAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQ 1704
Cdd:COG4913 595 ---------RRRIRSRYVLGFDnRAKLAALEAEL-------------AELEEELAEAEERLEALEAELDALQERREALQR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1705 AKLRLEMTLETmrKEARRESQQRDEELEEVRgNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDR-DRVDRDA 1783
Cdd:COG4913 653 LAEYSWDEIDV--ASAEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKElEQAEEEL 729
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1784 EEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKA 1842
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1371-2053 |
1.24e-11 |
|
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: 70.46 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1371 LLVRVTPL-LNVHRTEEQLKTANEELLMLRAKLE----------KIECDRS-EVKAENQKLEAKL-SELTVDLAEERSTA 1437
Cdd:TIGR00606 345 LLVEQGRLqLQADRHQEHIRARDSLIQSLATRLEldgfergpfsERQIKNFhTLVIERQEDEAKTaAQLCADLQSKERLK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1438 HIATERLEAETA--------ERLKLEKELGDQTNKVKNLQETTE------KLEMELICAKSDLNGISEDEDAENEDGvgg 1503
Cdd:TIGR00606 425 QEQADEIRDEKKglgrtielKKEILEKKQEELKFVIKELQQLEGssdrilELDQELRKAERELSKAEKNSLTETLKK--- 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1504 GVYKLKYERVarELEFTKRRLhtqhEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND------L 1577
Cdd:TIGR00606 502 EVKSLQNEKA--DLDRKLRKL----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1578 RMLLEEQNARNNLLEKKQRKFDAECQSLQdavrqerQAKERYGREKDVLQAEKFTLEQTLADTrLDLEFKEEKLASLQRE 1657
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLE-------QNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEE 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1658 LEEMT-----FGGGTEEEFAQLRRSKNETE------RRAKEQEEELDEMAGQIQlleqAKLRLEMT-LETMRKEARRESQ 1725
Cdd:TIGR00606 648 IEKSSkqramLAGATAVYSQFITQLTDENQsccpvcQRVFQTEAELQEFISDLQ----SKLRLAPDkLKSTESELKKKEK 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1726 QRDEELEEVRGngykkikalecqletEHEERTLLLREKHELERRLSSmedrdrVDRDAeealnQKLRRDLRKYKALLKDA 1805
Cdd:TIGR00606 724 RRDEMLGLAPG---------------RQSIIDLKEKEIPELRNKLQK------VNRDI-----QRLKNDIEEQETLLGTI 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1806 QTQLERLKADTPGKTLIRQLRNQLEDAESArslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQI 1885
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQMELKDVERK-----IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1886 EENEEElgelMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPsMAMMSKRLELRTKE 1965
Cdd:TIGR00606 853 QDQQEQ----IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP-LETFLEKDQQEKEE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1966 LESRLELEqatRARLEVQVNRHKEALEK-------LQNEVTQSKMRE-MQAQDVI--------------KKSQKSLRDMR 2023
Cdd:TIGR00606 928 LISSKETS---NKKAQDKVNDIKEKVKNihgymkdIENKIQDGKDDYlKQKETELntvnaqleecekhqEKINEDMRLMR 1004
|
730 740 750
....*....|....*....|....*....|...
gi 116008016 2024 EEFHAVSSRE---QESLTRRKdLEKKVEQMESE 2053
Cdd:TIGR00606 1005 QDIDTQKIQErwlQDNLTLRK-RENELKEVEEE 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1763-2116 |
1.40e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 KHELERRLSSMEDR-DRVDRDAEEALNQ--KLRRD---LRKYKALlkdaQTQLERLKAdtpgkTL----IRQLRNQLEDA 1832
Cdd:COG1196 174 KEEAERKLEATEENlERLEDILGELERQlePLERQaekAERYREL----KEELKELEA-----ELlllkLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1833 ESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIeeneeelgelmkkySATVKQLNTEQIN 1912
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------------ARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1913 VSEAEFKLNEMEAERNNLKEQVAELQhrldnvenlgdpsmammsKRLELRTKEL---ESRLELEQATRARLEVQVNRHKE 1989
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELE------------------EELEELEEELeeaEEELEEAEAELAEAEEALLEAEA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1990 ALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIA 2069
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 116008016 2070 DLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPVHVKRSSQQSL 2116
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1796-2073 |
1.53e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1796 RKYKALLK--DAQTQLERLKAdtpgktLIRQLRNQLEDAESARSLAMKARQTaEAELTEVQAMFdeshrarndAEERANA 1873
Cdd:TIGR02168 173 RRKETERKleRTRENLDRLED------ILNELERQLKSLERQAEKAERYKEL-KAELRELELAL---------LVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1874 AHRDRAELQAQIeeneeelgelmkkySATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsma 1953
Cdd:TIGR02168 237 LREELEELQEEL--------------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1954 mmSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSRE 2033
Cdd:TIGR02168 297 --ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 116008016 2034 QESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1385-1934 |
1.56e-11 |
|
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: 70.37 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTvDLAEERSTAHIATERLEAETAERLKLEKELGDQtnk 1464
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA-ARAPAWLAAQDALERLREQSGEALADSQEVTAA--- 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 vknLQETTEKlEMELIcaksdlngISEDEDAENEdgvgggvyklkyervaRELEFTKRRLHTQHEHDLEQLVALKKHLE- 1543
Cdd:COG3096 632 ---MQQLLER-EREAT--------VERDELAARK----------------QALESQIERLSQPGGAEDPRLLALAERLGg 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 MKLSDAYEEVV------------EQRQ--VV---GQWKRKAQKMTNEMNDLRmlleeqnarnnLLEKKQRKFDA---ECQ 1603
Cdd:COG3096 684 VLLSEIYDDVTledapyfsalygPARHaiVVpdlSAVKEQLAGLEDCPEDLY-----------LIEGDPDSFDDsvfDAE 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1604 SLQDAV------RQERQAK-------ERYGREK--DVLQAEKFTLEQTLADTRLDLEfkeeKLASLQRELEE-------M 1661
Cdd:COG3096 753 ELEDAVvvklsdRQWRYSRfpevplfGRAAREKrlEELRAERDELAEQYAKASFDVQ----KLQRLHQAFSQfvgghlaV 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1662 TFGGGTEEEFAQLRRSKNETER-----RAKEQE--EELDEMAGQIQLLE----QAKLRLEMTLETMRKEARRESQQRDEE 1730
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERelaqhRAQEQQlrQQLDQLKEQLQLLNkllpQANLLADETLADRLEELREELDAAQEA 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1731 LEEVRGNGyKKIKALECQLETeheertllLR---EKHE-LERRLSSMEDRDRVDRDAEEALNQKLRRdlRKYKALlKDAQ 1806
Cdd:COG3096 909 QAFIQQHG-KALAQLEPLVAV--------LQsdpEQFEqLQADYLQAKEQQRRLKQQIFALSEVVQR--RPHFSY-EDAV 976
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1807 TQLERlkadtpGKTLIRQLRNQLEDAESARS---LAMKARQTAEAELTEVQAMFDESHRARND----------------- 1866
Cdd:COG3096 977 GLLGE------NSDLNEKLRARLEQAEEARRearEQLRQAQAQYSQYNQVLASLKSSRDAKQQtlqeleqeleelgvqad 1050
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1867 --AEERanaAHRDRAELQAQIEENEEelgelmkKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQV 1934
Cdd:COG3096 1051 aeAEER---ARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1300-1721 |
1.90e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1300 SQILFRSGVLSELEAKRDVLLSDRIIQLQAFCR----GYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRV 1375
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAElrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1376 TpllnvhRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAetaerlkLE 1455
Cdd:TIGR02168 750 A------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------LN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1456 KELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEdaenedgvgggvykLKYERVARELEFTKRRLHTQHEHDLEQL 1535
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI--------------ESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1536 VALKKHLeMKLSDAYEEVVEQRqvvgqwkrkaQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRqerqa 1615
Cdd:TIGR02168 883 ASLEEAL-ALLRSELEELSEEL----------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----- 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1616 kERYGREKDVLQAEKFTLEqtladtrLDLEFKEEKLASLQRELEEmtFGG---GTEEEFaqlrrskneterraKEQEEEL 1692
Cdd:TIGR02168 947 -EEYSLTLEEAEALENKIE-------DDEEEARRRLKRLENKIKE--LGPvnlAAIEEY--------------EELKERY 1002
|
410 420
....*....|....*....|....*....
gi 116008016 1693 DEMAGQIQLLEQAKLRLEMTLETMRKEAR 1721
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1410-2055 |
3.08e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1410 SEVKAENQKLEAKLSELTVDLAEERSTAHIATERleAETAERLKlEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGI 1489
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK--AEDARKAE-EARKAEDARKAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1490 SEDEDAENEdgvgggvyklKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQV-----VGQWK 1564
Cdd:PTZ00121 1167 EEARKAEDA----------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavkkAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1565 RKAQ--KMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVR---QERQAKERYGRE--KDVLQAEKFTLEQTL 1637
Cdd:PTZ00121 1237 KDAEeaKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaeEKKKADEAKKAEekKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1638 ADtrlDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGqiqllEQAKLR---LEMTLE 1714
Cdd:PTZ00121 1317 AD---EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-----EEAKKKadaAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1715 TMRK--EARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEAlnQKLR 1792
Cdd:PTZ00121 1389 EKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA--KKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1793 RDLRKYKALLKDAQtqlERLKADTPGKTlirqlrnqledAESARSLAMKARQTAEAELTEVQAMFDESHRARND---AEE 1869
Cdd:PTZ00121 1467 EEAKKADEAKKKAE---EAKKADEAKKK-----------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkAEE 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1870 RANAAHRDRAElqaqieeneeelgelMKKYSATVKQlnTEQINVSEAEFKLNEM--EAERNNLKEQVAELQHRLDnvenl 1947
Cdd:PTZ00121 1533 AKKADEAKKAE---------------EKKKADELKK--AEELKKAEEKKKAEEAkkAEEDKNMALRKAEEAKKAE----- 1590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1948 gdpsmammSKRLELRTK--ELESRLELEQATRA----------RLEVQVNRHKEALEKLQNEVTQ--SKMREMQAQDVIK 2013
Cdd:PTZ00121 1591 --------EARIEEVMKlyEEEKKMKAEEAKKAeeakikaeelKKAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIK 1662
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 116008016 2014 KSQKSLRDMREEFHAVSSRE--------QESLTRRKDLEKKVEQMESEGA 2055
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKaeedekkaAEALKKEAEEAKKAEELKKKEA 1712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1320-1998 |
3.76e-11 |
|
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: 68.94 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1320 LSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQrnVKAFLAVRDWPWWRLLVRVTPLLNVHR-TEEQLKTANEELLML 1398
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDYREKLEKL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1399 RAKLEKIECDRSEVKAENQKLEAKLSELTVDLA--EERSTAHIAT-----ERLEAETAERLKLEKELGDQTNKVKNLQET 1471
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEkedkaLEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1472 TEKLEMELICAKSDLNgISEDEDAENEDGVGGGVyklkyeRVARELEFTKRRLHTQhehdLEQLVALK----KHLEMKLS 1547
Cdd:TIGR02169 478 YDRVEKELSKLQRELA-EAEAQARASEERVRGGR------AVEEVLKASIQGVHGT----VAQLGSVGeryaTAIEVAAG 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1548 DAYEEVVEQRQVVGQW------KRKAQKMT----NEMNDLRMLLE---EQNARN---NLLEKKQRKFDAECQSLQDAVRQ 1611
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEaiellkRRKAGRATflplNKMRDERRDLSilsEDGVIGfavDLVEFDPKYEPAFKYVFGDTLVV 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ER--QAKERYGREKDVlqaekfTLEQTLAD--------------TRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLR 1675
Cdd:TIGR02169 627 EDieAARRLMGKYRMV------TLEGELFEksgamtggsraprgGILFSRSEPAELQRLRERLEGL------KRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1676 RSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMR---KEARRESQQRDEELEEVRgngyKKIKALECQLEtE 1752
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVK----SELKELEARIE-E 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1753 HEErtlllrEKHELERRLSSMEDRDRVDRDAE-EALNQKLRRDLRKYKALLKDAQTQLERLkadTPGKTLIRQLRN---- 1827
Cdd:TIGR02169 770 LEE------DLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRL---TLEKEYLEKEIQelqe 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1828 QLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLN 1907
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1908 TEQINVSEAEFKLNEMEAERNNLKEQVAE------LQHRLDNVE----NLGDPSMAMMS--KRLELRTKELESRLELEQA 1975
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEelsledVQAELQRVEeeirALEPVNMLAIQeyEEVLKRLDELKEKRAKLEE 1000
|
730 740
....*....|....*....|...
gi 116008016 1976 TRARLEVQVNRhkeaLEKLQNEV 1998
Cdd:TIGR02169 1001 ERKAILERIEE----YEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1649-2075 |
5.24e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1649 EKLASLQRELEEMTfggGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLEtmRKEARRESQQRD 1728
Cdd:COG4717 71 KELKELEEELKEAE---EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1729 EELEEVRgNGYKKIKALECQLETEHEERTLLlREKHELERRLSSMEDRDRVDRDAEEAlnQKLRRDLRKYKALLKDAQTQ 1808
Cdd:COG4717 146 ERLEELE-ERLEELRELEEELEELEAELAEL-QEELEELLEQLSLATEEELQDLAEEL--EELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1809 LERLKADtpgktlIRQLRNQLEDAESARSLAmKARQTAEAeLTEVQAMFDESHRARNDAEERANAAhRDRAELQAQIEEN 1888
Cdd:COG4717 222 LEELEEE------LEQLENELEAAALEERLK-EARLLLLI-AAALLALLGLGGSLLSLILTIAGVL-FLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1889 EEELGELMKKYSATVKQLnTEQINVSEAEFKlNEMEAERNNLKEQVAELQHRLDNVENLgdpsmammsKRLELRTKELES 1968
Cdd:COG4717 293 LAREKASLGKEAEELQAL-PALEELEEEELE-ELLAALGLPPDLSPEELLELLDRIEEL---------QELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1969 RLELEQATRARLEVQVNRHKEALEKLQNEVTQSKmREMQAQDVIKKSQKSLRDMREEFHAVSSREQEsltrrKDLEKKVE 2048
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELE 435
|
410 420
....*....|....*....|....*..
gi 116008016 2049 QMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAEL 462
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1532-2067 |
5.44e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQLVALKKHLEmKLSDAYEEVVEQRQvvgqwkrkaQkmtnemndlRMLLEEQNARNNLLEKKQRKFDaECQSLQDAVR- 1610
Cdd:COG4913 224 FEAADALVEHFD-DLERAHEALEDARE---------Q---------IELLEPIRELAERYAAARERLA-ELEYLRAALRl 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1611 -QERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtFGGGTEEefaQLRRSKNETERRAKEQE 1689
Cdd:COG4913 284 wFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLE---QLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 EELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALEcQLETEHEErtlLLREKHELERR 1769
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRE---LEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1770 LSSMEDR--------------DRVD---------------------------------------RDAEEALNQ-KLRRDL 1795
Cdd:COG4913 435 KSNIPARllalrdalaealglDEAElpfvgelievrpeeerwrgaiervlggfaltllvppehyAAALRWVNRlHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1796 RKYKALLKDAQTQLERLKADT-PGKTLIRQ------LRNQLED------AESARSLAMKARQ-TAEAELTEVQAMF---D 1858
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSlAGKLDFKPhpfrawLEAELGRrfdyvcVDSPEELRRHPRAiTRAGQVKGNGTRHekdD 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1859 ESHRARN-----DAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQiNVSEAEFKLNEMEAernnLKEQ 1933
Cdd:COG4913 595 RRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS----AERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1934 VAELQHRLDNVENlGDPSMAMMSKRLElrtkELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIK 2013
Cdd:COG4913 670 IAELEAELERLDA-SSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 116008016 2014 KSQKSLRDmrEEFHAVSSREQESLTRRkDLEKKVEQMESEGAALKNDLRLALQR 2067
Cdd:COG4913 745 LELRALLE--ERFAAALGDAVERELRE-NLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1619-2028 |
5.98e-11 |
|
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: 68.17 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1619 YGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggteEEFAQLRRSKNETE-----RRAKEQEEELD 1693
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-------ERYQALLKEKREYEgyellKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1694 EMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSM 1773
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 EDRdrvdrdaeealNQKLRRDLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEDAEsarslamKARQTAEAELTEV 1853
Cdd:TIGR02169 321 EER-----------LAKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEEYAELK-------EELEDLRAELEEV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1854 QAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGelmkkysatvkqlnteqinvsEAEFKLNEMEAERNNLKEQ 1933
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ---------------------RLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1934 VAELQHRLDnvenlgdpsmammSKRLELrtKELESRLELEQATRARLEVQVNRHKEALEKLQNEVT--QSKMREMQAQ-D 2010
Cdd:TIGR02169 436 INELEEEKE-------------DKALEI--KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSklQRELAEAEAQaR 500
|
410
....*....|....*...
gi 116008016 2011 VIKKSQKSLRDMREEFHA 2028
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKA 518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1383-1872 |
7.39e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEellMLRAKLEKIECDRSEVKAENQKleaKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQT 1462
Cdd:PTZ00121 1399 KAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1463 NKVKNLQETTEKLEmelicaksDLNGISEDEDAENEDGVGGGVYKLKYERvARELEFTKRRLHTQHEHDLEQLVALKKHL 1542
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--------EAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1543 EMKLSDAYEEVVEQRQvvGQWKRKAQKMTNEMNDLRMLLEeqnaRNNLLEKKQRKFDAECQSLQDAVRQERqAKERYGRE 1622
Cdd:PTZ00121 1544 EKKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALR----KAEEAKKAEEARIEEVMKLYEEEKKMK-AEEAKKAE 1616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAEKFTLEQTLADTRLDLEFKEE----KLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKE----QEEELDE 1694
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKK 1696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGQIQLLEQAKLRLEmtlETMRK--EARRESQQRDEELEEVRGNGYKKIKALEcQLETEHEERTLLLREKHELERRlsS 1772
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEA---EEKKKaeELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKK--A 1770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTE 1852
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
490 500
....*....|....*....|
gi 116008016 1853 vQAMFDESHRARNDAEERAN 1872
Cdd:PTZ00121 1851 -KHKFNKNNENGEDGNKEAD 1869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1727 |
1.05e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1378 LLNVHRTEEQLKTANEELLMLRAKLEKIE---CDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLK- 1453
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEe 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1454 -------LEKELGDQTNKVKNLQETTEKLEMELIcAKSDLNGISE------------------DEDAENEDGVGG----- 1503
Cdd:COG4717 204 lqqrlaeLEEELEEAQEELEELEEELEQLENELE-AAALEERLKEarlllliaaallallglgGSLLSLILTIAGvlflv 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1504 -------GVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND 1576
Cdd:COG4717 283 lgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1577 LRmLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADtrLDLEFKEEKLASLQR 1656
Cdd:COG4717 363 LQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA--LDEEELEEELEELEE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1657 ELEEmtfgggTEEEFAQLRRSKNETERRAK--EQEEELDEMAGQIQLLEQ---------AKLRL-EMTLETMRKEARRES 1724
Cdd:COG4717 440 ELEE------LEEELEELREELAELEAELEqlEEDGELAELLQELEELKAelrelaeewAALKLaLELLEEAREEYREER 513
|
...
gi 116008016 1725 QQR 1727
Cdd:COG4717 514 LPP 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1385-1688 |
1.05e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERST-----AHIATERLEAETAERLKLEKELG 1459
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1460 DQTNKVKNLQETTEKLEMELICAKSDLNGISED----EDAENEDGVGGGVYKLKYERVARELEftkrrlhtQHEHDLEQL 1535
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlKEQIKSIEKEIENLNGKKEELEEELE--------ELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1536 VALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLE--KKQRKFDAECQSLQDAVRQER 1613
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpKGEDEEIPEEELSLEDVQAEL 960
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1614 QAKErygREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQ 1688
Cdd:TIGR02169 961 QRVE---EEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI------LERIEEYEKKKREVFMEAFEA 1026
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1393-2048 |
1.47e-10 |
|
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: 66.77 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1393 EELLMLRAKLEKIEcdrSEVKAENQKLEAKLSELTVDLAEERSTAHiaTERLEAETAERlklEKELGDQTNKVKNLQETT 1472
Cdd:pfam10174 130 KELFLLRKTLEEME---LRIETQKQTLGARDESIKKLLEMLQSKGL--PKKSGEEDWER---TRRIAEAEMQLGHLEVLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1473 EKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLK------YERVARELEFTKRRLHT-------QHEHDLEQLVALK 1539
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKdtkissLERNIRDLEDEVQMLKTngllhteDREEEIKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLE-MKlsdayeevveqrQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNN------------LLEKKQRKfdAECQSLQ 1606
Cdd:pfam10174 282 SHSKfMK------------NKIDQLKQELSKKESELLALQTKLETLTNQNSdckqhievlkesLTAKEQRA--AILQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1607 DAVRQERQAKERYGREKDV----LQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETE 1682
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKqlqdLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL------QEQLRDKDKQLAGLK 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEH----EERTL 1758
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK----KENKDLKEKVSALQpeltEKESS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1759 LLREKHELERRLSSMEDRDRVDRDAEEALNQKlRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNqledaesarsl 1838
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQ----------- 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1839 amkarqtaeaeltEVQAMFDESHRARNDAEERANAahrdraelqaqieeneeelgelmkkysatvkqlnteqinvseaef 1918
Cdd:pfam10174 566 -------------EVARYKEESGKAQAEVERLLGI--------------------------------------------- 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1919 kLNEMEAERNNLKEQVAELQHRLD--------NVENLGDPSMAMMSKRLELRTkelESRLELEQATRARLEVQVNRHKEA 1990
Cdd:pfam10174 588 -LREVENEKNDKDKKIAELESLTLrqmkeqnkKVANIKHGQQEMKKKGAQLLE---EARRREDNLADNSQQLQLEELMGA 663
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1991 LEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEfhavssreqesltRRKDLEKKVE 2048
Cdd:pfam10174 664 LEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE-------------RRKQLEEILE 708
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1454-2059 |
1.83e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1454 LEKELGDQTNKVKNLQETTEKLEMELicakSDLNgiseDEDAENEDgvgggvyklKYERVARELEFTKRRLHTqhehDLE 1533
Cdd:TIGR04523 59 LDKNLNKDEEKINNSNNKIKILEQQI----KDLN----DKLKKNKD---------KINKLNSDLSKINSEIKN----DKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1534 QLVALKKHLEmKLSDAYEEVVE-QRQVVGQWKRKAQ---KMTNEMNDLRMLLEEqnarnnlLEKKQRKFDAECQSLQ--- 1606
Cdd:TIGR04523 118 QKNKLEVELN-KLEKQKKENKKnIDKFLTEIKKKEKeleKLNNKYNDLKKQKEE-------LENELNLLEKEKLNIQkni 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1607 DAVRQERQAKE-------RYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKN 1679
Cdd:TIGR04523 190 DKIKNKLLKLElllsnlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN------TQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1680 ETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEArreSQQRDEELEEVRGNGYKKIKALECQLETEHEERTLL 1759
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK---EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1760 LREKHELERRLSSME-DRDRVDRDAEEALNQ--KLRRDLRKYKALLKDAQTQLERLKADTPG-KTLIRQLRNQLEDAESA 1835
Cdd:TIGR04523 341 NEQISQLKKELTNSEsENSEKQRELEEKQNEieKLKKENQSYKQEIKNLESQINDLESKIQNqEKLNQQKDEQIKKLQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1836 RSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQL--NTEQINV 1913
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELksKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1914 SEAEFKlnEMEAERNNLKEQVAELQHRLDNVENLgdpsmammSKRLELRTKELESRLEL--EQATRARLEVQVNRHKEAL 1991
Cdd:TIGR04523 501 LNEEKK--ELEEKVKDLTKKISSLKEKIEKLESE--------KKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEI 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 1992 EKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEfhaVSSREQ--ESLTRR-KDLEKKVEQMESEGAALKN 2059
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---IEEKEKkiSSLEKElEKAKKENEKLSSIIKNIKS 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1384-1883 |
4.20e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELtvdlaEERSTAHIATERLEAETAERLKLEKElgDQTN 1463
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-----EEERDDLLAEAGLDDADAEAVEARRE--ELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGggvYKLKYERVARELEFTKRRLHTQHehdlEQLVALKKHLE 1543
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE---LREEAAELESELEEAREAVEDRR----EEIEELEEEIE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 mKLSDAYEEVVEQRqvvGQWKRKAQKMTNEMNDLRMLLEE-----QNARNNlLEKKQRKFDA----EC-QSLQDAVRQER 1613
Cdd:PRK02224 395 -ELRERFGDAPVDL---GNAEDFLEELREERDELREREAEleatlRTARER-VEEAEALLEAgkcpECgQPVEGSPHVET 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1614 QAKERYGREKdvlqaekftLEQTLADTRLDLEFKEEKLASLQrELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELD 1693
Cdd:PRK02224 470 IEEDRERVEE---------LEAELEDLEEEVEEVEERLERAE-DLVE------AEDRIERLEERREDLEELIAERRETIE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1694 EMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVrgngykkiKALECQLETEHEERTLLLRekheLERRLSSM 1773
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV--------AELNSKLAELKERIESLER----IRTLLAAI 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 ED-RDRVDRDAEEALNQKLRRDLRKykallkdaqtqlERLKADtpgKTLIRQLRNQLEDA--ESARSlamkARQTAEAEL 1850
Cdd:PRK02224 602 ADaEDEIERLREKREALAELNDERR------------ERLAEK---RERKRELEAEFDEAriEEARE----DKERAEEYL 662
|
490 500 510
....*....|....*....|....*....|...
gi 116008016 1851 TEVQAMFDESHRARNDAEERANAAHRDRAELQA 1883
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1577-2053 |
8.01e-10 |
|
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: 63.76 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1577 LRMLLEE-QNARNNLLekkqRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQ 1655
Cdd:pfam07888 32 LQNRLEEcLQERAELL----QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1656 RELEEMTfgggteEEFAQLRRSKNETERRAKEQEEEldemagqIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVr 1735
Cdd:pfam07888 108 ASSEELS------EEKDALLAQRAAHEARIRELEED-------IKTLTQRVLERETELERMKERAKKAGAQRKEEEAER- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1736 gngykkiKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKykallkdaQTQLERLKAD 1815
Cdd:pfam07888 174 -------KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK--------EAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1816 tpgktlIRQLRNQLEDAEsarslamkarQTAEAELTEVQAMfdESHRARNDAEeranaAHRDRAELqAQIEENEEELGEL 1895
Cdd:pfam07888 239 ------LRSLQERLNASE----------RKVEGLGEELSSM--AAQRDRTQAE-----LHQARLQA-AQLTLQLADASLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1896 MKKYSATVKQlnteqinvsEAEFKLNEMEAERNNLKEQVAELQhrldnvenlgdpsmammskrlelrtkELESRLELEQA 1975
Cdd:pfam07888 295 LREGRARWAQ---------ERETLQQSAEADKDRIEKLSAELQ--------------------------RLEERLQEERM 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1976 TRARLEVQVNRHKEAlEKLQNEVTQSKMREMQAqdvikksqkSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:pfam07888 340 EREKLEVELGREKDC-NRVQLSESRRELQELKA---------SLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1382-1850 |
9.79e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.22 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1382 HRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEA---KLSELTVDLAEERSTAHIATERLEAETAERLKL---E 1455
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaK 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1456 KELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQL 1535
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1536 ValkkHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQ--------- 1606
Cdd:TIGR00618 511 I----HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQcdnrskedi 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1607 DAVRQERQAKERYGREKD--------VLQAEKFTLEQTLADTRLDLE---FKEE---KLASLQRELEEMTFgggtEEEFA 1672
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSeaedmlacEQHALLRKLQPEQDLQDVRLHlqqCSQElalKLTALHALQLTLTQ----ERVRE 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARREsQQRDEELEEVRGNGYKKIKALECQLETE 1752
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDAL 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1753 HEertLLLREKHELERRLSSMEDRDRVDRDAEEALNQKlrrdLRKYKALLKDAQTQLERLKADTPG-KTLIRQLRNQLED 1831
Cdd:TIGR00618 742 NQ---SLKELMHQARTVLKARTEAHFNNNEEVTAALQT----GAELSHLAAEIQFFNRLREEDTHLlKTLEAEIGQEIPS 814
|
490
....*....|....*....
gi 116008016 1832 AESARSLAMKARQTAEAEL 1850
Cdd:TIGR00618 815 DEDILNLQCETLVQEEEQF 833
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1668-2117 |
1.08e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1668 EEEFAQLRRSKNETERRAKEQEEELDEMAGQiqlLEQAKLRLEMTLETMrkEARRESQQRDEELEEvrgngykKIKALEC 1747
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQ---REQARETRDEADEVL--EEHEERREELETLEA-------EIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1748 QLETEHEERTLLLREKHELERRLSSMEDRdrvdrdaeealnqklRRDLRkykallkdAQTQLERLKADTpgktlIRQLRN 1827
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEE---------------RDDLL--------AEAGLDDADAEA-----VEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1828 QLEDAESArslamkARQTAEAELTEVQAMFDESHRARNDA---EERANAAHRDRAELQAQIEENEEELGELMKKYSATVK 1904
Cdd:PRK02224 318 ELEDRDEE------LRDRLEECRVAAQAHNEEAESLREDAddlEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQ-------INVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEN--------------------LGDPSMAMMSK 1957
Cdd:PRK02224 392 EIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagkcpecgqpVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 RLELRTKELESRLELEQATRARLEVQVNRhKEALEKLQNEVTQSKMREmqaqdviKKSQKSLRDMREEFHAVSSREQESL 2037
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERR-------EDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 2038 TRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVgSISDLEDRLRPVHVKRSSQQSLN 2117
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELN 622
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1383-2005 |
1.58e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 63.30 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECdrsevKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKEL---- 1458
Cdd:pfam10174 145 RIETQKQTLGARDESIKKLLEMLQS-----KGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrn 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 --GDQTNKVKNLQETtekLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELE-------FTKRRLHtQHE 1529
Cdd:pfam10174 220 qlQPDPAKTKALQTV---IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvykshskFMKNKID-QLK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1530 HDLE----QLVALKKHLEM---KLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNArnnLLEKKQRKfdaec 1602
Cdd:pfam10174 296 QELSkkesELLALQTKLETltnQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKES---FLNKKTKQ----- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1603 qsLQDavrqerqakerygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETE 1682
Cdd:pfam10174 368 --LQD------------------LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL------QEQLRDKDKQLAGLK 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEH----EERTL 1758
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK----KENKDLKEKVSALQpeltEKESS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1759 LLREKHELERRLSSMEDRDRVDRDAEEALNQKlRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLrnqleDAESARSL 1838
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-----EQEVARYK 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1839 AMKARQTAEAE-----LTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIeeneEELGELMKKYSATVKQL---NTEQ 1910
Cdd:pfam10174 572 EESGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI----KHGQQEMKKKGAQLLEEarrREDN 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1911 INVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQ-----------ATRAR 1979
Cdd:pfam10174 648 LADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQeallaaisekdANIAL 727
|
650 660
....*....|....*....|....*.
gi 116008016 1980 LEVQVNRHKealeKLQNEVTQSKmRE 2005
Cdd:pfam10174 728 LELSSSKKK----KTQEEVMALK-RE 748
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1382-2063 |
1.78e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.45 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1382 HRTEEQLKTANEELLMLRAKLEKIE-------CDRSEVKAENQKLEAKLSELTVDLAEERS-------TAHIATERLEAE 1447
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEeklaqvlKENKEEEKEKKLQEEELKLLAKEEEELKSellklerRKVDDEEKLKES 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1448 TAERLKLEKELgdqtnkvKNLQETTEKLEMElicaKSDLNGISEDEDAENEDgvgggvyklkYERVARELEFTKRRLHTQ 1527
Cdd:pfam02463 320 EKEKKKAEKEL-------KKEKEEIEELEKE----LKELEIKREAEEEEEEE----------LEKLQEKLEQLEEELLAK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1528 HEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKqrkfDAECQSLQD 1607
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK----LTEEKEELE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1608 AVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEM-------------------TFGGGTE 1668
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvllalikdgvggriisaHGRLGDL 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1669 EEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELE-EVRGNGYKKIKALEC 1747
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEiDPILNLAQLDKATLE 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1748 QLETEHEERTLLLREKHELE----RRLSSMEDRDRVDRDAEEALNQKLRR----DLRKYKALLKDAQTQLERLKADTPgK 1819
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELtklkESAKAKESGLRKGVSLEEGLAEKSEVkaslSELTKELLEIQELQEKAESELAKE-E 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1820 TLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDES--HRARNDAEERANAAHRDRAELQAQIEENEEELGELMK 1897
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIneELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1898 KYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQV---AELQHRLDNVENLgdpsmamMSKRLELRTKELESRLELEQ 1974
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELkeeAELLEEEQLLIEQ-------EEKIKEEELEELALELKEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1975 ATRARLEVQVNRHKE-ALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:pfam02463 847 KLEKLAEEELERLEEeITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
730
....*....|
gi 116008016 2054 GAALKNDLRL 2063
Cdd:pfam02463 927 AEILLKYEEE 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1622-1857 |
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 116008016 1622 EKDVLQAEKFTLEQ--TLADTRLDLEFKEEKLASLQRELEemtfgggTEEEFAQLRRSKNETER-----RAKEQEEELDE 1694
Cdd:COG4913 220 EPDTFEAADALVEHfdDLERAHEALEDAREQIELLEPIRE-------LAERYAAARERLAELEYlraalRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1775 DRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKAD-TPGKTLIRQLRNQLEDAESARS------LAMKARQTAE 1847
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAlRDLRRELRELEAEIASLERRKSniparlLALRDALAEA 452
|
250
....*....|
gi 116008016 1848 AELTEVQAMF 1857
Cdd:COG4913 453 LGLDEAELPF 462
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1624-2035 |
2.87e-09 |
|
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: 62.01 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1624 DVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTfggGTEEEFAQLRRSKN---ETERRAKEQE----------E 1690
Cdd:pfam05622 69 EQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELT---SLAEEAQALKDEMDilrESSDKVKKLEatvetykkklE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1691 ELDEMAGQIQLLE-------QAKLRLE----------MTLETMRKEARRESQQRDEELeevrgngyKKIKALECQLETEH 1753
Cdd:pfam05622 146 DLGDLRRQVKLLEernaeymQRTLQLEeelkkanalrGQLETYKRQVQELHGKLSEES--------KKADKLEFEYKKLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1754 EERTLLLREKhelerrlssmeDRDRVDRDAEEALNQKLR------RDLRKYKALLKDAQTQLERLKADT-PGKTLIRQLR 1826
Cdd:pfam05622 218 EKLEALQKEK-----------ERLIIERDTLRETNEELRcaqlqqAELSQADALLSPSSDPGDNLAAEImPAEIREKLIR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1827 NQLEDaesaRSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKY--SATVK 1904
Cdd:pfam05622 287 LQHEN----KMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAedSSLLK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQINvseaefKLNEMEAERNNLKEQVAELQHRLDNvenlgdpSMAMMSKRLE--LRTKELESRleleqATRARLEV 1982
Cdd:pfam05622 363 QKLEEHLE------KLHEAQSELQKKKEQIEELEPKQDS-------NLAQKIDELQeaLRKKDEDMK-----AMEERYKK 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1983 QVNRHKEALEKLQNEVTQSKMREMQAQDV-IKKSQKSLRDMREEFHAVSS-REQE 2035
Cdd:pfam05622 425 YVEKAKSVIKTLDPKQNPASPPEIQALKNqLLEKDKKIEHLERDFEKSKLqREQE 479
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1383-1731 |
3.13e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERS------------TAHIATERLEAETAE 1450
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1451 RLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQH-- 1528
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKge 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1529 ----EHDLEQLVALKKH---LEMKLSDAYEEVVEqrqVVGQWKRKAQKMtnemndlrmlLEEQNARNNLLEKKQRKFdae 1601
Cdd:PRK03918 541 ikslKKELEKLEELKKKlaeLEKKLDELEEELAE---LLKELEELGFES----------VEELEERLKELEPFYNEY--- 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1602 cQSLQDAVRQERQAKERYGREKDVLQAEkftlEQTLADTRLDLEFKEEKLASLQRELEEMTFGG-------------GTE 1668
Cdd:PRK03918 605 -LELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEKKYSEEEYEElreeylelsrelaGLR 679
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1669 EEFAQLRRSKNETERRAKEQEEELDEM---AGQIQLLEQAKLRLEMTLETMRK---EARRESQQRDEEL 1731
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELREKVKKykaLLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1383-1812 |
3.23e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIAT-----ERLEAETAERLKLEKE 1457
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 LGDQTNKVKNLQEtteklEMELICAKSDLNGISEDEDAENEdgvgggvyklkYERVARELEFTKRRLHTQHEHDLEQLVA 1537
Cdd:COG4717 165 LEELEAELAELQE-----ELEELLEQLSLATEEELQDLAEE-----------LEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1538 LKKHLEMKLSDAYEEVVEQRQ-----------VVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQ 1606
Cdd:COG4717 229 LEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1607 DAVRQER-------QAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEE-----KLASLQRELEEM--TFGGGTEEEFa 1672
Cdd:COG4717 309 ALPALEEleeeeleELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALlaEAGVEDEEEL- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 qlrRSKNETERRAKEQEEELDEMAGQI-QLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLET 1751
Cdd:COG4717 388 ---RAALEQAEEYQELKEELEELEEQLeELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1752 EHEERTL--LLREKHELERRLSSMEDRDRVDRDAEEALnQKLRRDLRKYK--ALLKDAQTQLERL 1812
Cdd:COG4717 465 LEEDGELaeLLQELEELKAELRELAEEWAALKLALELL-EEAREEYREERlpPVLERASEYFSRL 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1397-1852 |
3.74e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1397 MLRAKLEKIEcdRSEVKAENQKLEAKLSELTvDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLE 1476
Cdd:COG4717 46 MLLERLEKEA--DELFKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1477 MelicAKSDLNGISEDEDAENEdgvgggvyklkYERVARELEFTKRRLHtQHEHDLEQLVALKKHLEMKlsdayeevveQ 1556
Cdd:COG4717 123 K----LLQLLPLYQELEALEAE-----------LAELPERLEELEERLE-ELRELEEELEELEAELAEL----------Q 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1557 RQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLeqt 1636
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1637 LADTRLDLEFKEEKLASLQRELEEMTF--GGGTEEEFAQLRRSKNETERRAKE----------QEEELDEMAGQIQLLEQ 1704
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFlvLGLLALLFLLLAREKASLGKEAEElqalpaleelEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1705 AKLRLEMTLETMRKEARRESQQRDEELEEVRGNGY-KKIKAL--ECQLETEHE--ERTLLLREKHELERRLSSMEDR-DR 1778
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELeQEIAALlaEAGVEDEEElrAALEQAEEYQELKEELEELEEQlEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1779 VDRDAEEALNQ----KLRRDLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSL--AMKARQTAEAELTE 1852
Cdd:COG4717 414 LLGELEELLEAldeeELEEELEELEEELEELEEELEELREE------LAELEAELEQLEEDGELaeLLQELEELKAELRE 487
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1647-2025 |
4.07e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1647 KEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETErRAKEQEEELdeMAGQIQLLEQAKLRLEMtletmrKEARRESQQ 1726
Cdd:PRK04863 784 REKRIEQLRAEREEL------AERYATLSFDVQKLQ-RLHQAFSRF--IGSHLAVAFEADPEAEL------RQLNRRRVE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRGN------GYKKIKALeCQLETEHEERTLLLREKHELERrlsSMEDRDRVDRdAEEAlnqklRRDLRKYKA 1800
Cdd:PRK04863 849 LERALADHESQeqqqrsQLEQAKEG-LSALNRLLPRLNLLADETLADR---VEEIREQLDE-AEEA-----KRFVQQHGN 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1801 LLKDAQTQLERLKADtPGKtlIRQLRNQLEDAESARSLAmKARQTAEAELTEVQAmfdesHRARNDAEERANAAhrdrAE 1880
Cdd:PRK04863 919 ALAQLEPIVSVLQSD-PEQ--FEQLKQDYQQAQQTQRDA-KQQAFALTEVVQRRA-----HFSYEDAAEMLAKN----SD 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1881 LQAQIEENEEELGELMKKYSatvKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDnveNLGDPSMAMMSKRLE 1960
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRAR---EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQ---DLGVPADSGAEERAR 1059
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1961 LRTKELESRLeleQATRARlevqvnrhKEALEKlQNEVTQSKMREMQAQdvIKKSQKSLRDMREE 2025
Cdd:PRK04863 1060 ARRDELHARL---SANRSR--------RNQLEK-QLTFCEAEMDNLTKK--LRKLERDYHEMREQ 1110
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1564-1885 |
4.52e-09 |
|
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: 61.68 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1564 KRKAQKMT-NE-MNDLRMLLEEQNARNNllEKKQRKFDaecQSLQDAVRQERQAKER-YGREKDVLQAEKftLEQTLADT 1640
Cdd:pfam17380 259 RYNGQTMTeNEfLNQLLHIVQHQKAVSE--RQQQEKFE---KMEQERLRQEKEEKAReVERRRKLEEAEK--ARQAEMDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1641 RLDLEFKEEKLAsLQRELEemtfgggteeefaqLRRSKNETERRAKEQ--EEELDEMAGQIQLLEQAKLRLEMTLETMRK 1718
Cdd:pfam17380 332 QAAIYAEQERMA-MERERE--------------LERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERVRQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1719 EARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLssmedrDRVdRDAEEALNQKLRRdLRKY 1798
Cdd:pfam17380 397 ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM------ERV-RLEEQERQQQVER-LRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1799 KALLKDAQTQLERLKADtpgKTLIRQLRNQ-LEDAESARSLAM----KARQTAEAELTEVQ-AMFDESHRARNDAEERAN 1872
Cdd:pfam17380 469 EEERKRKKLELEKEKRD---RKRAEEQRRKiLEKELEERKQAMieeeRKRKLLEKEMEERQkAIYEEERRREAEEERRKQ 545
|
330
....*....|...
gi 116008016 1873 AAHRDRAELQAQI 1885
Cdd:pfam17380 546 QEMEERRRIQEQM 558
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1584-2070 |
5.43e-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: 61.89 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEkkqRKFDAEcQSLQDAVRQ---ERQAKERYGREKDVLQAEKFTLEQTL--ADTRLDLEF----KEEKLASL 1654
Cdd:COG3096 277 ANERRELSE---RALELR-RELFGARRQlaeEQYRLVEMARELEELSARESDLEQDYqaASDHLNLVQtalrQQEKIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1655 QRELEEMTFGggTEEE---FAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrLEMtLETmRKEARRESQQRDEEL 1731
Cdd:COG3096 353 QEDLEELTER--LEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA---LDV-QQT-RAIQYQQAVQALEKA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1732 EEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSsmedrdrvdrDAEEALNQklrrdLRKYKALLKDAQTQLER 1811
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS----------VADAARRQ-----FEKAYELVCKIAGEVER 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1812 LKADTPGKTLIRQLRNQledaesaRSLAMKArQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQaqieeneee 1891
Cdd:COG3096 491 SQAWQTARELLRRYRSQ-------QALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE--------- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1892 lgelmkkysatvkQLNTEQinvSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsmammSKRLELRTKELesrle 1971
Cdd:COG3096 554 -------------ELEELL---AELEAQLEELEEQAAEAVEQRSELRQQLEQLR----------ARIKELAARAP----- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1972 leqatrARLEVQvnrhkEALEKLQNEVTQSKmreMQAQDVIKKSQKSLRDMREefhaVSSREQESLTRRKDLEKKVEQME 2051
Cdd:COG3096 603 ------AWLAAQ-----DALERLREQSGEAL---ADSQEVTAAMQQLLERERE----ATVERDELAARKQALESQIERLS 664
|
490
....*....|....*....
gi 116008016 2052 SEGAAlkNDLRlaLQRIAD 2070
Cdd:COG3096 665 QPGGA--EDPR--LLALAE 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1647-1885 |
5.93e-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: 60.55 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1647 KEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQaklrlemtletmrkearrESQQ 1726
Cdd:COG4942 25 AEAELEQLQQEIAE------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ------------------ELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRgngyKKIKALECQLEteheertlllREKHELERRLSSMEDRDRVDRDAE----EALNQKLRRdLRKYKALL 1802
Cdd:COG4942 81 LEAELAELE----KEIAELRAELE----------AQKEELAELLRALYRLGRQPPLALllspEDFLDAVRR-LQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1803 KDAQTQLERLKADTPG-KTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAEL 1881
Cdd:COG4942 146 PARREQAEELRADLAElAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....
gi 116008016 1882 QAQI 1885
Cdd:COG4942 226 EALI 229
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1383-1947 |
8.69e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKL-EKIECDRSEVKAENQKLEAKLSELtvDLAEER---------STAHIATERLEAETAERL 1452
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWkEKRDELNGELSAADAAVAKDRSEL--EALEDQhgafldadiETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1453 KLEKELGDQTNKVKNLQETTEKLEMELICA-KSDLNGISEDEDAENEdgvgggvyklkyervarelefTKRRLHTQHEHD 1531
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIRE---------------------ARDRQLAVAEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQL-VALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEmNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVR 1610
Cdd:pfam12128 417 LQALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEVERLQSELR 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1611 QER----QAKERYGREKDVLQAEKFTLEQT-----------LADTRLDLEFKEEKLASL-QREL---------------- 1658
Cdd:pfam12128 496 QARkrrdQASEALRQASRRLEERQSALDELelqlfpqagtlLHFLRKEAPDWEQSIGKViSPELlhrtdldpevwdgsvg 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1659 EEMTFGGGT------------------EEEFAQLRRSKNETERRAKEQEEELDEMAGQI-----------QLLEQAKLRL 1709
Cdd:pfam12128 576 GELNLYGVKldlkridvpewaaseeelRERLDKAEEALQSAREKQAAAEEQLVQANGELekasreetfarTALKNARLDL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1710 EMTLETMRKEARRESQQRDEEL----EEVRG-NGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDrvdrDAE 1784
Cdd:pfam12128 656 RRLFDEKQSEKDKKNKALAERKdsanERLNSlEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD----AQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1785 EALNQKLRRDLRKYKALLKDAQTQLER-LKADTPGKTLIRQLRNQLEDAEsaRSLAMKARQtaEAELTEVQAMFDESHRA 1863
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKRdLASLGVDPDVIAKLKREIRTLE--RKIERIAVR--RQEVLRYFDWYQETWLQ 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1864 RNDA-EERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQ--VAELQ-- 1938
Cdd:pfam12128 808 RRPRlATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDanSEQAQgs 887
|
650
....*....|.
gi 116008016 1939 --HRLDNVENL 1947
Cdd:pfam12128 888 igERLAQLEDL 898
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1574-1752 |
9.60e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.01 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1574 MNDLRMLLEEQN--ARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKL 1651
Cdd:COG1579 3 PEDLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1652 ASL--QRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDE 1729
Cdd:COG1579 83 GNVrnNKEYEAL------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170 180
....*....|....*....|...
gi 116008016 1730 ELEEVRgngyKKIKALECQLETE 1752
Cdd:COG1579 157 ELEELE----AEREELAAKIPPE 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1593-1835 |
2.02e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1593 KKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELeemtfgggteeefA 1672
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------A 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQEEELDEMAGQIQLL-EQAKLRLEMTLETMRKEARRE------SQQRDEELEEVRGNgYKKIKAL 1745
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRAD-LAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1746 ECQLETEHEERTLLLREKHELERRLSSmedrdrvDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKAdtpgktLIRQL 1825
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEA------LIARL 232
|
250
....*....|
gi 116008016 1826 RNQLEDAESA 1835
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1380-1767 |
2.08e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1380 NVHRTEEQLKTANEelLMLRAKlEKIECDRSEVKAENQKleaKLSELTVDLAEERSTAHIATERLEAETAERLKL--EKE 1457
Cdd:PTZ00121 1461 EAKKKAEEAKKADE--AKKKAE-EAKKADEAKKKAEEAK---KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAK 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 LGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGggvykLKYERVARELEFTKRRLHTQHEHDLEQLVA 1537
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA-----LRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1538 --LKKHLEMKL-SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQ 1614
Cdd:PTZ00121 1610 eeAKKAEEAKIkAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1615 AKERYGREKDvlqaEKFTLEQTladtRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAkeqeEELDE 1694
Cdd:PTZ00121 1690 AAEALKKEAE----EAKKAEEL----KKKEAEEKKKAEELKKAEEE------NKIKAEEAKKEAEEDKKKA----EEAKK 1751
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1695 MAGQIQLLEQAKLRLEMTLETMRKEARRESQQR-DEELEEVRGNGYKKIKALECQLETEHE---ERTLLLREKHELE 1767
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFDNFANIIEggkEGNLVINDSKEME 1828
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1405-1877 |
2.32e-08 |
|
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: 59.60 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1405 IECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKV------KNLQETTEKLEME 1478
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvveGILKDTELTKLKE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1479 LICAKSD--LNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKhLEMKLSDAYEEVVEQ 1556
Cdd:pfam02463 640 SAKAKESglRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK-KEQREKEELKKLKLE 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1557 RQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQT 1636
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1637 LADTRLDLEFKEEKLASLQRELEEMTFG--GGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLE 1714
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQeeKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1715 TMRKEARRESQQRDEELEEVRgNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRD 1794
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1795 LRKYKALLKDAQTQLERLKadtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAA 1874
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVN--------LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
...
gi 116008016 1875 HRD 1877
Cdd:pfam02463 1030 NKG 1032
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1648-2104 |
2.80e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1648 EEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEmagqIQLLEQAKLRLEMTL---ETMRKEARRES 1724
Cdd:PRK02224 212 ESELAELDEEIERY------EEQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIaetEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1725 QQRDEELEEVRgngyKKIKAL--ECQLETEHEERTLLLREkhELERRLSSMEDRDRVDR-DAEEALNQ--KLRRDLRKYK 1799
Cdd:PRK02224 282 RDLRERLEELE----EERDDLlaEAGLDDADAEAVEARRE--ELEDRDEELRDRLEECRvAAQAHNEEaeSLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1800 ALLKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRA 1879
Cdd:PRK02224 356 ERAEELREEAAELESE------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1880 ELQAQIEENEEELGELMKKYSA----TVKQLNTEQINV---SEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdPSM 1952
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1953 AMMSKRLELRTKELESRLEL------------------------------EQATRARLEVQVNRH------------KEA 1990
Cdd:PRK02224 508 EDRIERLEERREDLEELIAErretieekreraeelreraaeleaeaeekrEAAAEAEEEAEEAREevaelnsklaelKER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1991 LEKLQNEVTQSKMREMQAQDVikksqKSLRDMREEFHAVSSREQESL----TRRKDLEKKVEQMESEGAalkndlRLALQ 2066
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEI-----ERLREKREALAELNDERRERLaekrERKRELEAEFDEARIEEA------REDKE 656
|
490 500 510
....*....|....*....|....*....|....*...
gi 116008016 2067 RIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLR 2104
Cdd:PRK02224 657 RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1510-2075 |
3.72e-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: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1510 YERVARELEFTKRRLHTqhehdLEQLVALKKHLEmKLSDAYEEVVEQRQVVGQWK--RKAQKMTNEMNDLRMLLEEQNAR 1587
Cdd:COG4913 237 LERAHEALEDAREQIEL-----LEPIRELAERYA-AARERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQ-ERQAKERYGREKDVLQAEKFT-------LEQTLADTRLDLEFKEEKLASLQRELE 1659
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEErerrrarLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1660 EmtFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDE------ELEE 1733
Cdd:COG4913 391 A--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgELIE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1734 VRG----------------------------------NGYK--------KIKALECQLETEHEERTLLLRE--------- 1762
Cdd:COG4913 469 VRPeeerwrgaiervlggfaltllvppehyaaalrwvNRLHlrgrlvyeRVRTGLPDPERPRLDPDSLAGKldfkphpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 ---KHELERRLS------------------------------SMEDRDRVDR------DAEEALN------QKLRRDLRK 1797
Cdd:COG4913 549 awlEAELGRRFDyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRIRSryvlgfDNRAKLAaleaelAELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1798 YKALLKDAQTQLERLKADtpgKTLIRQLRNQLEDAESARSLAMKARQTAE---------AELTEVQAMFDESHRARNDAE 1868
Cdd:COG4913 629 AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAelerldassDDLAALEEQLEELEAELEELE 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1869 ERANAAHRDRAELQAQIeeneeelgelmkkysatvkqlnteqinvseaefklnemeaerNNLKEQVAELQHRLDNVENLG 1948
Cdd:COG4913 706 EELDELKGEIGRLEKEL------------------------------------------EQAEEELDELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1949 DPSMAmmsKRLELRTKELESRlELEQATRARLEVQVNRHKEALEKLQNEVTQsKMREMQAQ--DVIKKSQKSLRDmREEF 2026
Cdd:COG4913 744 RLELR---ALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER-AMRAFNREwpAETADLDADLES-LPEY 817
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 2027 HAVSSR-EQESLTRRKD--LEKKVEQMESE----GAALKNDLRLALQRIADLQQAM 2075
Cdd:COG4913 818 LALLDRlEEDGLPEYEErfKELLNENSIEFvadlLSKLRRAIREIKERIDPLNDSL 873
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1802-2032 |
4.52e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1802 LKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAEL 1881
Cdd:COG4942 22 AAEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1882 QAQIEENEEELGELMKKYSATVKQ------LNTEqiNVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsmamm 1955
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQpplallLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1956 SKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSR 2032
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1383-1727 |
9.83e-08 |
|
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: 56.61 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERS-----TAHIAT--ERLEAETAERLKLE 1455
Cdd:pfam19220 59 QERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIelrdkTAQAEAleRQLAAETEQNRALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1456 KELGDQTNKVKNLQETTEKLEMELICAKSDLnGISEDEdaenedgvGGGVYKLKYERVARELEFTKRrlHTQHEHDLEQL 1535
Cdd:pfam19220 139 EENKALREEAQAAEKALQRAEGELATARERL-ALLEQE--------NRRLQALSEEQAAELAELTRR--LAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1536 VALKKHLEMKLSdayEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQ-ERQ 1614
Cdd:pfam19220 208 RARLRALEGQLA---AEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAaERR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1615 AKErygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQR---ELEEMTfgggteEEFAQLRRSKNETERRAKEQEEE 1691
Cdd:pfam19220 285 LKE--------ASIERDTLERRLAGLEADLERRTQQFQEMQRaraELEERA------EMLTKALAAKDAALERAEERIAS 350
|
330 340 350
....*....|....*....|....*....|....*..
gi 116008016 1692 L-DEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQR 1727
Cdd:pfam19220 351 LsDRIAELTKRFEVERAALEQANRRLKEELQRERAER 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1600-1823 |
1.81e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1600 AECQSLQDAVRQERQAKERygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKN 1679
Cdd:COG4942 23 AEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1680 ETERRAKEQEEELDEMAGQIQLLEQAK-----------LRLEMTLETM------RKEARRESQQRDEELEEVRGNGYKKI 1742
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLkylapaRREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1743 KALECQLETEHEERTLLLREKHELERRLSSMEDRdrvdRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLI 1822
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 116008016 1823 R 1823
Cdd:COG4942 250 A 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1838-2059 |
1.97e-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: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1838 LAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAE 1917
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1918 FKLNEMEAERNNLKEQVAEL---------QHRLDNVENLGDPS----MAMMSKRLELRTKELESRLELEQATRARLEVQV 1984
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLdavrRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1985 NRHKEALEKLQNEVTQSKmREMQAQdvIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKN 2059
Cdd:COG4942 170 EAERAELEALLAELEEER-AALEAL--KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1379-2077 |
2.40e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1379 LNVHRTEEQLKTANEELLMLRAKLEKIECD-----RSEVKAE-NQKLEAKLSELTVDL-AEERSTAHIATERLEAETAER 1451
Cdd:PTZ00121 1024 FNIEKIEELTEYGNNDDVLKEKDIIDEDIDgnhegKAEAKAHvGQDEGLKPSYKDFDFdAKEDNRADEATEEAFGKAEEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1452 LKLEKELGDQTNKVKNLQETTEKL-EMELICAKSDLNGISEDEDAENEdgvgggvyklKYERVARELEFTKRRLHTQHEH 1530
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDARKAEEARKAEDA----------KRVEIARKAEDARKAEEARKAE 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1531 DLEQLVALKKHLEMKLSdayEEVveqrqvvgqwkRKAQkmtnemnDLRMLLEEQNARNNLLEKKQRKFDAECQSlqDAVR 1610
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKA---EEL-----------RKAE-------DARKAEAARKAEEERKAEEARKAEDAKKA--EAVK 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1611 QERQAKerygreKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRsKNETERRAKEQE- 1689
Cdd:PTZ00121 1231 KAEEAK------KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKAEEKKk 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 -EELDEMAGQIQLLEQAKLRLEMTletmrKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELER 1768
Cdd:PTZ00121 1304 aDEAKKKAEEAKKADEAKKKAEEA-----KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1769 RLSSMEDRDRVDRDAEEAlNQKLRRDLRKYKALLKDAQtqlERLKADtpgktlirQLRNQLEDAESARSLAMKARQTAEA 1848
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEA-KKKAEEDKKKADELKKAAA---AKKKAD--------EAKKKAEEKKKADEAKKKAEEAKKA 1446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1849 EltEVQAMFDESHRARNDAEERANAAHRDRAELQAQieenEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAern 1928
Cdd:PTZ00121 1447 D--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK--- 1517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1929 nlkeqvAELQHRLDNVENLGDPSMAMMSKRLElrtkELESRLELEQATrarlEVQVNRHKEALEKLQNEVTQSKMREMQA 2008
Cdd:PTZ00121 1518 ------AEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAE----ELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2009 QDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEE 2077
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
390-425 |
2.72e-07 |
|
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467250 [Multi-domain] Cd Length: 75 Bit Score: 49.94 E-value: 2.72e-07
10 20 30
....*....|....*....|....*....|....*.
gi 116008016 390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEV 425
Cdd:cd06769 39 PGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTV 74
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1592-1906 |
3.61e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1592 EKKQRKfDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLE--QTLADTRLDLEFKEEKLASLQRELEEMTFGGGtee 1669
Cdd:COG4913 610 AKLAAL-EAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSD--- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1670 EFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKE----ARRESQQRDEELEEVRGN--GYKKIK 1743
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaEDLARLELRALLEERFAAalGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHE-ERTLLLREKHELERRLSS-----MEDRDRVDRDAEealnqklrrDLRKYKALLKDAQTQ-LERLKADt 1816
Cdd:COG4913 766 ELRENLEERIDaLRARLNRAEEELERAMRAfnrewPAETADLDADLE---------SLPEYLALLDRLEEDgLPEYEER- 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 pgktlIRQLRNQLEDAESAR--SLAMKARQTAEAELTEVQAM-----FDESHRARNDAEERANAAHRD-RAELQAQIEEN 1888
Cdd:COG4913 836 -----FKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSlkripFGPGRYLRLEARPRPDPEVREfRQELRAVTSGA 910
|
330
....*....|....*...
gi 116008016 1889 EEELGELMKKYSATVKQL 1906
Cdd:COG4913 911 SLFDEELSEARFAALKRL 928
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1600-1873 |
5.09e-07 |
|
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: 54.30 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1600 AECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKN 1679
Cdd:pfam19220 20 EDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAA------EGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1680 ETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGyKKIKALECQLETEHEERTLL 1759
Cdd:pfam19220 94 KLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAE-KALQRAEGELATARERLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1760 LREKH--------------ELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKT----- 1820
Cdd:pfam19220 173 EQENRrlqalseeqaaelaELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRmklea 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1821 ----------LIRQLRNQLED-------AESARSLAMKARQTAEAELTEVQA-------MFDESHRARNDAEERANA 1873
Cdd:pfam19220 253 ltaraaateqLLAEARNQLRDrdeairaAERRLKEASIERDTLERRLAGLEAdlerrtqQFQEMQRARAELEERAEM 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1720-1947 |
5.78e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1720 ARRESQQRDEELEEVRgngyKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRdrvDRDAEEALNQkLRRDLRKYK 1799
Cdd:COG4942 18 QADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAA-LEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1800 ALLKDAQTQLERLKADtpgktLIRQLRnQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARndaEERANAAHRDRA 1879
Cdd:COG4942 90 KEIAELRAELEAQKEE-----LAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR---REQAEELRADLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1880 ELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENL 1947
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1762-2074 |
7.60e-07 |
|
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: 53.92 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1762 EKHELER-RLSSMEDRDRVDRDAEEALNQKLR------RDLRKYKALLKDAQTQLERLKADTpgktliRQLRNQLEDAES 1834
Cdd:pfam19220 3 QRNELLRvRLGEMADRLEDLRSLKADFSQLIEpieailRELPQAKSRLLELEALLAQERAAY------GKLRRELAGLTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1835 ARSLAMKARQTAEAELTEVQAMFDESHRA--------------RNDAEERANAAHRDRAELQAQIEENEEELGELMKKYS 1900
Cdd:pfam19220 77 RLSAAEGELEELVARLAKLEAALREAEAAkeelrielrdktaqAEALERQLAAETEQNRALEEENKALREEAQAAEKALQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1901 ATVKQLNTEQINVSEAEfklNEMEAERNNLKEQVAE---LQHRLDNVENLGDPSMAmmskrlelRTKELESRLELEQATR 1977
Cdd:pfam19220 157 RAEGELATARERLALLE---QENRRLQALSEEQAAElaeLTRRLAELETQLDATRA--------RLRALEGQLAAEQAER 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1978 ARLEVQvnrHKEALEKLQNEVTQSKM-------REMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEqm 2050
Cdd:pfam19220 226 ERAEAQ---LEEAVEAHRAERASLRMklealtaRAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLA-- 300
|
330 340
....*....|....*....|....
gi 116008016 2051 esegaALKNDLRLALQRIADLQQA 2074
Cdd:pfam19220 301 -----GLEADLERRTQQFQEMQRA 319
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1647-2036 |
7.88e-07 |
|
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: 54.59 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1647 KEEKLA--SLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLL---EQAKLRLEMTLETMRKEAR 1721
Cdd:pfam02463 143 KIEIIAmmKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELklkEQAKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1722 RESQQRDEELEEVRgngyKKIKALECQLETEHEERTLLLRekhELERRLSSMEDRDRVDRDAEEAlnQKLRRDLRKYKAL 1801
Cdd:pfam02463 223 EEYLLYLDYLKLNE----ERIDLLQELLRDEQEEIESSKQ---EIEKEEEKLAQVLKENKEEEKE--KKLQEEELKLLAK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1802 LKDAQtQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVqamfdESHRARNDAEERANAAHRDRAEL 1881
Cdd:pfam02463 294 EEEEL-KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-----KELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1882 QAQIeeneeelgelmKKYSATVKQLNTEQINVSEAEfkLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsMAMMSKRLEL 1961
Cdd:pfam02463 368 LEQL-----------EEELLAKKKLESERLSSAAKL--KEEELELKSEEEKEAQLLLELARQLE------DLLKEEKKEE 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1962 RTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQES 2036
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1867-2113 |
8.79e-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: 53.61 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1867 AEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEn 1946
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1947 lgdpsmammsKRLELRTKELESRLeleqatrARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEF 2026
Cdd:COG4942 97 ----------AELEAQKEELAELL-------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 2027 HAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPV 2106
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
....*..
gi 116008016 2107 HVKRSSQ 2113
Cdd:COG4942 240 AERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1622-1864 |
1.37e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQL 1701
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA------LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1702 LEQAKLRLEMTLETMRKEARRESQQRDEEL--------EEVRGNGYKK--IKALECQLETEHEERTLLLREKHELERRls 1771
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALllspedflDAVRRLQYLKylAPARREQAEELRADLAELAALRAELEAE-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1772 smedrdrvdRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTpgKTLIRQLRNQLEDAESARSLAMKARQTAEAELT 1851
Cdd:COG4942 173 ---------RAELEALLAELEEERAALEALKAERQKLLARLEKEL--AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|...
gi 116008016 1852 EVQAMFDESHRAR 1864
Cdd:COG4942 242 RTPAAGFAALKGK 254
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1532-1870 |
1.94e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQ 1611
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEE 1691
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES------LQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1692 ldemagqiQLLEQAKLRLEMTLETmrKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLS 1771
Cdd:COG4372 187 --------ELLKEANRNAEKEEEL--AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1772 SMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELT 1851
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|....*....
gi 116008016 1852 EVQAMFDESHRARNDAEER 1870
Cdd:COG4372 337 AELADLLQLLLVGLLDNDV 355
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1384-1735 |
1.99e-06 |
|
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: 53.20 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEaetaerlklekELGDQTN 1463
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ-----------HLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELicAKSDLNGISEDEDAEN------EDGVGGGVykLKYERVARELEFTKRRLHTQHEHDLEQLVA 1537
Cdd:pfam15921 542 HLRNVQTECEALKLQM--AEKDKVIEILRQQIENmtqlvgQHGRTAGA--MQVEKAQLEKEINDRRLELQEFKILKDKKD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1538 LK-KHLEMKLSDAYEEVV-------EQRQVVGQWKRKAQKMTNEM----NDLRMLLEE-----QNARNNL--LEKKQRKF 1598
Cdd:pfam15921 618 AKiRELEARVSDLELEKVklvnagsERLRAVKDIKQERDQLLNEVktsrNELNSLSEDyevlkRNFRNKSeeMETTTNKL 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1599 DAECQSLQDAVRQERQA-KERYGREKDVLQAEKFTLEQTLAdtrldlefKEEKLASLQRE---LEEMTFGGGTEEEFaqL 1674
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTlKSMEGSDGHAMKVAMGMQKQITA--------KRGQIDALQSKiqfLEEAMTNANKEKHF--L 767
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1675 RRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQ--------RDEELEEVR 1735
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiQRQEQESVR 836
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1384-1833 |
2.06e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahiaterLEAETaERLKLEKElgdqTN 1463
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ-----------LKSEI-SDLNNQKE----QD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggVYKLKYERvaRELEFTKRRLHTQHEHDLEQLVALKKHLE 1543
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ-----ISQLKKEL--TNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 MKlsdayeevveqrqvvgqwKRKAQKMTNEMNDLRMLLEEQnarnnllEKKQRKFDAECQSLQdavrQERQAKErygREK 1623
Cdd:TIGR04523 381 SY------------------KQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQ----QEKELLE---KEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1624 DVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLE 1703
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL------ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1704 QAKLRLEMTLETMRKEaRRESQQRDEELEEVRGNGYKKIKALECQLETEHEE--RTLLLREKHELERRLSSMEDrdrvDR 1781
Cdd:TIGR04523 503 EEKKELEEKVKDLTKK-ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQ----TQ 577
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 116008016 1782 DAEEALNQKLRRDLRKYKALLKDAQTQLERLkadtpgKTLIRQLRNQLEDAE 1833
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEK------EKKISSLEKELEKAK 623
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1511-1821 |
2.49e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1511 ERVARELEfTKRRL---HTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQvvGQWKRKAQKMTNEmnDLRMLLEEQNAR 1587
Cdd:pfam17380 306 EEKAREVE-RRRKLeeaEKARQAEMDRQAAIYAEQERMAMERERELERIRQ--EERKRELERIRQE--EIAMEISRMREL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKD-VLQAEKFTLEQTLADTRLDLEFKEEKLASLQR-ELEEMTfgg 1665
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqKVEMEQIRAEQEEARQREVRRLEEERAREMERvRLEEQE--- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1666 gTEEEFAQLRRSKNETERRAKEQEEELDEmagQIQLLEQAKLRLEMTLETMRKEARRESQQR---DEELEEVRGNGYkki 1742
Cdd:pfam17380 458 -RQQQVERLRQQEEERKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEERKRkllEKEMEERQKAIY--- 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1743 kalecqletEHEERtlllREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDL----RKYKALLKDAQTQLERLKADTPG 1818
Cdd:pfam17380 531 ---------EEERR----REAEEERRKQQEMEERRRIQEQMRKATEERSRLEAmereREMMRQIVESEKARAEYEATTPI 597
|
...
gi 116008016 1819 KTL 1821
Cdd:pfam17380 598 TTI 600
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1564-1790 |
2.56e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 51.74 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1564 KRKAQKMTNEMNDLRMLLEE----------QNARNNLLEKKQRKFDAEcqsLQDAVRQ-----------ERQAKErYGRE 1622
Cdd:pfam15905 62 KKKSQKNLKESKDQKELEKEiralvqergeQDKRLQALEEELEKVEAK---LNAAVREktslsasvaslEKQLLE-LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAeKF----------TLEQTLADTRLDLEFK-----------EEKLASLQRELEEmtfgggTEEEFAQLRRSKNET 1681
Cdd:pfam15905 138 NELLKA-KFsedgtqkkmsSLSMELMKLRNKLEAKmkevmakqegmEGKLQVTQKNLEH------SKGKVAQLEEKLVST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1682 ERRAKEQEEELDEMAGQIQLLEQAKLRLEMT------LETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEE 1755
Cdd:pfam15905 211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYkldiaqLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESE 290
|
250 260 270
....*....|....*....|....*....|....*....
gi 116008016 1756 RTLLLREKHELERRLSS----MEDRDRVDRDAEEALNQK 1790
Cdd:pfam15905 291 KEELLREYEEKEQTLNAeleeLKEKLTLEEQEHQKLQQK 329
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1414-1718 |
5.69e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.69 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1414 AENQKLEAKLSELTVDLAEERSTAHIATER--------LEAETAERLKLEKELGdqtnkvkNLQETTE----KLEMElic 1481
Cdd:pfam00038 25 QQNKLLETKISELRQKKGAEPSRLYSLYEKeiedlrrqLDTLTVERARLQLELD-------NLRLAAEdfrqKYEDE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1482 aksdlngISEDEDAENEdgvgggVYKLKyeRVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVG 1561
Cdd:pfam00038 95 -------LNLRTSAEND------LVGLR--KDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1562 QWKRKAQKMTNEMNDLRMLLEEQNARNnlLEKKQRKFDAECQSLQDAVRQE----RQAKE----------RYGREKDVLQ 1627
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKN--REEAEEWYQSKLEELQQAAARNgdalRSAKEeitelrrtiqSLEIELQSLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1628 AEKFTLEQTLADT--RLDLEFK--EEKLASLQRELEEMtfgggteeefaqlrrsKNETERRAKEQEEELDemagqiqlle 1703
Cdd:pfam00038 238 KQKASLERQLAETeeRYELQLAdyQELISELEAELQET----------------RQEMARQLREYQELLN---------- 291
|
330
....*....|....*
gi 116008016 1704 qAKLRLEMTLETMRK 1718
Cdd:pfam00038 292 -VKLALDIEIATYRK 305
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1706-2051 |
5.81e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1706 KLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEHEErtlllreKHELERRLSSMEDRdrvdrdaEE 1785
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELE----KKASALKRQLDRESDR-------NQELQKRIRLLEKR-------EA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1786 ALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESA-RSLAMKARQTAEAELTEVQAM---FDESH 1861
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSElRRQIQRAELELQSTNSELEELqerLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1862 RARNDAEERA---NAAHRDRAELQAQIEENEEELGELmKKYSATVKQLNTEQINVSEAEF----------KLNEMEAERN 1928
Cdd:pfam05557 146 AKASEAEQLRqnlEKQQSSLAEAEQRIKELEFEIQSQ-EQDSEIVKNSKSELARIPELEKelerlrehnkHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1929 NLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTkELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQA 2008
Cdd:pfam05557 225 LLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ-ELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLT 303
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 116008016 2009 QDViKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQME 2051
Cdd:pfam05557 304 SSA-RQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ 345
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1385-1927 |
6.28e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETaERLKLEKELGDQTNK 1464
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR-SGLKVLLALIKDGVG 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 VKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVA--------RELEFTKRRLHTQHEHDLEQLV 1536
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgarkLRLLIPKLKLPLKSIAVLEIDP 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1537 ALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNL------------LEKKQRKFDAECQS 1604
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeksevkasLSELTKELLEIQEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1605 LQDAVRQERQAKERYGREKDVLQAEKFTLEQT---LADTRLDLEFKEEKLA----SLQRELEEMTFGGGTEEEFAQLRRS 1677
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDkineELKLLKQKIDEEEEEEEKSRLKKEE 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1678 KNETERRAKEQEEELDEMAGQIQL------LEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALEcQLET 1751
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKlkveeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE-ELAL 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1752 EHEERTLLLREKHELERRLSSM----EDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTpGKTLIRQLRN 1827
Cdd:pfam02463 841 ELKEEQKLEKLAEEELERLEEEitkeELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-NLLEEKENEI 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1828 QLEDAESARSLAMKARQTAEaELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLN 1907
Cdd:pfam02463 920 EERIKEEAEILLKYEEEPEE-LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
570 580
....*....|....*....|
gi 116008016 1908 TEQINVSEAEFKLNEMEAER 1927
Cdd:pfam02463 999 RLEEEKKKLIRAIIEETCQR 1018
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1642-1815 |
6.48e-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: 49.54 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1642 LDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEmagqiqlLEQAKLRLEMTLETMRKEAR 1721
Cdd:COG1579 10 LDLQELDSELDRLEHRLKEL------PAELAELEDELAALEARLEAAKTELED-------LEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1722 RESQQrdeeLEEVRGNgyKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKAL 1801
Cdd:COG1579 77 KYEEQ----LGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....
gi 116008016 1802 LKDAQTQLERLKAD 1815
Cdd:COG1579 151 LAELEAELEELEAE 164
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1584-1940 |
9.05e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEK--KQRKFDAECQSLQDAvrqERQAKERYGREKDVLQAEKFTLEQTL--ADTRLDL----EFKEEKLASLQ 1655
Cdd:PRK04863 278 ANERRVHLEEalELRRELYTSRRQLAA---EQYRLVEMARELAELNEAESDLEQDYqaASDHLNLvqtaLRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1656 RELEEMTFGGGTEEEFAQLRRS-KNETERRAKEQEEELDEMAGQIQLLEQAklrLEMtLETmRKEARRESQQRDEELEEV 1734
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQQA---LDV-QQT-RAIQYQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1735 RGN---GYKKIKALECQLETEHEERTLLLREkheLERRLSSMED-RDRVDR------------DAEEALN--QKLRRDLR 1796
Cdd:PRK04863 430 CGLpdlTADNAEDWLEEFQAKEQEATEELLS---LEQKLSVAQAaHSQFEQayqlvrkiagevSRSEAWDvaRELLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1797 KYKALlkDAQTQLERLKAdtpgKTLIRQLRNQLEDAESARSLAMKARQTAEAElTEVQAMFDESHRARNDAEERANAAHR 1876
Cdd:PRK04863 507 EQRHL--AEQLQQLRMRL----SELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1877 DRAELQAQIEENEEELGELMKK------YSATVKQLNTE------------------QINVSEAEFKLNEMEAERNNLKE 1932
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARapawlaAQDALARLREQsgeefedsqdvteymqqlLERERELTVERDELAARKQALDE 659
|
....*...
gi 116008016 1933 QVAELQHR 1940
Cdd:PRK04863 660 EIERLSQP 667
|
|
| PDZ4_GRIP1-2-like |
cd06686 |
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
345-430 |
9.17e-06 |
|
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467174 [Multi-domain] Cd Length: 99 Bit Score: 46.18 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 345 SPRQDFGFSLRKAICLdrTESLTSPifrPVI-FAEPGAGGGAT-GLLPGDRLIKVNGTPVGELPREIIIEMIRNSGEAVT 422
Cdd:cd06686 15 DPLKGFGIQLQGGVFA--TETLSSP---PLIsFIEPDSPAERCgVLQVGDRVLSINGIPTEDRTLEEANQLLRDSASKVT 89
|
....*....
gi 116008016 423 VEVQ-PVAE 430
Cdd:cd06686 90 LEIEfDVAE 98
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1663-1843 |
1.31e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.09 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1663 FGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEE----LEEVRGNG 1738
Cdd:PRK12705 17 LLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEErlvqKEEQLDAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1739 YKKIKALECQLETehEERTLLLREKhELERRLSSMEDR-DRVDRDAEEALNQ----KLRRDLRKYKALLKDAQTQLERLK 1813
Cdd:PRK12705 97 AEKLDNLENQLEE--REKALSAREL-ELEELEKQLDNElYRVAGLTPEQARKlllkLLDAELEEEKAQRVKKIEEEADLE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 116008016 1814 ADTPGKTLIRQLRNQL-EDAESARSL--------AMKAR 1843
Cdd:PRK12705 174 AERKAQNILAQAMQRIaSETASDLSVsvvpipsdAMKGR 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1781-2074 |
1.34e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1781 RDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDES 1860
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREE------LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1861 HRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHR 1940
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1941 LDNVENlgdpsmAMMSKRLELRTKELESRLELEQATRarlEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLR 2020
Cdd:COG4372 173 LQALSE------AEAEQALDELLKEANRNAEKEEELA---EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 116008016 2021 DMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQA 2074
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1540-1884 |
1.47e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLEMKLSDAY------EEVVEQRQVVGQWKRKAQKMTNEMNDLRM-LLEEQNARNNLLEKKQRKFDAE-CQSLQDAVRQ 1611
Cdd:pfam13868 9 RELNSKLLAAKcnkerdAQIAEKKRIKAEEKEEERRLDEMMEEERErALEEEEEKEEERKEERKRYRQElEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKERYGREKDVLQAEkftLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggteeefaqlRRSKNETERRAKEQEEE 1691
Cdd:pfam13868 89 RQEEYEEKLQEREQMDEI---VERIQEEDQAEAEEKLEKQRQLREEIDEF-------------NEEQAEWKELEKEEERE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1692 LDEmagqiQLLEQAKLRLEMTLETMRKEARREsQQRDEELEEVRGNGYKKIKALEcqletEHEE-RTLLLREKHELERRL 1770
Cdd:pfam13868 153 EDE-----RILEYLKEKAEREEEREAEREEIE-EEKEREIARLRAQQEKAQDEKA-----ERDElRAKLYQEEQERKERQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1771 SSMEDRDRvdRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADtpgktliRQLRNQLEDAESARSLAMKARQTAEAEL 1850
Cdd:pfam13868 222 KEREEAEK--KARQRQELQQAREEQIELKERRLAEEAEREEEEFE-------RMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
330 340 350
....*....|....*....|....*....|....
gi 116008016 1851 TEVQAMFDESHRARNDAEERANAAHRDRAELQAQ 1884
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1630-1838 |
1.82e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1630 KFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKN--ETERRAKEQEEELDEMAGQIQLLEQAKL 1707
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE------AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1708 RLEMTLETMRKEARRESQQRDEELEEVRGNGYK-KIKALECQLET-------EHEERTLLLREKHELERRLSSMEDRDRV 1779
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPVIQQLRaQLAELEAELAElsarytpNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1780 DRDAE----EALNQKLRRDLRKYKALLK---DAQTQLERLKAD-TPGKTLIRQLRNQLEDAESARSL 1838
Cdd:COG3206 317 SLEAElealQAREASLQAQLAQLEARLAelpELEAELRRLEREvEVARELYESLLQRLEEARLAEAL 383
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1634-2067 |
1.91e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1634 EQTLADTRLDLEFKEEKLASLQRELEEM-----------------TFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMA 1696
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLqrlhqafsrfigshlavAFEADPEAELRQLNRRRVELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1697 GQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEvrgngyKKIKALECQLETEHEERTLllrekHELERRLSSM--- 1773
Cdd:PRK04863 865 SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIRE------QLDEAEEAKRFVQQHGNAL-----AQLEPIVSVLqsd 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 -EDRDRVDRDAEEAlnQKLRRDLRKYKALLKDAQTQLERLK-ADTPGKT-----LIRQLRNQLEDAESARSLAMKARQTA 1846
Cdd:PRK04863 934 pEQFEQLKQDYQQA--QQTQRDAKQQAFALTEVVQRRAHFSyEDAAEMLaknsdLNEKLRQRLEQAEQERTRAREQLRQA 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTE---VQAMFDESHRARND-------------------AEERAnAAHRDraELQAQIEENEEELGELMKKYSATVK 1904
Cdd:PRK04863 1012 QAQLAQynqVLASLKSSYDAKRQmlqelkqelqdlgvpadsgAEERA-RARRD--ELHARLSANRSRRNQLEKQLTFCEA 1088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQINVSEAEFKLNEMEAERNNLK-------EQVAE--LQHRLDNVE--NLGDPSMAMMS-KRLELRTKELESRLEL 1972
Cdd:PRK04863 1089 EMDNLTKKLRKLERDYHEMREQVVNAKagwcavlRLVKDngVERRLHRRElaYLSADELRSMSdKALGALRLAVADNEHL 1168
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1973 EQATR-----ARLEVQVNRHKEALEKLqnevtqskmREMQAQDVIKKSQKslRDMREEFHAVSSREQESLTRRkdlEKKV 2047
Cdd:PRK04863 1169 RDVLRlsedpKRPERKVQFYIAVYQHL---------RERIRQDIIRTDDP--VEAIEQMEIELSRLTEELTSR---EQKL 1234
|
490 500
....*....|....*....|
gi 116008016 2048 eQMESEGAAlkNDLRLALQR 2067
Cdd:PRK04863 1235 -AISSESVA--NIIRKTIQR 1251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1384-2051 |
2.20e-05 |
|
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: 50.05 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1384 TEEQLKTANEELLMLRAKLEKIECDRSEV-------------KAENQKLEAKLSELTVDL-------------------- 1430
Cdd:TIGR00606 236 SREIVKSYENELDPLKNRLKEIEHNLSKImkldneikalksrKKQMEKDNSELELKMEKVfqgtdeqlndlyhnhqrtvr 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1431 --AEERSTAHIATERLEAE----TAERLKLEKELGDQTNKVKNLQETTEK--LEMELICAKSDLNGISEDEDAENEDGvg 1502
Cdd:TIGR00606 316 ekERELVDCQRELEKLNKErrllNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDGFERGPFSERQIK-- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1503 gGVYKLKYERVAREleftkRRLHTQHEHDLEQLVALKKHLEMKLSDayeevvEQRQVVGQWKRKAQKMTNEMNDLRMLLE 1582
Cdd:TIGR00606 394 -NFHTLVIERQEDE-----AKTAAQLCADLQSKERLKQEQADEIRD------EKKGLGRTIELKKEILEKKQEELKFVIK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1583 E-QNAR---NNLLEKKQrkfdaecqSLQDAVRQERQAkerygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQREL 1658
Cdd:TIGR00606 462 ElQQLEgssDRILELDQ--------ELRKAERELSKA------EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1659 EEMTFGGGTEEEFAQLRRSKNETERRAKEQEEelDEMAGQIQLLEQAKLrLEMTLETMRKEARresqQRDEELEEVRgng 1738
Cdd:TIGR00606 528 NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHS--DELTSLLGYFPNKKQ-LEDWLHSKSKEIN----QTRDRLAKLN--- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1739 yKKIKALEcqlETEHEERtlllREKHELERRLSSMEDR--DRVDRDAEEALNQKLRRDL---RKYKALL----------- 1802
Cdd:TIGR00606 598 -KELASLE---QNKNHIN----NELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIeksSKQRAMLagatavysqfi 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1803 ---------------KDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDA 1867
Cdd:TIGR00606 670 tqltdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1868 EERANAAHRDRAELQAQIEENEEELGELM-KKYSATVKQLNTEQINVSEAEFKLNEMEAER--------------NNLKE 1932
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEEQETLLGTIMpEEESAKVCLTDVTIMERFQMELKDVERKIAQqaaklqgsdldrtvQQVNQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1933 QVAELQHRLDNVENLGDPSMAMMSKRLElRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVT--QSKMREM-QAQ 2009
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIELNRKLIQDQQE-QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevQSLIREIkDAK 908
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 116008016 2010 DVIKKSQKSLRDMREefhavssrEQESLTRRKDLEKKVEQME 2051
Cdd:TIGR00606 909 EQDSPLETFLEKDQQ--------EKEELISSKETSNKKAQDK 942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1715-1885 |
2.40e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1715 TMRKEARR--ESQQRD---EELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMED-----RDRVDRDaE 1784
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieevEARIKKY-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1785 EALNQKlrRDLRKYKALLKDAQTqLERLKADTpgKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDEshrAR 1864
Cdd:COG1579 80 EQLGNV--RNNKEYEALQKEIES-LKRRISDL--EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---EL 151
|
170 180
....*....|....*....|.
gi 116008016 1865 NDAEERANAAHRDRAELQAQI 1885
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| PDZ |
smart00228 |
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
390-427 |
2.42e-05 |
|
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 44.68 E-value: 2.42e-05
10 20 30
....*....|....*....|....*....|....*...
gi 116008016 390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQP 427
Cdd:smart00228 46 VGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLR 83
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1648-1912 |
2.71e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1648 EEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQI-QLLEQAKLRLEMtLETMRKEARRESQQ 1726
Cdd:COG1340 7 SSSLEELEEKIEEL------REEIEELKEKRDELNEELKELAEKRDELNAQVkELREEAQELREK-RDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRGNgYKKIKalecQLETEHEERTLLLREKHELERRLSSMEDR---DRVDRDAEEALNQKLRRdlrkYKALLK 1803
Cdd:COG1340 80 RDELNEKLNEL-REELD----ELRKELAELNKAGGSIDKLRKEIERLEWRqqtEVLSPEEEKELVEKIKE----LEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1804 DAQTQLERLKADTPGKTLIRQLRNQLEDA-ESARSLAMKARQTAEA------ELTEVQAMFDESHRARNDAEERANAAHR 1876
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIhKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 116008016 1877 DRAELQAQIEENEEELGELMKKYSATVKQLNTEQIN 1912
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1372-2060 |
2.88e-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: 49.66 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1372 LVRVTPllnvHRTEEQLKTANEELLMLRAKLEKIECDrsEVKAENQKLEAKLSELTVDLAEERStahiateRLEaetaer 1451
Cdd:TIGR01612 639 LAKISP----YQVPEHLKNKDKIYSTIKSELSKIYED--DIDALYNELSSIVKENAIDNTEDKA-------KLD------ 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1452 lKLEKELGDQTNKVKNLQETTEKLEMELIcaksdlngisedEDAENEdgvgggvyklkyerVARELEFTKRRLHTQHEHD 1531
Cdd:TIGR01612 700 -DLKSKIDKEYDKIQNMETATVELHLSNI------------ENKKNE--------------LLDIIVEIKKHIHGEINKD 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDlrmlleeQNARNNLLEkkqrkfdaecqslQDAVRQ 1611
Cdd:TIGR01612 753 LNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-------QINIDNIKD-------------EDAKQN 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKErYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGgtEEEFAQL-RRSKNETerrakeQEE 1690
Cdd:TIGR01612 813 YDKSKE-YIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSE--HEQFAELtNKIKAEI------SDD 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1691 ELDEMAGQIQlleQAKLRLEMTLETMRKEarresQQRDEELEEVrgNGYKKI-KALECQLETEHEERTLLlreKHELERR 1769
Cdd:TIGR01612 884 KLNDYEKKFN---DSKSLINEINKSIEEE-----YQNINTLKKV--DEYIKIcENTKESIEKFHNKQNIL---KEILNKN 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1770 LSSMEDRDRVDRDAEEalnqklrrdlrKYKALLKDAQTQLERLKADTpgktlirqlrnQLEDAESARSLAMKARQTAEAE 1849
Cdd:TIGR01612 951 IDTIKESNLIEKSYKD-----------KFDNTLIDKINELDKAFKDA-----------SLNDYEAKNNELIKYFNDLKAN 1008
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1850 LTEVQA-----MFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKK-YSATVKQLNT---EQINVSEAEFkl 1920
Cdd:TIGR01612 1009 LGKNKEnmlyhQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKeIGKNIELLNKeilEEAEINITNF-- 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1921 nemeaerNNLKEQVaelqhRLDNVENLGDPSMAMMSKRLELRTKELESrleleqatrarLEVQVNRHKEALEKLQNEvTQ 2000
Cdd:TIGR01612 1087 -------NEIKEKL-----KHYNFDDFGKEENIKYADEINKIKDDIKN-----------LDQKIDHHIKALEEIKKK-SE 1142
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 2001 SKMREMQAQ--DVIKKSQKSLRDmrEEFHAVSSREQESLT---RRKDLEKKVEQMESEGAALKND 2060
Cdd:TIGR01612 1143 NYIDEIKAQinDLEDVADKAISN--DDPEEIEKKIENIVTkidKKKNIYDEIKKLLNEIAEIEKD 1205
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1568-1704 |
3.32e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.82 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1568 QKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDavrqERQAKERYGREKDVLQAEKftLEQTLADTRLDLEFK 1647
Cdd:pfam15619 63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRD----QLKRLEKLSEDKNLAEREE--LQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1648 EEKLASLQRELEEMTfgggteeefAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQ 1704
Cdd:pfam15619 137 DEKIQDLERKLELEN---------KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQ 184
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1613-2070 |
3.39e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1613 RQAKERYGREKDVLqaekfTLEQTLADTRLDLEFKEEKLASLQRELEEMTFG-GGTEEEFAQLRRSKN--ETERRAKEQE 1689
Cdd:PRK04863 276 RHANERRVHLEEAL-----ELRRELYTSRRQLAAEQYRLVEMARELAELNEAeSDLEQDYQAASDHLNlvQTALRQQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 E----ELDEMagQIQLLEQAKLRLEMTLETMRKEARRES---------------QQRDEE--------------LEEVRG 1736
Cdd:PRK04863 351 EryqaDLEEL--EERLEEQNEVVEEADEQQEENEARAEAaeeevdelksqladyQQALDVqqtraiqyqqavqaLERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1737 -NGY-----KKIKALECQLETEHEERTLLLRekhELERRLSSmedrdrvdrdAEEALNQklrrdLRKYKALLKDAQTQLE 1810
Cdd:PRK04863 429 lCGLpdltaDNAEDWLEEFQAKEQEATEELL---SLEQKLSV----------AQAAHSQ-----FEQAYQLVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1811 RLKADTPGKTLIRQLRNQLEDAESARSLamkarqtaEAELTEVQamfdESHRARNDAEERANAAHrdraelqaqieenee 1890
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQLQQL--------RMRLSELE----QRLRQQQRAERLLAEFC--------------- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1891 elgelmkkysatvKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRldnvenlgdpsmammskRLELRT--KELES 1968
Cdd:PRK04863 544 -------------KRLGKNLDDEDELEQLQEELEARLESLSESVSEARER-----------------RMALRQqlEQLQA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1969 RL-ELEQATRARLEVQvnrhkEALEKLQnevTQSKMREMQAQDVIKKSQKSLRDMREefhaVSSREQESLTRRKDLEKKV 2047
Cdd:PRK04863 594 RIqRLAARAPAWLAAQ-----DALARLR---EQSGEEFEDSQDVTEYMQQLLERERE----LTVERDELAARKQALDEEI 661
|
490 500
....*....|....*....|...
gi 116008016 2048 EQMESEGAAlkNDLRlaLQRIAD 2070
Cdd:PRK04863 662 ERLSQPGGS--EDPR--LNALAE 680
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1381-1823 |
3.83e-05 |
|
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: 48.80 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1381 VHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1461 QTNKVKNLQETTEKLEmELICAKSDLNGISEDEDAENEDGVGGGVYKLK------YERVARELEFTKRRLHTQHEHDLEQ 1534
Cdd:COG5185 241 PESELEDLAQTSDKLE-KLVEQNTDLRLEKLGENAESSKRLNENANNLIkqfentKEKIAEYTKSIDIKKATESLEEQLA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1535 LVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNaRNNLLEKKQRKFDAECQSLQDAVRQERQ 1614
Cdd:COG5185 320 AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1615 AKERYGREkdvlqaekftLEQTLADTrldLEFKEEKLASLQRELEemtfggGTEEEFAQLRRSKNETERRAKEQEEELDE 1694
Cdd:COG5185 399 NQRGYAQE----------ILATLEDT---LKAADRQIEELQRQIE------QATSSNEEVSKLLNELISELNKVMREADE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGqiQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:COG5185 460 ESQ--SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAH 537
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 116008016 1775 DRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIR 1823
Cdd:COG5185 538 ILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAR 586
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1380-1862 |
3.86e-05 |
|
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: 49.02 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1380 NVHRTEEQLKTANEELLMLRAKLEKIECDRSEvkAENQKLeaklsELTVDLaeerstahiatERLEAETAERLKLEKELG 1459
Cdd:pfam01576 679 NVHELERSKRALEQQVEEMKTQLEELEDELQA--TEDAKL-----RLEVNM-----------QALKAQFERDLQARDEQG 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1460 DQtnKVKNLQETTEKLEMELicaksdlngisEDEDAENEDGVGGgvyKLKYERVARELEFTKRRLHTQHEHDLEQLvalk 1539
Cdd:pfam01576 741 EE--KRRQLVKQVRELEAEL-----------EDERKQRAQAVAA---KKKLELDLKELEAQIDAANKGREEAVKQL---- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLEMKLSDAYEEVVEQRQ----VVGQWKRKAQKMTNEMNDLRMLLEEQNARnnllEKKQRKFDAECQSLQDAVRQERQA 1615
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARAsrdeILAQSKESEKKLKNLEAELLQLQEDLAAS----ERARRQAQQERDELADEIASGASG 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1616 KERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRS-KNETERRAKEQEEELDE 1694
Cdd:pfam01576 877 KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESaRQQLERQNKELKAKLQE 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGQIqlleqaKLRLEMTLETMrkEArresqqrdeeleevrgngykKIKALECQLETEHEERT----LLLREKHELERRL 1770
Cdd:pfam01576 957 MEGTV------KSKFKSSIAAL--EA--------------------KIAQLEEQLEQESRERQaankLVRRTEKKLKEVL 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1771 SSMEDRdrvdrdaeealnqklRRDLRKYKallkdaqTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAEL 1850
Cdd:pfam01576 1009 LQVEDE---------------RRHADQYK-------DQAEKGNSR------MKQLKRQLEEAEEEASRANAARRKLQREL 1060
|
490
....*....|..
gi 116008016 1851 TEVQAMFDESHR 1862
Cdd:pfam01576 1061 DDATESNESMNR 1072
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
339-426 |
5.15e-05 |
|
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467153 [Multi-domain] Cd Length: 81 Bit Score: 43.69 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 339 VIRRQKSPRQDFGFSLRkaicldRTESLTSPIFrpVIFAEPGAGGGATGL-LPGDRLIKVNGTPVGELPREIIIEMIRNS 417
Cdd:cd00136 1 TVTLEKDPGGGLGFSIR------GGKDGGGGIF--VSRVEPGGPAARDGRlRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 116008016 418 GEAVTVEVQ 426
Cdd:cd00136 73 GGEVTLTVR 81
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1818-2005 |
5.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1818 GKTLIRQLRnQLEDAESARslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEElgelmK 1897
Cdd:COG4717 63 GRKPELNLK-ELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY-----Q 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1898 KYSATVKQLNTEQINVSEAEFK---LNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQ 1974
Cdd:COG4717 133 ELEALEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|.
gi 116008016 1975 ATRARLEVQVNRHKEALEKLQNEVTQSKMRE 2005
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
693-829 |
5.27e-05 |
|
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: 48.59 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 693 ILEAFGNTKTCLNSNATRMTQLLSLDF-----DQTGQIASASLQVLLPERQRA----GRRLG--HEHSFHIMTRLLAGAA 761
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVtserGRESGdqNELNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 762 G-----LLQKELHLENIT-------SEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG 829
Cdd:cd14894 335 AfpfmrLLAKELHLDGIDcsaltylGRSDHKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWLG 414
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1682-1872 |
5.80e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1682 ERRAKEQEEELDEMAGQIqlLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLEtEHEERtlllr 1761
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI--LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL-QKEEN----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1762 ekheLERRLSSMEDRDRVDRDAEEALNQKLrRDLRK----YKALLKDAQTQLERLKADTpgktlirqlrnqledAESARS 1837
Cdd:PRK12704 98 ----LDRKLELLEKREEELEKKEKELEQKQ-QELEKkeeeLEELIEEQLQELERISGLT---------------AEEAKE 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 116008016 1838 LAMKarqTAEAEL-TEVQAMFDESH-RARNDAEERAN 1872
Cdd:PRK12704 158 ILLE---KVEEEArHEAAVLIKEIEeEAKEEADKKAK 191
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1527-2065 |
6.74e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.98 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1527 QHEHDLEQLVALkkhLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTN-EMNDLRMLLEEQNARNNLLEKKQRKFDAECQSL 1605
Cdd:pfam15964 64 QHSHAVNQLKAL---LQQQTKKENELSPRRRKLSPSRTSEDESSSLpTVHDLVPIINDQSQYIHHLEAEVKFCKEELSEM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1606 QDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQlRRSKNETERRA 1685
Cdd:pfam15964 141 KQRVQVVVLENEKLQQELKSQTQEETLREQTLLDSSGNMQNSWCTPEDSRVHQTSKRPASHNLAERLK-SATTGEDEKWR 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1686 KEQEeeldemagQIQLLEQAKLR-LEMTLETMRKEARrESQQRDEELEE--------VRGNGYKKIKALeCQLETEHEEr 1756
Cdd:pfam15964 220 LELE--------KLKLLYEAKTEvLESQVKSLRKDLA-ESQKTCEDLKErlkhkeslVAASTSSRVGGL-CLKCAQHEA- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1757 tlLLREKHE------LERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYK----ALLKDAQTQLERLKAdtpgktLIR--Q 1824
Cdd:pfam15964 289 --VLAQTHTnvhmqtIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEqvkqAVQMTEEANFEKTKA------LIQceQ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1825 LRNQLEDAESARSLAMKARQTAEAEltEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVK 1904
Cdd:pfam15964 361 LKSELERQKERLEKELASQQEKRAQ--EKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQINVS----EAEFKLNEmeaerNNLKEQVAELQHRldnvenlgdpsmammskrlELRTKeLESRLELEQATRARL 1980
Cdd:pfam15964 439 QLASQEMDVTkvcgEMRYQLNQ-----TKMKKDEAEKEHR-------------------EYRTK-TGRQLEIKDQEIEKL 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1981 EVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAV--------SSREQESLTRRKDLEKKVEQMES 2052
Cdd:pfam15964 494 GLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIqqsfsneaKAQALQAQQREQELTQKMQQMEA 573
|
570
....*....|...
gi 116008016 2053 EGAALKNDLRLAL 2065
Cdd:pfam15964 574 QHDKTVNEQYSLL 586
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1745-2074 |
9.05e-05 |
|
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: 47.38 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1745 LECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQklrrdLRKYKALLKDAQTQLE------RLKADTPG 1818
Cdd:pfam05622 19 LDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLL-----LQKQLEQLQEENFRLEtarddyRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1819 KTLIR-QLRNQledaesarslamkarqtaeaELT----EVQAMFDESHRARNDAEERAnaahrdRAELQAQIEENEEELG 1893
Cdd:pfam05622 94 KEVLElQHRNE--------------------ELTslaeEAQALKDEMDILRESSDKVK------KLEATVETYKKKLEDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1894 ELMKKysaTVKQL---NTEQI-NVSEAEFKLNEMEAERNNL---KEQVAELQHRLDnvenlgdpSMAMMSKRLELRTKEL 1966
Cdd:pfam05622 148 GDLRR---QVKLLeerNAEYMqRTLQLEEELKKANALRGQLetyKRQVQELHGKLS--------EESKKADKLEFEYKKL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1967 ESRLELEQATRARLEVQVNRHKEALEKLQneVTQSKMREM-QAQDVIKKSQKSLRDMREEFHAVSSRE------------ 2033
Cdd:pfam05622 217 EEKLEALQKEKERLIIERDTLRETNEELR--CAQLQQAELsQADALLSPSSDPGDNLAAEIMPAEIREklirlqhenkml 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 116008016 2034 ---QESLTRRK--DLEKKVEQMESEGAALKNDLRLALQRIADLQQA 2074
Cdd:pfam05622 295 rlgQEGSYRERltELQQLLEDANRRKNELETQNRLANQRILELQQQ 340
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1524-2004 |
9.52e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1524 LHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQK-------MTNEMNDLRMLLEEQNARNNLLEKKQR 1596
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1597 KFDAECQSLQDAvrqERQAKErygrekdvlqaekftLEQTLA---DTRLDLEFKEEKLAS---LQRELEEMtfgggtEEE 1670
Cdd:pfam05557 157 NLEKQQSSLAEA---EQRIKE---------------LEFEIQsqeQDSEIVKNSKSELARipeLEKELERL------REH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1671 FAQLRrSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEArresqQRDEELEEVRGNGYKKIKALECQLE 1750
Cdd:pfam05557 213 NKHLN-ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQEL-----QSWVKLAQDTGLNLRSPEDLSRRIE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1751 TEHEERTLLLREKHELERRLSSMEdrdrvdrdaeeALNQKLRRDLRKYKALLKDAQTQLERLKAdtpgktLIRQLRNQLE 1830
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLE-----------KARRELEQELAQYLKKIEDLNKKLKRHKA------LVRRLQRRVL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1831 DAESARSLAMKARQTAEAELTEVQAMFDESHRARnDAEERANAAHRDRAELQAQIEENEEelgelmkkySATVKQLNTEQ 1910
Cdd:pfam05557 350 LLTKERDGYRAILESYDKELTMSNYSPQLLERIE-EAEDMTQKMQAHNEEMEAQLSVAEE---------ELGGYKQQAQT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1911 INVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsmaMMSKRLELRTKELESRLE-------LEQATRARLEVQ 1983
Cdd:pfam05557 420 LERELQALRQQESLADPSYSKEEVDSLRRKLETLE--------LERQRLREQKNELEMELErrclqgdYDPKKTKVLHLS 491
|
490 500
....*....|....*....|....*...
gi 116008016 1984 VN-------RHKEALEKLQNEVTQSKMR 2004
Cdd:pfam05557 492 MNpaaeayqQRKNQLEKLQAEIERLKRL 519
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1612-1775 |
1.03e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKERYGREK---DVLQAEkfTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggteEEFAQLRRSKNETERRAKEQ 1688
Cdd:COG2433 356 EKKVPPDVDRDEvkaRVIRGL--SIEEALEELIEKELPEEEPEAEREKEHEE--------RELTEEEEEIRRLEEQVERL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1689 EEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESqQRDEELEEVRgngyKKIKALECQLETEHEERtlllrekHELER 1768
Cdd:COG2433 426 EAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLD----REIERLERELEEERERI-------EELKR 493
|
....*..
gi 116008016 1769 RLSSMED 1775
Cdd:COG2433 494 KLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1414-1661 |
1.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1414 AENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELicaksdlngisede 1493
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1494 daenedgvgggvyklkyERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMklsdAYEEVVEQRQVVGQWKRKAQKMTNE 1573
Cdd:COG4942 86 -----------------AELEKEIAELRAELEAQKEELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1574 MNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLAS 1653
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....*...
gi 116008016 1654 LQRELEEM 1661
Cdd:COG4942 225 LEALIARL 232
|
|
| PDZ4_MAGI-1_3-like |
cd06734 |
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
390-427 |
1.46e-04 |
|
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467216 [Multi-domain] Cd Length: 84 Bit Score: 42.22 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*...
gi 116008016 390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQP 427
Cdd:cd06734 47 VGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1515-1832 |
1.48e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1515 RELEFTKRRLHTQHEH------DLEQLVALKKHLEMklsdAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRML---LEEQN 1585
Cdd:COG3096 292 RELFGARRQLAEEQYRlvemarELEELSARESDLEQ----DYQAASDHLNLVQTALRQQEKIERYQEDLEELterLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1586 -----ARNNLLEKKQRKFDAECQ----------------SLQDAVRQERQAKERYGREKDVLQAEKFTLEQtLADTRLDL 1644
Cdd:COG3096 368 evveeAAEQLAEAEARLEAAEEEvdslksqladyqqaldVQQTRAIQYQQAVQALEKARALCGLPDLTPEN-AEDYLAAF 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1645 EFKEEKLASLQRELEE-MTFGGGTEEEFAQ----LRRSKNETER-----RAKEQEEELDE---MAGQIQLLEQAKLRLEM 1711
Cdd:COG3096 447 RAKEQQATEEVLELEQkLSVADAARRQFEKayelVCKIAGEVERsqawqTARELLRRYRSqqaLAQRLQQLRAQLAELEQ 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1712 TLETMRKE-------ARRESQQRD--EELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRD 1782
Cdd:COG3096 527 RLRQQQNAerlleefCQRIGQQLDaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA 606
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 116008016 1783 AEEALNQkLRRD----LRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDA 1832
Cdd:COG3096 607 AQDALER-LREQsgeaLADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1599-1942 |
1.52e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1599 DAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSK 1678
Cdd:pfam13868 2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKE------EERKEERKRYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1679 NE-----TERRAKEQEEELDEMAGQIQLLE-QAKLRLEMTLETMRKEARRESQQRD-EELEEVRgngyKKIKALECQLET 1751
Cdd:pfam13868 76 QEleeqiEEREQKRQEEYEEKLQEREQMDEiVERIQEEDQAEAEEKLEKQRQLREEiDEFNEEQ----AEWKELEKEEER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1752 EHEERTLL-LREKHELERRLssmEDRDRVDRDAEEALNQKLRRDLRKykalLKDAQTQLERLKADTPGKTLIRQLR-NQL 1829
Cdd:pfam13868 152 EEDERILEyLKEKAEREEER---EAEREEIEEEKEREIARLRAQQEK----AQDEKAERDELRAKLYQEEQERKERqKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1830 EDAESARSLAMKARQTAEAELTEVQAMFDEshrARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTE 1909
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQIELKERRLAE---EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350
....*....|....*....|....*....|...
gi 116008016 1910 QINVSEAEFKlnEMEAERNNLKEQVAELQHRLD 1942
Cdd:pfam13868 302 REEQRAAERE--EELEEGERLREEEAERRERIE 332
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1725-2060 |
1.70e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.64 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1725 QQRDEELEEVRGNGYKkikaLECQLETEHEERTLLLREKHelerrLSSMEDRDRvdrdaEEALNQKLRRDLRKYKALLKD 1804
Cdd:pfam03528 7 QQRVAELEKENAEFYR----LKQQLEAEFNQKRAKFKELY-----LAKEEDLKR-----QNAVLQEAQVELDALQNQLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1805 AQTQLERLKA-----DTPGKTLIRQLRNQLEDAESARSLAMKA-----------------------RQTAEAELTEVQAM 1856
Cdd:pfam03528 73 ARAEMENIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKEtvreyevqfhrrleqeraqwnqyRESAEREIADLRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1857 FDESHRARNdAEERANAAHRDRAELQAQIeeneeelgELMKKYSATVKQlnteqiNVSEAEFKLNEMEAERnnlkeqVAE 1936
Cdd:pfam03528 153 LSEGQEEEN-LEDEMKKAQEDAEKLRSVV--------MPMEKEIAALKA------KLTEAEDKIKELEASK------MKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1937 LQHRLDnVENLGDPSMAMMSKRLELRTKELEsrlelEQATRARLEVQVNRHKEALEKLQNevTQSKMREMQAQDVIKKSQ 2016
Cdd:pfam03528 212 LNHYLE-AEKSCRTDLEMYVAVLNTQKSVLQ-----EDAEKLRKELHEVCHLLEQERQQH--NQLKHTWQKANDQFLESQ 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 116008016 2017 KSL-RDMREEFHAVSS---REQESLTRRKDLEKKVEQMESEGAALKND 2060
Cdd:pfam03528 284 RLLmRDMQRMESVLTSeqlRQVEEIKKKDQEEHKRARTHKEKETLKSD 331
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1381-1735 |
1.71e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1381 VHRTEEQLKTANEELLmlRAKLEKIEcdrsevkaENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:pfam13868 1 LRENSDELRELNSKLL--AAKCNKER--------DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1461 QTNKVKNLQETTEKLEMELICAKSDlngisEDEDAENEDGVgggVYKLKYERVARELEFTKRRLHTQHEHDLeqlvALKK 1540
Cdd:pfam13868 71 RKRYRQELEEQIEEREQKRQEEYEE-----KLQEREQMDEI---VERIQEEDQAEAEEKLEKQRQLREEIDE----FNEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1541 HLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcQSLQDAVRQERQ--AKER 1618
Cdd:pfam13868 139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE-KAERDELRAKLYqeEQER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1619 YGREKDVLQAEK--FTLEQTLADTRLDLEFKEEKLAsLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMA 1696
Cdd:pfam13868 218 KERQKEREEAEKkaRQRQELQQAREEQIELKERRLA-EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
330 340 350
....*....|....*....|....*....|....*....
gi 116008016 1697 GQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVR 1735
Cdd:pfam13868 297 KQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1578-2075 |
1.84e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1578 RMLLEEQNARNNLLEKKQRKFDAECQSLQDAVrQERQAKERYGRE-KDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQR 1656
Cdd:pfam10174 45 RALRKEEAARISVLKEQYRVTQEENQHLQLTI-QALQDELRAQRDlNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1657 ELEEmtfgggTEEEFAQLRRSKNETERR---------------------------AKEQEEELDEMAGQIQLLEQAKLRL 1709
Cdd:pfam10174 124 EHER------QAKELFLLRKTLEEMELRietqkqtlgardesikkllemlqskglPKKSGEEDWERTRRIAEAEMQLGHL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1710 EMTLETMRKE--ARRESQQRDEELEevrgNGYKKIKALECQLETEHEERTLLLREKHELERRLSS--------MEDRdrv 1779
Cdd:pfam10174 198 EVLLDQKEKEniHLREELHRRNQLQ----PDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhTEDR--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1780 drdaEEALNQ----------------KLRRDLRKYKALLKDAQTQLERL--------------KADTPGK--------TL 1821
Cdd:pfam10174 271 ----EEEIKQmevykshskfmknkidQLKQELSKKESELLALQTKLETLtnqnsdckqhievlKESLTAKeqraailqTE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1822 IRQLRNQLEDAESArsLAMKARQ---------TAEAELTEVQAMFDESHRarndaeeRANAAHRDRAELQAQIEENEEEL 1892
Cdd:pfam10174 347 VDALRLRLEEKESF--LNKKTKQlqdlteeksTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1893 GELMKKysatVKQLNTEQINVSEAEFKLNEMEAERN----NLKEQVA-ELQHRLDNVENLG----------DPSMAMMSK 1957
Cdd:pfam10174 418 AGLKER----VKSLQTDSSNTDTALTTLEEALSEKEriieRLKEQRErEDRERLEELESLKkenkdlkekvSALQPELTE 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 R------LELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQ------DVIKKSQKSLRDMREE 2025
Cdd:pfam10174 494 KesslidLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQEVARYKEE 573
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 2026 fhavSSREQESLTR-----------RKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:pfam10174 574 ----SGKAQAEVERllgilreveneKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1529-1842 |
1.89e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1529 EHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQkMTNEMNDLRMLLEEqnarnNLLEKKQRKFDAECQSLQDA 1608
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLS-ALNRLLPRLNLLAD-----ETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1609 VRQERQakerYGRekdvlQAEKftLEQTLADTRLDlefkEEKLASLQRELEEMTfgggteeefAQLRRSKNET------- 1681
Cdd:PRK04863 910 KRFVQQ----HGN-----ALAQ--LEPIVSVLQSD----PEQFEQLKQDYQQAQ---------QTQRDAKQQAfaltevv 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1682 ERRAK-EQEEELDEMAGQIQLLEQAKLRLEMtLETMRKEARRESQQRDEELEEvrgngYKKIKA-LECQLETEHEERTLL 1759
Cdd:PRK04863 966 QRRAHfSYEDAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQ-----YNQVLAsLKSSYDAKRQMLQEL 1039
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1760 LREKHELERRL-SSMEDRDRVDRDaeeALNQKLRRDLRKYKALLKdaQTQLERLKADTPGKTL------IRQLRNQLEDA 1832
Cdd:PRK04863 1040 KQELQDLGVPAdSGAEERARARRD---ELHARLSANRSRRNQLEK--QLTFCEAEMDNLTKKLrklerdYHEMREQVVNA 1114
|
330
....*....|
gi 116008016 1833 ESARSLAMKA 1842
Cdd:PRK04863 1115 KAGWCAVLRL 1124
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1439-1784 |
2.13e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1439 IATERLEAETAERLKLeKELGDQTNKVKNLQETTEK-LEMELICAKSdlngiSEDEDAENEDGVgggvyklkYERVAREL 1517
Cdd:pfam02029 7 AARERRRRAREERRRQ-KEEEEPSGQVTESVEPNEHnSYEEDSELKP-----SGQGGLDEEEAF--------LDRTAKRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1518 EFTKRRLHTQHEHdleqlvalKKHLEMKLSDAYEEVVEQRQVVGQ-----WKRKAQKMTNEMNDLrmllEEQNARNNLLE 1592
Cdd:pfam02029 73 ERRQKRLQEALER--------QKEFDPTIADEKESVAERKENNEEeenssWEKEEKRDSRLGRYK----EEETEIREKEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1593 KKQRKFDAECQSLQDAVRQERQAKErygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFA 1672
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEE----AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMT---LETMRKEARRESQQRDE-ELEEVRGNGYKKIKALEcq 1748
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRrqeKESEEFEKLRQKQQEAElELEELKKKREERRKLLE-- 294
|
330 340 350
....*....|....*....|....*....|....*.
gi 116008016 1749 letEHEERtlllREKHELERRLSSMEDRDRVDRDAE 1784
Cdd:pfam02029 295 ---EEEQR----RKQEEAERKLREEEEKRRMKEEIE 323
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
390-426 |
2.65e-04 |
|
PDZ domain; PDZ domains are found in diverse signaling proteins.
Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 41.50 E-value: 2.65e-04
10 20 30
....*....|....*....|....*....|....*..
gi 116008016 390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQ 426
Cdd:pfam00595 45 VGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1439-1657 |
2.73e-04 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 45.36 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1439 IATERLEAETAERLKLEKE---LGDqtnkVKNLQETTEKLEMEL-----------ICAKSDLNgISEDEDA------ENE 1498
Cdd:pfam14915 8 IAMLRLEIDTIKNQNQEKEkkyLED----IEILKEKNDDLQKTLklneetltktvFQYNGQLN-VLKAENTmlnsklENE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1499 dgvgggvyKLKYERVARELEFTKRRLHTQhEHDLEQLVALKKHLEMKLSDAYEEvveqrqvvgqWKRKAQKMTNEMNDLR 1578
Cdd:pfam14915 83 --------KQNKERLETEVESYRSRLAAA-IQDHEQSQTSKRDLELAFQRERDE----------WLRLQDKMNFDVSNLR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1579 mllEEQNARNNLLEKKQRKFDA---ECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDL-------EFKE 1648
Cdd:pfam14915 144 ---DENEILSQQLSKAESKANSlenELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVnkyigkqESLE 220
|
....*....
gi 116008016 1649 EKLASLQRE 1657
Cdd:pfam14915 221 ERLAQLQSE 229
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1588-1902 |
2.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQERQAK---ERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFG 1664
Cdd:COG4372 16 FGLRPKTGILIAALSEQLRKALFELDKLQeelEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1665 -GGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIK 1743
Cdd:COG4372 96 lAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIR 1823
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1824 QLRNQLEDAESARslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSAT 1902
Cdd:COG4372 256 ILKEIEELELAIL----VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1610-2062 |
3.09e-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: 45.72 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNEterRAKEQE 1689
Cdd:COG5185 89 LKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETG---IIKDIF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 EELDEMAGQIQLLEQAKLRLEMTLETMRKEARRES-----QQRDEELEEVRGNGYKKIKALECQLETEHEERtllLREKH 1764
Cdd:COG5185 166 GKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPsgtvnSIKESETGNLGSESTLLEKAKEIINIEEALKG---FQDPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1765 ELERRLSSMEDRdrvdrdAEEALNQklRRDLRKYKalLKDAQTQLERLKADTpgKTLIRQLRNQLED-AESARSLAMKAR 1843
Cdd:COG5185 243 SELEDLAQTSDK------LEKLVEQ--NTDLRLEK--LGENAESSKRLNENA--NNLIKQFENTKEKiAEYTKSIDIKKA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1844 QTAEAELTEvqamfdeSHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQiNVSEAEFKLNEM 1923
Cdd:COG5185 311 TESLEEQLA-------AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSF 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1924 EAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESrlELEQATRARLEVQvnrhkEALEKLQNEVTQSkM 2003
Cdd:COG5185 383 KDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQR--QIEQATSSNEEVS-----KLLNELISELNKV-M 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2004 REMQAqdvikksqKSLRDMREEFHAVSSREQESLtrrKDLEKKVEQMESEGAALKNDLR 2062
Cdd:COG5185 455 READE--------ESQSRLEEAYDEINRSVRSKK---EDLNEELTQIESRVSTLKATLE 502
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1922-2057 |
3.23e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1922 EMEAERNNLKEQVAELQHRLDNVENLGDPSMAmmsKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQ- 2000
Cdd:COG1842 55 RLERQLEELEAEAEKWEEKARLALEKGREDLA---REALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEl 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2001 -SKMREMQAQDvikKSQKSLRDMREEFHAVSSRE-QESLTRrkdLEKKVEQMESEGAAL 2057
Cdd:COG1842 132 kAKKDTLKARA---KAAKAQEKVNEALSGIDSDDaTSALER---MEEKIEEMEARAEAA 184
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1392-1847 |
3.27e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1392 NEELLMLRAKLEKIECDRSEVKAENQKLEA------KLSELTVDLAEERSTAHIATERLEAETAERL-KLEKELGDQTNK 1464
Cdd:PRK10246 362 NNELAGWRAQFSQQTSDREQLRQWQQQLTHaeqklnALPAITLTLTADEVAAALAQHAEQRPLRQRLvALHGQIVPQQKR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 VKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGggvYKLKYERVAR--ELEFTKRRLH----------TQHEHdL 1532
Cdd:PRK10246 442 LAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD---VKTICEQEARikDLEAQRAQLQagqpcplcgsTSHPA-V 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1533 EQLVALKKHLEMKLSDAYEEVVEQRQ-----VVGQWKRKAQKMTNEMNDLRMLLEEQNArnnLLEKKQrkfdAECQSL-- 1605
Cdd:PRK10246 518 EAYQALEPGVNQSRLDALEKEVKKLGeegaaLRGQLDALTKQLQRDESEAQSLRQEEQA---LTQQWQ----AVCASLni 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1606 ----QDAVRQERQAKERYGREKDVLqAEKFTLEQTLAD-TRLDLEFK---EEKLASLQRELEEMTFGGGTEEEFAQLRRS 1677
Cdd:PRK10246 591 tlqpQDDIQPWLDAQEEHERQLRLL-SQRHELQGQIAAhNQQIIQYQqqiEQRQQQLLTALAGYALTLPQEDEEASWLAT 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1678 KNETERRAKEQEEELDEMAGQIQlleqaklRLEMTLETMRKEARRESQQRDEELEEVRgNGYKKIKALECQLETEHEERT 1757
Cdd:PRK10246 670 RQQEAQSWQQRQNELTALQNRIQ-------QLTPLLETLPQSDDLPHSEETVALDNWR-QVHEQCLSLHSQLQTLQQQDV 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1758 LLLREKHELERRL------SSMEDR--------DRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKtlir 1823
Cdd:PRK10246 742 LEAQRLQKAQAQFdtalqaSVFDDQqaflaallDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDG---- 817
|
490 500
....*....|....*....|....
gi 116008016 1824 qlrnqLEDAESARSLAMKARQTAE 1847
Cdd:PRK10246 818 -----LDLTVTVEQIQQELAQLAQ 836
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1372-1699 |
3.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1372 LVRVTPLLNVHRTEEQLKTANEELLMLRAKLEKIecDRSEVKAENQKLEaKLSELTVDLAEERSTAHIATERLEAETAER 1451
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKY--NLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1452 LKLEKELGDQTNKVKNLQETTEKLEMElicaksdlngiSEDEDaenedgvgggvyklkyERVARELE-FTKRRLHTQH-E 1529
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFE-----------SVEEL----------------EERLKELEpFYNEYLELKDaE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1530 HDLEQLVALKKHLEMKLSDAYEEVVEQrqvvgqwKRKAQKMTNEMNDLRMLLEEQNARNnlLEKKQRKFDAECQSLQDAV 1609
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAET-------EKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAEL 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERYGREKDVLQAEKFTLEQtladtrldlefKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKeqe 1689
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREK-----------AKKELEKLEKALERV------EELREKVKKYKALLKERAL--- 742
|
330
....*....|
gi 116008016 1690 EELDEMAGQI 1699
Cdd:PRK03918 743 SKVGEIASEI 752
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1622-1855 |
5.35e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQL 1701
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA------LQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1702 LEQAKLRLEMTLE-----------TMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRL 1770
Cdd:COG3883 98 SGGSVSYLDVLLGsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1771 SSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAEL 1850
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*
gi 116008016 1851 TEVQA 1855
Cdd:COG3883 258 AAGSA 262
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1822-1993 |
5.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1822 IRQLRNQLEDAEsarslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM--KKY 1899
Cdd:COG1579 19 LDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1900 SATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsmammsKRLELRTKELESRLELEQATRAR 1979
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE-----------AELEEKKAELDEELAELEAELEE 160
|
170
....*....|....
gi 116008016 1980 LEVQVNRHKEALEK 1993
Cdd:COG1579 161 LEAEREELAAKIPP 174
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1669-1885 |
5.83e-04 |
|
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: 44.94 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1669 EEFAQLRRSknETERRAKEQEEEldemagqiQLLEQAKLRLEmtlETMRKEARRESQQRDEELEevrgngYKKIKALECQ 1748
Cdd:pfam15709 340 AERAEMRRL--EVERKRREQEEQ--------RRLQQEQLERA---EKMREELELEQQRRFEEIR------LRKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1749 LETEHEERTLLLREKHELERRlssmedrdrvdRDAEEALNQKLRRDLRKYKallkdaQTQLERLKADtpgKTLIRQLRNQ 1828
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERA-----------RQQQEEFRRKLQELQRKKQ------QEEAERAEAE---KQRQKELEMQ 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1829 LedAESARSLAmkarQTAEAELTEVQAMFDESH-RARNDAEERanaahRDRAELQAQI 1885
Cdd:pfam15709 461 L--AEEQKRLM----EMAEEERLEYQRQKQEAEeKARLEAEER-----RQKEEEAARL 507
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1668-1910 |
6.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1668 EEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEArresqqrdEELEEvrgngykKIKALEC 1747
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------DKLQA-------EIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1748 QLETEHEertlllrekhELERRLSSM----EDRDRVD-----RDAEEALNQ--KLRRDLRKYKALLKDAQTQLERLKADT 1816
Cdd:COG3883 80 EIEERRE----------ELGERARALyrsgGSVSYLDvllgsESFSDFLDRlsALSKIADADADLLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 pgktliRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM 1896
Cdd:COG3883 150 ------AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....
gi 116008016 1897 KKYSATVKQLNTEQ 1910
Cdd:COG3883 224 AAAAAAAAAAAAAA 237
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
1592-1709 |
7.27e-04 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 43.76 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1592 EKKQRKFDAECQslqdavrQERQAKERYGREKDvlqaEKFTLEQTLAD-TRLDlefkeEKLASLQRELEEMtfgggteee 1670
Cdd:pfam15991 23 ERKKQEQEAKME-------EERLRREREEREKE----DRMTLEETKEQiLKLE-----KKLADLKEEKHQL--------- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 116008016 1671 FAQLRRSKNETERR---AKEQeEELDEMAGQIQLLEQAKLRL 1709
Cdd:pfam15991 78 FLQLKKVLHEDETRkrqLKEQ-SELFALQQAAAQVFLPQLSM 118
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1540-1750 |
7.31e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.72 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLEMKLSDAYEEVVEQRQVVGQwkrkaQKMTNEMNDLRMLLEEQNARNNLLekKQRKFDAECQSLQDAVRQERQAKERY 1619
Cdd:cd16269 93 KKLMEQLEEKKEEFCKQNEEASS-----KRCQALLQELSAPLEEKISQGSYS--VPGGYQLYLEDREKLVEKYRQVPRKG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1620 GREKDVLQ---AEKFTLEQTL--ADTRLDLEFKEEKLASLQRELEEMtfgggteeEFAQLRRSKNETERRAKEQEEELDE 1694
Cdd:cd16269 166 VKAEEVLQeflQSKEAEAEAIlqADQALTEKEKEIEAERAKAEAAEQ--------ERKLLEEQQRELEQKLEDQERSYEE 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1695 MagqiqlLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYK-KIKALECQLE 1750
Cdd:cd16269 238 H------LRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKeQAELLQEEIR 288
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1634-1793 |
7.47e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1634 EQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKeQEEELDEMAGQIQLLEQAKLRLEMTL 1713
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQ-KEEQLDARAEKLDNLENQLEEREKAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1714 ETMRKEARRESQQRDEELEEVRGngykkikalecqlETEHEERTLLLRE-----KHELERRLSSMEDR--DRVDRDAEEA 1786
Cdd:PRK12705 115 SARELELEELEKQLDNELYRVAG-------------LTPEQARKLLLKLldaelEEEKAQRVKKIEEEadLEAERKAQNI 181
|
....*..
gi 116008016 1787 LNQKLRR 1793
Cdd:PRK12705 182 LAQAMQR 188
|
|
| PDZ_NHERF-like |
cd06768 |
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ... |
390-425 |
8.38e-04 |
|
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467249 [Multi-domain] Cd Length: 80 Bit Score: 40.11 E-value: 8.38e-04
10 20 30
....*....|....*....|....*....|....*.
gi 116008016 390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEV 425
Cdd:cd06768 43 DGDRLVEVNGENVEGESHEQVVEKIKASGNQVTLLV 78
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1385-1618 |
8.57e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTV--DLAEERSTAHIATERLEAETAERLKLEKELgdqT 1462
Cdd:pfam15905 93 DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKL---E 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1463 NKVKNLQETTEKLEMELICAKSDLNGISEDedaenedgvgggVYKLKYERVARELEFTKRRLHTQH-EHDLEQLVALKKH 1541
Cdd:pfam15905 170 AKMKEVMAKQEGMEGKLQVTQKNLEHSKGK------------VAQLEEKLVSTEKEKIEEKSETEKlLEYITELSCVSEQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1542 LEMK----------LSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARN-NLLEKKQRKFDAECQSLQDAVR 1610
Cdd:pfam15905 238 VEKYkldiaqleelLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELlREYEEKEQTLNAELEELKEKLT 317
|
....*...
gi 116008016 1611 QERQAKER 1618
Cdd:pfam15905 318 LEEQEHQK 325
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1655-1946 |
9.35e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1655 QRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARresqqrdeelEEV 1734
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLL----------ELT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1735 RGNGYKKIKALECQleTEHEERTLLLrekhELERRLSSMEDRDRVDRDAEEALNQKLrrdlrkykallKDAQTQLERLKA 1814
Cdd:pfam15905 136 RVNELLKAKFSEDG--TQKKMSSLSM----ELMKLRNKLEAKMKEVMAKQEGMEGKL-----------QVTQKNLEHSKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1815 DtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARND---AEERANAAHRDRAELQAQIEENEEE 1891
Cdd:pfam15905 199 K------VAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDiaqLEELLKEKNDEIESLKQSLEEKEQE 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1892 LGELMKKYSATVKQLNteqinvSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEN 1946
Cdd:pfam15905 273 LSKQIKDLNEKCKLLE------SEKEELLREYEEKEQTLNAELEELKEKLTLEEQ 321
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1684-2075 |
1.04e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1684 RAKEQEEELDEMAG-----QI--QLLEQaklrlemtletmRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEER 1756
Cdd:PRK10246 165 KPKERAELLEELTGteiygQIsaMVFEQ------------HKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1757 TLLLREKHELERRLSSMEDRDRVDRDAeealnQKLRRDLRKYKALLKDAQTQLERLKADTPGktliRQLRNQLEDAESAR 1836
Cdd:PRK10246 233 KQLLTAQQQQQQSLNWLTRLDELQQEA-----SRRQQALQQALAAEEKAQPQLAALSLAQPA----RQLRPHWERIQEQS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1837 SLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEEL--GELMKKYSATVKQLNTEQinvs 1914
Cdd:PRK10246 304 AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRqwNNELAGWRAQFSQQTSDR---- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1915 eaefklnemeAERNNLKEQVAELQHRLDNVENLG-----DPSMAMMSKRLELRTkeLESRLELEQATRARLEVQVNRHKE 1989
Cdd:PRK10246 380 ----------EQLRQWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQRP--LRQRLVALHGQIVPQQKRLAQLQV 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1990 ALEKLQNEVTQ-SKMREMQAQDVIKKSQ---------------KSLRDMRE--------------EFHAVSSREQESLT- 2038
Cdd:PRK10246 448 AIQNVTQEQTQrNAALNEMRQRYKEKTQqladvkticeqeariKDLEAQRAqlqagqpcplcgstSHPAVEAYQALEPGv 527
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 116008016 2039 ---RRKDLEKKVEQMESEGAALK---NDLRLALQRIADLQQAM 2075
Cdd:PRK10246 528 nqsRLDALEKEVKKLGEEGAALRgqlDALTKQLQRDESEAQSL 570
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1820-2023 |
1.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1820 TLIRQLRNQLEDAESARslamkarQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKY 1899
Cdd:COG3883 16 PQIQAKQKELSELQAEL-------EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1900 SATVKQLNTEQINVSEAEF--------------------------KLNEMEAERNNLKEQVAELQHRLDNVENLgdpsma 1953
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEAL------ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1954 mmSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMR 2023
Cdd:COG3883 163 --KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1685-2025 |
1.15e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1685 AKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKA-LECQLETEHEERTLLLREK 1763
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqIEEREQKRQEEYEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1764 HELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQtQLERLKADtpgKTLIRQLRNQLEDAESARSLAMKAR 1843
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWK-ELEKEEER---EEDERILEYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1844 QTAEAELTEVQAMFDESHRARNDAEER------ANAAHRDRAELQAQIEeneeelgelmkkysatvkqlnteqinvsEAE 1917
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKAERdelrakLYQEEQERKERQKERE----------------------------EAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1918 FKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsMAMMSKRLELRTKELEsrlELEQATRARLEVQVNRHKEALEKLQNE 1997
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKERRLAEEAER----EEEEFERMLRKQAEDE---EIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340
....*....|....*....|....*...
gi 116008016 1998 VTQSKMREMQAQDVIKKSQKSLRDMREE 2025
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRE 329
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1673-1885 |
1.18e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQ--EEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRG-----NGYKKIKA- 1744
Cdd:pfam00038 35 SELRQKKGAEPSRLYSlyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSaendlVGLRKDLDe 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1745 -------LECQLET----------EHEERTLLLREKHELERRLSSMEDRDRVD--------RDAEEALNQKLRRDLRK-Y 1798
Cdd:pfam00038 115 atlarvdLEAKIESlkeelaflkkNHEEEVRELQAQVSDTQVNVEMDAARKLDltsalaeiRAQYEEIAAKNREEAEEwY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1799 KALLKDAQTQLERLKADTPG-KTLIRQLRNQLedaesarslamkarQTAEAELTEVQAMFDESHRARNDAEERANAAHRD 1877
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSaKEEITELRRTI--------------QSLEIELQSLKKQKASLERQLAETEERYELQLAD 260
|
250
....*....|..
gi 116008016 1878 ----RAELQAQI 1885
Cdd:pfam00038 261 yqelISELEAEL 272
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1378-1476 |
1.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1378 LLNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKE 1457
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90
....*....|....*....
gi 116008016 1458 LGDQTNKVKNLQETTEKLE 1476
Cdd:COG4372 117 LEELQKERQDLEQQRKQLE 135
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1591-1799 |
1.31e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1591 LEKKQRKFDAECQSLQDAVRQERQAKERygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEM--------- 1661
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEK-------AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAekaadeser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1662 ------TFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrLEmtletmRKEAR-RESQQRDEELEEV 1734
Cdd:pfam00261 79 grkvleNRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD---LE------RAEERaELAESKIVELEEE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116008016 1735 RGNGYKKIKALECQlETEHEERTLLLREK-HELERRLSSMEDRdrvDRDAE------EALNQKLRRDLRKYK 1799
Cdd:pfam00261 150 LKVVGNNLKSLEAS-EEKASEREDKYEEQiRFLTEKLKEAETR---AEFAErsvqklEKEVDRLEDELEAEK 217
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1721-2053 |
1.33e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1721 RRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERR-LSSMEDRDRVDRDAEEALNQKLRRDLRKYK 1799
Cdd:PLN02939 41 GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKsTSSDDDHNRASMQRDEAIAAIDNEQQTNSK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1800 ALLKDAQTQLERL----KADTPGKTLIRQLRNQ-LEDAE---SARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERA 1871
Cdd:PLN02939 121 DGEQLSDFQLEDLvgmiQNAEKNILLLNQARLQaLEDLEkilTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1872 NAAHRDRAELQAQIEENEEELGELMKKYS----------ATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRL 1941
Cdd:PLN02939 201 EQLEKLRNELLIRGATEGLCVHSLSKELDvlkeenmllkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1942 -------------------DNVENLG----------DPSMAMMSKRLELRTK--ELESRLEleqatrarlevQVNRHKEA 1990
Cdd:PLN02939 281 ivaqedvsklsplqydcwwEKVENLQdlldratnqvEKAALVLDQNQDLRDKvdKLEASLK-----------EANVSKFS 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1991 LEKLqnEVTQSKMR----EMQAQDVIKKSQKSL-RDMREEFHAVSSREQESlTRRKDLEKKVEQMESE 2053
Cdd:PLN02939 350 SYKV--ELLQQKLKlleeRLQASDHEIHSYIQLyQESIKEFQDTLSKLKEE-SKKRSLEHPADDMPSE 414
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1741-1978 |
1.36e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1741 KIKALECQLETEHEERTLllreKHELERRLSSMEDRDRVDRDAEEalnqkLRRDLRKYKALLKDAQTQLERLKADTP--- 1817
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLV----QQDLEQTLALLDKIDRQKEETEQ-----LKQQLAQAPAKLRQAQAELEALKDDNDeet 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1818 ----GKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAmfdeshrarndAEERANAAHRDRAELQAQIEENEEELG 1893
Cdd:PRK11281 115 retlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT-----------QPERAQAALYANSQRLQQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1894 ELMKKYSATVK-QLNTEQINVsEAEFKLNEMEAERNN------------LKEQVAELQHRLDNVENLGDpsmammSKRLE 1960
Cdd:PRK11281 184 VGGKALRPSQRvLLQAEQALL-NAQNDLQRKSLEGNTqlqdllqkqrdyLTARIQRLEHQLQLLQEAIN------SKRLT 256
|
250
....*....|....*...
gi 116008016 1961 LRTKELESRLELEQATRA 1978
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARI 274
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1765-2071 |
1.51e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1765 ELERRLSSMEDRDRvdrdAEEALNQKLRRdlrkyKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQ 1844
Cdd:pfam00038 8 ELNDRLASYIDKVR----FLEQQNKLLET-----KISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1845 TAEAELTEVQAMFDESHRARNDAEERANAAHRD-------RAELQAQIEENEEELGELMKKYSATVKQLNT----EQINV 1913
Cdd:pfam00038 79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDldeatlaRVDLEAKIESLKEELAFLKKNHEEEVRELQAqvsdTQVNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1914 seaefklnEMEAERN-NLKEQVAELQHRLDnvenlgdpSMAMMSKrlelrtKELEsrlELEQATRARLEVQVNRHKEALE 1992
Cdd:pfam00038 159 --------EMDAARKlDLTSALAEIRAQYE--------EIAAKNR------EEAE---EWYQSKLEELQQAAARNGDALR 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1993 KLQNEVTQSKMReMQAQDVIKKSQKSLRDMREefHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADL 2071
Cdd:pfam00038 214 SAKEEITELRRT-IQSLEIELQSLKKQKASLE--RQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1534-1826 |
1.55e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1534 QLVALKKHLEMKLSDAYEevVEQRQVvgqwKRKAQKMTNEMNDLRMLLEEQNARNNLLEkkqrkfdAECQSLQDAVRQER 1613
Cdd:pfam00038 22 FLEQQNKLLETKISELRQ--KKGAEP----SRLYSLYEKEIEDLRRQLDTLTVERARLQ-------LELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1614 QAKERYGREKDVLQAEKFTLEQTLAD---TRLDLEFKEEklaSLQRELEEMTfgGGTEEEFAQLRRSKNETER------- 1683
Cdd:pfam00038 89 QKYEDELNLRTSAENDLVGLRKDLDEatlARVDLEAKIE---SLKEELAFLK--KNHEEEVRELQAQVSDTQVnvemdaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1684 RAKEQEEELDEMAGQI-QLLEQAKLRLEMT----LETMRKEARRES---QQRDEELEEVRgngyKKIKALECQLETehee 1755
Cdd:pfam00038 164 RKLDLTSALAEIRAQYeEIAAKNREEAEEWyqskLEELQQAAARNGdalRSAKEEITELR----RTIQSLEIELQS---- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 1756 rtlLLREKHELERRLSSMEDRdrvdrdaeealnqkLRRDLRKYKALLKDAQTQLERLKADtpgktLIRQLR 1826
Cdd:pfam00038 236 ---LKKQKASLERQLAETEER--------------YELQLADYQELISELEAELQETRQE-----MARQLR 284
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1815-2018 |
1.91e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1815 DTPGKTLIRQLRNQLEDAESARSLAM-----------KARQTAEAELTEVQAMFDEshrarndAEERANAAHRDRAELQA 1883
Cdd:PHA02562 169 DKLNKDKIRELNQQIQTLDMKIDHIQqqiktynknieEQRKKNGENIARKQNKYDE-------LVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1884 QIEENEEElgelMKKYSATVKQLNTEQINVS--------EAEF------------KLNEMEAERNNLKEQVAELQHRLDN 1943
Cdd:PHA02562 242 ELLNLVMD----IEDPSAALNKLNTAAAKIKskieqfqkVIKMyekggvcptctqQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1944 VENLGDPSMAMMSKRLELRTK--ELESRLELEQATRARLEVQVNRHKEALEKLQNEVT--QSKMREMQAQDVIKKSQKS 2018
Cdd:PHA02562 318 LDTAIDELEEIMDEFNEQSKKllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVdnAEELAKLQDELDKIVKTKS 396
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1718-2053 |
2.21e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1718 KEARRESQQRDEElEEVRGNGYKKIKALECQLETEHEERTlllrekHELERRLSSMEDRDRvdrDAEEALNQKL-RRDLR 1796
Cdd:pfam02029 5 EEAARERRRRARE-ERRRQKEEEEPSGQVTESVEPNEHNS------YEEDSELKPSGQGGL---DEEEAFLDRTaKREER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1797 KYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHR 1876
Cdd:pfam02029 75 RQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1877 DRAELQAQIEENEEELGELMKKYSATVKQLNTEqINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgDPSMAMMS 1956
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE-KKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT---TKRRQGGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1957 KRLELRTKELESRLELEQatraRLEVQVNRHKEALEKlqnEVTQSKMREMQAQ---DVIKKSQKSLRDMREEfhAVSSRE 2033
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQ----KLEELRRRRQEKESE---EFEKLRQKQQEAElelEELKKKREERRKLLEE--EEQRRK 301
|
330 340
....*....|....*....|
gi 116008016 2034 QESLTRRKDLEKKVEQMESE 2053
Cdd:pfam02029 302 QEEAERKLREEEEKRRMKEE 321
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1958-2070 |
2.33e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 RLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMR--EEFHAVSsREQE 2035
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQ-KEIE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 116008016 2036 SLTRRKD---------------LEKKVEQMESEGAALKNDLRLALQRIAD 2070
Cdd:COG1579 100 SLKRRISdledeilelmerieeLEEELAELEAELAELEAELEEKKAELDE 149
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1382-1850 |
2.34e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1382 HRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTA-----HIATERLEAETAErLKLEK 1456
Cdd:pfam05701 66 AQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVAakaqlEVAKARHAAAVAE-LKSVK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1457 ELGDQTNK------------VKNLQETT----------EKLEMELICAKSDLNGISEDEDAENEDGVGGGVYK----LKY 1510
Cdd:pfam05701 145 EELESLRKeyaslvserdiaIKRAEEAVsaskeiektvEELTIELIATKESLESAHAAHLEAEEHRIGAALAReqdkLNW 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1511 ErvaRELEftkrrlhtQHEHDLEQL---VALKKHLEMKLSDAYEEVVEQRQ-----VVGQWKRKAQKMTNE---MNDLRM 1579
Cdd:pfam05701 225 E---KELK--------QAEEELQRLnqqLLSAKDLKSKLETASALLLDLKAelaayMESKLKEEADGEGNEkktSTSIQA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1580 LLEeqNARNNLLEKKQ--RKFDAECQSLQDAVrqerqakerygrekdvlqaekftleqtlADTRLDLEFKEEKLASLQRe 1657
Cdd:pfam05701 294 ALA--SAKKELEEVKAniEKAKDEVNCLRVAA----------------------------ASLRSELEKEKAELASLRQ- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1658 LEEMTFGGGTEEEfAQLRRSKNETE---RRAKEQEEELDEMAGQIQL----LEQAKLRLEMTLETMRKeARRESQQRDEE 1730
Cdd:pfam05701 343 REGMASIAVSSLE-AELNRTKSEIAlvqAKEKEAREKMVELPKQLQQaaqeAEEAKSLAQAAREELRK-AKEEAEQAKAA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1731 LE--EVRGNGYKK---------------IKALEcqlETEHEER-----------TLLLREKHELERRLssmedrdrvdRD 1782
Cdd:pfam05701 421 AStvESRLEAVLKeieaakaseklalaaIKALQ---ESESSAEstnqedsprgvTLSLEEYYELSKRA----------HE 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116008016 1783 AEEALNQKLRRDLRKYKaLLKDAQTQ-LERLKAdtpgktLIRQLRNQLEDAESARSLAMKARQ---TAEAEL 1850
Cdd:pfam05701 488 AEELANKRVAEAVSQIE-EAKESELRsLEKLEE------VNREMEERKEALKIALEKAEKAKEgklAAEQEL 552
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1440-1763 |
2.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1440 ATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEmELICAKSDLNGISEDEdaenedgvgggvykLKYERVARELEf 1519
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDE--------------IDVASAEREIA- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1520 tkrrlhtQHEHDLEQLVALK---KHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQR 1596
Cdd:COG4913 672 -------ELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1597 KFDAEC------QSLQDAVrqERQAKERYGREKDVLQAEKFTLEQTLADTRL---------------------------- 1642
Cdd:COG4913 745 LELRALleerfaAALGDAV--ERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadleslpeylalld 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1643 -----DLEFKEEKLASLQRELeemtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMT----- 1712
Cdd:COG4913 823 rleedGLPEYEERFKELLNEN--------SIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPFGPGRYLRLEARprpdp 894
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1713 ----LETMRKEARRESQQRDEELEEVRgngYKKIKALECQLETEHEERTLLLREK 1763
Cdd:COG4913 895 evreFRQELRAVTSGASLFDEELSEAR---FAALKRLIERLRSEEEESDRRWRAR 946
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1430-1830 |
3.54e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1430 LAEERSTAHIATERLEAETAERLKLEKELgdQTNKV---KNLQETTEKLEMELIcAKSD----LNGISEDEDA-ENEDGV 1501
Cdd:pfam15818 76 LEEEKGKYQLATEIKEKEIEGLKETLKAL--QVSKYslqKKVSEMEQKLQLHLL-AKEDhhkqLNEIEKYYATiTGQFGL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1502 GGGVYKlKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQ----WKRKAQKMTNEMNDL 1577
Cdd:pfam15818 153 VKENHG-KLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEeninLTIKEQKFQELQERL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1578 RMLLE------EQNARnnLLEKKQRKFdAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKL 1651
Cdd:pfam15818 232 NMELElnkkinEEITH--IQEEKQDII-ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1652 ASLQRELEEmtfgggteeefaQLRRSKNETErrakEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEEL 1731
Cdd:pfam15818 309 LNLQNEHEK------------ALGTWKKHVE----ELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1732 EEVRGNGYkkikalecQLETEHEERTLLLREKHELERRLSSMEDRdrvDRDAEEALNQKlRRDLRKYKALLKDAQTQLER 1811
Cdd:pfam15818 373 PEVNNENS--------EMSTEKSENLIIQKYNSEQEIREENTKSF---CSDTEYRETEK-KKGPPVEEIIIEDLQVLEKS 440
|
410
....*....|....*....
gi 116008016 1812 LKADTpgKTLIRQLRNQLE 1830
Cdd:pfam15818 441 FKNEI--DTSVPQDKNQSE 457
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1761-1884 |
4.00e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1761 REKHELERRLSSMEDRDRvdrDAEEALnQKLRRDLRKYKALLKDAQTQLER---LKADTpGKTLiRQLRNQLEDAESARS 1837
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAA---DAEAQL-QKLQEDLEKQAEIAREAQQNYERelvLHAED-IKAL-QALREELNELKAEIA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 116008016 1838 LAMKARQTAEAELTEVQAMFDEshrARNDAEERANAAHRDRAELQAQ 1884
Cdd:pfam07926 75 ELKAEAESAKAELEESEESWEE---QKKELEKELSELEKRIEDLNEQ 118
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1552-1721 |
4.08e-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: 42.25 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1552 EVVEQRQVVGQWKRKAQKMTNEMN-DLRMLLEEQNARNNLLEKKQRKFDAE--CQSLQDAVRQER--QAKERYGREKDVL 1626
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELElEQQRRFEEIRLRKQRLEEERQRQEEEerKQRLQLQAAQERarQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1627 QAEKFT--LEQTLADTRLDLEFkEEKLASLQRELEEMTfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGqiqllEQ 1704
Cdd:pfam15709 436 QRKKQQeeAERAEAEKQRQKEL-EMQLAEEQKRLMEMA-----EEERLEYQRQKQEAEEKARLEAEERRQKEE-----EA 504
|
170
....*....|....*..
gi 116008016 1705 AKLRLEMTLETMRKEAR 1721
Cdd:pfam15709 505 ARLALEEAMKQAQEQAR 521
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1556-1814 |
4.73e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1556 QRQVVGQW---KRKAQK--MTNEMNDLRMLLEEQNARNNLLEKKQRKFDaecqslqdavRQERQAKERygREKDVLQAEK 1630
Cdd:pfam15558 27 QQQAALAWeelRRRDQKrqETLERERRLLLQQSQEQWQAEKEQRKARLG----------REERRRADR--REKQVIEKES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1631 FTLEQTladtrldlefkEEKLASLQRELEEmtfgggteeEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklRLE 1710
Cdd:pfam15558 95 RWREQA-----------EDQENQRQEKLER---------ARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQE--RLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1711 MTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHEL--ERRLSSMEDRDRVDRdaEEALN 1788
Cdd:pfam15558 153 EACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRsqENYEQLVEERHRELR--EKAQK 230
|
250 260
....*....|....*....|....*.
gi 116008016 1789 QKLRRDLRKYKALLKDAQTQlERLKA 1814
Cdd:pfam15558 231 EEEQFQRAKWRAEEKEEERQ-EHKEA 255
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1727-2074 |
4.98e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRgNGYKKIKALECQLE--TEHEERTLLLREKHELERRLSSMEDRDRvdrdaEEALNQKLRRDLRKYKALLKD 1804
Cdd:pfam13868 1 LRENSDELR-ELNSKLLAAKCNKErdAQIAEKKRIKAEEKEEERRLDEMMEEER-----ERALEEEEEKEEERKEERKRY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1805 AQtqlerlkadtpgktlirQLRNQLEDAESARSLA-MKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQA 1883
Cdd:pfam13868 75 RQ-----------------ELEEQIEEREQKRQEEyEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1884 QIEENEEELGELMKK-----YSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsmamMSKR 1958
Cdd:pfam13868 138 EQAEWKELEKEEEREederiLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL-------RAKL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1959 LELRTKELESRLELEQAT---RARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAvssREQE 2035
Cdd:pfam13868 211 YQEEQERKERQKEREEAEkkaRQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMK 287
|
330 340 350
....*....|....*....|....*....|....*....
gi 116008016 2036 SLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQA 2074
Cdd:pfam13868 288 RLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1577-1924 |
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 116008016 1577 LRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKErygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQR 1656
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1657 ELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARReSQQRDEELEEVRG 1736
Cdd:COG4372 109 EAEEL------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA-LEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1737 NGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADT 1816
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 PGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM 1896
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
330 340
....*....|....*....|....*...
gi 116008016 1897 KKYSATVKQLNTEQINVSEAEFKLNEME 1924
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PDZ7_MUPP1-PD6_PATJ-like |
cd06671 |
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ... |
334-426 |
5.46e-03 |
|
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467159 [Multi-domain] Cd Length: 96 Bit Score: 38.07 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 334 PPRQLVIRRQksPRQDFGFSL---RKAICLDRTESLTSPIFRPVIfAEPGAGGGATGLLPGDRLIKVNGTPVGELPREII 410
Cdd:cd06671 1 PPRRVELWRE--PGKSLGISIvggRVMGSRLSNGEEIRGIFIKHV-LEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEA 77
|
90
....*....|....*.
gi 116008016 411 IEMIRNSGEAVTVEVQ 426
Cdd:cd06671 78 VEAIRNAGNPVVFLVQ 93
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1643-2071 |
5.75e-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: 41.93 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1643 DLEFK--EEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEeldemagQIQLLEQAKLRL---EMTLETMR 1717
Cdd:TIGR04523 32 DTEEKqlEKKLKTIKNELKN------KEKELKNLDKNLNKDEEKINNSNN-------KIKILEQQIKDLndkLKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1718 KEARRESQQRDEELEEVRGNGYKK---IKALECQLETEHEERTLLLREKHELERRLSSmedrdrvdrdaeeaLNQKLRrD 1794
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEK--------------LNNKYN-D 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1795 LRKYKALLKDAQTQLERLKADTpgKTLIRQLRNQLedaeSARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAA 1874
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNI--QKNIDKIKNKL----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1875 HRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNN-------------------LKEQVA 1935
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlkseisdlnnqkeqdwnkeLKSELK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1936 ELQHRLDNVENLGDPSMAMMSKrLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEvTQSKMREmqaqdvIKKS 2015
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE-NQSYKQE------IKNL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 2016 QKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADL 2071
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1582-1762 |
6.16e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1582 EEQNARNNLLE--KKQRKFDAECQSLQDAVRQERQ--AKERYGREKDVLQAEKFTLE------QTLADtrlDLEFK---- 1647
Cdd:PRK11448 58 PPCENQHDLLRrlGKEGFLPDEILDVFHKLRKIGNkaVHEFHGDHREALMGLKLAFRlavwfhRTYGK---DWDFKpgpf 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1648 ------EEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEAR 1721
Cdd:PRK11448 135 vppedpENLLHALQQEVLTL------KQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAA 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116008016 1722 RESQQRDEELEEVRGNGYKKIKAlecqleTEHEERTLL---LRE 1762
Cdd:PRK11448 209 ETSQERKQKRKEITDQAAKRLEL------SEEETRILIdqqLRK 246
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1622-1793 |
7.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKfTLEQTLADTRLDLE-FKEEKLASLQRELEEMTfgGGTEEEFAQLRRSKNETERRAKEQEEELDEmagQIQ 1700
Cdd:PRK12704 30 EAKIKEAEE-EAKRILEEAKKEAEaIKKEALLEAKEEIHKLR--NEFEKELRERRNELQKLEKRLLQKEENLDR---KLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1701 LLEQAKLRLEM----------TLETMRKEARRESQQRDEELEEVRGngykkikalecqlETEHEERTLLLRE-KHELERR 1769
Cdd:PRK12704 104 LLEKREEELEKkekeleqkqqELEKKEEELEELIEEQLQELERISG-------------LTAEEAKEILLEKvEEEARHE 170
|
170 180 190
....*....|....*....|....*....|
gi 116008016 1770 LSSM------EDRDRVDRDAEEALNQKLRR 1793
Cdd:PRK12704 171 AAVLikeieeEAKEEADKKAKEILAQAIQR 200
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1673-1885 |
7.55e-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: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrlemtLETMRKearresQQRDEELEEVRGNGYKKIKALECQLETe 1752
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAA-------LEEFRQ------KNGLVDLSEEAKLLLQQLSELESQLAE- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1753 heertlLLREKHELERRLSSMEDRDRVDRDAEEALNQKlrRDLRKYKALLKDAQTQLERLKAD-TPGKTLIRQLRNQLED 1831
Cdd:COG3206 231 ------ARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAA 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1832 AESA-RSLAMKARQTAEAELTEVQAMFDESHRARNDAEERA---NAAHRDRAELQAQI 1885
Cdd:COG3206 303 LRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLEREV 360
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1678-1817 |
7.71e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.17 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1678 KNETERRAKeQEEELDEMAGQIQLLEQ--AKLRLEM-TLETMRKEARRESQQRDEELEEvRGNGYKK------------- 1741
Cdd:pfam05667 324 ETEEELQQQ-REEELEELQEQLEDLESsiQELEKEIkKLESSIKQVEEELEELKEQNEE-LEKQYKVkkktldllpdaee 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1742 -IKALEC----------QLETEHEE-RTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRR---DLRKYKALLKDAQ 1806
Cdd:pfam05667 402 nIAKLQAlvdasaqrlvELAGQWEKhRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEvaeEAKQKEELYKQLV 481
|
170
....*....|.
gi 116008016 1807 TQLERLKADTP 1817
Cdd:pfam05667 482 AEYERLPKDVS 492
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1859-2116 |
7.74e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1859 ESHRARNDAEERANAAHRDR----AELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEaefKLNEMEAERnnlKEQV 1934
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRkleeAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEE---RKRELERIR---QEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1935 AELQHRLDNVENLgdpSMAMMSKRLELRtKELES--RLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVI 2012
Cdd:pfam17380 371 AMEISRMRELERL---QMERQQKNERVR-QELEAarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 2013 KKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLAlQRIADLQQAMEEEGEEELSESDESLSS 2092
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE-KELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260
....*....|....*....|....
gi 116008016 2093 VGSISDLEDRlRPVHVKRSSQQSL 2116
Cdd:pfam17380 526 QKAIYEEERR-REAEEERRKQQEM 548
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1641-1762 |
8.35e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1641 RLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLrrsKNETERRAKEQEEELDEmagqiqllEQAKLRLEMTLETMRKEA 1720
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQL------EIEKEAL---KKEQDEASFERLAELRD--------ELAELEEELEALKARWEA 465
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 116008016 1721 RRESQQRDEELEEVRGNGYKKIKALECQL---ETEHEERTLLLRE 1762
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELaelEEELAELAPLLRE 510
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1958-2073 |
9.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 RLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEV--TQSKMREM-----QAQDVIKKSQKSLRDMR--EEFHA 2028
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELedLEKEIKRLeleieEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116008016 2029 VsSREQESLTRRK-DLEKKVEQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:COG1579 94 L-QKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEA 138
|
|
|