|
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 ... |
625-1361 |
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: 1055.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKV---PRG-RQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVakmFKGcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVL 780
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 781 LENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEGEQ 860
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 861 QAIWRVLAAIYHLGAAGACK---VGRKQFMRFEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGPqRQGLQDNEAC 937
Cdd:cd01386 241 RAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSS-GQESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 938 SGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQGKDRAATFEELCYNYAQERLQL 1017
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1018 LFYHRTFVSTLERYKEEGIPVPFDLPESSPGTTVAVVDQNPSQVHLPAGRGAEDAGGLFWVLDEEVRVQGSSDSTVLERL 1097
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1098 RAAFEKKKeaGAEEPPSMRTCEQPLQCELFHQLGRDPVRYDLTGWLRRAKPNLAALEAPQILQQSKREelqslfqarakl 1177
Cdd:cd01386 480 FSHYGDKE--GGKGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1178 ppvcravaglegtsqqalhrsrvvrrafassLAAVKRKAPCAQIKLQMDALISLLRRSRLHFIHCLVPTTVESKAGQRTP 1257
Cdd:cd01386 546 -------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTS 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1258 SPSQPsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLDLTSEELDERKVV 1337
Cdd:cd01386 595 SPAAG---------DELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAV 665
|
730 740
....*....|....*....|....
gi 291327510 1338 EELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd01386 666 EELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
626-1361 |
6.97e-108 |
|
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: 359.98 E-value: 6.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKV----PRGRQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPfKWLPLYSEEVMekyrGKGRSADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVS------VEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAA 774
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSssassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 775 QLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNL---HQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAME 851
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLellLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 852 LLGISEGEQQAIWRVLAAIYHLG----------AAGACKVGRKqfmrfEWANHAAEALGCDYEELNTATFKhhlRQIIeq 921
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGniefeedeedEDSSAEVADD-----ESLKAAAKLLGVDAEDLEEALTT---RTIK-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 922 MTSGPQRQGLQDNEACsglkmtgvECVEGMASGLYQELFVAVVSLINRSFSS--HHLSMASIMVVDTPGFQNPRHQGkdr 999
Cdd:cd00124 312 VGGETITKPLTVEQAE--------DARDALAKALYSRLFDWLVNRINAALSPtdAAESTSFIGILDIFGFENFEVNS--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1000 aatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLPESSPgtTVAVVDQNPsqvhlpagrgaedaGGLFWV 1078
Cdd:cd00124 381 ---FEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFiDFPDNQD--CLDLIEGKP--------------LGILSL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1079 LDEEVRVQGSSDSTVLERLRAAFEKKKeAGAEEPPSMRTCeqplqcelF---HQLGrdPVRYDLTGWLRRAKPNLAalea 1155
Cdd:cd00124 442 LDEECLFPKGTDATFLEKLYSAHGSHP-RFFSKKRKAKLE--------FgikHYAG--DVTYDADGFLEKNKDTLP---- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1156 pqilqqskrEELQSLFQAraklppvcravaglegtsqqalhrsrvvrrafasslaavkrkapCAQIKLQMDALISLLRRS 1235
Cdd:cd00124 507 ---------PDLVDLLRS--------------------------------------------GSQFRSQLDALMDTLNST 533
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1236 RLHFIHCLVPTTveskagqrtpspsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQV 1315
Cdd:cd00124 534 QPHFVRCIKPND---------------------EKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 291327510 1316 LDPALLKKLDLTSEElderkVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd00124 593 LAPGATEKASDSKKA-----AVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
606-1373 |
1.20e-101 |
|
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: 343.37 E-value: 1.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 606 NPSELDQAEDLASLVSVNESSVMNTLLQRYRAQLPYTCSGPDLITLQPqTTTVPSSG----KVPRGRQDG-LPAHVTSLA 680
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNP-YKQLPIYTdeviKKYRGKSRGeLPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 681 QRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK--LRATFtVLRAFGCVSTGHSRRATRFA 758
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDqiLESNP-ILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 759 MVMSLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhQMAESSAF-GMGLWSK---PE 834
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL-KSPEDYRYlNQGGCLTvdgID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 835 DKQKaataFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG----------AAGACKVGRKQFMRfewanhAAEALGCDYE 904
Cdd:smart00242 238 DAEE----FKETLNAMRVLGFSEEEQESIFKILAAILHLGniefeegrndNAASTVKDKEELSN------AAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 905 ELNTA-TFKhhlrqiieQMTSGPQ--RQGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASI 981
Cdd:smart00242 308 ELEKAlTKR--------KIKTGGEviTKPLNVEQA--------LDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 982 MVVDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF----------DLPESSPgttv 1051
Cdd:smart00242 372 GVLDIYGFEIFEVNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFidffdnqdciDLIEKKP---- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1052 avvdqnpsqvhlpagrgaedaGGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKeagAEEPPSMRTCEQplqcelF---H 1128
Cdd:smart00242 442 ---------------------PGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP---HFSKPKKKGRTE------FiikH 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1129 QLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQSLFQARAklppvcravaglegtsqqalhrsrvvrrafasS 1208
Cdd:smart00242 492 YAGD--VTYDVTGFLEKNKDTLSD-DLIELLQSSKNPLIASLFPSGV--------------------------------S 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1209 LAAVKRKAPCA--QIKLQMDALISLLRRSRLHFIHCLVPTTvESKAGQrtpspsqpsgdqgvaneptaLDIPALRVQLAG 1286
Cdd:smart00242 537 NAGSKKRFQTVgsQFKEQLNELMDTLNSTNPHFIRCIKPNE-EKKPGD--------------------FDSSLVLHQLRY 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1287 SHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKkldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLKAGVVS 1366
Cdd:smart00242 596 LGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP-----PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLA 670
|
....*..
gi 291327510 1367 RLERQRE 1373
Cdd:smart00242 671 ELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
606-2126 |
1.63e-83 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 305.08 E-value: 1.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 606 NPSELDQAEDLASLVSVNESSVMNTLLQRYRAQLPYTCSGPDLITLQP--------QTTTVPSSGKvprgRQDGLPAHVT 677
Cdd:COG5022 61 KLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPyrdlgiytDDIIQSYSGK----NRLELEPHVF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 678 SLAQRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSV-DGRVSVE-KLRATFTVLRAFGCVSTGHSRRAT 755
Cdd:COG5022 137 AIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSStVEISSIEkQILATNPILEAFGNAKTVRNDNSS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 756 RFAMVMSLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnLHQMAESSAFGMGLWSKPED 835
Cdd:COG5022 217 RFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLL-LLQNPKDYIYLSQGGCDKID 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 836 KQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-------AAGACKVGRKQFMRFewanhAAEALGCDYEELNT 908
Cdd:COG5022 296 GIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGniefkedRNGAAIFSDNSVLDK-----ACYLLGIDPSLFVK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 909 ATFKhhlRQIieQMTSGPQRQGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPG 988
Cdd:COG5022 371 WLVK---RQI--KTGGEWIVVPLNLEQA--------LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 989 FQNPRHQGkdraatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGI---PVPF-------DLPESSpgttvavvdqNP 1058
Cdd:COG5022 438 FEIFEKNS------FEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIewsFIDYfdnqpciDLIEKK----------NP 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1059 SqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAgAEEPPSMRTCEQPLQcelfHQLGrDpVRYD 1138
Cdd:COG5022 502 L--------------GILSLLDEECVMPHATDESFTSKLAQRLNKNSNP-KFKKSRFRDNKFVVK----HYAG-D-VEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1139 LTGWLRRAKPNLaALEAPQILQQSKREELQSLFQARAKLPPvcravaglegtsqqalhrsrvvrrafasslaavKRKAPC 1218
Cdd:COG5022 561 VEGFLDKNKDPL-NDDLLELLKASTNEFVSTLFDDEENIES---------------------------------KGRFPT 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1219 A--QIKLQMDALISLLRRSRLHFIHCLVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLH 1296
Cdd:COG5022 607 LgsRFKESLNSLMSTLNSTQPHYIRCIKPNEEKS---------------------PWTFDNQMVLSQLRCCGVLETIRIS 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1297 RAGYAEHMGLAQFRRRFQVLDPALLKKLDLTSEELDeRKVVEELLKTLDLEKKAVAVGHSQVFLKAGVVSRLERQREKLV 1376
Cdd:COG5022 666 RAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKEDT-KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKL 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1377 SRNIVLFQAACRGFLSRQEY-KKLKIRRLATLcIQKNLAVFLKVKDWPWWGLLASLRPLLSSTLGTEQLRAKEE-----E 1450
Cdd:COG5022 745 DNIATRIQRAIRGRYLRRRYlQALKRIKKIQV-IQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAciiklQ 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1451 LTLLRQKLQKSENSRSELRQNTDLLESKItdlTSELADERFKGDVACQALESERAERLQALREVQELKTKYQQVqDALGE 1530
Cdd:COG5022 824 KTIKREKKLRETEEVEFSLKAEVLIQKFG---RSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSI-SSLKL 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1531 VQKQLEEAQQRIqganleekpaggadewqmrldcaqmendflrKRLQQCEERLDSEMKAR--TELEQKLGELQSAyEEAK 1608
Cdd:COG5022 900 VNLELESEIIEL-------------------------------KKSLSSDLIENLEFKTEliARLKKLLNNIDLE-EGPS 947
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1609 KMAHQLKRkchhltwdledtrvlLENQQSRNHELEKRQKKFDlqlaqalgesMFEKSLREKVSQENngvrwelgqlqqql 1688
Cdd:COG5022 948 IEYVKLPE---------------LNKLHEVESKLKETSEEYE----------DLLKKSTILVREGN-------------- 988
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1689 eqkeqeasKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQLRQRFELEIE-- 1766
Cdd:COG5022 989 --------KANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLEnn 1060
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1767 ----RMKQMH-----QKDREDQEEELEDVRqSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIghrdfdve 1837
Cdd:COG5022 1061 qlqaRYKALKlrrenSLLDDKQLYQLESTE-NLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEI-------- 1131
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1838 krlrrdlrrtHALLSdvqLLLATIEDSKTSISKEELE----KVHSQLEQSEAKCEDALKTQKVLTADleNMHSEL--ENV 1911
Cdd:COG5022 1132 ----------SKFLS---QLVNTLEPVFQKLSVLQLEldglFWEANLEALPSPPPFAALSEKRLYQS--ALYDEKskLSS 1196
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1912 TRSKSLVDE--QLYRLQFE---RADLLKRIDEDQGDLNDLMQKHKDliAQSAADIGQiqelqlqlEETKKEKQKLREQL- 1985
Cdd:COG5022 1197 SEVNDLKNEliALFSKIFSgwpRGDKLKKLISEGWVPTEYSTSLKG--FNNLNKKFD--------TPASMSNEKLLSLLn 1266
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1986 HMAQLRIQYLEQSTVERAIVSRQEAIICDLEnktefqkvqikrFEVLVIRLRDSMIKMGEELSRAVKaeaqqRENSQYYQ 2065
Cdd:COG5022 1267 SIDNLLSSYKLEEEVLPATINSLLQYINVGL------------FNALRTKASSLRWKSATEVNYNSE-----ELDDWCRE 1329
|
1530 1540 1550 1560 1570 1580
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291327510 2066 QRLEELKAEMQELAQReeeasRRCMELEKY-VEELATVRQTLQTDLETSIRRI-ADLQAALEE 2126
Cdd:COG5022 1330 FEISDVDEELEELIQA-----VKVLQLLKDdLNKLDELLDACYSLNPAEIQNLkSRYDPADKE 1387
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
614-1361 |
3.01e-82 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 286.48 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 614 EDLASLVSVNESSVMNTLLQRYRAQLPYTCSGPDLITLQP--------QTTTVPSSGKvprgRQDGLPAHVTSLAQRAYW 685
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPykqlpiysEDMIKAYRGK----RRGELPPHIFAIADEAYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 686 ALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVD----GRVSvEKLRATFTVLRAFGCVSTGHSRRATRFAMVM 761
Cdd:pfam00063 78 SMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLE-EQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 762 SLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNL---------HQMAESSAFGMglwsk 832
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 833 pEDKQKaataFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-------AAGACKVGRKQfmrfEWANHAAEALGCDYEE 905
Cdd:pfam00063 232 -DDSEE----FKITDKAMDILGFSDEEQMGIFRIVAAILHLGniefkkeRNDEQAVPDDT----ENLQKAASLLGIDSTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 906 LNTATFKHHLRQIIEQMTsgpqrQGLQDNEACSGlkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVV 984
Cdd:pfam00063 303 LEKALCKRRIKTGRETVS-----KPQNVEQANYA--------RDALAKAIYSRLFDWLVDRINKSLDVKTIEKASfIGVL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 985 DTPGFQ----NprhqgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF----------DLPESSPgtt 1050
Cdd:pfam00063 370 DIYGFEifekN----------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFidfgdnqpciDLIEKKP--- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1051 vavvdqnpsqvhlpagrgaedaGGLFWVLDEEVRVQGSSDSTVLERLRAAFEkkKEAGAEEP-PSMRTCeqplqcelF-- 1127
Cdd:pfam00063 437 ----------------------LGILSLLDEECLFPKATDQTFLDKLYSTFS--KHPHFQKPrLQGETH--------Fii 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1128 -HQLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQSLFQARAKlppvcRAVAGLEGTSQQALHRSRVVRRAFA 1206
Cdd:pfam00063 485 kHYAGD--VEYNVEGFLEKNKDPLND-DLVSLLKSSSDPLLAELFPDYET-----AESAAANESGKSTPKRTKKKRFITV 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1207 SSlaavkrkapcaQIKLQMDALISLLRRSRLHFIHCLVPTTvESKAGQrtpspsqpsgdqgvaneptaLDIPALRVQLAG 1286
Cdd:pfam00063 557 GS-----------QFKESLGELMKTLNSTNPHYIRCIKPNE-KKRAGV--------------------FDNSLVLHQLRC 604
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 1287 SHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLDltseeLDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:pfam00063 605 NGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWK-----GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
625-1361 |
1.67e-61 |
|
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: 225.04 E-value: 1.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTV----PSSGKVPRG-RQDGLPAHVTSLAQRAYWALL----SQRRDQS 695
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdlysEERMLLYHGtTAGELPPHVFAIADHAYTQLIqsgvLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 696 IVALGRSGAGKT-------------TCCEQVLEHLVGMAGSVDGRVSVEKLRATF----TVLRAFGCVSTGHSRRATRFA 758
Cdd:cd14890 81 IIISGESGAGKTeatkiimqylariTSGFAQGASGEGEAASEAIEQTLGSLEDRVlssnPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 759 MVMSLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAF-GMGLWSKPEDKq 837
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLrGECSSIPSCDD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 838 kaATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-----AAGACKVGRKQfMRFEWANHAAEALGCDYEELNTATFK 912
Cdd:cd14890 240 --AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfeSENDTTVLEDA-TTLQSLKLAAELLGVNEDALEKALLT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 913 HHL----RQIIEQMTSgpqrqglqdNEACsglkmtgvECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPG 988
Cdd:cd14890 317 RQLfvggKTIVQPQNV---------EQAR--------DKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 989 FQNPRHQgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFdlpesspgttVAVVDQNPSQVHLPAGRG 1068
Cdd:cd14890 380 FEKFEWN------TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQY----------ITFNDNQACLELIEGKVN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1069 AEdaGGLFWVLDEEVRVQGS-SDSTVLERLRAAFEKKKEAGAEEPPSMRTCE--QP-----LQCELFHQLGRdpVRYDLT 1140
Cdd:cd14890 444 GK--PGIFITLDDCWRFKGEeANKKFVSQLHASFGRKSGSGGTRRGSSQHPHfvHPkfdadKQFGIKHYAGD--VIYDAS 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1141 GWLRRAKPNLAAlEAPQILQQSKReelqslfqaraklppvcravaglegtsqqalhrsrvvrrafasslaAVKRKAPCAQ 1220
Cdd:cd14890 520 GFNEKNNETLNA-EMKELIKQSRR----------------------------------------------SIREVSVGAQ 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1221 IKLQMDALISLLRRSRLHFIHCLVPTTveskagqrtpspsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRAGY 1300
Cdd:cd14890 553 FRTQLQELMAKISLTNPRYVRCIKPNE---------------------TKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGF 611
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1301 A---EHmglAQFRRRFQVLDPallkkldlTSEELDErkVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14890 612 AlreEH---DSFFYDFQVLLP--------TAENIEQ--LVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
622-1360 |
9.39e-60 |
|
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: 219.34 E-value: 9.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 622 VNESSVMNTLLQRYRAQLPYTCSGPD-LITLQPQTTTVPSSG-----------KVPRGRQDGLPAHVTSLAQRAYWALLS 689
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDaslgeygseyyDTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 690 QRRDQSIVALGRSGAGKTTCCEQVLEHLVGM-AGSVDGRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNAT 768
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 769 GRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHqmaESSAFGmGLWS--------KP--EDkqk 838
Cdd:cd14879 161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD---DPSDYA-LLASygchplplGPgsDD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 839 aATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLgaagackvGRKQFM-----RFEWA--------NHAAEALGCDYEE 905
Cdd:cd14879 234 -AEGFQELKTALKTLGFKRKHVAQICQLLAAILHL--------GNLEFTydhegGEESAvvkntdvlDIVAAFLGVSPED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 906 LNTA-TFK-HHLRQiiEQMTS--GPQRQGLQDNEacsglkmtgvecvegMASGLYQELFVAVVSLINRSFSSHHLSMAS- 980
Cdd:cd14879 305 LETSlTYKtKLVRK--ELCTVflDPEGAAAQRDE---------------LARTLYSLLFAWVVETINQKLCAPEDDFATf 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 981 IMVVDTPGFQNprhQGKDRAATFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPfdlpesspgtTVAVVDqNPSQ 1060
Cdd:cd14879 368 ISLLDFPGFQN---RSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVP----------ATSYFD-NSDC 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1061 VHLPAGRGaedaGGLFWVLDEEV-RVQGSSDSTVLERLRAAFEKKKEAGAEEPPSMRTceqplQCELF---HQLGrdPVR 1136
Cdd:cd14879 434 VRLLRGKP----GGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRS-----GSASFtvnHYAG--EVT 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1137 YDLTGWLRRAkpnlaaleapqilqqskREELQSLFqaraklppvcraVAGLEGTSQqalhrsrvvrraFASSLaavkrka 1216
Cdd:cd14879 503 YSVEGFLERN-----------------GDVLSPDF------------VNLLRGATQ------------LNAAL------- 534
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1217 pcaqiklqmDALISLLRRSRLHFIHCLVPTtveskagqRTPSPSQPSGdQGVANEPTALDIPALrvqlagshileaLRLH 1296
Cdd:cd14879 535 ---------SELLDTLDRTRLWSVFCIRPN--------DSQLPNSFDK-RRVKAQIRSLGLPEL------------AARL 584
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1297 RAGYAEHMGLAQFRRRFQVLDPAllkkldltseeLDERKVVEELLKTLDLEKKAVAVGHSQVFL 1360
Cdd:cd14879 585 RVEYVVSLEHAEFCERYKSTLRG-----------SAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
626-1361 |
7.27e-59 |
|
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: 216.80 E-value: 7.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPqTTTVPSSGK--VPRGRQDGL-PAHVTSLAQRAYWALLSQRRDQSIVALGRS 702
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNP-FKDVPLYGNefITAYRQKLLdSPHVYAVADTAYREMMRDEINQSIIISGES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 703 GAGKTTCCEQVLEHLVGMAGSVDGrVSVEKLRaTFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVLLE 782
Cdd:cd01383 81 GAGKTETAKIAMQYLAALGGGSSG-IENEILQ-TNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 783 NSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEGEQQA 862
Cdd:cd01383 159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 863 IWRVLAAIYHLG--------AAGACKVGRKqfmrfEWANHAAEALGCDYEELNTATFKHHLR---QIIEQMTSGPQrqgl 931
Cdd:cd01383 238 IFQMLAAVLWLGnisfqvidNENHVEVVAD-----EAVSTAASLLGCNANDLMLALSTRKIQaggDKIVKKLTLQQ---- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 932 qdneacsglkmtGVECVEGMASGLYQELFVAVVSLINRSF-SSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEELCYNY 1010
Cdd:cd01383 309 ------------AIDARDALAKAIYASLFDWLVEQINKSLeVGKRRTGRSISILDIYGFESFQKN------SFEQLCINY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1011 AQERLQLLFYHRTFVSTLERYKEEGIPVpfdlpesspgTTVAVVDqNPSQVHLPAGRGAedagGLFWVLDEEVRVQGSSD 1090
Cdd:cd01383 371 ANERLQQHFNRHLFKLEQEEYELDGIDW----------TKVDFED-NQECLDLIEKKPL----GLISLLDEESNFPKATD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1091 STVLERLRAAFEKKKEAGAEEPPSMRTCeqplqcelfHQLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQQSKReelqSL 1170
Cdd:cd01383 436 LTFANKLKQHLKSNSCFKGERGGAFTIR---------HYAGE--VTYDTSGFLEKNRDLLHS-DLIQLLSSCSC----QL 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1171 FQARAklppvcravAGLEGTSQQALHRSRVVRRAFasslaavKRKAPCAQIKLQMDALISLLRRSRLHFIHCLVPTTVES 1250
Cdd:cd01383 500 PQLFA---------SKMLDASRKALPLTKASGSDS-------QKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQL 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1251 kagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPallkklDLTSEE 1330
Cdd:cd01383 564 ---------------------PGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP------EDVSAS 616
|
730 740 750
....*....|....*....|....*....|.
gi 291327510 1331 LDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd01383 617 QDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
626-1361 |
1.67e-58 |
|
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: 216.18 E-value: 1.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP------QTTTVPSS--GKvprgRQDGLPAHVTSLAQRAYWALLSQRRDQSIV 697
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPykrlpiYTEEVIDKykGK----RREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 698 ALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATF--------TVLRAFGCVSTGHSRRATRFAMVMSLDFNATG 769
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 770 RVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGmglwSKPE---DKQKAATAFSQL 846
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFL----SQGEltiDGVDDAEEFKLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 847 RGAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMRF---EWANHAAEALGCDYEELNTATFKHHL---RQIIE 920
Cdd:cd01377 234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELdgtEEADKAAHLLGVNSSDLLKALLKPRIkvgREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 921 QmtsgpqrqglqdneacsGLKMTGVEC-VEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQ----Nprhq 995
Cdd:cd01377 314 K-----------------GQNKEQVVFsVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 996 gkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----------DLPEsSPGTtvavvdqnpsqvhlp 1064
Cdd:cd01377 373 ------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgldlqptiDLIE-KPNM--------------- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1065 agrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAGAEEPPSmrtceQPLQC-ELFHQLGRdpVRYDLTGWL 1143
Cdd:cd01377 431 ---------GILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPK-----KSEAHfILKHYAGD--VEYNIDGWL 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1144 RRAK----PNLAALeapqiLQQSKREELQSLFQAraklppvcravaglegtsqqalhrsrvVRRAFASSLAAVKRKAP-- 1217
Cdd:cd01377 495 EKNKdplnENVVAL-----LKKSSDPLVASLFKD---------------------------YEESGGGGGKKKKKGGSfr 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1218 -CAQI-KLQMDALISLLRRSRLHFIHCLVPTTveskagQRTPspsqpsgdqGVANEPTALDipalrvQLAGSHILEALRL 1295
Cdd:cd01377 543 tVSQLhKEQLNKLMTTLRSTHPHFVRCIIPNE------EKKP---------GKIDAPLVLH------QLRCNGVLEGIRI 601
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291327510 1296 HRAGYAEHMGLAQFRRRFQVLDPALLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd01377 602 CRKGFPNRIIFAEFKQRYSILAPNAIPK-----GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
625-1361 |
3.69e-58 |
|
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: 215.26 E-value: 3.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVP--RGRQ-DGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPyKNLPIYSENIIEmyRGKKrHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMA--------GSVDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVT 772
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQAN-PILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 773 AAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGlwSKPEDKQKAATAFSQLRGAMEL 852
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG--YIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 853 LGISEGEQQAIWRVLAAIYHLGAAGACKvGRKQFMRFEWANHAAEALgCDYEELNTATFKHHLrqIIEQMTSGpqRQGLQ 932
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKL-CHLLGMNVMEFTRAI--LTPRIKVG--RDYVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 933 DNEAcsglKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQnprhqgKDRAATFEELCYNYA 1011
Cdd:cd14920 312 KAQT----KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFE------IFELNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1012 QERLQLLFYHRTFVSTLERYKEEGIP---VPFDLpESSPGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGS 1088
Cdd:cd14920 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDLIERPANPP--------------GVLALLDEECWFPKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1089 SDSTVLERLRAafekkkEAGAEepPSMRTCEQP---LQCELFHQLGRdpVRYDLTGWL-RRAKP---NLAALeapqiLQQ 1161
Cdd:cd14920 447 TDKTFVEKLVQ------EQGSH--SKFQKPRQLkdkADFCIIHYAGK--VDYKADEWLmKNMDPlndNVATL-----LHQ 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1162 SKREELQSLFQARAKlppvcraVAGLEGTSQQALhrsrvvrRAFASSLAAVKRK-APCAQI-KLQMDALISLLRRSRLHF 1239
Cdd:cd14920 512 SSDRFVAELWKDVDR-------IVGLDQVTGMTE-------TAFGSAYKTKKGMfRTVGQLyKESLTKLMATLRNTNPNF 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1240 IHCLVPTTvESKAGQRTPSpsqpsgdqgvanepTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPA 1319
Cdd:cd14920 578 VRCIIPNH-EKRAGKLDPH--------------LVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 636
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 291327510 1320 LLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14920 637 AIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
625-1361 |
1.36e-56 |
|
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: 210.61 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVP---RG-RQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMeryKGiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGS-----------------VDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSL 763
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavLIGELEQQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 764 DFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKP--EDKQKaat 841
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPgvDDYAE--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 842 aFSQLRGAMELLGISEGEQQAIWRVLAAIYHLGAagackvgrkqfMRFEWANHAAEALGCDyeelNTATFK--HHLRQII 919
Cdd:cd14911 237 -FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-----------MKFRQERNNDQATLPD----NTVAQKiaHLLGLSV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 920 EQMTSG---PQRQGLQDNEACSGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQnprhq 995
Cdd:cd14911 301 TDMTRAfltPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFE----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 996 gKDRAATFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLpesSPgtTVAVVDQnpsqvhlpagrgae 1070
Cdd:cd14911 376 -IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFidfglDL---QP--TIDLIDK-------------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1071 dAGGLFWVLDEEVRVQGSSDSTVLERLRAAFekkkeagAEEPPSMRTCEQPL-QCELFHQLGRdpVRYDLTGWLRRakpN 1149
Cdd:cd14911 436 -PGGIMALLDEECWFPKATDKTFVDKLVSAH-------SMHPKFMKTDFRGVaDFAIVHYAGR--VDYSAAKWLMK---N 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1150 LAALEapqilqqskrEELQSLFQArAKLPPVCR--AVAGLEGTSQQALHRSRVVRRAFASSLAAVKRkapcaQIKLQMDA 1227
Cdd:cd14911 503 MDPLN----------ENIVSLLQG-SQDPFVVNiwKDAEIVGMAQQALTDTQFGARTRKGMFRTVSH-----LYKEQLAK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1228 LISLLRRSRLHFIHCLVPTTvESKAGQrtpspsqpsgdqgvaneptaLDIPALRVQLAGSHILEALRLHRAGYAEHMGLA 1307
Cdd:cd14911 567 LMDTLRNTNPNFVRCIIPNH-EKRAGK--------------------IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1308 QFRRRFQVLDPALLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14911 626 EFRQRYELLTPNVIPK-----GFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
629-1361 |
2.68e-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: 206.41 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 629 NTLLQ-RYRAQLPYTCSGPDLITLQP--------QTTTVPSSGKvprgRQDGLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14883 4 NTNLKvRYKKDLIYTYTGSILVAVNPykelpiytQDIVKQYFGK----RMGALPPHIFALAEAAYTNMQEDGKNQSVIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVgmagSVDGRVS-VEK--LRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQL 776
Cdd:cd14883 80 GESGAGKTETTKLILQYLC----AVTNNHSwVEQqiLEAN-TILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 777 QTVLLENSRVARQPQGEGNFEVFSQLLAG--MDVDLRTELNL------HQMAESSAFGMGLWSkpeDKQKaataFSQLRG 848
Cdd:cd14883 155 QDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLgepedyHYLNQSGCIRIDNIN---DKKD----FDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 849 AMELLGISEGEQQAIWRVLAAIYHLG--AAGACKVGRKQFMRFEWANHAAEA--LGCDYEELNTA-TFKHhlRQIIEQMT 923
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGnlTFEDIDGETGALTVEDKEILKIVAklLGVDPDKLKKAlTIRQ--INVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 924 SGPqrqgLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTF 1003
Cdd:cd14883 306 EIP----LKVQEA--------RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1004 EELCYNYAQERLQLLFYHRTFVSTLERYKEEGI---PVPF-------DLPESSPgttvavvdqnpsqvhlpagrgaedaG 1073
Cdd:cd14883 368 EQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGInwsHIVFtdnqeclDLIEKPP-------------------------L 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1074 GLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAgaeEPPSMRTCEqplqcELF---HQLGRdpVRYDLTGWLRRAKP-- 1148
Cdd:cd14883 423 GILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYY---EKPDRRRWK-----TEFgvkHYAGE--VTYTVQGFLDKNKDtq 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1149 --NLAALeapqiLQQSKREELQSLFQARAKLPPVCRAVAGLEGTSQqalhrsrvvrrafasslAAVKRKAP--CAQIKLQ 1224
Cdd:cd14883 493 qdDLFDL-----MSRSKNKFVKELFTYPDLLALTGLSISLGGDTTS-----------------RGTSKGKPtvGDTFKHQ 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1225 MDALISLLRRSRLHFIHCLVPTTVEskagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAEHM 1304
Cdd:cd14883 551 LQSLVDVLSATQPWYVRCIKPNSLK---------------------EPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHL 609
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 1305 GLAQFRRRFQVLDPALLKKLDltseeLDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14883 610 TFKEFVDRYLCLDPRARSADH-----KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
625-1361 |
4.26e-54 |
|
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: 202.78 E-value: 4.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP----QTTTvPSSGKVPRGRQD-GLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGHVLISVNPfkdlGIYT-DEVLESYRGKNRyEVPPHVFALADSAYRNMKSEKENQCVIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDGRVS--VEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQ 777
Cdd:cd01378 80 GESGAGKTEASKRIMQYIAAVSGGSESEVErvKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 778 TVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPE---DKQKaataFSQLRGAMELLG 854
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDgidDAAD----FKEVLNAMKVIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 855 ISEGEQQAIWRVLAAIYHLG-------AAGACKVGRKQFMRFewanhAAEALGCDYEELNTATfkhhlrqIIEQMTSGPQ 927
Cdd:cd01378 236 FTEEEQDSIFRILAAILHLGniqfaedEEGNAAISDTSVLDF-----VAYLLGVDPDQLEKAL-------THRTIETGGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 928 RQG-----LQDNEACSGLkmtgvecvEGMASGLYQELFVAVVSLINRSFSSHHLSMASIM-VVDTPGFQNPRHQGkdraa 1001
Cdd:cd01378 304 GRSvyevpLNVEQAAYAR--------DALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKNS----- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1002 tFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGI---PVPF-------DLPESSPgttvavvdqnpsqvhlpagrgaed 1071
Cdd:cd01378 371 -FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIewtPIKYfnnkiicDLIEEKP------------------------ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1072 aGGLFWVLDEEV-RVQGSSDSTVLERLRAAFEKKKEAgaeEPPSMRTcEQPLQC-ELFHQLGrdPVRYDLTGWLRRAKPN 1149
Cdd:cd01378 426 -PGIFAILDDAClTAGDATDQTFLQKLNQLFSNHPHF---ECPSGHF-ELRRGEfRIKHYAG--DVTYNVEGFLDKNKDL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1150 LAA--LEApqiLQQSKREELQSLFqaraklppvcravagLEGTSQqalhrsrvvrrafasslaAVKRKAPCA--QIKLQM 1225
Cdd:cd01378 499 LFKdlKEL---MQSSSNPFLRSLF---------------PEGVDL------------------DSKKRPPTAgtKFKNSA 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1226 DALISLLRRSRLHFIHCLVPTtvESKAgqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMG 1305
Cdd:cd01378 543 NALVETLMKKQPSYIRCIKPN--DNKS-------------------PGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQT 601
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 291327510 1306 LAQFRRRFQVLDPAllkkldlTSE--ELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd01378 602 YEKFLERYKLLSPK-------TWPawDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
625-1330 |
4.33e-54 |
|
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: 202.70 E-value: 4.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP-----QTTTVPSSGKVPRGRQDGLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyqwlpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTV 779
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 780 LLENSRVARQPQGEGNFEVFSQLLAGMDVDLRteLNLHQMAESSAFGMGLWSKPEDKQKAAtAFSQLRGAMELLGISEGE 859
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTGANKTIKIEGMSDRK-HFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 860 QQAIWRVLAAIYHLGAA-----------GACKVGRkqfmrfEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSgPQR 928
Cdd:cd14903 237 QEVLFEVLAGILHLGQLqiqskpnddekSAIAPGD------QGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV-PLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 929 QglQDNEACSGlkmtgvecveGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEELCY 1008
Cdd:cd14903 310 K--DQAEDCRD----------ALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1009 NYAQERLQLLFYHRTFVSTLERYKEEGIP---VPFdlpeSSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFWVLDEEV-R 1084
Cdd:cd14903 372 NYANEKLQQKFTQDVFKTVQIEYEEEGIRwahIDF----ADNQDVLAVI---------------EDRLGIISLLNDEVmR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1085 VQGSSDSTVLeRLRAAFEKKKEAgAEEPPSMRTceqplQCELFHQLGrdPVRYDLTGWLRRAK----PNLAALeapqiLQ 1160
Cdd:cd14903 433 PKGNEESFVS-KLSSIHKDEQDV-IEFPRTSRT-----QFTIKHYAG--PVTYESLGFLEKHKdallPDLSDL-----MR 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1161 QSKREELQSLFQARaklppvcravAGLEGTSQQALHRSRVVRRAFASSLAAVKrkapcAQIKLQMDALISLLRRSRLHFI 1240
Cdd:cd14903 499 GSSKPFLRMLFKEK----------VESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNELMTTIRSTNVHYV 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1241 HCLVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDP-- 1318
Cdd:cd14903 564 RCIKPNSIKS---------------------PTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPeg 622
|
730 740
....*....|....*....|....
gi 291327510 1319 ------------ALLKKLDLTSEE 1330
Cdd:cd14903 623 rntdvpvaerceALMKKLKLESPE 646
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
626-1361 |
5.08e-54 |
|
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: 202.97 E-value: 5.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVPRG-----RQDGlPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGyrgkkRQEA-PPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVD-GRVSVEKLRATFT--------VLRAFGCVSTGHSRRATRFAMVMSLDFNATGRV 771
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 772 TAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnlhqMAESSAFGMGLWSKPEDKQKAATAFSQL---RG 848
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL----LITTNPYDYPFISQGEILVASIDDAEELlatDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 849 AMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSG 925
Cdd:cd14913 237 AIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 926 PQRQGLQDNeacsglkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEE 1005
Cdd:cd14913 317 QTVDQVHHA-------------VNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1006 LCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLpesspGTTVAVVdqnpsqVHLpagrgAEDAGGLFWVLDEEVR 1084
Cdd:cd14913 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFiDF-----GMDLAAC------IEL-----IEKPMGIFSILEEECM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1085 VQGSSDSTVLERLraaFEKK--KEAGAEEPPSMRTcEQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQS 1162
Cdd:cd14913 442 FPKATDTSFKNKL---YDQHlgKSNNFQKPKVVKG-RAEAHFSLIHYAG--TVDYSVSGWLEKNKDPLNE-TVVGLYQKS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1163 KREELQSLFQ--ARAKLPPVCRAVAGLEGTSQQ---ALHRSrvvrrafasslaavkrkapcaqiklQMDALISLLRRSRL 1237
Cdd:cd14913 515 SNRLLAHLYAtfATADADSGKKKVAKKKGSSFQtvsALFRE-------------------------NLNKLMSNLRTTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1238 HFIHCLVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLD 1317
Cdd:cd14913 570 HFVRCIIPNETKT---------------------PGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 291327510 1318 PALLkkldLTSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14913 629 ASAI----PEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
627-1361 |
1.80e-53 |
|
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: 200.60 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 627 VMNTLLQRYRAQLPYTCSGPDLITLQPQTttvpssgKVP-----------RGRQDG-LPAHVTSLAQRAYWALLSQRRDQ 694
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPFK-------RLPhlydahmmeqyKGAPLGeLSPHVFAVADAAYRAMINEGKSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 695 SIVALGRSGAGKTTCCEQVLEHLVGMAG--SVDGRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVT 772
Cdd:cd01384 76 SILVSGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 773 AAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNL------HQMAESSAFGMglwskpeDKQKAATAFSQL 846
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFEL-------DGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 847 RGAMELLGISEGEQQAIWRVLAAIYHLG--------AAGACKVGRKQfMRFEWANhAAEALGCDYEELNTATFKhhlRQI 918
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGniefskgeEDDSSVPKDEK-SEFHLKA-AAELLMCDEKALEDALCK---RVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 919 ieQMTSGPQRQGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQnprhQGKD 998
Cdd:cd01384 304 --VTPDGIITKPLDPDAA--------TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE----SFKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 999 RaaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIP---VPF-------DLPESSPgttvavvdqnpsqvhlpagrg 1068
Cdd:cd01384 370 N--SFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDwsyIEFvdnqdvlDLIEKKP--------------------- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1069 aedaGGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEagAEEPPSMRTceqplQCELFHQLGrdPVRYDLTGWLRRAKp 1148
Cdd:cd01384 427 ----GGIIALLDEACMFPRSTHETFAQKLYQTLKDHKR--FSKPKLSRT-----DFTIDHYAG--DVTYQTDLFLDKNK- 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1149 NLAALEAPQILQQSKREELQSLFqaraklPPVCRavaglEGTSQQalhrsrvvrrafaSSLAAVKrkapcAQIKLQMDAL 1228
Cdd:cd01384 493 DYVVAEHQALLNASKCPFVAGLF------PPLPR-----EGTSSS-------------SKFSSIG-----SRFKQQLQEL 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1229 ISLLRRSRLHFIHCLVPTTVeskagqrtpspsqpsgdqgvaNEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQ 1308
Cdd:cd01384 544 METLNTTEPHYIRCIKPNNL---------------------LKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEE 602
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 291327510 1309 FRRRFQVLDPALLKKLDltseelDERKVVEELLKTLDLekKAVAVGHSQVFLK 1361
Cdd:cd01384 603 FLDRFGLLAPEVLKGSD------DEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
625-1361 |
3.73e-52 |
|
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: 197.48 E-value: 3.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQ------TTTVPSSGKVPRgRQDGlPAHVTSLAQRAYWALLSQRRDQSIVA 698
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYkwlpvyTAPVVAAYKGKR-RSEA-PPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 699 LGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATFT-------------VLRAFGCVSTGHSRRATRFAMVMSLDF 765
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 766 NATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnlhqMAESSAFGMGLWSKPEDKQKAATAFSQ 845
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML----LVSMNPYDYHFCSQGVTTVDNMDDGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 846 LRG---AMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQII 919
Cdd:cd14927 235 LMAtdhAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEadgTESADKAAYLMGVSSADLLKGLLHPRVKVGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 920 EQMTSGPQRQglQDNEAcsglkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdr 999
Cdd:cd14927 315 EYVTKGQSVE--QVVYA-----------VGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1000 aaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLPesspgttvAVVDQnpsqvhlpagrgAEDAGG 1074
Cdd:cd14927 378 --SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFidfglDLQ--------ACIDL------------IEKPLG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1075 LFWVLDEEVRVQGSSDSTVLERL-------RAAFEKKKeagaeePPSMRTCEQPLqcELFHQLGRDPvrYDLTGWLRRAK 1147
Cdd:cd14927 436 ILSILEEECMFPKASDASFKAKLydnhlgkSPNFQKPR------PDKKRKYEAHF--EVVHYAGVVP--YNIVGWLDKNK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1148 PNLAALEAPqILQQSKREELQSLFQARAklppvcravagleGTSQQALHRSRVVRRafasslaavKRKAPCAQI-----K 1222
Cdd:cd14927 506 DPLNETVVA-IFQKSQNKLLATLYENYV-------------GSDSTEDPKSGVKEK---------RKKAASFQTvsqlhK 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1223 LQMDALISLLRRSRLHFIHCLVPTtvESKAgqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAE 1302
Cdd:cd14927 563 ENLNKLMTNLRATQPHFVRCIIPN--ETKT-------------------PGVMDPFLVLHQLRCNGVLEGIRICRKGFPN 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 1303 HMGLAQFRRRFQVLDPALLKKldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14927 622 RILYADFKQRYRILNPSAIPD----DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
628-1361 |
1.36e-51 |
|
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: 195.36 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 628 MNTLLQRYRAQLPYTCSGPDLITLQPQTTtVPSSGKVP-----RGRQDGL---PAHVTSLAQRAYWALLS----QRRDQS 695
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKS-IPLLYDVPgfdsqRKEEATAsspPPHVFSIAERAYRAMKGvgkgQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 696 IVALGRSGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEK-LRATFTVLRAFGCVSTGHSRRATRFAMVMSLD 764
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLATASklakgastskGAANAHESIEEcVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 765 FNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhQMAESSAFGMGLWSKPEDKQKAATAFS 844
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALEL-TPAESFLFLNQGNCVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 845 QLRGAMELLGISEGEQQAIWRVLAAIYHLGAA--GACKVGRKQFMRF---EWANHAAEALGCDYEELntaTFKhhlrqII 919
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVrfEENADDEDVFAQSadgVNVAKAAGLLGVDAAEL---MFK-----LV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 920 EQMTSGPQRQGLQdneacsgLKMTGVECVE---GMASGLYQELFVAVVSLINRSFSSH----HLSMAS------IMVVDT 986
Cdd:cd14892 314 TQTTSTARGSVLE-------IKLTAREAKNaldALCKYLYGELFDWLISRINACHKQQtsgvTGGAASptfspfIGILDI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 987 PGFQN-PRHqgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGI---PVPFDlpesSPGTTVAVVDQNPSqvh 1062
Cdd:cd14892 387 FGFEImPTN-------SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIdvsAIEFQ----DNQDCLDLIQKKPL--- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1063 lpagrgaedagGLFWVLDEEVRV-QGSSDSTVLERLRAAFEKKKEAGAeePPSMrtceqplQCELF---HQLGRdpVRYD 1138
Cdd:cd14892 453 -----------GLLPLLEEQMLLkRKTTDKQLLTIYHQTHLDKHPHYA--KPRF-------ECDEFvlrHYAGD--VTYD 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1139 LTGWLRRAKPNLAaleapqilqqskrEELQSLfqaraklppvcravaglegtsqqaLHRSRVVRRafasslaavkrkapc 1218
Cdd:cd14892 511 VHGFLAKNNDNLH-------------DDLRDL------------------------LRSSSKFRT--------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1219 aqiklQMDALISLLRRSRLHFIHCLVPTTveskagqrtpspsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRA 1298
Cdd:cd14892 539 -----QLAELMEVLWSTTPSYIKCIKPNN---------------------LKFPGGFSCELVRDQLIYSGVLEVVRIRRE 592
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291327510 1299 GYAEHMGLAQFRRRFQVLDPAlLKKLDLTSEELD---ERKVVEELLKTLdLEKKAVAVGHSQVFLK 1361
Cdd:cd14892 593 GFPIRRQFEEFYEKFWPLARN-KAGVAASPDACDattARKKCEEIVARA-LERENFQLGRTKVFLR 656
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
626-1361 |
2.49e-51 |
|
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: 194.94 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQT---TTVPSSGKVPRGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALGR 701
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlpVYNAEVVAAYRGKKRSeAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 702 SGAGKTTCCEQVLEHLVGMAGSVD--------GRVSVE-KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVT 772
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDrskkdqtpGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 773 AAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnlhqMAESSAFGMGLWSKPEDKQKAATAFSQLRG---A 849
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML----LITNNPYDYAFISQGETTVASIDDAEELMAtdnA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 850 MELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGP 926
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEpdgTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 927 QRQGLqdneacsgLKMTGvecveGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEEL 1006
Cdd:cd14917 318 NVQQV--------IYATG-----ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1007 CYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLPesspgttvAVVDQnpsqvhlpagrgAEDAGGLFWVLDE 1081
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgmDLQ--------ACIDL------------IEKPMGIMSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1082 EVRVQGSSDSTVLERLraaFEKK--KEAGAEEPPSMRTcEQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQIL 1159
Cdd:cd14917 439 ECMFPKATDMTFKAKL---FDNHlgKSNNFQKPRNIKG-KPEAHFSLIHYAG--TVDYNIIGWLQKNKDPLNE-TVVGLY 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1160 QQSKREELQSLFQARAKlppvcrAVAGLEGTSQQALHRSRVvrrafaSSLAAVKRKapcaqiklQMDALISLLRRSRLHF 1239
Cdd:cd14917 512 QKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSF------QTVSALHRE--------NLNKLMTNLRSTHPHF 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1240 IHCLVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPA 1319
Cdd:cd14917 572 VRCIIPNETKS---------------------PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 291327510 1320 LLKKldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14917 631 AIPE----GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
625-1361 |
6.58e-51 |
|
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: 193.32 E-value: 6.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVPR----GRQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANmykgKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAG----SVDGRVSVE-KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQ 775
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGtgkqSSDGKGSLEdQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 776 LQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNL------HQMAESSAFGMGLWSKPEDKQKAATAFsqlrga 849
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvpnpkeYHWVSQGVTVVDNMDDGEELQITDVAF------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 850 mELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMRF---EWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGp 926
Cdd:cd14934 235 -DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVdttEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 927 qrqglQDNEACSglkmtgvECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEEL 1006
Cdd:cd14934 313 -----QNMEQCN-------NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFEQL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1007 CYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLPesspgttvAVVDQnpsqvhlpagrgAEDAGGLFWVLDE 1081
Cdd:cd14934 375 CINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFidfglDLQ--------ACIDL------------LEKPMGIFSILEE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1082 EVRVQGSSDSTvlerLRAAFEKK---KEAGAEEPPSMRTCEQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLaaleapqi 1158
Cdd:cd14934 435 QCVFPKATDAT----FKAALYDNhlgKSSNFLKPKGGKGKGPEAHFELVHYAG--TVGYNITGWLEKNKDPL-------- 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1159 lqqskREELQSLFQARAKLppvcraVAGLEGTSQQALHRSRVVRRafASSLAAVKRKapcaqIKLQMDALISLLRRSRLH 1238
Cdd:cd14934 501 -----NETVVGLFQKSSLG------LLALLFKEEEAPAGSKKQKR--GSSFMTVSNF-----YREQLNKLMTTLHSTAPH 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1239 FIHCLVPTTVESkagqrtpspsqpsgdQGVANEPTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDP 1318
Cdd:cd14934 563 FVRCIVPNEFKQ---------------SGVVDAHLIMH------QLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNP 621
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 291327510 1319 ALLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14934 622 NVIPQ-----GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
625-1361 |
3.23e-50 |
|
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: 191.21 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQT---TTVPSSGKVPRG-RQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKrypVYTNRCAKMYRGkRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------LRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTA 773
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 774 AQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAF-GMGLWSKPEDKQkaATAFSQLRGAMEL 852
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIvSQGKVTVPNVDD--GEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 853 LGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGPQRQ 929
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEqdgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 930 GLQDNeacsglkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQGkdraatFEELCYN 1009
Cdd:cd14909 319 QVTNS-------------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1010 YAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLpesspgttVAVVDQnpsqvhlpagrgAEDAGGLFWVLDEEVR 1084
Cdd:cd14909 380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFidfgmDL--------LACIDL------------IEKPMGILSILEEESM 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1085 VQGSSDSTVLERLRAAfEKKKEAGAEEPPSMRTCEQPLQCELFHQLGRdpVRYDLTGWLRRAKPNLaaleAPQILQQSKR 1164
Cdd:cd14909 440 FPKATDQTFSEKLTNT-HLGKSAPFQKPKPPKPGQQAAHFAIAHYAGC--VSYNITGWLEKNKDPL----NDTVVDQFKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1165 EELQSLFQARAKLPpvcravaGLEGTSQQALHRSRVVRRAFASSLAAVKRkapcaqiklQMDALISLLRRSRLHFIHCLV 1244
Cdd:cd14909 513 SQNKLLIEIFADHA-------GQSGGGEQAKGGRGKKGGGFATVSSAYKE---------QLNSLMTTLRSTQPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1245 PTTVEskagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKl 1324
Cdd:cd14909 577 PNEMK---------------------QPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQG- 634
|
730 740 750
....*....|....*....|....*....|....*..
gi 291327510 1325 dltseELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14909 635 -----EEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
625-1361 |
9.27e-50 |
|
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: 190.23 E-value: 9.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVP---RGRQ-DGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVdmyKGKKrHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGS--------VDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVT 772
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtsITGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 773 AAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPedKQKAATAFSQLRGAMEL 852
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIP--AAQDDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 853 LGISEGEQQAIWRVLAAIYHLGAAgACKVGRKQFMRFEWANHAAEALgCDYEELNTATFKhhlRQIIEqmtsgPQRQGLQ 932
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNI-VFKKERNTDQASMPDNTAAQKV-CHLMGINVTDFT---RSILT-----PRIKVGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 933 DNEACSGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIM-VVDTPGFQnprhqgKDRAATFEELCYNYA 1011
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFE------IFEVNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1012 QERLQLLFYHRTFVSTLERYKEEGIP---VPFDLpESSPGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGS 1088
Cdd:cd14921 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIELIERPNNPP--------------GVLALLDEECWFPKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1089 SDSTVLERLRAafEKKKEAGAEEPPSMRtceQPLQCELFHQLGRdpVRYDLTGWLRRakpNLAAL--EAPQILQQSKREE 1166
Cdd:cd14921 447 TDKSFVEKLCT--EQGNHPKFQKPKQLK---DKTEFSIIHYAGK--VDYNASAWLTK---NMDPLndNVTSLLNASSDKF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1167 LQSLFQARAKlppvcraVAGLE---GTSQQALHRSRVVRRAFASSLAAVKRKapcaqiklQMDALISLLRRSRLHFIHCL 1243
Cdd:cd14921 517 VADLWKDVDR-------IVGLDqmaKMTESSLPSASKTKKGMFRTVGQLYKE--------QLGKLMTTLRNTTPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1244 VPTTvESKAGQrtpspsqpsgdqgvaneptaLDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKK 1323
Cdd:cd14921 582 IPNH-EKRSGK--------------------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
730 740 750
....*....|....*....|....*....|....*...
gi 291327510 1324 ldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14921 641 -----GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
627-1361 |
1.67e-49 |
|
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: 189.17 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 627 VMNTLLQRYRAQLPYTCSGPDLITLQPQT---TTVPSSGKVPRG--RQDGlPAHVTSLAQRAYWALLSQRRDQSIVALGR 701
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpVYNPEVVAAYRGkkRQEA-PPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 702 SGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRV 771
Cdd:cd14918 82 SGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 772 TAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAF-GMGLWSKPE-DKQKAATAFSQlrgA 849
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvSQGEITVPSiDDQEELMATDS---A 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 850 MELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGP 926
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 927 QRQGLQDneacsglkmtgveCVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEEL 1006
Cdd:cd14918 318 TVQQVYN-------------AVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1007 CYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLPESSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFWVLDEEVRVQ 1086
Cdd:cd14918 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELI---------------EKPLGIFSILEEECMFP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1087 GSSDSTVLERLRAAfEKKKEAGAEEPPSMRTcEQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKREE 1166
Cdd:cd14918 444 KATDTSFKNKLYDQ-HLGKSANFQKPKVVKG-KAEAHFSLIHYAG--TVDYNITGWLDKNKDPLND-TVVGLYQKSAMKT 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1167 LQSLFQARAklppvcravaglegtSQQALHRSRVVRRAFASSLAAVKrkapcAQIKLQMDALISLLRRSRLHFIHCLVPT 1246
Cdd:cd14918 519 LASLFSTYA---------------SAEADSGAKKGAKKKGSSFQTVS-----ALFRENLNKLMTNLRSTHPHFVRCIIPN 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1247 TVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKldl 1326
Cdd:cd14918 579 ETKT---------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE--- 634
|
730 740 750
....*....|....*....|....*....|....*
gi 291327510 1327 tSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14918 635 -GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
626-1361 |
1.92e-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 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: 189.17 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVP---RG--RQDGlPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVtayRGkkRQEA-PPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKLRATFT--------VLRAFGCVSTGHSRRATRFAMVMSLDFNATG 769
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 770 RVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAF-GMGLWSKPE-DKQKAATAFSQlr 847
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvSQGEITVPSiDDQEELMATDS-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 848 gAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTS 924
Cdd:cd14910 239 -AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 925 GPQRQGLQDneacsglkmtgveCVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFE 1004
Cdd:cd14910 318 GQTVQQVYN-------------AVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1005 ELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLPESSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFWVLDEEVR 1084
Cdd:cd14910 379 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELI---------------EKPMGIFSILEEECM 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1085 VQGSSDSTVLERLRAAFEKKKEAGAEEPPSMRTCEQPLQceLFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKR 1164
Cdd:cd14910 444 FPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHFS--LIHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSM 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1165 EELQSLFQARAKLPpvCRAVAGLEGTSQQalhrsrvvrrafASSLAAVKrkapcAQIKLQMDALISLLRRSRLHFIHCLV 1244
Cdd:cd14910 519 KTLALLFSGAAAAE--AEEGGGKKGGKKK------------GSSFQTVS-----ALFRENLNKLMTNLRSTHPHFVRCII 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1245 PTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKl 1324
Cdd:cd14910 580 PNETKT---------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE- 637
|
730 740 750
....*....|....*....|....*....|....*..
gi 291327510 1325 dltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14910 638 ---GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
625-1361 |
1.97e-49 |
|
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: 189.03 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTtVPSSGK-----VPRGRQDGLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKW-LPVYQKevmaaYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATF----TVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQ 775
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQImqanPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 776 LQTVLLENSRVARQPQGEGNFEVFSQLLAGMDvDLRTEL----NLHQMAESSAFGMGLWSKPEDKQKAATafsqlRGAME 851
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLlvsaNPSDFHFCSCGAVAVESLDDAEELLAT-----EQAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 852 LLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGpqr 928
Cdd:cd14929 234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEadgTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 929 QGLQDneacsglkmtgVECVEG-MASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEELC 1007
Cdd:cd14929 311 QNIEQ-----------VTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------SLEQLC 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1008 YNYAQERLQLLFYHRTFVSTLERYKEEGI---PVPFDLpesspgTTVAVVDQnpsqvhlpagrgAEDAGGLFWVLDEEVR 1084
Cdd:cd14929 374 INFTNEKLQQFFNQHMFVLEQEEYRKEGIdwvSIDFGL------DLQACIDL------------IEKPMGIFSILEEECM 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1085 VQGSSDSTVLERLraaFEKK--KEAGAEEP-PSMRTCEqpLQCELFHQLGRDPvrYDLTGWLRRAKpNLAALEAPQILQQ 1161
Cdd:cd14929 436 FPKATDLTFKTKL---FDNHfgKSVHFQKPkPDKKKFE--AHFELVHYAGVVP--YNISGWLEKNK-DLLNETVVAVFQK 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1162 SKREELQSLFQARAklppvcravagLEGTSQQALHRSRVVRRAF--ASSLAavkrkapcaqiKLQMDALISLLRRSRLHF 1239
Cdd:cd14929 508 SSNRLLASLFENYI-----------STDSAIQFGEKKRKKGASFqtVASLH-----------KENLNKLMTNLKSTAPHF 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1240 IHCLVPTtveskagqrtpspsqpsgdqgVANEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPA 1319
Cdd:cd14929 566 VRCINPN---------------------VNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPR 624
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 291327510 1320 LLKKldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14929 625 TFPK----SKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
625-1361 |
2.18e-49 |
|
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: 188.76 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVPR----GRQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEmykgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSV-----DGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQ 775
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 776 LQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQKaaTAFSQLRGAMELLGI 855
Cdd:cd14919 160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 856 SEGEQQAIWRVLAAIYHLGAagackvgrkqfMRFEWANHAAEALGCDyeelNTATFK--HHLRQIIEQMTSG---PQRQG 930
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGN-----------IVFKKERNTDQASMPD----NTAAQKvsHLLGINVTDFTRGiltPRIKV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 931 LQDNEACSGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQnprhqgKDRAATFEELCYN 1009
Cdd:cd14919 303 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------IFDLNSFEQLCIN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1010 YAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLPesspgttvavVDQNP--SQVHLPAGrgaedAGGLFWVLDEEVRVQ 1086
Cdd:cd14919 377 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFiDFG----------LDLQPciDLIEKPAG-----PPGILALLDEECWFP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1087 GSSDSTVLERLRAafEKKKEAGAEEPPSMRtcEQPLQCeLFHQLGRdpVRYDLTGWLRR----AKPNLAALeapqiLQQS 1162
Cdd:cd14919 442 KATDKSFVEKVVQ--EQGTHPKFQKPKQLK--DKADFC-IIHYAGK--VDYKADEWLMKnmdpLNDNIATL-----LHQS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1163 KREELQSLFQARAKlppvcraVAGLE---GTSQQALHRSRVVRRAFASSLAAVKRKapcaqiklQMDALISLLRRSRLHF 1239
Cdd:cd14919 510 SDKFVSELWKDVDR-------IIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1240 IHCLVPTTvESKAGQRTPSpsqpsgdqgvanepTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPA 1319
Cdd:cd14919 575 VRCIIPNH-EKKAGKLDPH--------------LVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 633
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 291327510 1320 LLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14919 634 SIPK-----GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
626-1361 |
3.62e-49 |
|
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: 188.40 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQT---TTVPSSGKVPRG--RQDGlPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpVYNPEVVTAYRGkkRQEA-PPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKLRATFT--------VLRAFGCVSTGHSRRATRFAMVMSLDFNATG 769
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKkeeAASGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 770 RVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTEL----NLHQMAESSAFGMGLWSKPEDKQKAATafsq 845
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLlittNPYDFAFVSQGEITVPSIDDQEELMAT---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 846 lRGAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQM 922
Cdd:cd14915 237 -DSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 923 TSGPQRQGLQDNeacsglkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaT 1002
Cdd:cd14915 316 TKGQTVQQVYNS-------------VGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1003 FEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLPESSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFWVLDEE 1082
Cdd:cd14915 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELI---------------EKPMGIFSILEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1083 VRVQGSSDSTVLERLRAAFEKKKEAGAEEPPSMRTCEQPLQceLFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQS 1162
Cdd:cd14915 442 CMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHFS--LVHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1163 KREELQSLFQAraklppvcRAVAGLEGTSQQALHRSRvvrrafASSLAAVKrkapcAQIKLQMDALISLLRRSRLHFIHC 1242
Cdd:cd14915 517 GMKTLAFLFSG--------GQTAEAEGGGGKKGGKKK------GSSFQTVS-----ALFRENLNKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1243 LVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLK 1322
Cdd:cd14915 578 LIPNETKT---------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
730 740 750
....*....|....*....|....*....|....*....
gi 291327510 1323 KldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14915 637 E----GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
626-1361 |
5.60e-49 |
|
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: 187.57 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVP---RGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALGR 701
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVaayRGKKRSeAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 702 SGAGKTTCCEQVLEHLVGMAG-----------SVDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGR 770
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQAN-PALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 771 VTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTEL----NLHQMAESSAFGMGLWSKPEDKQKAATafsql 846
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLlvtnNPYDYAFVSQGEVSVASIDDSEELLAT----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 847 RGAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMT 923
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEpdgTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 924 SGPQRQGLQDNeacsglkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTF 1003
Cdd:cd14916 316 KGQSVQQVYYS-------------IGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1004 EELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLPesspgttvAVVDQnpsqvhlpagrgAEDAGGLFWV 1078
Cdd:cd14916 377 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFidfgmDLQ--------ACIDL------------IEKPMGIMSI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1079 LDEEVRVQGSSDSTVLERLraaFEKK--KEAGAEEPPSMRTcEQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAP 1156
Cdd:cd14916 437 LEEECMFPKASDMTFKAKL---YDNHlgKSNNFQKPRNVKG-KQEAHFSLVHYAG--TVDYNILGWLEKNKDPLNE-TVV 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1157 QILQQSKREELQSLFQARAKlppvcrAVAGLEGTSQQALHRSRVVRrafasSLAAVKRKapcaqiklQMDALISLLRRSR 1236
Cdd:cd14916 510 GLYQKSSLKLMATLFSTYAS------ADTGDSGKGKGGKKKGSSFQ-----TVSALHRE--------NLNKLMTNLKTTH 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1237 LHFIHCLVPTtvESKagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVL 1316
Cdd:cd14916 571 PHFVRCIIPN--ERK-------------------APGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 629
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 291327510 1317 DPALLKKldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14916 630 NPAAIPE----GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
626-1358 |
6.03e-49 |
|
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: 186.90 E-value: 6.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP------QTTTVPS--SGKVPRGrqdgLPAHVTSLAQRAYWALLSQRRDQSIV 697
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPfkrlplYTPTVMDqyMHKGPKE----MPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 698 ALGRSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQL 776
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG---VEqRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 777 QTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhqmaeSSAFGMGLWSKPEDKQKA--ATAFSQLRGAMELLG 854
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGS-----SAAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 855 ISEGEQQAIWRVLAAIYHLG------AAGACKVGRKQFMRFEWANHAAEALGCDYEELNTAtFKHHLRQIIEQmtsGPQR 928
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEA-LTSRLMEIKGC---DPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 929 QGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQ----NprhqgkdraaTF 1003
Cdd:cd14872 306 IPLTPAQA--------TDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifekN----------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1004 EELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPV-PFDLPESSPgttvaVVDqnpsqvhLPAGRGaedaGGLFWVLDEE 1082
Cdd:cd14872 368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFeHIDFIDNQP-----VLD-------LIEKKQ----PGLMLALDDQ 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1083 VRVQGSSDSTVLERLRAAFEKKKEAGAEEppsmrTCEQPLQCELFHQLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQQS 1162
Cdd:cd14872 432 VKIPKGSDATFMIAANQTHAAKSTFVYAE-----VRTSRTEFIVKHYAGD--VTYDITGFLEKNKDTLQK-DLYVLLSSS 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1163 KREELQSLFqaraklPPvcraVAGLEGTSQQALhrsrvvrrafasslaavkrkapCAQIKLQMDALISLLRRSRLHFIHC 1242
Cdd:cd14872 504 KNKLIAVLF------PP----SEGDQKTSKVTL----------------------GGQFRKQLSALMTALNATEPHYIRC 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1243 LVPTtveskagqrtpSPSQPSGDQGVAneptALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLK 1322
Cdd:cd14872 552 VKPN-----------QEKRARLFDGFM----SLE------QLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAK 610
|
730 740 750
....*....|....*....|....*....|....*.
gi 291327510 1323 kldltSEELDERKVVEELLKTLDLEKKAVAVGHSQV 1358
Cdd:cd14872 611 -----RVGPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
625-1361 |
7.48e-49 |
|
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: 187.54 E-value: 7.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVPR----GRQDGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNmykgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVD------------GRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNAT 768
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtkkdqssialshGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 769 GRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQKaaTAFSQLRG 848
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 849 AMELLGISEGEQQAIWRVLAAIYHLGAagackvgrkqfMRFEWANHAAEALGCDyeelNTATFK--HHLRQIIEQMTSG- 925
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGN-----------MSFKKERNSDQASMPD----DTAAQKvcHLLGMNVTDFTRAi 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 926 --PQRQGLQDNEACSGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQnprhqgKDRAAT 1002
Cdd:cd14932 303 lsPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1003 FEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLPesspgttvavVDQNP--SQVHLPAGrgaedAGGLFWVL 1079
Cdd:cd14932 377 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFiDFG----------LDLQPciELIEKPNG-----PPGILALL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1080 DEEVRVQGSSDSTVLERLraAFEKKKEAGAEEPPSMRtcEQPLQCeLFHQLGRdpVRYDLTGWLRRAKPNLAALEApQIL 1159
Cdd:cd14932 442 DEECWFPKATDKSFVEKV--VQEQGNNPKFQKPKKLK--DDADFC-IIHYAGK--VDYKANEWLMKNMDPLNENVA-TLL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1160 QQSKREELQSLFQARAKLPPVCRaVAGLEGTSQQALHRSRVVRRAFASslaavkrkapcaQIKLQMDALISLLRRSRLHF 1239
Cdd:cd14932 514 NQSTDKFVSELWKDVDRIVGLDK-VAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNTNPNF 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1240 IHCLVPTTvESKAGQRTPSpsqpsgdqgvanepTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPA 1319
Cdd:cd14932 581 VRCIIPNH-EKKAGKLAHH--------------LVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 291327510 1320 LLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14932 640 AIPK-----GFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
626-1361 |
4.72e-48 |
|
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: 184.37 E-value: 4.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTV----PSSGKVPRGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPklysSETIKSYQGKSLGtLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVL 780
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIE-QRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 781 LENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnLHQmaessafgmGLWSKPEDkqkaataFSQLRGAMELLGISEGEQ 860
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKD---------PLLDDVGD-------FIRMDKAMKKIGLSDEEK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 861 QAIWRVLAAIYHLG----------AAGACKVGRKQFMRFEwanHAAEALGCDYEELntatfKHHLRQIIEQMTSGPQ--- 927
Cdd:cd01382 224 LDIFRVVAAVLHLGniefeengsdSGGGCNVKPKSEQSLE---YAAELLGLDQDEL-----RVSLTTRVMQTTRGGAkgt 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 928 --RQGLQDNEACSGLkmtgvecvEGMASGLYQELFVAVVSLINRS--FSShhlSMASIMVVDTPGFQNPRHQgkdraaTF 1003
Cdd:cd01382 296 viKVPLKVEEANNAR--------DALAKAIYSKLFDHIVNRINQCipFET---SSYFIGVLDIAGFEYFEVN------SF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1004 EELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPfdlpesspgtTVAVVDqNPSQVHLPAGRGaedaGGLFWVLDEEV 1083
Cdd:cd01382 359 EQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVK----------EVEYVD-NQDCIDLIEAKL----VGILDLLDEES 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1084 RVQGSSD----STVLERLRAAF-----EKKKEAGAEEppsMRTCEQPLQCelfHQLGrdPVRYDLTGWLRRAKPNL-AAL 1153
Cdd:cd01382 424 KLPKPSDqhftSAVHQKHKNHFrlsipRKSKLKIHRN---LRDDEGFLIR---HFAG--AVCYETAQFIEKNNDALhASL 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1154 EapQILQQSKREELQSLFQARAKLPPVCRAVAGlegtsqqalhrsrvvRRAFASslaaVKRKapcaqIKLQMDALISLLR 1233
Cdd:cd01382 496 E--SLICESKDKFIRSLFESSTNNNKDSKQKAG---------------KLSFIS----VGNK-----FKTQLNLLMDKLR 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1234 RSRLHFIHCLVPTtveSKAgqrtpSPSQPSGDQgvaneptaldipaLRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRF 1313
Cdd:cd01382 550 STGTSFIRCIKPN---LKM-----TSHHFEGAQ-------------ILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMY 608
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 291327510 1314 QVLDPALLKKldltseeLDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd01382 609 KKYLPPKLAR-------LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
626-1361 |
1.33e-47 |
|
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: 183.73 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQT---TTVPSSGKVPRG--RQDGlPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpVYNPEVVAAYRGkkRQEA-PPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHL--VGMAGSVDGRVSVEKLRATFT--------VLRAFGCVSTGHSRRATRFAMVMSLDFNATGR 770
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFatIAVTGDKKKEQQPGKMQGTLEdqiiqanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 771 VTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnlhqMAESSAFGMGLWSKPEDKQKAATAFSQL---R 847
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLL----LISTNPFDFPFVSQGEVTVASIDDSEELlatD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 848 GAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTS 924
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 925 GPQRQGLQDNeacsglkmtgvecVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFE 1004
Cdd:cd14923 317 GQNVQQVTNS-------------VGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1005 ELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLPESSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFWVLDEEVR 1084
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELI---------------EKPMGIFSILEEECM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1085 VQGSSDSTVLERLRAAFEKKKEAGAEEPPSMRTCEQPLQceLFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKR 1164
Cdd:cd14923 443 FPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFS--LVHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSL 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1165 EELQSLFQARAKlppvcrAVAGLEGTSQQALHRSrvvrrafASSLAAVKrkapcAQIKLQMDALISLLRRSRLHFIHCLV 1244
Cdd:cd14923 518 KLLSFLFSNYAG------AEAGDSGGSKKGGKKK-------GSSFQTVS-----AVFRENLNKLMTNLRSTHPHFVRCLI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1245 PTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKl 1324
Cdd:cd14923 580 PNETKT---------------------PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE- 637
|
730 740 750
....*....|....*....|....*....|....*..
gi 291327510 1325 dltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14923 638 ---GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
626-1361 |
8.13e-47 |
|
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: 181.08 E-value: 8.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQT---TTVPSSGKVPRG--RQDGlPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpVYNPEVVTAYRGkkRQEA-PPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNAT 768
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 769 GRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTEL----NLHQMAESSAFGMGLWSKPEDKQKAATafs 844
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLlittNPYDYPFVSQGEISVASIDDQEELMAT--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 845 qlRGAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMR---FEWANHAAEALGCDYEELNTATFKHHLRQIIEQ 921
Cdd:cd14912 237 --DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEpdgTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 922 MTSGpqrqglQDNEACSglkmtgvECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraa 1001
Cdd:cd14912 315 VTKG------QTVEQVT-------NAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1002 TFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLPESSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFWVLDE 1081
Cdd:cd14912 376 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELI---------------EKPMGIFSILEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1082 EVRVQGSSDSTVLERLRAAfEKKKEAGAEEPPSMRTcEQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQ 1161
Cdd:cd14912 441 ECMFPKATDTSFKNKLYEQ-HLGKSANFQKPKVVKG-KAEAHFSLIHYAG--VVDYNITGWLDKNKDPLNE-TVVGLYQK 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1162 SKREELQSLFQAraklppvcRAVAGLEGTSQQALHRSRVVRRAFaSSLAAVKRKapcaqiklQMDALISLLRRSRLHFIH 1241
Cdd:cd14912 516 SAMKTLAYLFSG--------AQTAEGASAGGGAKKGGKKKGSSF-QTVSALFRE--------NLNKLMTNLRSTHPHFVR 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1242 CLVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALL 1321
Cdd:cd14912 579 CIIPNETKT---------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 637
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 291327510 1322 KKldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14912 638 PE----GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
625-1361 |
1.30e-46 |
|
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: 180.68 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTT---VPSSGKVPRGRQ-DGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiyTEAIVEMYRGKKrHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSV-------EKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTA 773
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPgvpgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 774 AQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQKaatAFSQLRGAMELL 853
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERE---LFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 854 GISEGEQQAIWRVLAAIYHLGAAgACKVGRKQFMRFEWANHAAEALgCDYEELNTATFKHHLRQiieqmtsgPQRQGLQD 933
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNI-VLKRERNTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLT--------PRIKVGRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 934 NEACSGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIM-VVDTPGFQnprhqgKDRAATFEELCYNYAQ 1012
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFE------IFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1013 ERLQLLFYHRTFVSTLERYKEEGIPVPF-----DLpesSPGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQG 1087
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPWTFldfglDL---QPCIDLIERPANPP--------------GLLALLDEECWFPK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1088 SSDSTVLERLraAFEKKKEAGAEEPPSMRtceQPLQCELFHQLGRdpVRYDLTGWLRRAKPNLAALEAPQILQQSKReel 1167
Cdd:cd14930 445 ATDKSFVEKV--AQEQGGHPKFQRPRHLR---DQADFSVLHYAGK--VDYKANEWLMKNMDPLNDNVAALLHQSTDR--- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1168 qslfqARAKLPPVCRAVAGLEGTSQ--QALHRSRvVRRAFASSLAAVKRKApcaqiklqMDALISLLRRSRLHFIHCLVP 1245
Cdd:cd14930 515 -----LTAEIWKDVEGIVGLEQVSSlgDGPPGGR-PRRGMFRTVGQLYKES--------LSRLMATLSNTNPSFVRCIVP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1246 TTvESKAGQRTPSpsqpsgdqgvanepTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKld 1325
Cdd:cd14930 581 NH-EKRAGKLEPR--------------LVLD------QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK-- 637
|
730 740 750
....*....|....*....|....*....|....*.
gi 291327510 1326 ltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14930 638 ---GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
625-1361 |
3.31e-46 |
|
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: 179.49 E-value: 3.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVP---RGRQ-DGLPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVemyKGKKrHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGS------------VDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNAT 768
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 769 GRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPedKQKAATAFSQLRG 848
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIP--GQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 849 AMELLGISEGEQQAIWRVLAAIYHLGAagackvgrkqfMRFEWANHAAEALGCDyeelNTATFK--HHLRQIIEQMTSG- 925
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGN-----------MSFKKERHTDQASMPD----NTAAQKvcHLMGMNVTDFTRAi 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 926 --PQRQGLQDNEACSGLKMTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQnprhqgKDRAAT 1002
Cdd:cd15896 303 lsPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1003 FEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLPesspgttvavVDQNP--SQVHLPAgrgaeDAGGLFWVL 1079
Cdd:cd15896 377 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFiDFG----------LDLQPciDLIEKPA-----SPPGILALL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1080 DEEVRVQGSSDSTVLERLRAafEKKKEAGAEEPPSMRtcEQPLQCeLFHQLGRdpVRYDLTGWLRRakpNLAAL--EAPQ 1157
Cdd:cd15896 442 DEECWFPKATDKSFVEKVLQ--EQGTHPKFFKPKKLK--DEADFC-IIHYAGK--VDYKADEWLMK---NMDPLndNVAT 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1158 ILQQSKREELQSLFQaraklpPVCRAVAGLEGTSQQALHRSRVVRRAFASSLAAVKRKapcaqiklQMDALISLLRRSRL 1237
Cdd:cd15896 512 LLNQSTDKFVSELWK------DVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRNTNP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1238 HFIHCLVPTTvESKAGQRTPSpsqpsgdqgvanepTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLD 1317
Cdd:cd15896 578 NFVRCIIPNH-EKKAGKLDPH--------------LVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 291327510 1318 PALLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd15896 637 PNAIPK-----GFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
626-1361 |
3.88e-46 |
|
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: 178.35 E-value: 3.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPqTTTVPSSGKVPRGR------QDGLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNP-CKPLPIFDKKHHEEysnlsvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDGRVsVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTV 779
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDL-LDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 780 LLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNL-----HQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLG 854
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLedpdcHRILRDDNRNRPVFNDSEELEYYRQMFHDLTNIMKLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 855 ISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMRFEWANH---AAEALGCDYEELNTATFKHHLRQIIEQMTSgpqRQGL 931
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPlhaVAKLLGIDEVELTEALISNVNTIRGERIQS---WKSL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 932 QDNEacsglkmtgvECVEGMASGLYQELFVAVVSLINRSFSSHHL-----SMASIMVVDTPGFQNPRHQGkdraatFEEL 1006
Cdd:cd14897 317 RQAN----------DSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINS------FDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1007 CYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPfDLPESSPGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQ 1086
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDNDDVLELFFKKPL--------------GILPLLDEESTFP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1087 GSSDSTVLERLRAAFEKKKEagAEEPPSMRTCeqplqCELFHQLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQQSKREE 1166
Cdd:cd14897 446 QSTDSSLVQKLNKYCGESPR--YVASPGNRVA-----FGIRHYAEQ--VTYDADGFLEKNRDNLSS-DIVGCLLNSNNEF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1167 LQSLFQaraklppvcravaglegtsqqalhrsrvvrRAFASSLaavkrkapcaqiklqmDALISLLRRSRLHFIHCLVPT 1246
Cdd:cd14897 516 ISDLFT------------------------------SYFKRSL----------------SDLMTKLNSADPLFVRCIKPN 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1247 TveskagqrtpspsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLdl 1326
Cdd:cd14897 550 N---------------------FLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVR-- 606
|
730 740 750
....*....|....*....|....*....|....*
gi 291327510 1327 tseELDERKVVeELLKTLDLekKAVAVGHSQVFLK 1361
Cdd:cd14897 607 ---SDDLGKCQ-KILKTAGI--KGYQFGKTKVFLK 635
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
625-1361 |
8.17e-46 |
|
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: 177.83 E-value: 8.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVP--RGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPyQILPIYTAEQIRlyRNKKIGeLPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLvgmaGSVDGRVS-VEK--LRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQ 777
Cdd:cd01381 81 ESGAGKTESTKLILQYL----AAISGQHSwIEQqiLEAN-PILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 778 TVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISE 857
Cdd:cd01381 156 QYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 858 GEQQAIWRVLAAIYHLGAAG----------ACKVGRKQFmrfewANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGPQ 927
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKfeatvvdnldASEVRDPPN-----LERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 928 RQGlqdneacsglkmtGVECVEGMASGLYQELFVAVVSLINRSF---SSHHLSMASIMVVDTPGFQNPRHQgkdraaTFE 1004
Cdd:cd01381 310 AEQ-------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN------SFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1005 ELCYNYAQERLQLLFYHRTFVSTLERYKEEGIpvpfdlpesspgttvavvdqNPSQVHLPAGRGAEDAGG-----LFWVL 1079
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGI--------------------NWQHIEFVDNQDVLDLIAlkpmnIMSLI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1080 DEEVRVQGSSDSTVLERLRAAFEKKkeagaeeppsmRTCEQPlQCELFHQLG----RDPVRYDLTGWLRRAKPNLAAlEA 1155
Cdd:cd01381 431 DEESKFPKGTDQTMLEKLHSTHGNN-----------KNYLKP-KSDLNTSFGinhfAGVVFYDTRGFLEKNRDTFSA-DL 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1156 PQILQQSKREELQSLFQAraklppvCRAvaglegtsqqalhrsrvvrrafASSLAAVKRKAPCAQIKLQMDALISLLRRS 1235
Cdd:cd01381 498 LQLVQSSKNKFLKQLFNE-------DIS----------------------MGSETRKKSPTLSSQFRKSLDQLMKTLSAC 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1236 RLHFIHCLVPTtvESKagqrtpspsqpsgdqgvanEPTALDiPALRV-QLAGSHILEALRLHRAGYAEHMGLAQFRRRFQ 1314
Cdd:cd01381 549 QPFFVRCIKPN--EYK-------------------KPMLFD-RELCVrQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 291327510 1315 VLDPAlLKKLDLTSEELDERKVVEELLKTLDLEKkavaVGHSQVFLK 1361
Cdd:cd01381 607 VLVPG-IPPAHKTDCRAATRKICCAVLGGDADYQ----LGKTKIFLK 648
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
626-1325 |
1.04e-45 |
|
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: 177.44 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQT------TTVPSSGKVPRGRqDGLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKwidnlyGDHLHEQYLKKPR-DKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDGRvSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTV 779
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDK-TIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 780 LLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEGE 859
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 860 QQAIWRVLAAIYHLGAAgackvgrkQFMRFE---WANHAAEALGCDYEELNTATFKhhlrqiIEQMTSgpQRQGLQDNEA 936
Cdd:cd14904 240 QRTLFKILSGVLHLGEV--------MFDKSDengSRISNGSQLSQVAKMLGLPTTR------IEEALC--NRSVVTRNES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 937 CSgLKMTGVECVE---GMASGLYQELFVAVVSLINRSFSS-HHLSMASIMVVDTPGFQNPRHQGkdraatFEELCYNYAQ 1012
Cdd:cd14904 304 VT-VPLAPVEAEEnrdALAKAIYSKLFDWMVVKINAAISTdDDRIKGQIGVLDIFGFEDFAHNG------FEQFCINYAN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1013 ERLQLLFYHRTFVSTLERYKEEGIpvPFDLPEsspgttvavVDQNPSQVHLPAGRgaedaGGLFWVLDEEVRVQGSSDST 1092
Cdd:cd14904 377 EKLQQKFTTDVFKTVEEEYIREGL--QWDHIE---------YQDNQGIVEVIDGK-----MGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1093 VLERLRA-AFEKKKEAGAEEPPSMRTceqplQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQSLF 1171
Cdd:cd14904 441 LVNKIRTnHQTKKDNESIDFPKVKRT-----QFIINHYAG--PVTYETVGFMEKHRDTLQN-DLLDLVLLSSLDLLTELF 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1172 QAraklppvcravagLEGTSQQALHRSRVVRRAfASSLAavkrkapcAQIKLQMDALISLLRRSRLHFIHCLVPTTVESk 1251
Cdd:cd14904 513 GS-------------SEAPSETKEGKSGKGTKA-PKSLG--------SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKS- 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1252 agqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLD 1325
Cdd:cd14904 570 --------------------PTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKD 623
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
626-1361 |
3.03e-45 |
|
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: 177.07 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPqTTTVPSSGKVPRGRQD-----GLPAHVTSLAQRAYWALLSQ-------RRD 693
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNP-FKHIPGLYDLHKYREEmpgwtALPPHVFSIAEGAYRSLRRRlhepgasKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 694 QSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATFT--------VLRAFGCVSTGHSRRATRFAMVMSLDF 765
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGKFVRMFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 766 -----NATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAF---GMGLWSKpEDKQ 837
Cdd:cd14895 161 eghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQyisGGQCYQR-NDGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 838 KAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG------------------AAGACKVGR---KQFMRFEWANHAA 896
Cdd:cd14895 240 RDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngaASAPCRLASaspSSLTVQQHLDIVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 897 EALGCDYEELNTATFKhhlRQIieqmTSGPQRQGLQDNEACSGlkmtgvECVEGMASGLYQELFVAVVSLIN-----RSF 971
Cdd:cd14895 320 KLFAVDQDELVSALTT---RKI----SVGGETFHANLSLAQCG------DARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 972 SSHHLSMAS------IMVVDTPGFQnprhqgKDRAATFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIP-VPFDLPE 1044
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFE------EFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwNAVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1045 SSpgTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAGAEeppsmRTCEQPLQC 1124
Cdd:cd14895 461 NS--VCLEMLEQRPS--------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSAS-----RTDQADVAF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1125 ELFHQLGRdpVRYDLTGWLR--RAKPNlaaleapqilqqskrEELQSLF--QARAKLPPVCRAVAGLEgTSQQALHRSRV 1200
Cdd:cd14895 520 QIHHYAGA--VRYQAEGFCEknKDQPN---------------AELFSVLgkTSDAHLRELFEFFKASE-SAELSLGQPKL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1201 VRRafASSLAAVkrkAPCAQIKLQMDALISLLRRSRLHFIHCLVPTTvESKAGQrtpspsqpsgdqgvaneptaLDIPAL 1280
Cdd:cd14895 582 RRR--SSVLSSV---GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND-ESASDQ--------------------FDMAKV 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1281 RVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPAlLKKLDLTSEELderkvvEELLKTLDLEKkavavGHSQVFL 1360
Cdd:cd14895 636 SSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-KNASDATASAL------IETLKVDHAEL-----GKTRVFL 703
|
.
gi 291327510 1361 K 1361
Cdd:cd14895 704 R 704
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
626-1323 |
1.54e-44 |
|
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: 175.08 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPqTTTVP---SSGKV-----------PRGRQDGLPAHVTSLAQRAYWALL-SQ 690
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNP-LKPLPdlySESQLnaykasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 691 RRDQSIVALGRSGAGKTTCCEQVLEHL--VG-----MAGSVDGRVSVEK-LRATFTVLRAFGCVSTGHSRRATRFAMVMS 762
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLtsVGrdqssTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 763 LDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAES---SAFGMGLWSKPEDKQKA 839
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellNSYGPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 840 ATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFM-------RFEWANhAAEALGCDYEELNTATFK 912
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAtavtaasRFHLAK-CAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 913 HHLRQIIEQMTSgpQRQGLQDNEACSGLkmtgvecvegmASGLYQELFVAVVSLIN---------RSFSSHHLSMASIMV 983
Cdd:cd14902 320 REIKAGVEVMVL--KLTPEQAKEICGSL-----------AKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 984 VDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIP-VPFDLPESSPgtTVAVVDQNPSqvh 1062
Cdd:cd14902 387 LDIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwKNISYPSNAA--CLALFDDKSN--- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1063 lpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKeagaeeppsmrtceqplQCELFHQLGRdpVRYDLTGW 1142
Cdd:cd14902 456 -----------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG-----------------QFVVHHFAGR--VCYNVEQF 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1143 LRRAKPNLAAlEAPQILQQSKREELQSLFqARAKlppvcraVAGLEGTSQQALHRSRVVRRAFASSlaavkrkapcAQIK 1222
Cdd:cd14902 506 VEKNTDALPA-DASDILSSSSNEVVVAIG-ADEN-------RDSPGADNGAAGRRRYSMLRAPSVS----------AQFK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1223 LQMDALISLLRRSRLHFIHCLVPTTVEskagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAE 1302
Cdd:cd14902 567 SQLDRLIVQIGRTEAHYVRCLKPNEVK---------------------KPGIFDRERMVEQMRSVGVLEAVRIARHGYSV 625
|
730 740
....*....|....*....|.
gi 291327510 1303 HMGLAQFRRRFQVLDPALLKK 1323
Cdd:cd14902 626 RLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
631-1361 |
5.27e-44 |
|
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: 172.08 E-value: 5.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 631 LLQRYRAQLPYTCSGPDLITLQPQTTTV---PSSGKVPRGR-QDGLPAHVTSLAQRAYWALLSQRRDQSIVALGRSGAGK 706
Cdd:cd01379 7 LQKRYSRDQIYTYIGDILIAVNPFQNLGiytEEHSRLYRGAkRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 707 TTCCEQVLEHLVGMaGSVDGRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVLLENSRV 786
Cdd:cd01379 87 TESANLLVQQLTVL-GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 787 ARQPQGEGNFEVFSQLLAGMDVDLRTE---LNLHQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEGEQQAI 863
Cdd:cd01379 166 VHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKEEVDSV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 864 WRVLAAIYHLG-------AAGACKVGRKQFMRFEWANHAAEALGCDYEELNTATFKHHLrqiieqMTSGpqRQGLQDN-- 934
Cdd:cd01379 246 YSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSV------VTRG--ETIIRNNtv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 935 -EACsglkmtgvECVEGMASGLYQELFVAVVSLINR--SFSSHHLSMA-SIMVVDTPGFQNPRHQgkdraaTFEELCYNY 1010
Cdd:cd01379 318 eEAT--------DARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPlSIGILDIFGFENFQKN------SFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1011 AQERLQLLFYHRTFVSTLERYKEEGIPVpfdlpesspgTTVAVVDQNPS-----QVHLpagrgaedagGLFWVLDEEVRV 1085
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDV----------DLIEYEDNRPLldmflQKPM----------GLLALLDEESRF 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1086 QGSSDSTVLERLRAAFEKKKeagAEEPPSMRtceqpLQCELFHQLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQQSKre 1165
Cdd:cd01379 444 PKATDQTLVEKFHNNIKSKY---YWRPKSNA-----LSFGIHHYAGK--VLYDASGFLEKNRDTLPP-DVVQLLRSSE-- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1166 elqslfqaraklppvcravaglegtsqqalhrSRVVRRAFAS----SLaavkrkapcaqiklqMDaLISLLRRSRLHFIH 1241
Cdd:cd01379 511 --------------------------------NPLVRQTVATyfrySL---------------MD-LLSKMVVGQPHFVR 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1242 CLVPTtveskagqrtpspsqpsgDQgvaNEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALL 1321
Cdd:cd01379 543 CIKPN------------------DS---RQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 291327510 1322 KKLDLTSEElderkvVEELLKTLDLEKkaVAVGHSQVFLK 1361
Cdd:cd01379 602 EEVVANREN------CRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
626-1361 |
7.43e-44 |
|
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: 172.56 E-value: 7.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP---QTTTVPSSGKVPRGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALGR 701
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPfkfLPIYNPKYVKMYQNRRLGkLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 702 SGAGKTTCCEQVLEHLVgmAGSVDGRVS-VEK--LRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQT 778
Cdd:cd01385 82 SGSGKTESTNFLLHHLT--ALSQKGYGSgVEQtiLGAG-PVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 779 VLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQmAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEG 858
Cdd:cd01385 159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 859 EQQAIWRVLAAIYHLgaagackvGRKQFMRfeWANHAAEALGCDYEE-LNT-ATFKHHLRQIIEQMTSGPQRQGLQDNEA 936
Cdd:cd01385 238 TQRQIFSVLSAVLHL--------GNIEYKK--KAYHRDESVTVGNPEvLDIiSELLRVKEETLLEALTTKKTVTVGETLI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 937 CSGLKMTGVECVEGMASGLYQELFVAVV-----SLINRSFSSHHlSMASIMVVDTPGFQNPRHQgkdraaTFEELCYNYA 1011
Cdd:cd01385 308 LPYKLPEAIATRDAMAKCLYSALFDWIVlrinhALLNKKDLEEA-KGLSIGVLDIFGFEDFGNN------SFEQFCINYA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1012 QERLQLLFYHRTFVSTLERYKEEGIpvpfdlpessPGTTVAVVDqNPSQVHLPAGRgaedAGGLFWVLDEEVRVQGSSDS 1091
Cdd:cd01385 381 NEHLQYYFNQHIFKLEQEEYKKEGI----------SWHNIEYTD-NTGCLQLISKK----PTGLLCLLDEESNFPGATNQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1092 TVLERLRAAFEKKKEagAEEPPSMRTC--------EQPLQCELFHQLGRDPVRYDLTGWLRRAKP----NLAALEAPQIL 1159
Cdd:cd01385 446 TLLAKFKQQHKDNKY--YEKPQVMEPAfiiahyagKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvrELIGIDPVAVF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1160 qqsKREELQSLFQARAKLPPVCRAVAGLEGTSQQALHR----SRVVRRAfasslaavKRKAPC--AQIKLQMDALISLLR 1233
Cdd:cd01385 524 ---RWAVLRAFFRAMAAFREAGRRRAQRTAGHSLTLHDrttkSLLHLHK--------KKKPPSvsAQFQTSLSKLMETLG 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1234 RSRLHFIHClvpttVESKAGQRtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRF 1313
Cdd:cd01385 593 QAEPFFIRC-----IKSNAEKK----------------PLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQF 651
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 291327510 1314 QVLDPALLKKldltseELDERKVVEELLKtLDLEKkaVAVGHSQVFLK 1361
Cdd:cd01385 652 QVLLPKGLIS------SKEDIKDFLEKLN-LDRDN--YQIGKTKVFLK 690
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
638-1103 |
9.14e-44 |
|
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: 171.38 E-value: 9.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 638 QLPYTCSGPDLITLQPQTTTV-PSSGKVPRGRQDGLPAHVTSLAQRAYWALLSQR---RDQSIVALGRSGAGKTTCCEQV 713
Cdd:cd14891 16 QRPYTFMANVLIAVNPLRRLPePDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 714 LEHLV--GMAGSVDGRVSVE---------------KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATG-RVTAAQ 775
Cdd:cd14891 96 LRFLTtrAVGGKKASGQDIEqsskkrklsvtsldeRLMDTNPILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 776 LQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhqmaessafgmglwSKPEDKQKA-------------ATA 842
Cdd:cd14891 176 IETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL--------------LSPEDFIYLnqsgcvsddniddAAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 843 FSQLRGAMELLGISEGEQQAIWRVLAAIYHLG---------AAGACKVGRKQFMrfEWANHAAEALGCDYEELntatfkh 913
Cdd:cd14891 242 FDNVVSALDTVGIDEDLQLQIWRILAGLLHLGniefdeedtSEGEAEIASESDK--EALATAAELLGVDEEAL------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 914 hLRQIIEQ--MTSGpQRQGLQDNEAcsglkmTGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQN 991
Cdd:cd14891 313 -EKVITQReiVTRG-ETFTIKRNAR------EAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 992 prhqgKDRAATFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPfdlpesspgttVAVVDQNPSQVHLPAGRgaed 1071
Cdd:cd14891 385 -----FETKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVG-----------VITWPDNRECLDLIASK---- 444
|
490 500 510
....*....|....*....|....*....|..
gi 291327510 1072 AGGLFWVLDEEVRVQGSSDSTVLERLRAAFEK 1103
Cdd:cd14891 445 PNGILPLLDNEARNPNPSDAKLNETLHKTHKR 476
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
626-1361 |
1.15e-43 |
|
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: 171.13 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP--QTTTVPSSGKVPR--GRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyqPIAGLYEPATMEQysRRHLGeLPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------LRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTA 773
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKtscveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 774 AQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTEL------NLHQMAESsafgmGLWSKP--EDKQkaatAFSQ 845
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFylstpeNYHYLNQS-----GCVEDKtiSDQE----SFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 846 LRGAMELLGISEGEQQAIWRVLAAIYHLG-----AAGACKVGRKQFMrfewaNHAAEALGCDYEELNTATFKhhlRQIIe 920
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGniefiTAGGAQVSFKTAL-----GRSAELLGLDPTQLTDALTQ---RSMF- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 921 qmtsgpqrqgLQDNEACSGLKMT-GVECVEGMASGLYQELFVAVVSLINRSFSSHHlSMASIMVVDTPGFQNPRHQgkdr 999
Cdd:cd14873 304 ----------LRGEEILTPLNVQqAVDSRDSLAMALYARCFEWVIKKINSRIKGKE-DFKSIGILDIFGFENFEVN---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1000 aaTFEELCYNYAQERLQLLFYHRTFvsTLER--YKEEGIpVPFDLPESSPGTTVAVVdqnpsqvhlpagrgaEDAGGLFW 1077
Cdd:cd14873 369 --HFEQFNINYANEKLQEYFNKHIF--SLEQleYSREGL-VWEDIDWIDNGECLDLI---------------EKKLGLLA 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1078 VLDEEVRVQGSSDSTVLERLRAAFekkkeagAEEPPSMRTCEQPLQCELFHQLGRdpVRYDLTGWLRRAKPNLAAlEAPQ 1157
Cdd:cd14873 429 LINEESHFPQATDSTLLEKLHSQH-------ANNHFYVKPRVAVNNFGVKHYAGE--VQYDVRGILEKNRDTFRD-DLLN 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1158 ILQQSKREELQSLFQaraklppvcravaglegtsqqalhrsRVVRRAFASSLA-AVKRKAPC--AQIKLQMDALISLLRR 1234
Cdd:cd14873 499 LLRESRFDFIYDLFE--------------------------HVSSRNNQDTLKcGSKHRRPTvsSQFKDSLHSLMATLSS 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1235 SRLHFIHCLVPTTveskagQRTPSPSQPSgdqGVANeptaldipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQ 1314
Cdd:cd14873 553 SNPFFVRCIKPNM------QKMPDQFDQA---VVLN------------QLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 291327510 1315 VLDPALLKKLDLtseeldeRKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14873 612 VLMRNLALPEDV-------RGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
626-1323 |
4.05e-43 |
|
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: 169.87 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTT-------------TVPSSGKVPrgrqdglpaHVTSLAQRAYWALLSQRR 692
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTipglysdemllkfIQPSISKSP---------HVFSTASSAYQGMCNNKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 693 DQSIVALGRSGAGKTTCCEQVLEHLVgMAGSVD--GRVSVE-KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNAT- 768
Cdd:cd14888 73 SQTILISGESGAGKTESTKYVMKFLA-CAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 769 --------GRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLA----GMDVDLRTELN---LHQMAESSAFGMGL-WSK 832
Cdd:cd14888 152 skrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareAKNTGLSYEENdekLAKGADAKPISIDMsSFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 833 PEDKQKAATA--------------FSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-----AAGACKVGRK-QFMRFEWA 892
Cdd:cd14888 232 PHLKFRYLTKsschelpdvddleeFESTLYAMQTVGISPEEQNQIFSIVAAILYLGnilfeNNEACSEGAVvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 893 NHAAEALGCDYEEL-NTATFkhhlRQIIEQmtSGPQRQGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSF 971
Cdd:cd14888 312 EKVASLLGVDAEDLlNALCY----RTIKTA--HEFYTKPLRVDEA--------EDVRDALARALYSCLFDKVVERTNESI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 972 S-SHHLSMASIMVVDTPGFQ----NprhqgkdraaTFEELCYNYAQERLQLLFyhRTFVSTLER--YKEEGIP-VPFDLP 1043
Cdd:cd14888 378 GySKDNSLLFCGVLDIFGFEcfqlN----------SFEQLCINFTNERLQQFF--NNFVFKCEEklYIEEGISwNPLDFP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1044 ESspGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLraafeKKKEAGAEEPPSMRTceQPLQ 1123
Cdd:cd14888 446 DN--QDCVDLLQEKPL--------------GIFCMLDEECFVPGGKDQGLCNKL-----CQKHKGHKRFDVVKT--DPNS 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1124 CELFHQLGrdPVRYDLTGWLRRAKPNLaALEAPQILQQSKREELQSLFQAraklppvcravaglegtsqqalhrsrVVRR 1203
Cdd:cd14888 503 FVIVHFAG--PVKYCSDGFLEKNKDQL-SVDAQEVIKNSKNPFISNLFSA--------------------------YLRR 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1204 AFASSLAAVKRKAPCAQIKLQMDALISLLRRSRLHFIHCLVPTtveskagqrtpspSQpsgdqgvaNEPTALDIPALRVQ 1283
Cdd:cd14888 554 GTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPN-------------SQ--------NVPDLFDRISVNEQ 612
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 291327510 1284 LAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKK 1323
Cdd:cd14888 613 LKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGEGKK 652
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
626-1360 |
1.92e-42 |
|
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: 167.66 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP-----------QTTTVPSSGKVPRGRQDgLPAHVTSLAQRAYWALLSQRR-- 692
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPfrrlplyddetKEAYYEHGERRAAGERK-LPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 693 --DQSIVALGRSGAGKTTCCEQVLEHLVGMA------GSVDGRVSV-EKLRATFTVLRAFGCVSTGHSRRATRFAMVMSL 763
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 764 DFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQKAATAF 843
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 844 SQLRGAMELLGISEGEQQAIWRVLAAIYHLGAAGACKVGRKQfMRFEWANHAAEALGCDYEELNTATFKHHL--RQII-- 919
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLctREIRag 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 920 -EQMT-SGPQRQGLQDNEAcsglkmtgvecvegMASGLYQELFVAVVSLINRS--FSSHHLSMASIMVVDTPGF----QN 991
Cdd:cd14901 320 gEYITmPLSVEQALLTRDV--------------VAKTLYAQLFDWLVDRINESiaYSESTGASRFIGIVDIFGFeifaTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 992 prhqgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLPESSpgTTVAVVDQNPSqvhlpagrgae 1070
Cdd:cd14901 386 ----------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFvEYPNND--ACVAMFEARPT----------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1071 dagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKkeagaeEPPSMRTCEQPLQC-ELFHQLGRdpVRYDLTGWLRRAKPN 1149
Cdd:cd14901 443 ---GLFSLLDEQCLLPRGNDEKLANKYYDLLAKH------ASFSVSKLQQGKRQfVIHHYAGA--VCYATDGFCDKNKDH 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1150 LAAlEAPQILQQSKreelqslfqaraklppvcravaglegtsqqalhrsrvvrRAFASSLAAvkrkapcAQIKLQMDALI 1229
Cdd:cd14901 512 VHS-EALALLRTSS---------------------------------------NAFLSSTVV-------AKFKVQLSSLL 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1230 SLLRRSRLHFIHCLVPTTVESkagqrtpspsqpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQF 1309
Cdd:cd14901 545 EVLNATEPHFIRCIKPNDVLS---------------------PSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 291327510 1310 RRRFQVLDPALLKKLDLTsEELDERKVVEELLKTLDLEKKAVA-VGHSQVFL 1360
Cdd:cd14901 604 VHTYSCLAPDGASDTWKV-NELAERLMSQLQHSELNIEHLPPFqVGKTKVFL 654
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
626-1105 |
2.92e-42 |
|
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: 166.56 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRY-RAQLPYTCSGPDLITLQPqTTTVPSSG----KVPRGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINP-YEDLPIYGediiQAYSGQNMGeLDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQT 778
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 779 VLLENSRVARQPQGEGNFEVFSQLLAGmdVDLRTELNLHQMAESSAFGMGLWSKPE-----DKQKaataFSQLRGAMELL 853
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAA--ASLPELKELHLGSAEDFFYTNQGGSPVidgvdDAAE----FEETRKALTLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 854 GISEGEQQAIWRVLAAIYHLGAAGACKVGRKQFMRFEWANH---AAEALGCDYEELNTATFKhhlRQII---EQMTSgpq 927
Cdd:cd01380 235 GISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHlqiACELLGIDESQLAKWLCK---RKIVtrsEVIVK--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 928 rqGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLS--MASIMVVDTPGFQ----Nprhqgkdraa 1001
Cdd:cd01380 309 --PLTLQQA--------IVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFEtfevN---------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1002 TFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF----------DLPESSPGttvaVVDqnpsqvhlpagrgaed 1071
Cdd:cd01380 369 SFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFidfydnqpciDLIEGKLG----ILD---------------- 428
|
490 500 510
....*....|....*....|....*....|....
gi 291327510 1072 agglfwVLDEEVRVQGSSDSTVLERLRAAFEKKK 1105
Cdd:cd01380 429 ------LLDEECRLPKGSDENWAQKLYNQHLKKP 456
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
625-1361 |
1.25e-41 |
|
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: 164.93 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTV---PSSGKVPRGRQDG-LPAHVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDiygLEQVQQYSGRALGeLPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATfTVLRAFGCVSTGHSRRATRFAMVMSLDFNAtGRVTAAQLQTVL 780
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEAT-PLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 781 LENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhQMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEGEQ 860
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-QEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 861 QAIWRVLAAIYHLGAAgackvgrkQFMRFEwANHAAEA--LGCDYEELNTAtfkhHLRQIieqMTSGPQRQGLQDNEACS 938
Cdd:cd01387 238 DSIFRILASVLHLGNV--------YFHKRQ-LRHGQEGvsVGSDAEIQWVA----HLLQI---SPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 939 GLKM-------TGVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEELCYNYA 1011
Cdd:cd01387 302 RERIftpltidQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN------SFEQLCINYA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1012 QERLQLLFYHRTFVSTLERYKEEGIpvpfdlpessPGTTVAVVDQNPSqVHLPAGRGAedagGLFWVLDEEVRVQGSSDS 1091
Cdd:cd01387 376 NENLQYYFNKHVFKLEQEEYIREQI----------DWTEIAFADNQPV-INLISKKPV----GILHILDDECNFPQATDH 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1092 TVLER------LRAAFEKkkeagaeepPSMRTCEQPLQcelfHQLGRdpVRYDLTGWLRRAKPNLaaleapqilqqskRE 1165
Cdd:cd01387 441 SFLEKchyhhaLNELYSK---------PRMPLPEFTIK----HYAGQ--VWYQVHGFLDKNRDQL-------------RQ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1166 ELQSLFqARAKLPPVCRAVAGLEGTSQQALHR---SRVVRRafasslaavKRKAPCAQIKLQmDALISLLRR-SRLH--F 1239
Cdd:cd01387 493 DVLELL-VSSRTRVVAHLFSSHRAQTDKAPPRlgkGRFVTM---------KPRTPTVAARFQ-DSLLQLLEKmERCNpwF 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1240 IHCLVPTTveskagqrtpspsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLdpa 1319
Cdd:cd01387 562 VRCLKPNH---------------------KKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL--- 617
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 291327510 1320 LLKKLDLTSEELDERKVVEELLKTldLEKKAVAVGHSQVFLK 1361
Cdd:cd01387 618 VALKLPRPAPGDMCVSLLSRLCTV--TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
625-1361 |
4.28e-41 |
|
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: 163.41 E-value: 4.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKV-----PRGRQDGLPaHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVlasyhPRKALNTTP-HIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNaTGRVTAAQLQTV 779
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQT-EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 780 LLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLhQMAESSAF----GMGLWSKPEDKQKaataFSQLRGAMELLGI 855
Cdd:cd14896 158 LLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYlnqgGACRLQGKEDAQD----FEGLLKALQGLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 856 SEGEQQAIWRVLAAIYHLGaaGACkvgrkqFMRFEWANHAAEALGCDYEELNTATFkhhLRQIIEQMTSGPQRQGLQD-- 933
Cdd:cd14896 233 CAEELTAIWAVLAAILQLG--NIC------FSSSERESQEVAAVSSWAEIHTAARL---LQVPPERLEGAVTHRVTETpy 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 934 NEACSGLKMTG-VECVEGMASGLYQELFVAVVSLINRSFS--SHHLSMASIMVVDTPGFQNPRHQGkdraatFEELCYNY 1010
Cdd:cd14896 302 GRVSRPLPVEGaIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNG------LEQLCINL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1011 AQERLQLLFYHRTFVSTLERYKEEGIP-VPFDLPESSpgttvAVVDQNPSQVHlpagrgaedagGLFWVLDEEVRVQGSS 1089
Cdd:cd14896 376 ASERLQLFSSQTLLAQEEEECQRELLPwVPIPQPPRE-----SCLDLLVDQPH-----------SLLSILDDQTWLSQAT 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1090 DSTVLErlraafekKKEAGAEEPPSMRTCEQPLQC-ELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQ 1168
Cdd:cd14896 440 DHTFLQ--------KCHYHHGDHPSYAKPQLPLPVfTVRHYAG--TVTYQVHKFLNRNRDQLDP-AVVEMLAQSQLQLVG 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1169 SLFQAraklppvcravaglegtsqqalhrsrvvrrafASSLAAVKRKAPCAQIKLQ--MDALISLLRRSRLHFIHCLvpt 1246
Cdd:cd14896 509 SLFQE--------------------------------AEPQYGLGQGKPTLASRFQqsLGDLTARLGRSHVYFIHCL--- 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1247 tveskagqrTPSPSQPSGdqgvaneptALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLdl 1326
Cdd:cd14896 554 ---------NPNPGKLPG---------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEAL-- 613
|
730 740 750
....*....|....*....|....*....|....*
gi 291327510 1327 tseeLDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14896 614 ----SDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
627-1361 |
2.29e-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: 158.15 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 627 VMNTLLQRYRAQLPYTCSGPDLITLQP----QTTTVPSSGKVPRGRQDGLPAHVTSLAQRAYWALL----SQRRDQSIVA 698
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPfkylHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 699 LGRSGAGKTTCCEQVLEHLVGMAgsvDGRVSVEK-LRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNaTGRVTAAQLQ 777
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQLEQqILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 778 TVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKpEDKQKAATAFSQLRGAMELLGISE 857
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCK-REVQYWKKKYDEVCNAMDMVGFTE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 858 GEQQAIWRVLAAIYHLGA-------AGACKVGRKQFmrfEWANHAAEALGCDYEEL-----NTATFkhhlrqiieqmTSG 925
Cdd:cd14889 238 QEEVDMFTILAGILSLGNitfemddDEALKVENDSN---GWLKAAAGQFGVSEEDLlktltCTVTF-----------TRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 926 PQRQGLQDneacsglKMTGVECVEGMASGLYQELFVAVVSLINRSFS---SHHLSMASIMVVDTPGFQnprHQGKDRaat 1002
Cdd:cd14889 304 EQIQRHHT-------KQQAEDARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFE---NFAVNR--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1003 FEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIpvpfdlpessPGTTVAVVDQNPSqVHLPAGRGAedagGLFWVLDEE 1082
Cdd:cd14889 371 FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGI----------DWKEITYKDNKPI-LDLFLNKPI----GILSLLDEQ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1083 VRVQGSSDSTVLERLRAAFEKKK--EAGAEEPPSMrtceqplqcELFHQLGRdpVRYDLTGWLRRAKPNLAAlEAPQILQ 1160
Cdd:cd14889 436 SHFPQATDESFVDKLNIHFKGNSyyGKSRSKSPKF---------TVNHYAGK--VTYNASGFLEKNRDTIPA-SIRTLFI 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1161 QSKREELQSLFQARAKLPPVCRAVAGLEGTSQQALHRSRvvrrafasslaavkRKAPCAQIKLQMDALISLLRRSRLHFI 1240
Cdd:cd14889 504 NSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTR--------------KQSVGAQFKHSLGVLMEKMFAASPHFV 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1241 HCLVPTTVEskagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVldpaL 1320
Cdd:cd14889 570 RCIKPNHVK---------------------VPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKI----L 624
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 291327510 1321 LKKLDLTSeeldERKVVEELLKTLDLekKAVAVGHSQVFLK 1361
Cdd:cd14889 625 LCEPALPG----TKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
591-1398 |
3.82e-39 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 159.43 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 591 DRTVIEVDEEQVHPANPS-ELDQAEDLASLVSVNESSVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVPRGR 668
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPfKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 669 Q----DGLPAHVTSLAQRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLV-GMAGSVDGRVSVEKLRATFtVLRAF 743
Cdd:PTZ00014 155 DakdsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAsSKSGNMDLKIQNAIMAANP-VLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 744 GCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESS 823
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 824 AFGMGLWSKPE--DKQKaataFSQLRGAMELLGISEGEQQAIWRVLAAIYHLGAA------------GACKVGRKQfmrf 889
Cdd:PTZ00014 314 YINPKCLDVPGidDVKD----FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVeiegkeeggltdAAAISDESL---- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 890 EWANHAAEALGCDYEEL-NTATFKHHL--RQIIEqmtsGPQRQglqdNEACSgLKMTgvecvegMASGLYQELFVAVVSL 966
Cdd:PTZ00014 386 EVFNEACELLFLDYESLkKELTVKVTYagNQKIE----GPWSK----DESEM-LKDS-------LSKAVYEKLFLWIIRN 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 967 INRSFSSHHLSMASIMVVDTPGFQ----NprhqgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPfDL 1042
Cdd:PTZ00014 450 LNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTE-EL 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1043 PESSpgttvavvdqNPSQVHLPAGRGAEdaggLFWVLDEEVRVQGSSDSTVLERLRAAFEK-KKEAGAEEPPSMRTCEQp 1121
Cdd:PTZ00014 519 EYTS----------NESVIDLLCGKGKS----VLSILEDQCLAPGGTDEKFVSSCNTNLKNnPKYKPAKVDSNKNFVIK- 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1122 lqcelfHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQSLFqaraklppvcravaglEGtsqQALHRSRVV 1201
Cdd:PTZ00014 584 ------HTIG--DIQYCASGFLFKNKDVLRP-ELVEVVKASPNPLVRDLF----------------EG---VEVEKGKLA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1202 RRAFASSlaavkrkapcaQIKLQMDALISLLRRSRLHFIHCLVPTtvESKagqrtpspsQPSGdqgvANEPTALdipalr 1281
Cdd:PTZ00014 636 KGQLIGS-----------QFLNQLDSLMSLINSTEPHFIRCIKPN--ENK---------KPLD----WNSSKVL------ 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1282 VQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKldltsEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:PTZ00014 684 IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSND-----SSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK 758
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 291327510 1362 AGVVSRL-ERQREKLVS-RNIV-LFQAACRGFLSRQEYKK 1398
Cdd:PTZ00014 759 KDAAKELtQIQREKLAAwEPLVsVLEALILKIKKKRKVRK 798
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
625-1251 |
3.88e-37 |
|
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: 151.34 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP----------QTTTVPSSGKVPRGR---QDGLPAHVTSLAQRAYWALLSQR 691
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPykqidnlfseEVMQMYKEQIIQNGEyfdIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 692 RDQSIVALGRSGAGKT---TCC--------------EQVLEHLVGMAGSVDGRVSVE-KLRATFTVLRAFGCVSTGHSRR 753
Cdd:cd14907 81 KKQAIVISGESGAGKTenaKYAmkfltqlsqqeqnsEEVLTLTSSIRATSKSTKSIEqKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 754 ATRFAMVMSLDFN-ATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDL---------RTELNLHQMAESS 823
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLlqqlglknqLSGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 824 AFGMglwskpeDKQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG----------AAGACKVGRKQFMRfewan 893
Cdd:cd14907 241 CYEV-------DTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfddstldDNSPCCVKNKETLQ----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 894 HAAEALGCDYEELNTA-TFKhhLRQIIEQMTSGPqrqgLQDNeacsglkmtgvECV---EGMASGLYQELFVAVVSLINR 969
Cdd:cd14907 309 IIAKLLGIDEEELKEAlTTK--IRKVGNQVITSP----LSKK-----------ECInnrDSLSKELYDRLFNWLVERLND 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 970 SFSSHHLS--------MASIMVVDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFD 1041
Cdd:cd14907 372 TIMPKDEKdqqlfqnkYLSIGLLDIFGFEVFQNNS------FEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1042 -LPESSPGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAgaeeppsmrTCEQ 1120
Cdd:cd14907 446 qLSYTDNQDVIDLLDKPPI--------------GIFNLLDDSCKLATGTDEKLLNKIKKQHKNNSKL---------IFPN 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1121 PLQCELF---HQLGrdPVRYDLTGWLRRAKPNLaALEAPQILQQSKREELQSLFQAraklppvcravaglEGTSQQALHR 1197
Cdd:cd14907 503 KINKDTFtirHTAK--EVEYNIEGFREKNKDEI-SQSIINCIQNSKNRIISSIFSG--------------EDGSQQQNQS 565
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1198 SRVVRRafasslaaVKRKAPCAQIKLQMDALISLLRRSRLHFIHCLVPTtvESK 1251
Cdd:cd14907 566 KQKKSQ--------KKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPN--EEK 609
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
671-1361 |
2.70e-34 |
|
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: 142.64 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 671 GLPAHVTSLAQRAYWALLSQ-RRDQSIVALGRSGAGKTTCCEQVLEHLVGMA---------GSVDGRVSvEKLRATFTVL 740
Cdd:cd14875 53 LLPPHIWQVAHKAFNAIFVQgLGNQSVVISGESGSGKTENAKMLIAYLGQLSymhssntsqRSIADKID-ENLKWSNPVM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 741 RAFGCVSTGHSRRATRFAMVMSLDFN-ATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTEL-NLHQ 818
Cdd:cd14875 132 ESFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 819 MAESSAFG-------MGLWSKPEDKqkaATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHL--------GAAGACKVGR 883
Cdd:cd14875 212 AQDYKCLNggntfvrRGVDGKTLDD---AHEFQNVRHALSMIGVELETQNSIFRVLASILHLmevefesdQNDKAQIADE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 884 KQFmrfewaNHAAEALGCDYEELNTATFKHHLRQIIEQMTSGPQRQGLQdNEACsglkmtgvecvegmaSGLYQELFVAV 963
Cdd:cd14875 289 TPF------LTACRLLQLDPAKLRECFLVKSKTSLVTILANKTEAEGFR-NAFC---------------KAIYVGLFDRL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 964 VSLINRSFSSHH--LSMASIMVVDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVP-F 1040
Cdd:cd14875 347 VEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNS------FEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPkI 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1041 DLPESSpgTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAGAeEPPSMrtceQ 1120
Cdd:cd14875 421 EFPDNS--ECVNMFDQKRT--------------GIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFV-LPKST----I 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1121 PLQCELFHQLGRdpVRYDLTGWLRRakpNLAAL--EAPQILQQSKREELQSLFQARAKLPpvcravaglegtsqqalHRS 1198
Cdd:cd14875 480 PNQFGVNHYAAF--VNYNTDEWLEK---NTDALkeDMYECVSNSTDEFIRTLLSTEKGLA-----------------RRK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1199 RVVRRAFASslaavkrkapcaqiklQMDALISLLRRSRLHFIHCLVPTTVESkagqrtpspsqpsgdqgvanePTALDIP 1278
Cdd:cd14875 538 QTVAIRFQR----------------QLTDLRTELESTETQFIRCIKPNMEAS---------------------PSFLDNL 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1279 ALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDP----ALLKKLDLTSEELDERKVVEELlktLDLEKKAVAVG 1354
Cdd:cd14875 581 LVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPrstaSLFKQEKYSEAAKDFLAYYQRL---YGWAKPNYAVG 657
|
....*..
gi 291327510 1355 HSQVFLK 1361
Cdd:cd14875 658 KTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
660-1330 |
1.59e-33 |
|
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: 139.95 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 660 SSGKvprgRQDGLPAHVTSLAQRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSvdGRVSVE-KLRATFT 738
Cdd:cd14878 47 SSGQ----LCSSLPPHLFSCAERAFHQLFQERRPQCFILSGERGSGKTEASKQIMKHLTCRASS--SRTTFDsRFKHVNC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 739 VLRAFGCVSTGHSRRATRFAMVMSLDF-NATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLH 817
Cdd:cd14878 121 ILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 818 QMAESSAFGMGLwskPEDKQKAATA-----FSQLRGAMELLGISEGEQQAIWRVLAAIYHLGAagackvgrkqfMRFEWA 892
Cdd:cd14878 201 NLCAHRYLNQTM---REDVSTAERSlnrekLAVLKQALNVVGFSSLEVENLFVILSAILHLGD-----------IRFTAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 893 NHAAEALGCDYeelntatfkhhlrQIIEQMTSGPQrqgLQDNEACSGLkMTGVECVEG------------------MASG 954
Cdd:cd14878 267 TEADSAFVSDL-------------QLLEQVAGMLQ---VSTDELASAL-TTDIQYFKGdmiirrhtiqiaefyrdlLAKS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 955 LYQELFVAVVSLINRSFSSHH----LSMASIMVVDTPGFQNPRHQgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLER 1030
Cdd:cd14878 330 LYSRLFSFLVNTVNCCLQSQDeqksMQTLDIGILDIFGFEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQEQTE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1031 YKEEGIPVPfdlPESSPGTTVAVVD---QNPSqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKK--- 1104
Cdd:cd14878 404 CVQEGVTME---TAYSPGNQTGVLDfffQKPS--------------GFLSLLDEESQMIWSVEPNLPKKLQSLLESSntn 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1105 ------KEAGAEEPPSmrtcEQPLQCELFHQLGRdpVRYDLTGWLRRAKPNLaaleaPQILqqskreelqsLFQARaklp 1178
Cdd:cd14878 467 avyspmKDGNGNVALK----DQGTAFTVMHYAGR--VMYEIVGAIEKNKDSL-----SQNL----------LFVMK---- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1179 pvcravaglegTSQQAlhrsrVVRRAFASSLAAVkrkapCAQIKLQMDALISLLRRSRLHFIHCLVPTTveskagqrtps 1258
Cdd:cd14878 522 -----------TSENV-----VINHLFQSKLVTI-----ASQLRKSLADIIGKLQKCTPHFIHCIKPNN----------- 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291327510 1259 psqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVL-DPALLKKLDLTSEE 1330
Cdd:cd14878 570 ----------SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTLLGEKKKQSAEE 632
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
626-1327 |
2.72e-33 |
|
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: 140.11 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVPRGRQD-----GLPAHVTSLAQRAYWALLSQRRDQSIVAL 699
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDinqnkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 700 GRSGAGKTTCCEQVLEHLVGMAGSV--------DGRVSVEK-LRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNAT-G 769
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnnNNNNSIEKdILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 770 RVTAAQLQTVLLENSRVARQPQGEG-NFEVFSQLLAGMDVDLRTELNLHQMAESSAF--------------GMGLWSKPE 834
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYldarddvissfksqSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 835 DKQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLGAagackvgrkqfMRFEW-ANHAAEALGCDyEELNTATFKH 913
Cdd:cd14906 242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGN-----------IEFEEdSDFSKYAYQKD-KVTASLESVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 914 HLRQIIEQMTSgpqrQGLQDNEacsgLKMTGVECV--------------EGMASGLYQELFVAVVSLINRSF----SSHH 975
Cdd:cd14906 310 KLLGYIESVFK----QALLNRN----LKAGGRGSVycrpmevaqseqtrDALSKSLYVRLFKYIVEKINRKFnqntQSND 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 976 LSMAS-------IMVVDTPGFQNPRHQgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIpvpfdlpessPG 1048
Cdd:cd14906 382 LAGGSnkknnlfIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI----------PW 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1049 TTVAVVDqNPSQVHLPAGRGAedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEagaeepPSMRTCEQpLQCELFH 1128
Cdd:cd14906 446 SNSNFID-NKECIELIEKKSD----GILSLLDDECIMPKGSEQSLLEKYNKQYHNTNQ------YYQRTLAK-GTLGIKH 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1129 QLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQSLFQARAKLPPvcravaglegTSQQALHRSRVVRRAFASs 1208
Cdd:cd14906 514 FAG--DVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT----------NTTKKQTQSNTVSGQFLE- 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1209 laavkrkapcaqiklQMDALISLLRRSRLHFIHCLVPTtveskagqrtpspsqpsgdqgVANEPTALDIPALRVQLAGSH 1288
Cdd:cd14906 580 ---------------QLNQLIQTINSTSVHYIRCIKPN---------------------QTMDCNNFNNVHVLSQLRNVG 623
|
730 740 750
....*....|....*....|....*....|....*....
gi 291327510 1289 ILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLDLT 1327
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNN 662
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
675-1361 |
2.86e-33 |
|
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: 140.17 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 675 HVTSLAQRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSV---EKLRATFTVLRAFGCVSTGHS 751
Cdd:cd14887 63 HPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQgleARLLQSGPVLEAFGNAHTVLN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 752 RRATRFAMVMSLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLagmdvdlrtelnlhQMAESSAfgmGLWS 831
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALC--------------NAAVAAA---TQKS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 832 KPEDKQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG----------------AAGACKVGRKQFMRFEwaNHA 895
Cdd:cd14887 206 SAGEGDPESTDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGnvefttdqepetskkrKLTSVSVGCEETAADR--SHS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 896 AEaLGCDYEELN-TATFKHHLRQIIEQMTSGPQRQGLQD----------NEACSGLKMTGVECVEGMAS-GLYQELFVAV 963
Cdd:cd14887 284 SE-VKCLSSGLKvTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvRETRSFFDLDGAAAARDAACkNLYSRAFDAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 964 VSLINRSFSSHHLSMAS--------------IMVVDTPGFQNPRHQGKDRaatFEELCYNYAQERLQLLFYHRTFVSTLE 1029
Cdd:cd14887 363 VARINAGLQRSAKPSESdsdedtpsttgtqtIGILDLFGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHM 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1030 RYKEEGIPV-------PFDLPESSPGTTvavvdqNPSQVHLPAGRGAEDAGGLFWVLDEEVrvqgsSDSTVLERLRAAFE 1102
Cdd:cd14887 440 LYTQEGVFQnqdcsafPFSFPLASTLTS------SPSSTSPFSPTPSFRSSSAFATSPSLP-----SSLSSLSSSLSSSP 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1103 KKKEAgaeeppsmRTCEQpLQCELFHQLGRDPVRYDL-TGWLRRAKPNLAALE-APQILQQSK----------REELQSL 1170
Cdd:cd14887 509 PVWEG--------RDNSD-LFYEKLNKNIINSAKYKNiTPALSRENLEFTVSHfACDVTYDARdfcranreatSDELERL 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1171 FQAraklppvCRAVAGLEGTSQQALhrsrvvRRAFASslaavKRKAPCAQIKLQMDALISLLRRSRLHFIHCLVPTTVEs 1250
Cdd:cd14887 580 FLA-------CSTYTRLVGSKKNSG------VRAISS-----RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1251 kagqrtpspsqpsgDQGVANEPTALDipalrvQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKkldltsEE 1330
Cdd:cd14887 641 --------------EAGIFEDAYVHR------QLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALR------EA 694
|
730 740 750
....*....|....*....|....*....|.
gi 291327510 1331 LDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14887 695 LTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
625-1318 |
6.44e-33 |
|
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: 138.44 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVPR-----GRQDGLPAHVTSLAQRAYWALLSQRR--DQSI 696
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMReyhaaPQPQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 697 VALGRSGAGKTTCCEQVLEHLVGMAGSV---DGRVSVEKLRATF----TVLRAFGCVSTGHSRRATRFAMVMSLDFNATG 769
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRIlnsnPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 770 RVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSafgmglWSKPEDKQKAATAFSQLRGA 849
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS------WLPNPERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 850 MELLGISEGEQQAIWRVLAAIYHLGaagackvgrkqfmRFEWANHAAEALGC---DYEELNTAT--------FKHHLRQI 918
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLG-------------NIQFADSEDEAQPCqpmDDTKESVRTsalllklpEDHLLETL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 919 -IEQMTSGPQRQGLQdnEACSGLKM-TGVECvegMASGLYQELFVAVVSLINRSFSSHHLSMAS-IMVVDTPGFQNPRHQ 995
Cdd:cd14880 302 qIRTIRAGKQQQVFK--KPCSRAECdTRRDC---LAKLIYARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESFPEN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 996 gkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF----------DLPESSPGTtvavvdqnpsqvhlpa 1065
Cdd:cd14880 377 ------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFinyqdnqtclDLIEGSPIS---------------- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1066 grgaedaggLFWVLDEEVRVQGSSDSTVLE-RLRAAFEKKKEAG----AEEPPSMrtceqplqceLFHQLGrdPVRYDLT 1140
Cdd:cd14880 435 ---------ICSLINEECRLNRPSSAAQLQtRIESALAGNPCLGhnklSREPSFI----------VVHYAG--PVRYHTA 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1141 GWLRRAKPNLAAlEAPQILQQSKREELQSLFQARAKlppvcravaglEGTSQQALHRSRvvrrafASSLAAVkrkapcAQ 1220
Cdd:cd14880 494 GLVEKNKDPVPP-ELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSR------APVLTVV------SK 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1221 IKLQMDALISLLRRSRLHFIHCLVPtTVESKAgqrtpspsQPSGDQGVANeptaldipalrvQLAGSHILEALRLHRAGY 1300
Cdd:cd14880 550 FKASLEQLLQVLHSTTPHYIRCIKP-NSQCQA--------QTFLQEEVLS------------QLEACGLVETIHISAAGF 608
|
730
....*....|....*...
gi 291327510 1301 AEHMGLAQFRRRFQVLDP 1318
Cdd:cd14880 609 PIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
626-1326 |
2.11e-31 |
|
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: 132.71 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVPRGRQDG-LPAHVTSLAQRAYWALLSQRrDQSIVALGRSGA 704
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYShVEPHVYDVAEASVQDLLVHG-NQTIVISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 705 GKTTCCEQVLEHLV-GMAGSVdgrvSVEK-LRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNatGRVTAAQLQTVLLE 782
Cdd:cd14898 81 GKTENAKLVIKYLVeRTASTT----SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 783 NSRVARQPQGEGNFEVFSQLLAGMDVDLRTELnlhqMAESSAFGmglwsKPEDKQKAATAFSQLRGAMELLGISegEQQA 862
Cdd:cd14898 155 KSRVTHHEKGERNFHIFYQFCASKRLNIKNDF----IDTSSTAG-----NKESIVQLSEKYKMTCSAMKSLGIA--NFKS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 863 IWRVLAAIYHLGAAGACKVGRKQFMRFEWANHAAEALGCDYEELNTATFKHHLR---QIIEQMTSGPQRQGLQDNeacsg 939
Cdd:cd14898 224 IEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQvkgETIEVFNTLKQARTIRNS----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 940 lkmtgvecvegMASGLYQELFVAVVSLINRSFSSHhlSMASIMVVDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLF 1019
Cdd:cd14898 299 -----------MARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNG------LDQLCINWTNEKIQNDF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1020 YHRTFVSTLERYKEEGIPVPfdlpesspgtTVAVVDQNPSQvhlpagRGAEDAGGLFWVLDEEVRVQGSSDSTVLERLRA 1099
Cdd:cd14898 360 IKKMFRAKQGMYKEEGIEWP----------DVEFFDNNQCI------RDFEKPCGLMDLISEESFNAWGNVKNLLVKIKK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1100 AFEKKKEAGAEEppsmrtceqplQCELFHQLGrdPVRYDLTGWL--RRAKPNLAALEAPQILQQSKREELQSLFqarakl 1177
Cdd:cd14898 424 YLNGFINTKARD-----------KIKVSHYAG--DVEYDLRDFLdkNREKGQLLIFKNLLINDEGSKEDLVKYF------ 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1178 ppvcravaglegtsqqalhrsrvvrrafasslaavkrkapcaqiKLQMDALISLLRRSRLHFIHCLVPTTveskagqrtp 1257
Cdd:cd14898 485 --------------------------------------------KDSMNKLLNSINETQAKYIKCIRPNE---------- 510
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 1258 spsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLDL 1326
Cdd:cd14898 511 -----------ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFEVVDY 568
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
626-1328 |
1.31e-30 |
|
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: 130.81 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP-----------QTTTVPSS--GKVPRGRQDG---LPAHVTSLAQRAYWA--- 686
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfqklpglyssdTMAKYLLSfeARSSSTRNKGsdpMPPHIYQVAGEAYKAmml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 687 -LLSQRRDQSIVALGRSGAGKTTCCEQVLEHLvGMAGSVDGRVSV----------EKLRATFTVLRAFGCVSTGHSRRAT 755
Cdd:cd14900 82 gLNGVMSDQSILVSGESGSGKTESTKFLMEYL-AQAGDNNLAASVsmgkstsgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 756 RFAMVMSLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGmdvdlrtelnlhqmaessafgmglwSKPEd 835
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG-------------------------ASEA- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 836 kQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-------AAGACKVGRKQFM--RFEWA-NHAAEALGCDYEE 905
Cdd:cd14900 215 -ARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGnltfehdENSDRLGQLKSDLapSSIWSrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 906 LNTATFKHHLRQIIEQMT---SGPQRQGLQDneacsglkmtgvecveGMASGLYQELFVAVVSLINRSF-----SSHHLS 977
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSmklSAAQANNARD----------------ALAKALYGRLFDWLVGKMNAFLkmddsSKSHGG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 978 MASIMVVDTPGFQN-PRHqgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFdlpesspgttVAVVDq 1056
Cdd:cd14900 358 LHFIGILDIFGFEVfPKN-------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKY----------VEFCD- 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1057 NPSQVHLPAGRGAedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAGAEEPPSMRTceqplqceLF---HQLGRd 1133
Cdd:cd14900 420 NQDCVNLISQRPT----GILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARG--------LFtivHYAGH- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1134 pVRYDLTGWLRRAKPNLaaleapqilqqskREELQSLFQAraklppvcravaglegtsqqalhrsrvvrrafasslaavk 1213
Cdd:cd14900 487 -VEYSTDGFLEKNKDVL-------------HQEAVDLFVY---------------------------------------- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1214 rkapCAQIKLQMDALISLLRRSRLHFIHCLVPTTvESKAGQRTpspsqpsgDQGVANeptaldipalrvQLAGSHILEAL 1293
Cdd:cd14900 513 ----GLQFKEQLTTLLETLQQTNPHYVRCLKPND-LCKAGIYE--------RERVLN------------QLRCNGVMEAV 567
|
730 740 750
....*....|....*....|....*....|....*
gi 291327510 1294 RLHRAGYAEHMGLAQFRRRFQVLDPALLKKLDLTS 1328
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
626-1361 |
1.41e-30 |
|
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: 131.18 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVPRGRQDG------------LPAHVTSLAQRAYWALLS-QR 691
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPfQRLPLYGKEILESYRQEGllrsqgiespqaLGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 692 RDQSIVALGRSGAGKTTCCEQVLEHL--VGMAGSV-------DGRVSV-EKLRATFTVLRAFGCVSTGHSRRATRFAMVM 761
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLttLGNGEEGapnegeeLGKLSImDRVLQSNPILEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 762 SLDFNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLH-------QMAESSAFgMGLWSKPE 834
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHdgitgglQLPNEFHY-TGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 835 DKQ-KAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-----------AAGACKVGRKQFMrfewaNHAAEALGCD 902
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqlefeskeedgAAEIAEEGNEKCL-----ARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 903 YEELNTAtfkhhLRQIIEQMTSGPQRQGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINRSFSSHHLS--MAS 980
Cdd:cd14908 316 VDKLLRA-----LTSKIIVVRGKEITTKLTPHKA--------YDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 981 IMVVDTPGFQNPRHQgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPF-DLPEsspgttvavvdqNPS 1059
Cdd:cd14908 383 VGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFiEFPD------------NQD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1060 QVHLPAGRGAedagGLFWVLDEEVRV-QGSSDSTVLERLRAAF--EKKKEAGAEEppsmrtceqplqcelfhqlgrdpvR 1136
Cdd:cd14908 445 CLDTIQAKKK----GILTMLDDECRLgIRGSDANYASRLYETYlpEKNQTHSENT------------------------R 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1137 YdltgwlrrakpnlaalEAPQILqqskreelqslfqaRAKLppvCRAVAGLEGTSQQALHRSRVVRRAFASSLAAVKRKA 1216
Cdd:cd14908 497 F----------------EATSIQ--------------KTKL---IFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFE 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1217 PCAQIKLQMDALISLLRRSRLHFIHCLVPTTveskagqrtpspsqpsgdqgvANEPTALDIPALRVQLAGSHILEALRLH 1296
Cdd:cd14908 544 SGQQFKAQLHSLIEMIEDTDPHYIRCIKPND---------------------AAKPDLVTRKRVTEQLRYGGVLEAVRVA 602
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1297 RAGYAEHMGLAQFRRRFQVLDPALLKK------LDLTSEELDERKVVEELLKT---------LDLEKKAVAVGHSQVFLK 1361
Cdd:cd14908 603 RSGYPVRLPHKDFFKRYRMLLPLIPEVvlswsmERLDPQKLCVKKMCKDLVKGvlspamvsmKNIPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
630-1360 |
4.87e-29 |
|
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: 126.62 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 630 TLLQRYRAQLPYTCSGPDLITLQPQTTT---VPSSGKVPRGRQDGL-----------PAHVTSLAQRAYWALLSQRRDQS 695
Cdd:cd14893 6 TLRARYRMEQVYTWVDRVLVGVNPVTPLpiyTPDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDAGEDQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 696 IVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-----------KLRATFTVLRAFGCVSTGHSRRATRFAMVMSLD 764
Cdd:cd14893 86 VILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEgasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAKMISVE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 765 FNATGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGM--DVDLRTELNLHQMAESsaFGMGLWSKPEDKQKAATA 842
Cdd:cd14893 166 FSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVqhDPTLRDSLEMNKCVNE--FVMLKQADPLATNFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 843 --FSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-------AAGACKVGRKQfmrfewANHAAEALGCDYEELNTATFKH 913
Cdd:cd14893 244 rdYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdPEGGKSVGGAN------STTVSDAQSCALKDPAQILLAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 914 HLRQ----IIEQMTSGPQRQGLQDNEACSGLKMTGV----ECVEGMASGLYQELFVAVVSLIN-------RSFSSHHLSM 978
Cdd:cd14893 318 KLLEvepvVLDNYFRTRQFFSKDGNKTVSSLKVVTVhqarKARDTFVRSLYESLFNFLVETLNgilggifDRYEKSNIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 979 AS--IMVVDTPGFQN--PRHQGkdraatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLpesSPGTTVAVV 1054
Cdd:cd14893 398 NSqgVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRL---TVNSNVDIT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1055 DQNPSQVHLpagrgAEDAG-GLFWVLDEEVRVQGSSDSTVLERLraaFEKKKEAGAEEPPSMRT------CEQPLQCELF 1127
Cdd:cd14893 469 SEQEKCLQL-----FEDKPfGIFDLLTENCKVRLPNDEDFVNKL---FSGNEAVGGLSRPNMGAdttneyLAPSKDWRLL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1128 ----HQLGRdpVRYDLTGWLRRAKPNLAALEApQILQQSKREELQSLFQARAklppvcrAVAGLEGTSQQALHRSRvVRR 1203
Cdd:cd14893 541 fivqHHCGK--VTYNGKGLSSKNMLSISSTCA-AIMQSSKNAVLHAVGAAQM-------AAASSEKAAKQTEERGS-TSS 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1204 AFASSLAAVKR-----KAPCAQIKLQMDALISLLRRSRLHFIHCLVPTTveskagqrtpspsqpSGDQGVaneptaLDIP 1278
Cdd:cd14893 610 KFRKSASSAREsknitDSAATDVYNQADALLHALNHTGKNFLVCIKPNE---------------TLEEGV------FDSA 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1279 ALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLdpallkkldltseeLDERKVVEELLKTLD----LEKKAVAVG 1354
Cdd:cd14893 669 YVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNV--------------CGHRGTLESLLRSLSaigvLEEEKFVVG 734
|
....*.
gi 291327510 1355 HSQVFL 1360
Cdd:cd14893 735 KTKVYL 740
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
627-1361 |
1.41e-27 |
|
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: 121.25 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 627 VMNTLLQRYRAQLPYTCSGPDLITLQP-----QTT--------TVPSSGKvprgrqdgLPAHVTSLAQRAYWALLSQRRD 693
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgNATdewirkyrDAPDLTK--------LPPHVFYTARRALENLHGVNKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 694 QSIVALGRSGAGKTTCCEQVLEHL-VGMAGSVDGRVSvEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVT 772
Cdd:cd14876 75 QTIIVSGESGAGKTEATKQIMRYFaSAKSGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 773 AAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKP--EDKQKaataFSQLRGAM 850
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPgiDDVAD----FEEVLESL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 851 ELLGISEGEQQAIWRVLAAIYHLGAAgacKVGRKQFMRFEwanHAAEALGCDYEELNTATFKHHL------RQIIEQMTS 924
Cdd:cd14876 230 KSMGLTEEQIDTVFSIVSGVLLLGNV---KITGKTEQGVD---DAAAISNESLEVFKEACSLLFLdpealkRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 925 -GPQR-QGLQDNEACSGLKMTgvecvegMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaT 1002
Cdd:cd14876 304 aGGQEiEGRWTKDDAEMLKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNN------S 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1003 FEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPfDLPESSpgtTVAVVDqnpsqvhLPAGRGaedaGGLFWVLDEE 1082
Cdd:cd14876 371 LEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTA-ELEYTS---NAEVID-------VLCGKG----KSVLSILEDQ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1083 VRVQGSSDSTVLERLRAAFEKKKEAgaeePPSMRTceQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQS 1162
Cdd:cd14876 436 CLAPGGSDEKFVSACVSKLKSNGKF----KPAKVD--SNINFIVVHTIG--DIQYNAEGFLFKNKDVLRA-ELVEVVQAS 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1163 KREELQSLFqaraklppvcravaglEGtsqQALHRSRVVRRAFASSlaavkrkapcaQIKLQMDALISLLRRSRLHFIHC 1242
Cdd:cd14876 507 TNPVVKALF----------------EG---VVVEKGKIAKGSLIGS-----------QFLKQLESLMGLINSTEPHFIRC 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1243 LVPTtvESKagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLK 1322
Cdd:cd14876 557 IKPN--ETK-------------------KPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIAN 615
|
730 740 750
....*....|....*....|....*....|....*....
gi 291327510 1323 kldltSEELDERKVVEELLKTLDLEKKAVAVGHSQVFLK 1361
Cdd:cd14876 616 -----DKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1442-2129 |
5.59e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.85 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRqkLQKSENSRSELRQNTDLLESKITDLTSELaderfkgDVACQALESERAERLQALREVQELKTKY 1521
Cdd:TIGR02168 220 AELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAEL-------QELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGA-DEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGEL 1600
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1601 QSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGEsmFEKSLREKVSQENNGVRWE 1680
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1681 LGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELET------NALEQQKIHSQQENTIKQL 1754
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1755 EQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDqi 1829
Cdd:TIGR02168 529 ISVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD-- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1830 gHRDFDVE-------------------------KRLRRDLR---------------------RTHALLS------DVQLL 1857
Cdd:TIGR02168 607 -LVKFDPKlrkalsyllggvlvvddldnalelaKKLRPGYRivtldgdlvrpggvitggsakTNSSILErrreieELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1858 LATIEdSKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRID 1937
Cdd:TIGR02168 686 IEELE-EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1938 EDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHmaQLRIQYLEQSTVERAIVSRQEAIICDLEN 2017
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--LLNEEAANLRERLESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2018 KTEfqkvQIKRFEVLVIRLRDSMIKMG---EELSRAVKAEAQQRENSQyyqQRLEELKAEMQELAQREEEASRRCMELEK 2094
Cdd:TIGR02168 843 LEE----QIEELSEDIESLAAEIEELEeliEELESELEALLNERASLE---EALALLRSELEELSEELRELESKRSELRR 915
|
730 740 750
....*....|....*....|....*....|....*
gi 291327510 2095 YVEELATVRQTLQTDLETSIRRIADLQAALEEVVS 2129
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
625-1319 |
7.47e-26 |
|
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: 115.74 E-value: 7.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTttvpssgKVPRGRQDGLP-AHVTSLAQRAYWALLSQR-RDQSIVALGRS 702
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFN-------KLSIQDQLVIKkCHISGVAENALDRIKSMSsNAESIVFGGES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 703 GAGKTTCCEQVLEHLVGMAGSvdgRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVLLE 782
Cdd:cd14874 74 GSGKSYNAFQVFKYLTSQPKS---KVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTVPLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 783 NSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGlwSKPEDKQKAATAFSQLRGAMELLGISEGEQQA 862
Cdd:cd14874 151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQG--NSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 863 IWRVLAAIYHLG------------AAGACKVGRKQfmRFEWanhAAEALGCDYEEL-NTATFKHhlrqiiEQMTSGPQRQ 929
Cdd:cd14874 229 IYKIISTILHIGniyfrtkrnpnvEQDVVEIGNMS--EVKW---VAFLLEVDFDQLvNFLLPKS------EDGTTIDLNA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 930 GLQDNEAcsglkmtgvecvegMASGLYQELFVAVVSLINRSFSShHLSMASIMVVDTPGFQNPRHQGkdraatFEELCYN 1009
Cdd:cd14874 298 ALDNRDS--------------FAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNG------VEEFLIN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1010 YAQERLQLLFYHRTFVSTLERYKEEGIPVPFDLPES-SPGTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGS 1088
Cdd:cd14874 357 SVNERIENLFVKHSFHDQLVDYAKDGISVDYKVPNSiENGKTVELLFKKPY--------------GLLPLLTDECKFPKG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1089 SDSTVLERLRAAFEKKKEAGaeeppSMRTCEQpLQCELFHQLGRdpVRYDLTGWLRRAKpNLAALEAPQILQQSKREELQ 1168
Cdd:cd14874 423 SHESYLEHCNLNHTDRSSYG-----KARNKER-LEFGVRHCIGT--TWYNVTDFFSRNK-RIISLSAVQLLRSSKNPIIG 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1169 SLFQARAKlppvcravagleGTSQQALHRSRVVRRAfasslaavkrkapcAQiklqmdALISLLRRSRLHFIHCLvpttv 1248
Cdd:cd14874 494 LLFESYSS------------NTSDMIVSQAQFILRG--------------AQ------EIADKINGSHAHFVRCI----- 536
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 1249 eskagqRTPSPSQpsgdqgvanePTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPA 1319
Cdd:cd14874 537 ------KSNNERQ----------PKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG 591
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
627-1036 |
9.71e-26 |
|
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: 115.75 E-value: 9.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 627 VMNTLLQRYRAQLPYTCSGPDLITLQP--QTTTVPSSGKVPRGRQ--------DGLPAHVTSLAQRAYWALLSQRRDQSI 696
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfkQIRNLYGTEVIGRYRQadtsrgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 697 VALGRSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEKL-RATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQ 775
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFA--YGHSTSSTDVQSLiLGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 776 LQTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMaESSAF--GMGLWSKPE-DKQKaatAFSQLRGAMEL 852
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSL-ESYNFlnASKCYDAPGiDDQK---EFAPVRSQLEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 853 LgISEGEQQAIWRVLAAIYHLGAAGACKVGRkqfMRFEwaNHAAEALGCDYEEL------NTATFKhhlRQIIEQMTSgp 926
Cdd:cd14886 237 L-FSKNEIDSFYKCISGILLAGNIEFSEEGD---MGVI--NAAKISNDEDFGKMcellgiESSKAA---QAIITKVVV-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 927 qrqgLQDNEACSGLKMTGVEC-VEGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEE 1005
Cdd:cd14886 306 ----INNETIISPVTQAQAEVnIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYEQ 375
|
410 420 430
....*....|....*....|....*....|.
gi 291327510 1006 LCYNYAQERLQLLFYHRTFVSTLERYKEEGI 1036
Cdd:cd14886 376 LLINYANERLQQYFINQVFKSEIQEYEIEGI 406
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
625-1325 |
3.63e-25 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 114.04 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVPRG--------------RQDGLPAHVTSLAQRAYWALLS 689
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGyaydhnsqfgdrvtSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 690 QRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGS---------------VDGRVSVE-KLRATFTVLRAFGCVSTGHSRR 753
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnltnsesisppaSPSRTTIEeQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 754 ATRFAMVMSLDFNATGR-VTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAG----MDVDLRTELNLHQMAES-SAFGM 827
Cdd:cd14899 161 SSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 828 GLWSKPEDKQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLGA---------------AGACKVGRKQFMRFEWA 892
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 893 NHAAEALGCDYEELNTATFKHHLRQIIEQMTSGPQRQGLQDNEacSGLKMtgvECvegmasglYQELFVAVVSLINRSFS 972
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTR--NALTM---EC--------YRLLFEWLVARVNNKLQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 973 SH---------------HLSMASIMVVDTPGFQNPRHQgkdraaTFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIP 1037
Cdd:cd14899 388 RQasapwgadesdvddeEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1038 VPF-DLPESSpgTTVAVVDQNPSqvhlpagrgaedagGLFWVLDEEVRVQGSSDSTVLERLRAAFEKKKEAgaeepPSMR 1116
Cdd:cd14899 462 WSFvDFPNNR--ACLELFEHRPI--------------GIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSH-----PHFR 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1117 TC---EQPLQCELFHQLGrdPVRYDLTGWLRRAKPNLAAlEAPQILQQSKREELQSLFQARAKlppvcravAGLEGTSQQ 1193
Cdd:cd14899 521 SApliQRTTQFVVAHYAG--CVTYTIDGFLAKNKDSFCE-SAAQLLAGSSNPLIQALAAGSND--------EDANGDSEL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1194 ALHRSRVVRRAfASSLAAVkrkAPCAQIKLQMDALISLLRRSRLHFIHCLVPTtvESKAGQRTPSPSqpsgdqgvanept 1273
Cdd:cd14899 590 DGFGGRTRRRA-KSAIAAV---SVGTQFKIQLNELLSTVRATTPRYVRCIKPN--DSHVGSLFQSTR------------- 650
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 291327510 1274 aldipaLRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQVLDPALLKKLD 1325
Cdd:cd14899 651 ------VVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVLLSLYKWGD 696
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
625-1361 |
3.51e-24 |
|
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: 110.49 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 625 SSVMNTLLQRYRAQLPYTCSGPDLITLQPQTTTVPSSGKVPRGRQDGLPAHVTSLAQRAYWALLSQRRDQSIVALGRSGA 704
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 705 GKTTCCEQVLE-HLVGMagSVDGRVSVEKLRATFtVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVLLEN 783
Cdd:cd14937 81 GKTEASKLVIKyYLSGV--KEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 784 SRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGLWSKPEDKQkaATAFSQLRGAMELLGISEGEQQaI 863
Cdd:cd14937 158 IRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDD--AKDFGNLMISFDKMNMHDMKDD-L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 864 WRVLAAIYHLG--------AAGACKVGRKQFMRFEWANHAAEALGCDYEEL-NTATFKHhlRQIIEQMTSGPqrqgLQDN 934
Cdd:cd14937 235 FLTLSGLLLLGnveyqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLkDCLVFTE--KTIANQKIEIP----LSVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 935 EACSGLKmtgvecveGMASGLYQELFVAVVSLINRSFSSHHLSMASIMVVDTPGFQNPRHQgkdraaTFEELCYNYAQER 1014
Cdd:cd14937 309 ESVSICK--------SISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------SLEQLLINIANEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1015 LQLLFYHRTFVSTLERYKEEGIpvpfdLPESSPGTTvavvdqNPSQVHLPAGRGAedaggLFWVLDEEVRVQGSSDSTVL 1094
Cdd:cd14937 375 IHSIYLYIVYEKETELYKAEDI-----LIESVKYTT------NESIIDLLRGKTS-----IISILEDSCLGPVKNDESIV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1095 ERLRAAFEKKKEAGaeeppsmrTCEQPLQCELFHQLGRDPVRYDLTGWLRRAK----PNLAALeapqiLQQSKREELQSL 1170
Cdd:cd14937 439 SVYTNKFSKHEKYA--------STKKDINKNFVIKHTVSDVTYTITNFISKNKdilpSNIVRL-----LKVSNNKLVRSL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1171 FQaraklppvcravaglEGTSQQALHRSRVVRRAFASSLaavkrkapcaqiklqmDALISLLRRSRLHFIHCLVPTTVES 1250
Cdd:cd14937 506 YE---------------DVEVSESLGRKNLITFKYLKNL----------------NNIISYLKSTNIYFIKCIKPNENKE 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1251 KA--GQRTPSPsqpsgdqgvaneptaldipalrvQLAGSHILEALRLhRAGYAEHMGLAQFRRRFQVLDPALLKKLDLTs 1328
Cdd:cd14937 555 KNnfNQKKVFP-----------------------QLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLT- 609
|
730 740 750
....*....|....*....|....*....|...
gi 291327510 1329 eelDERKVVEELLKTLDleKKAVAVGHSQVFLK 1361
Cdd:cd14937 610 ---DKEKVSMILQNTVD--PDLYKVGKTMVFLK 637
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1427-2111 |
5.78e-24 |
|
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: 111.04 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1427 LLASLRPLLSSTLGTEQLRAK-EEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKgdvaCQALESERA 1505
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK----NIKLSKDVS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1506 ERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGADEWQMRLDCAQMENdfLRKRLQQCEERLDS 1585
Cdd:pfam01576 465 SLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD--MKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1586 EMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQalgesmfEKS 1665
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-------EKA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1666 LREKVSQENNGVRWELGQLQQQL---EQKEQEASKLKQEVER----LQGQKRELLSCASVGDQGVASLKERVWELETNAL 1738
Cdd:pfam01576 616 ISARYAEERDRAEAEAREKETRAlslARALEEALEAKEELERtnkqLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1739 EQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDL 1818
Cdd:pfam01576 696 EMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKL 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1819 EGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLATIEDSKTSI---SKEELEKVHS------QLEQSEAKCED 1889
Cdd:pfam01576 776 ELDLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQRELEEARASRDEIlaqSKESEKKLKNleaellQLQEDLAASER 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1890 ALKTQKvltADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGD---LNDLMQKHKDLIAQSAADIGQIQE 1966
Cdd:pfam01576 855 ARRQAQ---QERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNtelLNDRLRKSTLQVEQLTTELAAERS 931
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1967 LQLQLEETkkeKQKLREQLHMAQLRIQYLEQstverAIVSRQEAIICDLENK---TEFQKVQIKRFEVLVIRLRDSMIKM 2043
Cdd:pfam01576 932 TSQKSESA---RQQLERQNKELKAKLQEMEG-----TVKSKFKSSIAALEAKiaqLEEQLEQESRERQAANKLVRRTEKK 1003
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291327510 2044 GEELSRAVKAEaqqRENSQYYQQRLEELKAEMQELAQREEEAsrrcmelEKYVEELATVRQTLQTDLE 2111
Cdd:pfam01576 1004 LKEVLLQVEDE---RRHADQYKDQAEKGNSRMKQLKRQLEEA-------EEEASRANAARRKLQRELD 1061
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
626-1360 |
8.02e-24 |
|
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: 109.43 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTT-----TVPSSGKVPRGRQdglpahVTSLAQRAYWALLSQRRDQSIVALG 700
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnplTLTSTRSSPLAPQ------LLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 701 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATFTVLRAFGCVST---GHSRRATRFAMVMSLDfnatGRVTAAQLQ 777
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTatnSESSRIGHFIEVQVTD----GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 778 TVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNL--HQMAESSAFGMG--LWSKPEDkqkaATAFSQLRGAMELL 853
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdgYSPANLRYLSHGdtRQNEAED----AARFQAWKACLGIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 854 GISEGEqqaIWRVLAAIYHLGAAgackvgrkQFmrfewanhaAEALGCDYE-----ELNTAT--FKHHLRQIIEQMTSGP 926
Cdd:cd14881 228 GIPFLD---VVRVLAAVLLLGNV--------QF---------IDGGGLEVDvkgetELKSVAalLGVSGAALFRGLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 927 QRQGLQDNEACSGLKMTGVECvEGMASGLYQELFVAVVSLINR-----SFSSHHLSMASIMVVDTPGFQNPrhqgkdRAA 1001
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTR-DALAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFGFEDP------KPS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1002 TFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVPFDlpesspgttVAVVDQNPSQVHLPAGRgaedaGGLFWVLDE 1081
Cdd:cd14881 361 QLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVE---------VDYVDNVPCIDLISSLR-----TGLLSMLDV 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1082 EVRVQGSSDSTVlERLRAAFEKKKEAGAEEPPSMRtceqplqceLF---HQLGRdpVRYDLTGWL---RRAKPnlaalea 1155
Cdd:cd14881 427 ECSPRGTAESYV-AKIKVQHRQNPRLFEAKPQDDR---------MFgirHFAGR--VVYDASDFLdtnRDVVP------- 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1156 pqilqqskrEELQSLFqaraklppvcravaglegtsqqalhRSRVVRRAFASSLaavkrkapcAQIKLQMDALISLLRRS 1235
Cdd:cd14881 488 ---------DDLVAVF-------------------------YKQNCNFGFATHT---------QDFHTRLDNLLRTLVHA 524
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1236 RLHFIHCLVPTTVEskagqrtpspsqpsgdqgvanEPTALDIPALRVQLAGSHILEALRLHRAGYAEHMGLAQFRRRFQV 1315
Cdd:cd14881 525 RPHFVRCIRSNTTE---------------------TPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRL 583
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 291327510 1316 LDP-ALLKKLDltSEELDERKVVEELLKTLDLEKKAV-----AVGHSQVFL 1360
Cdd:cd14881 584 LAPfRLLRRVE--EKALEDCALILQFLEAQPPSKLSSvstswALGKRHIFL 632
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1366-2135 |
1.66e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 106.31 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1366 SRLERQREKL--VSRNIVLFQAACRgfLSRQEYKKLKIRRLATLciqKNLAVFLKVKDWPWWGLLASLRPLLSSTLGTE- 1442
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIID--EKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALERQKEAIEr 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1443 QLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELAdERFKGDVACQALESERAERLQAL--REVQELKTK 1520
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-LRVKEKIGELEAEIASLERSIAEkeRELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1521 YQQVQDALGEVQKQLEEAQQRIQGANLEEkpaggaDEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGEL 1600
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRR------DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1601 QSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLREKVSQEnngvrwe 1680
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE------- 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1681 lgqlqqqLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELETNAleqQKIHSqqenTIKQLEQLRQR 1760
Cdd:TIGR02169 471 -------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI---QGVHG----TVAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1761 FELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLRQL---EMQLEQEYEEKqvaLHEkhdlEGLIGTLCDQIghr 1832
Cdd:TIGR02169 537 YATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLSI---LSE----DGVIGFAVDLV--- 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1833 DFDVEKR-----------LRRDLRRTHALLSDVQLLlaTIE---------------DSKTSIS-----KEELEKVHSQLE 1881
Cdd:TIGR02169 607 EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYRMV--TLEgelfeksgamtggsrAPRGGILfsrsePAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1882 QSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADI 1961
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1962 GQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVErAIVSRQEAIICDLENKtefqkvqIKRFEVLVIRLRDsmi 2041
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE-EEVSRIEARLREIEQK-------LNRLTLEKEYLEK--- 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2042 KMGEELSRAVKAEAQQRENsqyyQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQ 2121
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSI----EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
810
....*....|....
gi 291327510 2122 AALEEVVSSDSDTE 2135
Cdd:TIGR02169 910 AQIEKKRKRLSELK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1441-2142 |
7.03e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 104.37 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1441 TEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELAD--ERFKGDVACQALESERAERLQAlrEVQELK 1518
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEleEKLEELKEELESLEAELEELEA--ELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1519 TKYQQVQDALGEVQKQLEEAQQRIQGANleekpaggadewqmrldcAQMENdfLRKRLQQCEERLDSEMKARTELEQKLG 1598
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLN------------------NEIER--LEARLERLEDRRERLQQEIEELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1599 ELQsaYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLREKVSQENNGVR 1678
Cdd:TIGR02168 432 EAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1679 WELGQLQQQLEQKEQEASKLK------QEVERLQGQKRELLSC--ASVGDQGVASLKE----RVWELETNALEQQKIHSQ 1746
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLSELISvdegyeAAIEAALGGRLQAVVVenLNAAKKAIAFLKQnelgRVTFLPLDSIKGTEIQGN 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1747 QENTIKQLEQLRQRFeleiermkqmhqKDREDQEEELEDVRQScqkRLRQLEMqleqeYEEKQVALHEKH--DLEGLIGT 1824
Cdd:TIGR02168 590 DREILKNIEGFLGVA------------KDLVKFDPKLRKALSY---LLGGVLV-----VDDLDNALELAKklRPGYRIVT 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1825 LCDQIGHRDFDVekrLRRDLRRTHALLS------DVQLLLATIEdSKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLT 1898
Cdd:TIGR02168 650 LDGDLVRPGGVI---TGGSAKTNSSILErrreieELEEKIEELE-EKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1899 ADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEK 1978
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1979 QKLREQLHmaQLRIQYLEQSTVERAIVSRQEAI---ICDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEA 2055
Cdd:TIGR02168 806 DELRAELT--LLNEEAANLRERLESLERRIAATerrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2056 QQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIA-----DLQAALEEVVSS 2130
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeyslTLEEAEALENKI 963
|
730
....*....|..
gi 291327510 2131 DSDTESVQTAVD 2142
Cdd:TIGR02168 964 EDDEEEARRRLK 975
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1502-2126 |
3.00e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.98 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1502 SERAERLQALREVQELKTKYQqvqdalgEVQKQLEEAQQRIQGANLEEKpAGGADEWQMRLDCAQMENDFLRKRLQQCEE 1581
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYK-------ELKAELRELELALLVLRLEEL-REELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1582 RLDSEMKARTELEQKLGELQSAYEEAK-------KMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLA 1654
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALAneisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1655 QALGESmfeKSLREKVSQENNGVRWELGQLQQQLEQKEQEASK---LKQEVERLQGQKRELLSCASVGDQGVASLKERVW 1731
Cdd:TIGR02168 348 ELKEEL---ESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1732 ELETNALEQQK--IHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKR-----LRQLEMQLEQE 1804
Cdd:TIGR02168 425 ELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldsLERLQENLEGF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1805 YEEKQVALHEKHDLEGLIGTLCDQIghrdfDVEKRLRRDL------RRTHALLSDVQLLLATIEdsktSISKEELEKVHS 1878
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELI-----SVDEGYEAAIeaalggRLQAVVVENLNAAKKAIA----FLKQNELGRVTF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1879 qleqseakCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRI---DEDQGDLNDLMQKHK---- 1951
Cdd:TIGR02168 576 --------LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPgyri 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1952 -----DLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQsTVERAIVSRQEaiicdLENKTEFQKVQI 2026
Cdd:TIGR02168 648 vtldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKELEE-----LEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2027 KRFEVLVIRLRdsmikmgEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTL 2106
Cdd:TIGR02168 722 EELSRQISALR-------KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
650 660
....*....|....*....|
gi 291327510 2107 QTDLETSIRRIADLQAALEE 2126
Cdd:TIGR02168 795 KEELKALREALDELRAELTL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1465-2117 |
9.42e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1465 RSELRQNTDLLE------SKITDLTSELadERFKGDVACQALESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEA 1538
Cdd:COG1196 195 LGELERQLEPLErqaekaERYRELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1539 QQRIQGANLEEKPAGGAD-EWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRK 1617
Cdd:COG1196 273 RLELEELELELEEAQAEEyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1618 CHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLREKVSQEnngvrwelgqlqqqleqkeqeASK 1697
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---------------------EEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1698 LKQEVERLQGQKRELlscasvgDQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE 1777
Cdd:COG1196 412 LLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1778 DQEEELedvrqscQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEK--RLRRDLRRTHALLSDVQ 1855
Cdd:COG1196 485 ELAEAA-------ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAalEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1856 LLLATIEDSKTS----ISKEELEKVHsQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERAd 1931
Cdd:COG1196 558 VAAAAIEYLKAAkagrATFLPLDKIR-ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1932 lLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLhmAQLRIQYLEQSTVERAIVSRQEAI 2011
Cdd:COG1196 636 -LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL--AEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2012 ICDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQEL------AQRE-EE 2084
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllAIEEyEE 792
|
650 660 670
....*....|....*....|....*....|...
gi 291327510 2085 ASRRcmeLEKYVEELATVRQTLQTdLETSIRRI 2117
Cdd:COG1196 793 LEER---YDFLSEQREDLEEARET-LEEAIEEI 821
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1442-2127 |
2.68e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.91 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLES------KITDLTSELadERFKGDVACQALESERAERLQALREVQ 1515
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEK--REYEGYELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1516 ELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGADEWQMRLDCAQMENDflRKRLQQCEERLDSEMKartELEQ 1595
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELE---DAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1596 KLGELQSAYEEAKKMAHQLKRkchhltwDLEDTRVLLENQQSrnhELEKRQKKFDLQLAQALGESMFEKSLREKVSQEnn 1675
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDY-- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1676 gvrwelgqlQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELETNALEQQKIHSQQENTIKQLE 1755
Cdd:TIGR02169 391 ---------REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1756 QLRQRFELEIERMKQmhqkDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHR--- 1832
Cdd:TIGR02169 462 ADLSKYEQELYDLKE----EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGery 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1833 ------------------DFDVEKR----LRRD---------LRRTHALLSDVQLL------------------------ 1857
Cdd:TIGR02169 538 ataievaagnrlnnvvveDDAVAKEaielLKRRkagratflpLNKMRDERRDLSILsedgvigfavdlvefdpkyepafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1858 -----------------------LATIE---------------DSKTSIS-----KEELEKVHSQLEQSEAKCEDALKTQ 1894
Cdd:TIGR02169 618 yvfgdtlvvedieaarrlmgkyrMVTLEgelfeksgamtggsrAPRGGILfsrsePAELQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1895 KVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEET 1974
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1975 KKEKQKLREQLHMAQLRIQYLEQSTVErAIVSRQEAIICDLENKTEF---------QKVQIKRFEVLVIRLRDSMIKMGE 2045
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLE-EEVSRIEARLREIEQKLNRltlekeyleKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2046 ELSRAVKAEaqqrensqyYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALE 2125
Cdd:TIGR02169 857 ENLNGKKEE---------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
..
gi 291327510 2126 EV 2127
Cdd:TIGR02169 928 AL 929
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1442-1997 |
4.27e-19 |
|
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: 94.70 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELR---QNTDLLESKITDL---TSELADErfkgdvacqaLESERAERLQALREVQ 1515
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELkkqNNQLKDN----------IEKKQQEINEKTTEIS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1516 ELKTKYQQVQDALGEVQKQLEEAQQRIQGAN--LEEKPAggadewqmRLDCAQMENDFLRKrlqQCEERLDSEMKarTEL 1593
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNkkIKELEK--------QLNQLKSEISDLNN---QKEQDWNKELK--SEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1594 EQ---KLGELQSAYEEAKKMAHQLKRKCHhltwDLEDTRVLLENQ-QSRNHELEKRQKKFdlqlaqalgesmfekslrEK 1669
Cdd:TIGR04523 317 KNqekKLEEIQNQISQNNKIISQLNEQIS----QLKKELTNSESEnSEKQRELEEKQNEI------------------EK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1670 VSQENNgvrwelgqlqqqleqkeqeasKLKQEVERLQGQKRELlscasvgdqgvaslkervwelETNALEQQKIHSQQEN 1749
Cdd:TIGR04523 375 LKKENQ---------------------SYKQEIKNLESQINDL---------------------ESKIQNQEKLNQQKDE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1750 TIKQLEQLRQRFELEIERMKQmhqkDREDQEEELEDV-RQSCQKRLRQLEMQLEQEYEEKQVALHE------KHDLEgli 1822
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKE----TIIKNNSEIKDLtNQDSVKELIIKNLDNTRESLETQLKVLSrsinkiKQNLE--- 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1823 gtlcdqighrdfDVEKRLRRDLRRTHALLSDVQLLLATIED--SKTSISKEELEKVHSQLEQSEAKCEDalKTQKVLTAD 1900
Cdd:TIGR04523 486 ------------QKQKELKSKEKELKKLNEEKKELEEKVKDltKKISSLKEKIEKLESEKKEKESKISD--LEDELNKDD 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1901 LENMHSELENVTRSKslvDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQK 1980
Cdd:TIGR04523 552 FELKKENLEKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
570
....*....|....*..
gi 291327510 1981 LREQLHMAQLRIQYLEQ 1997
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1441-2108 |
1.20e-18 |
|
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: 93.58 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1441 TEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKTK 1520
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1521 YQQVQDALGEVQKQLEEAQQRI-----QGANLEEKPAGGADEW-QMRLDCAQMENDF--LRKRLQQCEERLDSEMKARTE 1592
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELeeleaELEELESRLEELEEQLeTLRSKVAQLELQIasLNNEIERLEARLERLEDRRER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1593 LEQKLGELQSAYEEAKKMAHQ-----LKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLR 1667
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1668 EKVSQENNGVRWELGQLQQQLEQKEQEASKLKQE-------------------VERLQGQKR--ELLSCASVG------- 1719
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyeaaieaalggrlqavvVENLNAAKKaiAFLKQNELGrvtflpl 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1720 -------------------DQGVASLKERVWELE-------------------TNALEQQKIHS---------------- 1745
Cdd:TIGR02168 579 dsikgteiqgndreilkniEGFLGVAKDLVKFDPklrkalsyllggvlvvddlDNALELAKKLRpgyrivtldgdlvrpg 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1746 ---------------QQENTIKQLEQLRQRFELEIERMKQ---MHQKDREDQEEELEDVR---QSCQKRLRQLEMQLEQE 1804
Cdd:TIGR02168 659 gvitggsaktnssilERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRkelEELSRQISALRKDLARL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1805 YEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLATIEDSKTSIsKEELEKVHSQLEQSE 1884
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQIEQLKEELKAL-REALDELRAELTLLN 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1885 AKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDL----------MQKHKDLI 1954
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerasleeaLALLRSEL 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1955 AQSAADI----GQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIICDLENKTEFQKVQIKrfe 2030
Cdd:TIGR02168 897 EELSEELreleSKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR--- 973
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291327510 2031 vlVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCmeLEKYVEELATVRQTLQT 2108
Cdd:TIGR02168 974 --LKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA--RERFKDTFDQVNENFQR 1047
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1501-2126 |
2.82e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1501 ESERAERLQAL------REVQELKTKYQQVQDALGEVQKQLEEAQQRIQGanleekpaggadewqmrldcaqmendfLRK 1574
Cdd:COG1196 208 QAEKAERYRELkeelkeLEAELLLLKLRELEAELEELEAELEELEAELEE---------------------------LEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1575 RLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLA 1654
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1655 QALGEsmfEKSLREKVSQenngvrwelgqlqqqleqkeqEASKLKQEVERLQGQKRELlscasvgdqgvASLKERVWELE 1734
Cdd:COG1196 341 ELEEE---LEEAEEELEE---------------------AEAELAEAEEALLEAEAEL-----------AEAEEELEELA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1735 TNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHE 1814
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1815 KHDLEGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKTq 1894
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1895 kVLTADLENMHSELENVTRS--KSLVDEQLYRLQFERADLLKRIDEDQGDLNDLmqKHKDLIAQSAADIGQIQELQLQLE 1972
Cdd:COG1196 543 -ALAAALQNIVVEDDEVAAAaiEYLKAAKAGRATFLPLDKIRARAALAAALARG--AIGAAVDLVASDLREADARYYVLG 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1973 ETKKEKQKLREQLHMAQLRIQYLEQS----TVERAIVSRQEAIICDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELS 2048
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 2049 RAVKAEAQQRENSQYYQQRLEELKAEMQELAQRE-EEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEE 2126
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAErEELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
626-1098 |
3.79e-18 |
|
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: 91.31 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQP-QTTTVPSSGKVPRG--RQDGLPAHVTSLAQRAYWALLSQRRDQSIVALGRS 702
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNynQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 703 GAGKTTCCEQVLEHLVGMAGSvDGRVSVEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQLQTVLLE 782
Cdd:cd14905 82 GSGKSENTKIIIQYLLTTDLS-RSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 783 NSRVARQPQGEGNFEVFSQLLAGMDVDLRTELNLHQMAESSAFGMGlWSKPEDKQKAATAFSQLRGAMELLGISEGEQQA 862
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQG-GSISVESIDDNRVFDRLKMSFVFFDFPSEKIDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 863 IWRVLAAIYHLGAAgackvgrkQFMRFEWANHAAEALGCDYEELNTATFKHHLRQIIEQMTSGPQrqglqdNEAcsglkm 942
Cdd:cd14905 240 IFKTLSFIIILGNV--------TFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPV------NEA------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 943 tgVECVEGMASGLYQELFVAVVSLINRSFSSHHLSMaSIMVVDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLFYHR 1022
Cdd:cd14905 300 --VENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291327510 1023 TFVSTLERYKEEGIPVPfdlpesspgTTVAVVDQNPSqvhlpagrgAEDAGGLFWVLDEEVRVQGSSDSTVLERLR 1098
Cdd:cd14905 371 VLKQEQREYQTERIPWM---------TPISFKDNEES---------VEMMEKIINLLDQESKNINSSDQIFLEKLQ 428
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
626-1099 |
5.41e-17 |
|
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: 87.49 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 626 SVMNTLLQRYRAQLPYTCSGPDLITLQPQTTtvpsSGKVPRG---------RQDGLPaHVTSLAQRAYWALLSQRRDQSI 696
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEI----KQEYPQEfhakyrcksRSDNAP-HIFSVADSAYQDMLHHEEPQHI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 697 VALGRSGAGKTTCCEQVLEHLvGMAGSVDGRVSvEKLRATFTVLRAFGCVSTGHSRRATRFAMVMSLDFNATGRVTAAQL 776
Cdd:cd14882 77 ILSGESYSGKTTNARLLIKHL-CYLGDGNRGAT-GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 777 QTVLLENSRVARQPQGEGNFEVFSQLLAGMDVDLR-TELNL-------HQMAESSAFGMGLWSKPEDKQKAATAFSQLRG 848
Cdd:cd14882 155 WMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLkagrnyrYLRIPPEVPPSKLKYRRDDPEGNVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 849 AMELLGISEGEQQAIWRVLAAIYHLGAAGACKV-GRKQFMRFEWANHAAEALGcdyeeLNTATFKHHLRQIIEQMTSGPQ 927
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLR-----LDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 928 RQGLQDNEAcsglkmtgVECVEGMASGLYQELFVAVVSLINrsfssHHLSMA--------SIMVVDTPGFQNPRHQGkdr 999
Cdd:cd14882 310 RRKHTTEEA--------RDARDVLASTLYSRLVDWIINRIN-----MKMSFPravfgdkySISIHDMFGFECFHRNR--- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1000 aatFEELCYNYAQERLQLLFYHRTFVSTLERYKEEGIPVP----FDLPESspgttvavVDQNPSQVHlpagrgaedagGL 1075
Cdd:cd14882 374 ---LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTInlrfYDNKTA--------VDQLMTKPD-----------GL 431
|
490 500
....*....|....*....|....
gi 291327510 1076 FWVLDEEVRvQGSSDSTVLERLRA 1099
Cdd:cd14882 432 FYIIDDASR-SCQDQNYIMDRIKE 454
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
673-1036 |
7.41e-16 |
|
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: 84.19 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 673 PAHVTSLAQRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKLRATFTVLRAFGCVSTGHSR 752
Cdd:cd14884 61 KAHIYDIANMAYKNMRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 753 RATRFAMVMSLDFNA---------TGRVTAAQLQTVLLENSRVARQPQGEGNFEVFSQLLAGM-DVDL---RTELNLH-- 817
Cdd:cd14884 141 NSSRCGRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLsDEDLarrNLVRNCGvy 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 818 --------QMAESSAFGMGLWSK-----PEDKQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHLG-----AAGAC 879
Cdd:cd14884 221 gllnpdesHQKRSVKGTLRLGSDsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGnraykAAAEC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 880 kvgrkqfMRFEwANHAAEALgcDYEELNTA--TFKHHLRQiiEQMTSgpqrqglqdneacsglkmtgveCVEGMASGLYQ 957
Cdd:cd14884 301 -------LQIE-EEDLENVI--KYKNIRVSheVIRTERRK--ENATS----------------------TRDTLIKFIYK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 958 ELFVAVVSLINR---------SFSSHHLSM---ASIMVVDTPGFQNPRHQGkdraatFEELCYNYAQERLQLLFYHRTFV 1025
Cdd:cd14884 347 KLFNKIIEDINRnvlkckekdESDNEDIYSineAIISILDIYGFEELSGND------FDQLCINLANEKLNNYYINNEIE 420
|
410
....*....|.
gi 291327510 1026 STLERYKEEGI 1036
Cdd:cd14884 421 KEKRIYARENI 431
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1442-2111 |
3.59e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.15 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSEL-RQNTDLLESKI---------TDLTSELADERFKGDVACQALE---------- 1501
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNalqeqlqaeTELCAEAEEMRARLAARKQELEeilhelesrl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1502 SERAERLQALRevQELKTKYQQVQDalgeVQKQLEE---AQQRIQganlEEKPAGGADEWQMRLDCAQME--NDFLRKRL 1576
Cdd:pfam01576 85 EEEEERSQQLQ--NEKKKMQQHIQD----LEEQLDEeeaARQKLQ----LEKVTTEAKIKKLEEDILLLEdqNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1577 QQCEERLdsemkarTELEQKLGElqsaYEEAKKMAHQLKRKCHHLTWDLEDTrvlLENQQSRNHELEKRQKKFDlqlaqa 1656
Cdd:pfam01576 155 KLLEERI-------SEFTSNLAE----EEEKAKSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLE------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1657 lGESmfeKSLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEverlQGQKRELLSCASVGDQGVASLKErvwELETN 1736
Cdd:pfam01576 215 -GES---TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEE----TAQKNNALKKIRELEAQISELQE---DLESE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1737 ALEQQKIHSQQENTIKQLE-----------------QLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEM 1799
Cdd:pfam01576 284 RAARNKAEKQRRDLGEELEalkteledtldttaaqqELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1800 QLEQEYEEKQVALHEKHDLEGLIGTLCDQ---IGHRDFDVE---KRLRRDLRRTHALLSDVQLLLATIEDsKTSISKEEL 1873
Cdd:pfam01576 364 QLEQAKRNKANLEKAKQALESENAELQAElrtLQQAKQDSEhkrKKLEGQLQELQARLSESERQRAELAE-KLSKLQSEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1874 EKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQ----------GDL 1943
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEeakrnverqlSTL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1944 NDLMQKHKDLIAQSAADIGQIQE-----------LQLQLEETKKEKQKLREQLHMAQlriQYLEQSTVEraiVSRQEAII 2012
Cdd:pfam01576 523 QAQLSDMKKKLEEDAGTLEALEEgkkrlqreleaLTQQLEEKAAAYDKLEKTKNRLQ---QELDDLLVD---LDHQRQLV 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2013 CDLENKTefqkvqiKRFEVLVIRLRDSMIKMGEELSRAvKAEAQQRENSQYYQQR-LEE--------------LKAEMQE 2077
Cdd:pfam01576 597 SNLEKKQ-------KKFDQMLAEEKAISARYAEERDRA-EAEAREKETRALSLARaLEEaleakeelertnkqLRAEMED 668
|
730 740 750
....*....|....*....|....*....|....
gi 291327510 2078 LAQREEEASRRCMELEKYVEELATVRQTLQTDLE 2111
Cdd:pfam01576 669 LVSSKDDVGKNVHELERSKRALEQQVEEMKTQLE 702
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1838-2138 |
6.15e-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: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1838 KRLRRDLRRThallsDVQLLLATIEDSKtsiskEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSL 1917
Cdd:COG1196 216 RELKEELKEL-----EAELLLLKLRELE-----AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1918 VDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQ 1997
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1998 StvERAIVSRQEAIICDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENsqyyQQRLEELKAEMQE 2077
Cdd:COG1196 366 A--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EEALAELEEEEEE 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 2078 LAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQ 2138
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1500-2142 |
1.99e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1500 LESERaERLQALREVQELKtKYQQVQDALGEVQKQLEEAQQRI-----QGANLEEkpaggadewqmrldcaQMENdfLRK 1574
Cdd:PRK03918 141 LESDE-SREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLekfikRTENIEE----------------LIKE--KEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1575 RLQQCEERLDSEMKARTELEQKLGELQSAYEEakkmahqlkrkchhltwdLEDTRVLLENQQSRNHELEKRQKKFDLQLA 1654
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKE------------------LEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1655 QaLGESMFEKSLREKVSQENngvrwelGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELE 1734
Cdd:PRK03918 263 E-LEERIEELKKEIEELEEK-------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1735 TNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDR----------EDQEEELEDV---RQSCQKRLRQLEM-- 1799
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpEKLEKELEELekaKEEIEEEISKITAri 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1800 -QLEQEYEEKQVALHEkhdLEGLIGTlCDQIGhRDFDVEKRLRRdLRRTHALLSDVQLLLATIEDSKTSIsKEELEKVHS 1878
Cdd:PRK03918 415 gELKKEIKELKKAIEE---LKKAKGK-CPVCG-RELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKL-RKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1879 QLEQseakcEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKridedqGDLNDLmqkhkdliaqsA 1958
Cdd:PRK03918 488 VLKK-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK------GEIKSL-----------K 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1959 ADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVEraivsrqeaiicDLENKTEFQKVQIKRFevlvIRLRD 2038
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE------------ELEERLKELEPFYNEY----LELKD 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2039 SMIKMGEELSRAVKAEA---QQRENSQYYQQRLEELKAEMQELAQR-----EEEASRRCMELEKYVEELATVRQTLQTDL 2110
Cdd:PRK03918 610 AEKELEREEKELKKLEEeldKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRR 689
|
650 660 670
....*....|....*....|....*....|..
gi 291327510 2111 ETSIRRIADLQAALEEVVSSDSDTESVQTAVD 2142
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1443-2111 |
1.39e-13 |
|
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: 76.68 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1443 QLRAKEEELTLLR----------QKLQkSENSRSELRQNTDLLESKitDLTSELADERFKGDVACQ--ALESERAERLQA 1510
Cdd:pfam05483 100 ELKQKENKLQENRkiieaqrkaiQELQ-FENEKVSLKLEEEIQENK--DLIKENNATRHLCNLLKEtcARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1511 LREvqELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGADEWQMRldcaQMENDFlRKRLQQCEERLDSEMKAR 1590
Cdd:pfam05483 177 ERE--ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQ----HLEEEY-KKEINDKEKQVSLLLIQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1591 TELEQKLGELQSAYEEAKKMAHQLKRKC--------------HHLTWDLEDTRVLLENQQSRNHELEKrqkkfDLQLAQA 1656
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTklqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEE-----DLQIATK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1657 LGESMFEKslREKVSQENNGVRWELGQLQQQLEQKEQEASK-LKQEVERLQGQKRELLSCASVGDQGVASLKE------- 1728
Cdd:pfam05483 325 TICQLTEE--KEAQMEELNKAKAAHSFVVTEFEATTCSLEElLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknn 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1729 ---RVWELETNALEQQKIHSQQENTIKQLEQLRQRfELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQL-EMQLEQE 1804
Cdd:pfam05483 403 kevELEELKKILAEDEKLLDEKKQFEKIAEELKGK-EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVeDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1805 YEE-KQVALHEKHDLEGLIGTLCDQiGHRDFDVE-KRLRRDLRRTHALLSDVQLLLATIEDSKTSIsKEELEKVHSQLEQ 1882
Cdd:pfam05483 482 KEKlKNIELTAHCDKLLLENKELTQ-EASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVREEFIQ 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1883 S--EAKCEdalktqkvLTADLENMHSELENVTRSkslvDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAAD 1960
Cdd:pfam05483 560 KgdEVKCK--------LDKSEENARSIEYEVLKK----EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1961 IGQ-------IQELQLQLEETkkeKQKLREQLHMAQLRIQYLEQS------TVERAIVSRQEAIicdlenktEFQKVQIK 2027
Cdd:pfam05483 628 NKQlnayeikVNKLELELASA---KQKFEEIIDNYQKEIEDKKISeeklleEVEKAKAIADEAV--------KLQKEIDK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2028 RFEVlvirlrdsmiKMGEELSRAVKAEAQqrensqyYQQRLEELKAEMQELAQREEEAS--RRCMELE--KYVEELATVR 2103
Cdd:pfam05483 697 RCQH----------KIAEMVALMEKHKHQ-------YDKIIEERDSELGLYKNKEQEQSsaKAALEIElsNIKAELLSLK 759
|
....*...
gi 291327510 2104 QTLQTDLE 2111
Cdd:pfam05483 760 KQLEIEKE 767
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1410-2138 |
1.16e-12 |
|
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: 74.23 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1410 QKNLAVFLKVKDWPWWGLLASLRPLLSSTLGTEQLRAKEEELTLLRQKLQKsensRSELRqnTDLLESKITDLTSELade 1489
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTL----RSQLL--TLCTPCMPDTYHERK--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1490 rfkgdvacQALESERAERLQALREVQELKTKYQQVQDALGE---VQKQLEEAQQRIQGANLEEKpaggadewqmRLDCAQ 1566
Cdd:TIGR00618 222 --------QVLEKELKHLREALQQTQQSHAYLTQKREAQEEqlkKQQLLKQLRARIEELRAQEA----------VLEETQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1567 MENDFLRKRlqqceERLDSEMKARTELEQKlgeLQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRN--HELEK 1644
Cdd:TIGR00618 284 ERINRARKA-----APLAAHIKAVTQIEQQ---AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlHSQEI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1645 RQKKFDLQLAQALGESMFEKSLREKVSQenngvrweLGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVA 1724
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHT--------LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1725 SLKERVwELETNALEQQKIHSQQENTIKQLEQLRQRfeleiermkQMHQKDREDQEEeledvrqscqkrLRQLEMQLEQE 1804
Cdd:TIGR00618 428 HAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQ---------ESAQSLKEREQQ------------LQTKEQIHLQE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1805 YEEKQVALHEKHDLEGLIGTLCDQIGHrdfdvekrlrRDLRRTHALLSDV-QLLLATIEDSKTSISKEElekvhsqlEQS 1883
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIH----------PNPARQDIDNPGPlTRRMQRGEQTYAQLETSE--------EDV 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1884 EAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEdqgdlNDLMQKHKDLIAQSAADIGQ 1963
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-----LSEAEDMLACEQHALLRKLQ 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1964 IQ--ELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIICDLENKTEFQKVQIKRFEVLVIR--LRDS 2039
Cdd:TIGR00618 623 PEqdLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKemLAQC 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2040 MIKMGEEL----------------SRAVKAEAQQRENS------QYYQQRLEELKAEMQELAQREEEASRRCMELEKYvE 2097
Cdd:TIGR00618 703 QTLLRELEthieeydrefneienaSSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL-S 781
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 291327510 2098 ELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQ 2138
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1428-1983 |
1.26e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1428 LASLRPLLSSTLgtEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKgdvaCQALEsERAER 1507
Cdd:PRK03918 212 ISSELPELREEL--EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELE-EKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1508 LQALREVQE----LKTKYQQVQDALGEVQKQLEEAQQRIQGanLEEKpaggadewqmrldcaqmendflRKRLQQCEERL 1583
Cdd:PRK03918 285 LKELKEKAEeyikLSEFYEEYLDELREIEKRLSRLEEEING--IEER----------------------IKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1584 DSEMKARTELEQKLGELQS---AYEEAKKMAHQLKRKCHHLT-WDLEDTRVLLENQQSRNHELEKRQKKfdlqLAQALGE 1659
Cdd:PRK03918 341 EELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISK----ITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1660 SMFEKSLREKVSQENNGVRWE--LGQLQQQLEQKEQEASKLKQEVERLQGQKREllscasvgdqgvasLKERVWELETNA 1737
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKE--------------IEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1738 LEQQKIHSQQENTIKQLEQLRQRFELEiERMKQMHQKDREDQEEELEDVRQ---SCQKRLRQLEMQLE--QEYEEKQVAL 1812
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEYEKLKEkliKLKGEIKSLKKELEklEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1813 -HEKHDLEGLIGTLCDQIGHRDF----DVEKRLRRdLRRTHallsDVQLLLATIEDSKTSIsKEELEKVHSQLEQSEAKC 1887
Cdd:PRK03918 562 eKKLDELEEELAELLKELEELGFesveELEERLKE-LEPFY----NEYLELKDAEKELERE-EKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1888 EDALKTQKVLTADLENM--------HSELENVTRSKSlvdEQLYRLQFERADLLKRIDEDQGDLNDLmqkhkdliaqsAA 1959
Cdd:PRK03918 636 AETEKRLEELRKELEELekkyseeeYEELREEYLELS---RELAGLRAELEELEKRREEIKKTLEKL-----------KE 701
|
570 580
....*....|....*....|....
gi 291327510 1960 DIGQIQELQLQLEETKKEKQKLRE 1983
Cdd:PRK03918 702 ELEEREKAKKELEKLEKALERVEE 725
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1442-2109 |
2.43e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEEltllRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERL---QALREVQELK 1518
Cdd:PTZ00121 1233 EEAKKDAEE----AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1519 TKYQQVQDAlGEVQKQLEEAQQRIQGANLEEKPAGGADEwqmrldCAQMENDFLRKRLQQCEERLDSEMKARteleqklg 1598
Cdd:PTZ00121 1309 KKAEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAE------AAKAEAEAAADEAEAAEEKAEAAEKKK-------- 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1599 elqsayEEAKKMAHQLKRKCHHLTwDLEDTRVLLENQQSRNHELEKR--QKKFDLQLAQALGESMFEKSLREKVSQENNG 1676
Cdd:PTZ00121 1374 ------EEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAaaAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1677 VRWELGQLQQQLEQKEQEASKLKQEVERLQgQKRELLSCASVGDQGVASLKERVWELETNALEQQKI-HSQQENTIKQLE 1755
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAEEAKKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1756 QLRQRFEL-EIERMKQMHQKDREDQEEELEDVRQSCQKRLRQlemQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDF 1834
Cdd:PTZ00121 1526 EAKKAEEAkKADEAKKAEEKKKADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1835 DVEKRLRRDLRRTHALLSDVQLLLATIEDSKT--SISKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMH--SELEN 1910
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKK 1682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1911 VTRSKSLVDEQLYRLQFE--RADLLKRIDEDQgdlndlMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLR----EQ 1984
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEakKAEELKKKEAEE------KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeeEK 1756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1985 LHMAQLRIQylEQSTVERAIVSRQEAIICDLENKTEFQKVQIKR--------FEVLV-------IRLRDSMIKMGEELSR 2049
Cdd:PTZ00121 1757 KKIAHLKKE--EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkikdifdnFANIIeggkegnLVINDSKEMEDSAIKE 1834
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2050 AVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTD 2109
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1574-2126 |
3.91e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1574 KRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKmAHQLK-----RKCHHLTWDLEDTRVLLENQQSRNHELEKRQKK 1648
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERQAEKAER-YRELKeelkeLEAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1649 FDLQLAQAlgesmfEKSLRekvsqenngvrwelgqlqqqleQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKE 1728
Cdd:COG1196 258 LEAELAEL------EAELE----------------------ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1729 RV----WELETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLRQLEMQLEQE 1804
Cdd:COG1196 310 RRreleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1805 YEEKQVALHEKHDLEGLIGTLcDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLATIEDSKTSISKEELEKVHSQLEQSE 1884
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAE-EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1885 AKCEDALKTQKVLTADLEnmhsELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDL--------------------- 1943
Cdd:COG1196 468 LLEEAALLEAALAELLEE----LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligveaayeaaleaa 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1944 ---------NDLMQKHKDLIA-QSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIIC 2013
Cdd:COG1196 544 laaalqnivVEDDEVAAAAIEyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2014 DLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELE 2093
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590
....*....|....*....|....*....|...
gi 291327510 2094 KYVEELATVRQTLQTDLETSIRRIADLQAALEE 2126
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1566-2127 |
1.36e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1566 QMEN--DFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQL-------KRKCHHLTWDLE--DTRVLLEN 1634
Cdd:TIGR04523 37 QLEKklKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLndklkknKDKINKLNSDLSkiNSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1635 QQSRNHE-----LEKRQKKFDLQLAQALGESMFEKSLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQK 1709
Cdd:TIGR04523 117 EQKNKLEvelnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1710 REL---LSCASVGDQGVASLKERVWELE--TNALEQQKIHSQQEntIKQLEQLRQRFELEIERMKQMHQKDREDQEEELE 1784
Cdd:TIGR04523 197 LKLellLSNLKKKIQKNKSLESQISELKkqNNQLKDNIEKKQQE--INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1785 DVRQSCQK------RLRQLEMQLEQEYEEKQvalhekhdlEGLIGTLCDQIGHRD---FDVEKRLRRDLRRTHALLSDVQ 1855
Cdd:TIGR04523 275 ELEQNNKKikelekQLNQLKSEISDLNNQKE---------QDWNKELKSELKNQEkklEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1856 LLLATIEDSKTSISK--EELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLL 1933
Cdd:TIGR04523 346 QLKKELTNSESENSEkqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1934 KRIDEDQGDLNDLMQKHKDLIAqsaadigQIQELQLQLEETKKEKQKLREQLHMAQLRI----QYLEQSTVERAI----- 2004
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTN-------QDSVKELIIKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSkekel 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2005 ------VSRQEAIICDLENKTEFQKVQIKRFEVLVIR-------LRDSMIKMGEELSRAvKAEAQQRENsqyyQQRLEEL 2071
Cdd:TIGR04523 499 kklneeKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisdLEDELNKDDFELKKE-NLEKEIDEK----NKEIEEL 573
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 291327510 2072 KAEMQELAQREEeasrrcmELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEV 2127
Cdd:TIGR04523 574 KQTQKSLKKKQE-------EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1487-2157 |
1.37e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1487 ADERFKGDVACQALESERAERLQALREVQ--ELKTKYQQVQDAlGEVQKQLEEAQQRIQGANLEE-KPAGGADEWQMRLD 1563
Cdd:PTZ00121 1190 AEELRKAEDARKAEAARKAEEERKAEEARkaEDAKKAEAVKKA-EEAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARR 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1564 CAQMENDFLRK--RLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKmAHQLKRKCHHLTWDLEDTRVLLENQQSRNHE 1641
Cdd:PTZ00121 1269 QAAIKAEEARKadELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEA 1347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1642 LEKRQKKFDLQLAQALGESmfeKSLREKVSQENNgvrweLGQLQQQLEQKEQEASKLKQEVERLQGQKRELlscasvgdQ 1721
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKA---EAAEKKKEEAKK-----KADAAKKKAEEKKKADEAKKKAEEDKKKADEL--------K 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1722 GVASLKERVWELETNALEQQKihsqQENTIKQLEQLRQRFELeieRMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQL 1801
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKK----ADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1802 EQEYEEKQVALHEKHDlegligtlcdqiGHRDFDVEKRLRRDLRRThallsdvqlllatiEDSKTSiskEELEKVHSQLE 1881
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKAD------------EAKKAAEAKKKADEAKKA--------------EEAKKA---DEAKKAEEAKK 1535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1882 QSEA-KCEDALKTQKVLTADLENMHSELENVTRSKSlvDEQLYRLQFERADLLKRIDEDQgdLNDLMQKHKDLIAQSAAD 1960
Cdd:PTZ00121 1536 ADEAkKAEEKKKADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEE 1611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1961 IGQIQELQLQLEETKKEKQklrEQLHMAQLRIQYLEQstVERAIVSRQEaiicdlENKTEFQKVQIKRFEVLVIRLRDSM 2040
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEE---EKKKVEQLKKKEAEE--KKKAEELKKA------EEENKIKAAEEAKKAEEDKKKAEEA 1680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2041 IKMGEELSRAVKAEAQQRENSQYYQQ----------RLEELKAEMQ------ELAQRE-EEASRRCMELEKYVEELATVR 2103
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEElkkkeaeekkKAEELKKAEEenkikaEEAKKEaEEDKKKAEEAKKDEEEKKKIA 1760
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 291327510 2104 QTLQTDLETSIRRIADLQAALEEVVssDSDTESVQTAVDCSSRSGKegDNVSVI 2157
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEEL--DEEDEKRRMEVDKKIKDIF--DNFANI 1810
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1588-2126 |
2.54e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 69.62 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1588 KARTELEQKLGELQS---AYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEK 1664
Cdd:pfam02463 153 ERRLEIEEEAAGSRLkrkKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1665 SLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQG--------QKRELLSCASvgDQGVASLKERVWELETN 1736
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKeeekekklQEEELKLLAK--EEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1737 ALEQQKIHSQQENTIKQLEQL-------------------RQRFELEIERMKQMHQKDREDQEE---ELEDVRQSCQKRL 1794
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKkekeeieelekelkeleikREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1795 RQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCD--QIGHRDFDVEKRLRRDLRRTHALLSDVQLLLATIEDSKT-SISKE 1871
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEekKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1872 ELEKVHSQLEQSEAKCEDALKTQKVLTAD-LENMHSELENVTRSkSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKH 1950
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSqKESKARSGLKVLLA-LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1951 KDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLeqstverAIVSRQEAIICDLENKTEFQKVQIKRFE 2030
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-------AVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2031 VLVIRLRDSMIKMGeELSRAVKAEAQQRENSQYYQQRLEELKAEMQ-ELAQREEEASRRCMELEKYVEELATVRQTLQTD 2109
Cdd:pfam02463 623 KVVEGILKDTELTK-LKESAKAKESGLRKGVSLEEGLAEKSEVKASlSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570
....*....|....*..
gi 291327510 2110 LETSIRRIADLQAALEE 2126
Cdd:pfam02463 702 KKKEQREKEELKKLKLE 718
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1722-2143 |
3.81e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1722 GVASLKERvwELETnaleQQKIHSQQENtIKQLEQLRqrFELE-----IERMKQMHQKDRE--DQEEELEdvRQSCQKRL 1794
Cdd:TIGR02168 166 GISKYKER--RKET----ERKLERTREN-LDRLEDIL--NELErqlksLERQAEKAERYKElkAELRELE--LALLVLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1795 RQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQI-GHRDFDVEkrLRRDLRRTHALLSDVQLLLATIEDSKTSIsKEEL 1873
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSE--LEEEIEELQKELYALANEISRLEQQKQIL-RERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1874 EKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDL 1953
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1954 IAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIicdlenktefqkvqikrfevlv 2033
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL---------------------- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2034 irlrdsmIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTlQTDLETS 2113
Cdd:TIGR02168 450 -------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGI 521
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 291327510 2114 IRRIADL-------QAALEEVVSSDSD---TESVQTAVDC 2143
Cdd:TIGR02168 522 LGVLSELisvdegyEAAIEAALGGRLQavvVENLNAAKKA 561
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1501-2134 |
1.11e-10 |
|
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: 67.51 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1501 ESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGA-NLEEKPAGGADEWQMRLDCAQMENDF----LRKR 1575
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlQAETELCAEAEEMRARLAARKQELEEilheLESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1576 LQQCEERLDSEMKARTELEQKLGEL--QSAYEEAKKMAHQL-KRKCHHLTWDLEDTRVLLENQQSRNHE----LEKRQKK 1648
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLeeQLDEEEAARQKLQLeKVTTEAKIKKLEEDILLLEDQNSKLSKerklLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1649 FDLQLAQA------------LGESM---FEKSLR--EKVSQENNGVRwelgqlqqqlEQKEQEASKLKQEVERLQGQKRE 1711
Cdd:pfam01576 164 FTSNLAEEeekakslsklknKHEAMisdLEERLKkeEKGRQELEKAK----------RKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1712 LLSCASVGDQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQlrqrfELEIER-MKQMHQKDREDQEEELEDVRQSC 1790
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE-----DLESERaARNKAEKQRRDLGEELEALKTEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1791 QKRL------RQLEMQLEQEYEEKQVALHEK---HDLE---------GLIGTLCDQIghrdfDVEKRLRRDLRRT-HALL 1851
Cdd:pfam01576 309 EDTLdttaaqQELRSKREQEVTELKKALEEEtrsHEAQlqemrqkhtQALEELTEQL-----EQAKRNKANLEKAkQALE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1852 SDVQLL---LATIEDSKTSiSKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFE 1928
Cdd:pfam01576 384 SENAELqaeLRTLQQAKQD-SEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1929 RADLLKRIDEDQgdlnDLMQKHKDLIAQSAADIGQIQE----LQLQLEETKKEKQKLREQLHMAQLRIQYL------EQS 1998
Cdd:pfam01576 463 VSSLESQLQDTQ----ELLQEETRQKLNLSTRLRQLEDernsLQEQLEEEEEAKRNVERQLSTLQAQLSDMkkkleeDAG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1999 TVERAIVSRQ------EAIICDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQREnsqyYQQRLEELK 2072
Cdd:pfam01576 539 TLEALEEGKKrlqrelEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK----FDQMLAEEK 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291327510 2073 AEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDT 2134
Cdd:pfam01576 615 AISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDV 676
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1435-2135 |
2.06e-10 |
|
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: 66.74 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1435 LSSTLGTEQLRAK---------EEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERA 1505
Cdd:pfam01576 164 FTSNLAEEEEKAKslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1506 ERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQriqgaNLEEKPAGGADEWQMRLDCAQmENDFLRKRLqqcEERLDS 1585
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQE-----DLESERAARNKAEKQRRDLGE-ELEALKTEL---EDTLDT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1586 ---EMKARTELEQKLGELQSAYEEakkmahqlkrkchhltwdledtrvllenqQSRNHE---LEKRQKKFdlQLAQALGE 1659
Cdd:pfam01576 315 taaQQELRSKREQEVTELKKALEE-----------------------------ETRSHEaqlQEMRQKHT--QALEELTE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1660 SMfEKSLREKVSQENNgvRWELGQLQQQLEQKEQEASKLKQEVE----RLQGQKRELLSCASVGDQGVASLKERVWELET 1735
Cdd:pfam01576 364 QL-EQAKRNKANLEKA--KQALESENAELQAELRTLQQAKQDSEhkrkKLEGQLQELQARLSESERQRAELAEKLSKLQS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1736 ---------NALEQQKI---------HSQQENTIKQL-EQLRQRFELEiERMKQMH--QKDREDQEEELEDVRQSCQKRL 1794
Cdd:pfam01576 441 elesvssllNEAEGKNIklskdvsslESQLQDTQELLqEETRQKLNLS-TRLRQLEdeRNSLQEQLEEEEEAKRNVERQL 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1795 RQLEMQLEQeyeekqvalhEKHDLEGLIGTLcDQIGhrdfDVEKRLRRDLRRTHALLSDVQLLLATIEDSKTSISKE--- 1871
Cdd:pfam01576 520 STLQAQLSD----------MKKKLEEDAGTL-EALE----EGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEldd 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1872 ------ELEKVHSQLEQSEAKCEDALKTQKVLT---------ADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRi 1936
Cdd:pfam01576 585 llvdldHQRQLVSNLEKKQKKFDQMLAEEKAISaryaeerdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLR- 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1937 dedqGDLNDLMQKhKDLIAQSAADI--------GQIQELQLQLEETKKEKQ-----KLREQLHMAQLRIQYleqstvERA 2003
Cdd:pfam01576 664 ----AEMEDLVSS-KDDVGKNVHELerskraleQQVEEMKTQLEELEDELQatedaKLRLEVNMQALKAQF------ERD 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2004 IVSRQEAiicdLENKtefqkvqikrfevlvirlRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEelkAEMQELAQREE 2083
Cdd:pfam01576 733 LQARDEQ----GEEK------------------RRQLVKQVRELEAELEDERKQRAQAVAAKKKLE---LDLKELEAQID 787
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 291327510 2084 EASRRCMELEKYVEELATVRQTLQTDLEtsirriaDLQAALEEVVSSDSDTE 2135
Cdd:pfam01576 788 AANKGREEAVKQLKKLQAQMKDLQRELE-------EARASRDEILAQSKESE 832
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1439-1953 |
2.06e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1439 LGTEQLRAKEEELtLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALE------SERAERLQalr 1512
Cdd:PRK02224 176 LGVERVLSDQRGS-LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDeadevlEEHEERRE--- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1513 EVQELKTKYQQVQDALGEVQKQLEEAQQRIQGA-----NLEEKPAGGADEwqMRLDCAQMEN-----DFLRKRLQQCEER 1582
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLrerleELEEERDDLLAE--AGLDDADAEAvearrEELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1583 LdseMKARTELEQKLGELQSAYEEAKKM---AHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKR----QKKFDlQLAQ 1655
Cdd:PRK02224 330 L---EECRVAAQAHNEEAESLREDADDLeerAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRERFG-DAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1656 ALGESmfeKSLREKVSQENNGVRwelgqlqqqlEQKEQEASKLKQEVERLQgQKRELL------SCA-SVGDQG-VASLK 1727
Cdd:PRK02224 406 DLGNA---EDFLEELREERDELR----------EREAELEATLRTARERVE-EAEALLeagkcpECGqPVEGSPhVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1728 ERVWELETNALEQQKIHSQQENTIKQLEQLRQRFELE--IERMKQMHQ---KDREDQEEELEDVRQSCQkRLRQLEMQLE 1802
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEERREdleELIAERRETIEEKRERAE-ELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1803 QEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEKRLRRdlrrthalLSDVQLLLATIEDSKTSIskEELEKVHSQLEQ 1882
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--------LERIRTLLAAIADAEDEI--ERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1883 SEAKCEDALKTQKVLTADLENMH---------SELENVTRSKSLVDEQLYRLQFERADLLKRI---DEDQGDLNDLMQKH 1950
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEFdearieearEDKERAEEYLEQVEEKLDELREERDDLQAEIgavENELEELEELRERR 700
|
...
gi 291327510 1951 KDL 1953
Cdd:PRK02224 701 EAL 703
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1522-2142 |
2.15e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.68 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLEEAQQRIQGAN-LEEKPA----GGADEWQMRLDCAQMENDFL---RKRLQQCEERLdsemkaRTEL 1593
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNeLHEKQKfylrQSVIDLQTKLQEMQMERDAMadiRRRESQSQEDL------RNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1594 EQKLGELQSAYEEAKKMAHQLKRKchhltwdLEDTRVLLENQQSRNHELEKRQKKFDlqlaQALGESMFEKSLREKVSQE 1673
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQ-------IEQLRKMMLSHEGVLQEIRSILVDFE----EASGKKIYEHDSMSTMHFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1674 NNGvrwelgqlqqqleqkeQEASKLKQEVerlqgqkrellscasvgDQGVASLKERVWELEtNALEQQKIHSQQentikQ 1753
Cdd:pfam15921 217 SLG----------------SAISKILREL-----------------DTEISYLKGRIFPVE-DQLEALKSESQN-----K 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1754 LEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIgtlcdqighrd 1833
Cdd:pfam15921 258 IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTV----------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1834 fdveKRLRRDLRRTHALLSD------VQLLLATIEDSKTSISKEELEKVHSQL-EQSEAKCEDALKTQKVLTADLENmHS 1906
Cdd:pfam15921 327 ----SQLRSELREAKRMYEDkieeleKQLVLANSELTEARTERDQFSQESGNLdDQLQKLLADLHKREKELSLEKEQ-NK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1907 ELENVTRSKSLVDEQLYR------LQFERAD-LLKRI-DEDQGDlndlMQKHKDLIAQSAADIGQIQELQLQLEETKKEK 1978
Cdd:pfam15921 402 RLWDRDTGNSITIDHLRRelddrnMEVQRLEaLLKAMkSECQGQ----MERQMAAIQGKNESLEKVSSLTAQLESTKEML 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1979 QKLREQLHMAQLRIQYLEQsTVERAIVSRQE---------AIICDLENKTEFQKVQIKRFEVLVIRLRDSM-------IK 2042
Cdd:pfam15921 478 RKVVEELTAKKMTLESSER-TVSDLTASLQEkeraieatnAEITKLRSRVDLKLQELQHLKNEGDHLRNVQtecealkLQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2043 MGEElSRAVKAEAQQREN-SQYYQQRLEELKAEMQELAQREEEASRRCMELEKYveelatvrQTLQTDLETSIR----RI 2117
Cdd:pfam15921 557 MAEK-DKVIEILRQQIENmTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF--------KILKDKKDAKIReleaRV 627
|
650 660
....*....|....*....|....*
gi 291327510 2118 ADLQaaLEEVVSSDSDTESVQTAVD 2142
Cdd:pfam15921 628 SDLE--LEKVKLVNAGSERLRAVKD 650
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1442-2119 |
2.33e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLES------KITDLTSELADER----FKGDVACQALESERA------ 1505
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAlksrkkQMEKDNSELELKMekvfQGTDEQLNDLYHNHQrtvrek 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1506 --ERLQALREV-------QELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKpaggadEWQMRLDCAQMEND-FLRKR 1575
Cdd:TIGR00606 318 erELVDCQRELeklnkerRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ------SLATRLELDGFERGpFSERQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1576 LQQCEE--RLDSEMKARTeLEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSrnhelEKRQKKFDLQL 1653
Cdd:TIGR00606 392 IKNFHTlvIERQEDEAKT-AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----ELKFVIKELQQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1654 AQALGESMFE------KSLREKVSQENNGvrwelgqlqqqleqkeqEASKLKQEVERLQGQKRELLSCASVGDQGVASL- 1726
Cdd:TIGR00606 466 LEGSSDRILEldqelrKAERELSKAEKNS-----------------LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLn 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1727 --KERVWELETNALEQ----QKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKrLRQLE 1798
Cdd:TIGR00606 529 hhTTTRTQMEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKELAS-LEQNK 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1799 MQLEQEYEEKQVALHEKHDlegligTLCDQIGHRDFDVE-KRLRRDL---RRTHALLSDVQLLLAT-IEDSKTSIS---- 1869
Cdd:TIGR00606 608 NHINNELESKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIeksSKQRAMLAGATAVYSQfITQLTDENQsccp 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1870 --------KEELEKVHSQLEQSEAKCEDALKTQKVLTADLEN-----------MHSELENVTRSKSLVDEQLYRLQFERA 1930
Cdd:TIGR00606 682 vcqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKrrdemlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1931 DLLKRIDEDQGDLNDLMQKHKdLIAQSAADIGQIQELQLQLEETKKEKQKLREQLH-------MAQLRIQYLEQSTVERA 2003
Cdd:TIGR00606 762 RLKNDIEEQETLLGTIMPEEE-SAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrtVQQVNQEKQEKQHELDT 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2004 IVSRQEaiicDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAvkaeaqqrensQYYQQRLEELKAEMQELAQREE 2083
Cdd:TIGR00606 841 VVSKIE----LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR-----------QQFEEQLVELSTEVQSLIREIK 905
|
730 740 750
....*....|....*....|....*....|....*.
gi 291327510 2084 EASRRCMELEKYVEELATVRQTLQTDLETSIRRIAD 2119
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1498-1984 |
3.72e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1498 QALESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGADEWQmrldcaqmendFLRKRLQ 1577
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-----------ALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1578 QCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTrvlLENQQSRNHELEKRQKKFDLQLAQAL 1657
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1658 GEsmfEKSLREKVSQ-ENNGVRWELGQLQQQLEQKEQEASklkqEVERLQGQKRELLSCASVGDQGVASLKERVWELETN 1736
Cdd:COG4717 220 EE---LEELEEELEQlENELEAAALEERLKEARLLLLIAA----ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1737 ALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrLRQLEMQLEQEYEEKQVALHEKH 1816
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1817 DLEGLIGTLCDQIGhrdfDVEKRLRRDLRRthallsdVQLllatiedsktsisKEELEKVHSQLEQSEAKCEDALKtqkv 1896
Cdd:COG4717 372 IAALLAEAGVEDEE----ELRAALEQAEEY-------QEL-------------KEELEELEEQLEELLGELEELLE---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1897 lTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRID--EDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEET 1974
Cdd:COG4717 424 -ALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELL 502
|
490
....*....|
gi 291327510 1975 KKEKQKLREQ 1984
Cdd:COG4717 503 EEAREEYREE 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1442-2126 |
4.35e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.84 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTsELADERFKGDVACQALESERAERLQALREV-----QE 1516
Cdd:TIGR00606 224 DQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM-KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1517 LKTKYQQVQDALGEVQKQLEEAQQRIQGANLE-----------EKPAGGADEWQMRLDCAQMENDFLRKRLQQCEE---- 1581
Cdd:TIGR00606 303 LNDLYHNHQRTVREKERELVDCQRELEKLNKErrllnqektelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgf 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1582 -----------------RLDSEMKARTeLEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSrnhelEK 1644
Cdd:TIGR00606 383 ergpfserqiknfhtlvIERQEDEAKT-AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----EL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1645 RQKKFDLQLAQALGESMFE------KSLREKVSQENNGvrwelgqlqqqleqkeqEASKLKQEVERLQGQKRELLSCASV 1718
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILEldqelrKAERELSKAEKNS-----------------LTETLKKEVKSLQNEKADLDRKLRK 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1719 GDQGVASL---KERVWELETNALEQ----QKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQS 1789
Cdd:TIGR00606 520 LDQEMEQLnhhTTTRTQMEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKE 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1790 CQKrLRQLEMQLEQEYEEKQVALHEKHDlegligTLCDQIGHRDFDVE-KRLRRDLRRTHALLSDVQlllatiedSKTSI 1868
Cdd:TIGR00606 600 LAS-LEQNKNHINNELESKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIEKSSKQRAMLA--------GATAV 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1869 SKEELEKVHSQLEQSEAKCEDALKTQKVL---TADLENM-------HSELENVTRSKSLVDEQLYRLQFERADLLKRIDE 1938
Cdd:TIGR00606 665 YSQFITQLTDENQSCCPVCQRVFQTEAELqefISDLQSKlrlapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1939 DQGDLNDLMQKHKDLIAQSAADIGQiQELQLqleETKKEKQKLREQLHMAQLRIQ--YLEQSTVERAI---VSRQEAIIC 2013
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEE-QETLL---GTIMPEEESAKVCLTDVTIMErfQMELKDVERKIaqqAAKLQGSDL 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2014 DLENKTEFQKVQIKRFEVlvirlrDSMIKMGEELSRAVKaeaQQRENSQYYQQRLEELKAEMQELAqreeEASRRCMELE 2093
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHEL------DTVVSKIELNRKLIQ---DQQEQIQHLKSKTNELKSEKLQIG----TNLQRRQQFE 887
|
730 740 750
....*....|....*....|....*....|...
gi 291327510 2094 KYVEELATVRQTLQTDLETSIRRIADLQAALEE 2126
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEK 920
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1696-2145 |
4.82e-10 |
|
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: 65.58 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1696 SKLKQEVERLQGQKRELlscasvgDQGVASLKErvwelETNALEQQkIHSQQEnTIKQLEQLRQRF-----ELEiERMKQ 1770
Cdd:pfam01576 15 QKVKERQQKAESELKEL-------EKKHQQLCE-----EKNALQEQ-LQAETE-LCAEAEEMRARLaarkqELE-EILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1771 MhqKDREDQEEELEDVRQSCQKRLRQ----LEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDfDVEKRLRRDLRR 1846
Cdd:pfam01576 80 L--ESRLEEEEERSQQLQNEKKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1847 THALLSDVQLLLATIEDSKTSISKEEL--EKVHSQLEQSEAKCEDALKTQKVLTADLENMHSEL-ENVTRSKSLVDE--- 1920
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLSKLKNkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLqEQIAELQAQIAElra 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1921 QLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAqsaadigQIQELQLQLE-----ETKKEKQK--LREQLHMAQLRIQ 1993
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEA-------QISELQEDLEseraaRNKAEKQRrdLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1994 -YLEQSTVERAIVSRQEAIICDLENKTEFQKvqiKRFEVLVIRLR----DSMIKMGEELSRAVKAEAQQRENSQYYQQRL 2068
Cdd:pfam01576 310 dTLDTTAAQQELRSKREQEVTELKKALEEET---RSHEAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 2069 EELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVS--SDSDTESVQTAVDCSS 2145
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSllNEAEGKNIKLSKDVSS 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1498-2127 |
5.74e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1498 QALESERaERLQALREVQELKTKYQQVQDalgevqkQLEEAQQRIQGANLEEkpaggadewqmrldcAQMENDFLRKRLQ 1577
Cdd:COG4913 242 EALEDAR-EQIELLEPIRELAERYAAARE-------RLAELEYLRAALRLWF---------------AQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1578 QCEERLDSEMKARTELEQKLGELQSAYEEAKK--MAHQLKRKcHHLTWDLEDTRVLLENQQSRNHELEKRQKkfDLQLAQ 1655
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAqiRGNGGDRL-EQLEREIERLERELEERERRRARLEALLA--ALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1656 ALGESMFEKsLREKVSQEnngvrweLGQLQQQLEQKEQEASKLKQEVERLQGQKRELLScasvgdqgvaslkervwelET 1735
Cdd:COG4913 376 PASAEEFAA-LRAEAAAL-------LEALEEELEALEEALAEAEAALRDLRRELRELEA-------------------EI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1736 NALEQQK--IHSQQENTikqLEQLRQRFELEIERMK------QMHQKDREDQ-----------------EEELEDVRqsc 1790
Cdd:COG4913 429 ASLERRKsnIPARLLAL---RDALAEALGLDEAELPfvgeliEVRPEEERWRgaiervlggfaltllvpPEHYAAAL--- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1791 qKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLC---------------DQIGHRdFDV------------------- 1836
Cdd:COG4913 503 -RWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAgkldfkphpfrawleAELGRR-FDYvcvdspeelrrhpraitra 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1837 ----------EKRLRRDLRRTHALLSDVQLLLATIEDSKTSIsKEELEKVHSQLEQSEAKcEDALKTQKVLTADLENMHS 1906
Cdd:COG4913 581 gqvkgngtrhEKDDRRRIRSRYVLGFDNRAKLAALEAELAEL-EEELAEAEERLEALEAE-LDALQERREALQRLAEYSW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1907 ELENVTRskslVDEQLYRLQferaDLLKRIDEDQGDLNDLMQKHKDLIAQsaadigqIQELQLQLEETKKEKQKLREQLH 1986
Cdd:COG4913 659 DEIDVAS----AEREIAELE----AELERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1987 MAQLRIQYLeQSTVERAIVSRQEAIICDLENKteFQKVQI-KRFEVLVIRLRDSMIKMGEELSRAVKA--EAQQRENSQY 2063
Cdd:COG4913 724 QAEEELDEL-QDRLEAAEDLARLELRALLEER--FAAALGdAVERELRENLEERIDALRARLNRAEEEleRAMRAFNREW 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2064 ----------------YQQRLEELKAEmqELAQREEEASRRCMELEKyvEELATVRQTLQTDLETSIRRIADLQAALEEV 2127
Cdd:COG4913 801 paetadldadleslpeYLALLDRLEED--GLPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1476-2126 |
8.84e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1476 ESKITDlTSELADERFKGDVACQALESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEE----KP 1551
Cdd:PTZ00121 1102 EAKKTE-TGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDakkaEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1552 AGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAyEEAKKMAHQLKR----KCHHLTWDLED 1627
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA-EEAKKDAEEAKKaeeeRNNEEIRKFEE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1628 TRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLREKVSQENNGVRwelGQLQQQLEQKEQEASKLKQEVERLQG 1707
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK---AEEAKKADEAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1708 QKRELLSCASVGDqgvASLKERVWELETNALEQQKIHSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVR 1787
Cdd:PTZ00121 1337 KAEEAKKAAEAAK---AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKK 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1788 QSCQKRLRQlemQLEQEYEEKQVALHEKHDLEgligtlcdqighrdfdvEKRLRRDLRRTHALLSDVQLLLATIEDSKTS 1867
Cdd:PTZ00121 1413 AAAAKKKAD---EAKKKAEEKKKADEAKKKAE-----------------EAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1868 iskEELEKvhsqlEQSEAKCEDALKTQkvlTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGdlNDLM 1947
Cdd:PTZ00121 1473 ---DEAKK-----KAEEAKKADEAKKK---AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK--ADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1948 QKHKDLiaQSAADIGQIQELQlQLEETKK--EKQKLREQLHMAQLRIQYL---EQSTVERAIVSRQEAIICDLEN--KTE 2020
Cdd:PTZ00121 1540 KKAEEK--KKADELKKAEELK-KAEEKKKaeEAKKAEEDKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEEakKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2021 FQKV---QIKRFEVLVIRLRDSMIKMGEELSRA---VKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEK 2094
Cdd:PTZ00121 1617 EAKIkaeELKKAEEEKKKVEQLKKKEAEEKKKAeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
650 660 670
....*....|....*....|....*....|..
gi 291327510 2095 YVEELATVRQtLQTDLETSIRRIADLQAALEE 2126
Cdd:PTZ00121 1697 EAEEAKKAEE-LKKKEAEEKKKAEELKKAEEE 1727
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1500-2130 |
1.32e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.09 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1500 LESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQqriqgANLEEKPAGGADEWQMRLDCAQMENDFLRKRLQQC 1579
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETS-----AELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1580 EERLDSemkarteLEQKLGELQSAyeeakkmahqlkrkchhltwDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGE 1659
Cdd:pfam12128 321 RSELEA-------LEDQHGAFLDA--------------------DIETAAADQEQLPSWQSELENLEERLKALTGKHQDV 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1660 SMFEKSLREKVSQENNGVrweLGQLQQQLEQKEQEASKLKQEVER-LQGQKRELlscASVGDQGVASLKERVWELETNAL 1738
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRD---IAGIKDKLAKIREARDRQLAVAEDdLQALESEL---REQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1739 EQQKIHSQQENTIKQLEQLRQrFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEM--QLEQEYEEKQVALHE-K 1815
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLEN-FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEAlrQASRRLEERQSALDElE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1816 HDLEGLIGTLC-----------DQIGhRDFDVEKRLRRDL--RRTHALLSD------VQLLLATIEDSKTSISKEELEkv 1876
Cdd:pfam12128 527 LQLFPQAGTLLhflrkeapdweQSIG-KVISPELLHRTDLdpEVWDGSVGGelnlygVKLDLKRIDVPEWAASEEELR-- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1877 hSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVdeqlyrlqferADLLKRIDEDQGDLNDLMQKHKDLIAQ 1956
Cdd:pfam12128 604 -ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA-----------RTALKNARLDLRRLFDEKQSEKDKKNK 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1957 SAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTveraivsrqeaiicdleNKTEFQKVQIKRFEVLVIRL 2036
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREART-----------------EKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2037 RDSMIKMGEELSRAVKAEAQQRENS----QYYQQRLEELKAEMQELAQREEEASRRCMELEKYV----EELATVRQTLQT 2108
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDlaslGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqETWLQRRPRLAT 814
|
650 660
....*....|....*....|..
gi 291327510 2109 DLETSIRRIADLQAALEEVVSS 2130
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIAD 836
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1695-1997 |
1.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1695 ASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELETnalEQQKIHSQQENTIKQLEQLRQR----------FELE 1764
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE---DLSSLEQEIENVKSELKELEARieeleedlhkLEEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1765 IERMKQM--HQKDREDQEE--ELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEKrL 1840
Cdd:TIGR02169 781 LNDLEARlsHSRIPEIQAElsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-L 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1841 RRDLRRTHALLSDVQLLLATIEDSKTSISKE------ELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSEL----EN 1910
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKErdeleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseieDP 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1911 VTRSKSLVDEQLY--RLQFERADLLKRIdEDQGDLNDLMqkhkdliaqsaadIGQIQELQLQLEETKKEKQKLREQLHMA 1988
Cdd:TIGR02169 940 KGEDEEIPEEELSleDVQAELQRVEEEI-RALEPVNMLA-------------IQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
....*....
gi 291327510 1989 QLRIQYLEQ 1997
Cdd:TIGR02169 1006 LERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1442-1673 |
1.58e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERfkgdvacqaLESERAERLQALREVQELKTKY 1521
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE---------EALNDLEARLSHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGA--------DEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTEL 1593
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqelqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1594 EQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLrEKVSQE 1673
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAE 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1442-2088 |
2.05e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADerfkgdvacqaLESERAERLQalREVQELKTKY 1521
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----------NGGDRLEQLE--REIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLeeaqqriqgANLEEKPAGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQ 1601
Cdd:COG4913 355 EERERRRARLEALL---------AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1602 SAYEEAKKM-----AHQLKRK---CHHLTWDLEDTRVLLENQQSRNHE------LEK--RQKKFDLqlaqaLGESMFEKS 1665
Cdd:COG4913 426 AEIASLERRksnipARLLALRdalAEALGLDEAELPFVGELIEVRPEEerwrgaIERvlGGFALTL-----LVPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1666 LREKVSQENNG-------VRWELGQLQQQLEQKEQEASKLK-------QEVERLQGQKRELLSCASVGD----------Q 1721
Cdd:COG4913 501 ALRWVNRLHLRgrlvyerVRTGLPDPERPRLDPDSLAGKLDfkphpfrAWLEAELGRRFDYVCVDSPEElrrhpraitrA 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1722 GVASLKERVWELETnaleQQKIHSQ---QENTIKQLEQLRQrfelEIERMKQMHQKDREdQEEELEDVRQSCQKRLRQLE 1798
Cdd:COG4913 581 GQVKGNGTRHEKDD----RRRIRSRyvlGFDNRAKLAALEA----ELAELEEELAEAEE-RLEALEAELDALQERREALQ 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1799 MQLEQEYEEKQVALHEKHdleglIGTLCDQIGH--RDFDVEKRLRRDLRRTHALLSDVQLLLATIEDSKTSIsKEELEKV 1876
Cdd:COG4913 652 RLAEYSWDEIDVASAERE-----IAELEAELERldASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQA 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1877 HSQLEQSEAKCEDALKTQKV-LTADLENMHSELENVTRSKSLVDeqlyRLQFERADLLKRIDEDQGDLNDLMQKHK---- 1951
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERAMRAFNrewp 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1952 ----DLIAqSAADIGQIQELQLQLEETK--KEKQKLREQLH------MAQLrIQYLEQStvERAIVSRQEAIicdleNKt 2019
Cdd:COG4913 802 aetaDLDA-DLESLPEYLALLDRLEEDGlpEYEERFKELLNensiefVADL-LSKLRRA--IREIKERIDPL-----ND- 871
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 2020 EFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKA--EAQQRENSQYYQQRLEELKAEMQELAQREEEASRR 2088
Cdd:COG4913 872 SLKRIPFGPGRYLRLEARPRPDPEVREFRQELRAvtSGASLFDEELSEARFAALKRLIERLRSEEEESDRR 942
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1437-2137 |
2.51e-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: 63.32 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1437 STLGTEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADErfKGDVACQALESERAERlQALREVQE 1516
Cdd:pfam12128 261 SHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAA--DAAVAKDRSELEALED-QHGAFLDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1517 LKTKYQQVQDALGEVQKQLEEAQQRIQGanLEEKPAGGADEWQMR-----LDCAQMENDFLRKRLQQCEER--------- 1582
Cdd:pfam12128 338 DIETAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRrskikEQNNRDIAGIKDKLAKIREARdrqlavaed 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1583 ----LDSEMkaRTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDlEDTRVLLENQQSRNH----ELEKRQKKF-DLQL 1653
Cdd:pfam12128 416 dlqaLESEL--REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIErareEQEAANAEVeRLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1654 AQALGESMFEKSLrEKVSQENNGVRWELGQLQQQLEQKEQEASKL-----------KQEVERLQGqkRELL--------- 1713
Cdd:pfam12128 493 ELRQARKRRDQAS-EALRQASRRLEERQSALDELELQLFPQAGTLlhflrkeapdwEQSIGKVIS--PELLhrtdldpev 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1714 SCASVGDQ----GVA----------------SLKERVWELETNALEQQKIHSQQEntiKQLEQLRQRFE---LEIERMKQ 1770
Cdd:pfam12128 570 WDGSVGGElnlyGVKldlkridvpewaaseeELRERLDKAEEALQSAREKQAAAE---EQLVQANGELEkasREETFART 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1771 MHQKDREDQeEELEDVRQSCQkrlRQLEMQLEqeyEEKQVALHEKHDLEGLIGTLcdQIGHRDFDVEkrLRRDLRRTHAL 1850
Cdd:pfam12128 647 ALKNARLDL-RRLFDEKQSEK---DKKNKALA---ERKDSANERLNSLEAQLKQL--DKKHQAWLEE--QKEQKREARTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1851 LSDVQLLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKT---------QKV--LTADLENMHSELEN--VTRSKSL 1917
Cdd:pfam12128 716 KQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRdlaslgvdpDVIakLKREIRTLERKIERiaVRRQEVL 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1918 VDEQLYRLQF--ERADLLKRIDEDQGDLNDLMQkhkDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYL 1995
Cdd:pfam12128 796 RYFDWYQETWlqRRPRLATQLSNIERAISELQQ---QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1996 ----EQSTVERAIVSRQEAIIC--DLENKTEFQKVQIKRFevlvIRLRDSMIKmgeELSRAVKAEAQQ--RENSQYYQQR 2067
Cdd:pfam12128 873 atlkEDANSEQAQGSIGERLAQleDLKLKRDYLSESVKKY----VEHFKNVIA---DHSGSGLAETWEslREEDHYQNDK 945
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 2068 LEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTD----LETSIRRIADLQAALEEVVSSDSDTESV 2137
Cdd:pfam12128 946 GIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGEEAFFEGV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1700-2133 |
3.44e-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: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1700 QEVERLQgQKRELLSCASVGDQGVASLKERVWELET-----NALEQQKIHSQQENTIKQLEQLRQRFELEIERmkqmHQK 1774
Cdd:COG4913 242 EALEDAR-EQIELLEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELER----LEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1775 DREDQEEELEDVRQSCQKR-LRQLEmQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLsd 1853
Cdd:COG4913 317 RLDALREELDELEAQIRGNgGDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL-- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1854 vqlllatiedsktsiskEELEKVHSQLEQSEAKCEDALKTqkvLTADLENMHSELENVTRSKSLVDEQLYRLqfeRADLL 1933
Cdd:COG4913 394 -----------------EALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSNIPARLLAL---RDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1934 KRIDEDQGDLN---DLMQ-KHKDLIAQSAAD--IGQiQELQLqLEETKKEKQKLR--EQLHMaQLRIQYleqstvERAIV 2005
Cdd:COG4913 451 EALGLDEAELPfvgELIEvRPEEERWRGAIErvLGG-FALTL-LVPPEHYAAALRwvNRLHL-RGRLVY------ERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2006 SRQEAIICDLENKTEFQKVQIKRFEVLViRLRDSMIKMG--------EELSRAVKA----------------EAQQRENS 2061
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLDFKPHPFRA-WLEAELGRRFdyvcvdspEELRRHPRAitragqvkgngtrhekDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2062 QYY-----QQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQT---------DLETSIRRIADLQAALEEV 2127
Cdd:COG4913 601 RYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERL 680
|
....*.
gi 291327510 2128 VSSDSD 2133
Cdd:COG4913 681 DASSDD 686
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1445-1914 |
4.40e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.50 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1445 RAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSEladerfKGDVACQALESERAERLqALREVQELKTKYQQV 1524
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSS------KDDVGKNVHELERSKRA-LEQQVEEMKTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1525 QDALGEVqkqlEEAQQRIQgANLEEKPAGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKART-------ELEQKL 1597
Cdd:pfam01576 705 EDELQAT----EDAKLRLE-VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAqavaakkKLELDL 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1598 GELQS-------AYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLREKV 1670
Cdd:pfam01576 780 KELEAqidaankGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQA 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1671 SQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELeTNALEQQKIHSQQ-EN 1749
Cdd:pfam01576 860 QQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQL-TTELAAERSTSQKsES 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1750 TIKQLEqlRQRFELEIeRMKQMHQKDREDQEEELedvrQSCQKRLRQLEMQLEQEYEEKQVAlhekhdlegligtlcdqi 1829
Cdd:pfam01576 939 ARQQLE--RQNKELKA-KLQEMEGTVKSKFKSSI----AALEAKIAQLEEQLEQESRERQAA------------------ 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1830 ghrdfdvekrlRRDLRRTHALLSDVqLLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELE 1909
Cdd:pfam01576 994 -----------NKLVRRTEKKLKEV-LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELD 1061
|
....*
gi 291327510 1910 NVTRS 1914
Cdd:pfam01576 1062 DATES 1066
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1755-2124 |
9.06e-09 |
|
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: 60.68 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1755 EQLRQRFELEieRMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLcdQIGHRDF 1834
Cdd:pfam07888 38 ECLQERAELL--QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL--SASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1835 DVEKRLRRDLRRTHallsdVQLLLATIEDSKT----SISKE-ELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELe 1909
Cdd:pfam07888 114 SEEKDALLAQRAAH-----EARIRELEEDIKTltqrVLEREtELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1910 nvtRSKSLVDEQLYRLQFERADLLKRIdedQGDLNDLMQKhkdliaqsaadIGQIQELQLQLEETKKEKQKLREQLHMAQ 1989
Cdd:pfam07888 188 ---RSLSKEFQELRNSLAQRDTQVLQL---QDTITTLTQK-----------LTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1990 LRIQYLEQSTveRAIVSRQEAIICDLeNKTEFQKVQikrfevLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLE 2069
Cdd:pfam07888 251 RKVEGLGEEL--SSMAAQRDRTQAEL-HQARLQAAQ------LTLQLADASLALREGRARWAQERETLQQSAEADKDRIE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 2070 ELKAEMQELAQREEEASrrcMELEKYVEELATVRQTLQTDLETSIRRIADLQAAL 2124
Cdd:pfam07888 322 KLSAELQRLEERLQEER---MEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1449-1895 |
1.01e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1449 EELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSEladerfkgdVACQALESERAERLQALrEVQELKTKYQQVQDAL 1528
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE---------KEAQMEELNKAKAAHSF-VVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1529 GEVQKQLEEAQQRIQGANLE-EKPAGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEM---KARTELEQKLGELQSAY 1604
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMElQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKqfeKIAEELKGKEQELIFLL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1605 EEAKKMAHQL-------KRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQlAQALGESMFEKSLREKVSQEN-NG 1676
Cdd:pfam05483 446 QAREKEIHDLeiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE-NKELTQEASDMTLELKKHQEDiIN 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1677 VRWELGQLQQQLEQKEQEASKLKQEVERLQG---QKRELLSCA-SVGDQGVASLKERVWELETNALEQQK----IHSQQE 1748
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREefiQKGDEVKCKlDKSEENARSIEYEVLKKEKQMKILENkcnnLKKQIE 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1749 NTIKQLEQLRQ------------------------RFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLE------ 1798
Cdd:pfam05483 605 NKNKNIEELHQenkalkkkgsaenkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEkakaia 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1799 ---MQLEQEYEEK-------QVALHEKHDLEgligtlCDQI-GHRDFDVEKRLRRDLRRTHALLSdVQLLLATIEDSKTS 1867
Cdd:pfam05483 685 deaVKLQKEIDKRcqhkiaeMVALMEKHKHQ------YDKIiEERDSELGLYKNKEQEQSSAKAA-LEIELSNIKAELLS 757
|
490 500
....*....|....*....|....*....
gi 291327510 1868 ISKE-ELEKVHSQLEQSEAKCEDALKTQK 1895
Cdd:pfam05483 758 LKKQlEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1833-2141 |
1.17e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1833 DFDVEK-RLRRDLRRTHALLSDVQLLLATIedsktsisKEELEKVhsQLEQSEAKCEDALKTQK------VLTADLENMH 1905
Cdd:TIGR02169 167 EFDRKKeKALEELEEVEENIERLDLIIDEK--------RQQLERL--RREREKAERYQALLKEKreyegyELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1906 SELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAqsaadiGQIQELQLQLEETKKEKQKLREQL 1985
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------EEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1986 HMAQLRIQYLEQStvERAIVSRQEAIICDLEN-KTEFQKVQIKRfevlvirlrdsmIKMGEELsravkAEAQQRENSqyY 2064
Cdd:TIGR02169 311 AEKERELEDAEER--LAKLEAEIDKLLAEIEElEREIEEERKRR------------DKLTEEY-----AELKEELED--L 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2065 QQRLEELKAEMQELaqREEEASRRcMELEKYVEELATVRQTLQTDLETSIR---RIADLQAAL----EEVVSSDSDTESV 2137
Cdd:TIGR02169 370 RAELEEVDKEFAET--RDELKDYR-EKLEKLKREINELKRELDRLQEELQRlseELADLNAAIagieAKINELEEEKEDK 446
|
....
gi 291327510 2138 QTAV 2141
Cdd:TIGR02169 447 ALEI 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1696-2132 |
1.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1696 SKLKQEVERL---QGQKREL-LSCASVGDQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQLRQrfelEIERMKQM 1771
Cdd:COG4717 49 ERLEKEADELfkpQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE----ELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1772 HQKDREDQE-EELEDVRQSCQKRLRQLEMQLE--QEYEEKQVALHEKH-DLEGLIGTLCDQIghrDFDVEKRLRRDLRRT 1847
Cdd:COG4717 125 LQLLPLYQElEALEAELAELPERLEELEERLEelRELEEELEELEAELaELQEELEELLEQL---SLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1848 HALLSDVQLLLATIEDSKtsiskEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMhseLENVTRSKSLVDEQLYRLQF 1927
Cdd:COG4717 202 EELQQRLAELEEELEEAQ-----EELEELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1928 ERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQlQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSR 2007
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE-ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2008 QEAIIcDLENKTEFQKVQIKRFEVLV---IRLRDSMIKMGEELSRAVKAEAQQREnsqyYQQRLEELKAEMQELAQREEE 2084
Cdd:COG4717 353 LREAE-ELEEELQLEELEQEIAALLAeagVEDEEELRAALEQAEEYQELKEELEE----LEEQLEELLGELEELLEALDE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 291327510 2085 AsrrcmELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDS 2132
Cdd:COG4717 428 E-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1435-1965 |
1.52e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.52 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1435 LSSTLGTEQLRAKEEELTLLRQkLQKSENS----RSELRQNTDLLESKITDLTSELAderfkgdVACQALESERAERLQA 1510
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQ-LSDLESTvsqlRSELREAKRMYEDKIEELEKQLV-------LANSELTEARTERDQF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1511 LREVQELKTKYQQVQDALGEVQKQLeeAQQRIQGANLEEKPAGGA---DEWQMRLDCAQMENDFLRKRLQ----QCEERL 1583
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKEL--SLEKEQNKRLWDRDTGNSitiDHLRRELDDRNMEVQRLEALLKamksECQGQM 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1584 DSEMKA---RTELEQKLGELQSAYEEAKKMAHQL--------------KRKCHHLTWDLEDTRVLLEnqqSRNHELEKRQ 1646
Cdd:pfam15921 447 ERQMAAiqgKNESLEKVSSLTAQLESTKEMLRKVveeltakkmtlessERTVSDLTASLQEKERAIE---ATNAEITKLR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1647 KKFDLQLAQ-------------------ALGESMFEK-SLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQ 1706
Cdd:pfam15921 524 SRVDLKLQElqhlknegdhlrnvqteceALKLQMAEKdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1707 GQKRELLSCASVGDQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQE------ 1780
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkrnf 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1781 ----EELEDVRQSCQKRLRQLEMQLEQEYEE-KQVALHEKHDLEGLIGtlcdqighrdfdVEKRLRRDLRRTHALLSDVQ 1855
Cdd:pfam15921 684 rnksEEMETTTNKLKMQLKSAQSELEQTRNTlKSMEGSDGHAMKVAMG------------MQKQITAKRGQIDALQSKIQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1856 LLlatiEDSKTSISKEElekvhSQLEQSEAKCEDALKTqkvLTADLENMHSELEnVTRSkslvdeQLYRLQFERADLLKR 1935
Cdd:pfam15921 752 FL----EEAMTNANKEK-----HFLKEEKNKLSQELST---VATEKNKMAGELE-VLRS------QERRLKEKVANMEVA 812
|
570 580 590
....*....|....*....|....*....|....*..
gi 291327510 1936 IDEDQ---GDLNDLMQKHKD----LIAQSAADIGQIQ 1965
Cdd:pfam15921 813 LDKASlqfAECQDIIQRQEQesvrLKLQHTLDVKELQ 849
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1442-1991 |
1.64e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSEL-------RQNTDLLESKitdltSELADERFKGDVACQ-ALESERAE-RLQALR 1512
Cdd:pfam05483 233 KEINDKEKQVSLLLIQITEKENKMKDLtflleesRDKANQLEEK-----TKLQDENLKELIEKKdHLTKELEDiKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1513 EVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANlEEKPAGGADEWQMRLDCAQMEnDFLRKRLQQCEERLDSEMKARTE 1592
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELN-KAKAAHSFVVTEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITME 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1593 LEQKLGELqsayEEAKKMAHQLKRKCHHLTWDL-EDTRVLLENQQSrnhelekrqKKFDLQLAQALGESMFEKSLREKvs 1671
Cdd:pfam05483 386 LQKKSSEL----EEMTKFKNNKEVELEELKKILaEDEKLLDEKKQF---------EKIAEELKGKEQELIFLLQAREK-- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1672 qENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCAsvgDQGVASLKERVWELETNALEQQKihsQQENTI 1751
Cdd:pfam05483 451 -EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC---DKLLLENKELTQEASDMTLELKK---HQEDII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1752 KQLEQlRQRFELEIERMKQMHQKDREdqeeELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGH 1831
Cdd:pfam05483 524 NCKKQ-EERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1832 RDFDVEKRLR--RDLRRTHALLSDVqlllATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKT-QKVLTADLENMHSEL 1908
Cdd:pfam05483 599 LKKQIENKNKniEELHQENKALKKK----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKKISEEKLL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1909 ENVTRSKSLVDEQLyRLQFEradLLKRIDEDQGDLNDLMQKHK---DLIA----------------QSAADIGQIQEL-- 1967
Cdd:pfam05483 675 EEVEKAKAIADEAV-KLQKE---IDKRCQHKIAEMVALMEKHKhqyDKIIeerdselglyknkeqeQSSAKAALEIELsn 750
|
570 580 590
....*....|....*....|....*....|....
gi 291327510 1968 ----------QLQLEETKKEKQKLREQLHMAQLR 1991
Cdd:pfam05483 751 ikaellslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1442-1842 |
1.73e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERfkgdvacQALESERaERLQALREVQELKTKY 1521
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLE-------QDYQAAS-DHLNLVQTALRQQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLEEAQQRIQGANleekpaGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLgelq 1601
Cdd:PRK04863 351 ERYQADLEELEERLEEQNEVVEEAD------EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV---- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1602 SAYEEAKKMahqlkrkCHHLTWDLEDTRVLLEnqQSRNHELEKRQKKfdLQLAQALGESMFEKSLREKVSQenngvrwel 1681
Cdd:PRK04863 421 QALERAKQL-------CGLPDLTADNAEDWLE--EFQAKEQEATEEL--LSLEQKLSVAQAAHSQFEQAYQ--------- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1682 gqlqqqleqkeqEASKLKQEVERLQGQK--RELLSCAS---VGDQGVASLKERVWELETNALEQQ----------KIHSQ 1746
Cdd:PRK04863 481 ------------LVRKIAGEVSRSEAWDvaRELLRRLReqrHLAEQLQQLRMRLSELEQRLRQQQraerllaefcKRLGK 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1747 QENTIKQLEQLRQRFELEIERMKQMHQKDREDQeEELEDVRQSCQKRLRQLEMQ----------LEQEYEEKQVALHEKH 1816
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLESLSESVSEARERR-MALRQQLEQLQARIQRLAARapawlaaqdaLARLREQSGEEFEDSQ 627
|
410 420 430
....*....|....*....|....*....|....*.
gi 291327510 1817 DLEGLIGTLC----------DQIGHRDFDVEKRLRR 1842
Cdd:PRK04863 628 DVTEYMQQLLerereltverDELAARKQALDEEIER 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1439-2100 |
1.90e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.45 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1439 LGTEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTseLADERFKGDVACQALESERAERLQALREVQELK 1518
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1519 TKYQQvQDALGEVQKQLE-------EAQQRIQGANleekpaggadeWQMRLDCAQMENDFLRKRlqQCEERLDSEMKART 1591
Cdd:TIGR00606 522 QEMEQ-LNHHTTTRTQMEmltkdkmDKDEQIRKIK-----------SRHSDELTSLLGYFPNKK--QLEDWLHSKSKEIN 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1592 ELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLL------ENQQSRNHELEKRQKKFDLQLAQALGESMFEKS 1665
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1666 LREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELlscasvgDQGVASLKERVWELETNALEQQKIHS 1745
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST-------ESELKKKEKRRDEMLGLAPGRQSIID 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1746 QQENTIKQLEQLRQRFELEIERMK-----QMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEyeEKQVAlHEKHDLEG 1820
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKndieeQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDV--ERKIA-QQAAKLQG 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1821 LIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLATIEDSKTSIskEELEKVHSQLEQSEAKCEDALKTQKVLTAD 1900
Cdd:TIGR00606 818 SDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI--QHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1901 LENMHSELENVTRSKSLVDEQ-------LYRLQFERADLLKRIDED----QGDLNDLMQKHKDLIAQSAADIGQIQE--- 1966
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQdspletfLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGYMKDIENKIQDgkd 969
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1967 ------------LQLQLEETKKEKQKLREQLHMAQLRI--QYLEQSTVERAIVSRQeaiicdLENKTEFQKVQIKRF--- 2029
Cdd:TIGR00606 970 dylkqketelntVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRK------RENELKEVEEELKQHlke 1043
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291327510 2030 --EVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELA 2100
Cdd:TIGR00606 1044 mgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1504-1814 |
2.03e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1504 RAERLQALREVQElKTKYQQVQDALGEVQKQLEEAQQRIqganleEKPAGGADEWQMRLDCAQMENDFLRKRLQQCE--- 1580
Cdd:TIGR02169 660 RAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSEL------RRIENRLDELSQELSDASRKIGEIEKEIEQLEqee 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1581 ----ERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLEN---QQSRNH--ELEKRQKKFDL 1651
Cdd:TIGR02169 733 eklkERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsriPEIQAElsKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1652 QLA---QALGESMFEKSLREKVSQEnngvrwelgqLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKE 1728
Cdd:TIGR02169 813 RLReieQKLNRLTLEKEYLEKEIQE----------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1729 RVWELETNALEQQKIHSQQENTIKQLE-----------QLRQRFELEIERMKQMHQKDREDQE--------EELEDVRQS 1789
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEaqiekkrkrlsELKAKLEALEEELSEIEDPKGEDEEipeeelslEDVQAELQR 962
|
330 340
....*....|....*....|....*...
gi 291327510 1790 CQKRLRQLE---MQLEQEYEEKQVALHE 1814
Cdd:TIGR02169 963 VEEEIRALEpvnMLAIQEYEEVLKRLDE 990
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1443-1990 |
2.38e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1443 QLRAKEEELTLLRQKLQKSENSRSELRQNTDLL------ESKITDLTSELADERfkgDVACQALESEraerlQALREVQE 1516
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtlhsqEIHIRDAHEVATSIR---EISCQQHTLT-----QHIHTLQQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1517 LKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAggadewQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQK 1596
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL------QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1597 LGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDlQLAQALGESMFEKSLREKVSQENNG 1676
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQ 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1677 VRWELGQLQQQLEQKEQEASKLKQEVERLQ------GQKRELLSCASVGDQGVASLKERVWELETNALEQQKIHSQQENT 1750
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQqsfsilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1751 IKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQK----RLRQLEMQLEQEYEEKQVAL-HEKHDLEGLIGTL 1825
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehalSIRVLPKELLASRQLALQKMqSEKEQLTYWKEML 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1826 --CDQIGHRDFDVEKRLRRDLRR----THALLSDVQLLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLT- 1898
Cdd:TIGR00618 700 aqCQTLLRELETHIEEYDREFNEienaSSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAe 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1899 -----ADLENMHSELENVTRSKSLVDEQLYrlQFERADLLKRIDEDQGDLNDLMQKHKdLIAQSAADIGQIQELQLQLEE 1973
Cdd:TIGR00618 780 lshlaAEIQFFNRLREEDTHLLKTLEAEIG--QEIPSDEDILNLQCETLVQEEEQFLS-RLEEKSATLGEITHQLLKYEE 856
|
570
....*....|....*...
gi 291327510 1974 TKKEK-QKLREQLHMAQL 1990
Cdd:TIGR00618 857 CSKQLaQLTQEQAKIIQL 874
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1457-1928 |
2.98e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 59.10 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1457 KLQKSENSRSELRQNTDLLESKITDLTSELAderfkgdvacQALESERAERLqalrEVQELKTKYQQVQ----------- 1525
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEELD----------ELLESEEKNRE----EVEELKDKYRELRktllanrfsyg 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1526 DALGEVQKQLEEAQQRIQGANlEEKPAGGADEWQMRLDCAQMENDFLRKRLQQCEERLDsemKARTELEQKLGELQSAYE 1605
Cdd:pfam06160 146 PAIDELEKQLAEIEEEFSQFE-ELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYE---ELKTELPDQLEELKEGYR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1606 EAKKMAHQLKRKchhltwDLEDTRVLLENQqsrNHELEKRQKKFDLqlaqalgesmfekslrEKVSQENngvrwelgqlq 1685
Cdd:pfam06160 222 EMEEEGYALEHL------NVDKEIQQLEEQ---LEENLALLENLEL----------------DEAEEAL----------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1686 qqleqkeqeaSKLKQEVERLQgqkrELLscasvgdqgvaslkervwELETNAleQQKIHSQQENTIKQLEQLRQRF---E 1762
Cdd:pfam06160 266 ----------EEIEERIDQLY----DLL------------------EKEVDA--KKYVEKNLPEIEDYLEHAEEQNkelK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1763 LEIERMKQMHQKDredqEEELEDVRQScQKRLRQLE---MQLEQEYEEKQVALHE-KHDLEGLIGTLcDQI--GHRDFDV 1836
Cdd:pfam06160 312 EELERVQQSYTLN----ENELERVRGL-EKQLEELEkryDEIVERLEEKEVAYSElQEELEEILEQL-EEIeeEQEEFKE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1837 E-KRLRRDLRRTHALLSDVQLLLATIedsKTSISK------------------EELEKVHSQLEQS-------EAKCEDA 1890
Cdd:pfam06160 386 SlQSLRKDELEAREKLDEFKLELREI---KRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVplnmdevNRLLDEA 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 291327510 1891 lktqkvlTADLENMHSELENVTRSKSLVdEQL------YRLQFE 1928
Cdd:pfam06160 463 -------QDDVDTLYEKTEELIDNATLA-EQLiqyanrYRSSNP 498
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1426-1609 |
4.96e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1426 GLLASLRPLLSStlgteqLRAKEEELTLLRQKLQKSENSRSELRQNTDLLES--------------KITDLTSELaDERF 1491
Cdd:PRK04863 918 NALAQLEPIVSV------LQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfsyedaaEMLAKNSDL-NEKL 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1492 KGDVAcqALESERAERLQALREVQELKTKYQQVQDALGE----VQKQLEEAQQRIQG------ANLEEKPAGGADEWQMR 1561
Cdd:PRK04863 991 RQRLE--QAEQERTRAREQLRQAQAQLAQYNQVLASLKSsydaKRQMLQELKQELQDlgvpadSGAEERARARRDELHAR 1068
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 291327510 1562 LDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKK 1609
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1924-2126 |
5.65e-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: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1924 RLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQstvera 2003
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2004 ivsrqeaiicDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREE 2083
Cdd:COG4942 98 ----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 291327510 2084 EASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEE 2126
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
55-472 |
7.51e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 55 RKAAAFTAPEVE-IPAVPTNQTNKTNNVPKPGSQQTSQDSSSTTQNSADIPGKEPPGAGDkdstPVTS-TSGERPQESGP 132
Cdd:PHA03247 2631 PSPAANEPDPHPpPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARP----TVGSlTSLADPPPPPP 2706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 133 TGTPAKRTLpfkrgvrrgdVLLMVAKLDPELAKADQKVQPRD-VPVDKTPAPAKDSGGTKKGVTTGTSSAPQPSMPektR 211
Cdd:PHA03247 2707 TPEPAPHAL----------VSATPLPPGPAAARQASPALPAApAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP---A 2773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 212 TRGVGDTGQSTKGGKCQGTEGKGSrdpqtigqkegeSQSTEEQGTRSQAQEAGNKEQLGTAEKEGGGPPKKMEKEDEPKV 291
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASLSESRES------------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 292 AGAevrPVEPPVPLRKW---GGFLGWRSKWDSPQSKDrVTESHRKDEKtgdLQSPAVDRSCGQLAEPTGQPSGPTgQPSG 368
Cdd:PHA03247 2842 PPG---PPPPSLPLGGSvapGGDVRRRPPSRSPAAKP-AAPARPPVRR---LARPAVSRSTESFALPPDQPERPP-QPQA 2913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 369 PTGQLSESTGQPSgPTGQPAGPTgqPAGPTGQPAgPTGQPAGPTGQQQEAPVKMEGKVGRPQKKLVTPRKPRELPGVAAk 448
Cdd:PHA03247 2914 PPPPQPQPQPPPP-PQPQPPPPP--PPRPQPPLA-PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREA- 2988
|
410 420
....*....|....*....|....
gi 291327510 449 tqnPEESCKAPDRIPTTGISAEAA 472
Cdd:PHA03247 2989 ---PASSTPPLTGHSLSRVSSWAS 3009
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1726-2128 |
7.61e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1726 LKERVWELETNaleQQKIHsQQENTIK-------QLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLE 1798
Cdd:TIGR00606 250 LKNRLKEIEHN---LSKIM-KLDNEIKalksrkkQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1799 MQLEQEYEEKQVALHEKHDLEGLIGTLC-------DQIGHRDFD-----------------------------VEKRLRR 1842
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLiqslatrleldgfergpfserqiknfhtlVIERQED 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1843 DLRRTHALLSDVQLLLAT-------IEDSKTSISK-------------EELEKVHSQLEQSEAKCEDALKTQKVLTADLE 1902
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLkqeqadeIRDEKKGLGRtielkkeilekkqEELKFVIKELQQLEGSSDRILELDQELRKAER 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1903 NMhSELENVTRSKSLVDEQLYrLQFERADLLK---RIDEDQGDLN------------------------DLMQKHKDLIA 1955
Cdd:TIGR00606 486 EL-SKAEKNSLTETLKKEVKS-LQNEKADLDRklrKLDQEMEQLNhhtttrtqmemltkdkmdkdeqirKIKSRHSDELT 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1956 QSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVE-RAIVSRQEAIICDLENKTeFQKVQIKRFEVLVI 2034
Cdd:TIGR00606 564 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHiNNELESKEEQLSSYEDKL-FDVCGSQDEESDLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2035 RLRdsmikmgEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSI 2114
Cdd:TIGR00606 643 RLK-------EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
490
....*....|....
gi 291327510 2115 RRIADLQAALEEVV 2128
Cdd:TIGR00606 716 SELKKKEKRRDEML 729
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1444-2044 |
7.74e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1444 LRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELaderfkgdvacQALESERAERLQALREVQELKTKYQQ 1523
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEI-----------ERLSIEYNNAMDDYNNLKSALNELSS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1524 VQDALGEVQKQLEEAQQRIQGANLEEKPAGGADEWQMRL-------------DCAQMENDFLRKRlqQCEERLDSEMKAR 1590
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIindpvyknrnyinDYFKYKNDIENKK--QILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1591 TELEQKLGELQS---AYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRN---HELEKRQKKFDLQLAQALGESMFEK 1664
Cdd:PRK01156 325 HAIIKKLSVLQKdynDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1665 SLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVER----LQGQKRELLSCASVGDQGVASLKERVWElETNALEQ 1740
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRnmemLNGQSVCPVCGTTLGEEKSNHIINHYNE-KKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1741 QKIHSqqENTIKQLEQlrqrfeleiermKQMHQKDREDQEEElEDVRQSCQ--KRLRQLEMQLEqEYEEKQVALHEKHD- 1817
Cdd:PRK01156 484 KIREI--EIEVKDIDE------------KIVDLKKRKEYLES-EEINKSINeyNKIESARADLE-DIKIKINELKDKHDk 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1818 LEGLIGTlcdqigHRDFDVEKrlrRDLRRTHALLSDVQlllatiedsktsISKEELEKVHSQLEQSEAKCEDALKTQKVL 1897
Cdd:PRK01156 548 YEEIKNR------YKSLKLED---LDSKRTSWLNALAV------------ISLIDIETNRSRSNEIKKQLNDLESRLQEI 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1898 TADLENMHSELENVTRSkslVDEQL--YRLQFERADLLKR-IDEDQGDLNDLmqkhKDLIAQSAADIGQIQELQLQLEET 1974
Cdd:PRK01156 607 EIGFPDDKSYIDKSIRE---IENEAnnLNNKYNEIQENKIlIEKLRGKIDNY----KKQIAEIDSIIPDLKEITSRINDI 679
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291327510 1975 KKEKQKLREQLHMAQLRiQYLEQSTVE--RAIVSRQEAIICDLENKTEFQKvQIKRFEVLVIRLRDSMIKMG 2044
Cdd:PRK01156 680 EDNLKKSRKALDDAKAN-RARLESTIEilRTRINELSDRINDINETLESMK-KIKKAIGDLKRLREAFDKSG 749
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1572-2117 |
7.99e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1572 LRKRLQ-QCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRkchhLTWDLEDTRVLLENQQSRNHELEKRQKKFD 1650
Cdd:COG4717 47 LLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1651 lQLAQALGESMFEKSLREKVSQENNGVRwelgqlqqqleqkeqeasKLKQEVERLQGQKRELlscasvgdqgvASLKERV 1730
Cdd:COG4717 123 -KLLQLLPLYQELEALEAELAELPERLE------------------ELEERLEELRELEEEL-----------EELEAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1731 WELEtNALEQQKIHSQQEnTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQscqkRLRQLEMQLEQEYEEKQv 1810
Cdd:COG4717 173 AELQ-EELEELLEQLSLA-TEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEER- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1811 aLHEKHDLEGLIGTLCDQIGHRDFDVEKRLRrdlrrthaLLSDVQLLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDA 1890
Cdd:COG4717 245 -LKEARLLLLIAAALLALLGLGGSLLSLILT--------IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1891 LKTQKVLTADLENMHSELENVTRSKSLVD--EQLYRLQFERADLLKRIDedqgdLNDLMQKHKDLIAQsaADIGQIQELQ 1968
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDriEELQELLREAEELEEELQ-----LEELEQEIAALLAE--AGVEDEEELR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1969 LQLEEtKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIicdlenktefqKVQIKRFEVLVIRLRDSMIKMGEELS 2048
Cdd:COG4717 389 AALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEEL-----------EEELEELEEELEELEEELEELREELA 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 2049 RaVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRI 2117
Cdd:COG4717 457 E-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEY 524
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1727-2136 |
8.89e-08 |
|
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: 57.88 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1727 KERVWELETNALEQQKIHSQ--QENTIKQlEQLRQRFEL--EIERM-------KQ-----MHQ-KDREDQEEELEDVRQS 1789
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlcEEKNALQ-EQLQAETELcaEAEEMrarlaarKQeleeiLHElESRLEEEEERSQQLQN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1790 CQKRLRQ----LEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLATIEDSK 1865
Cdd:pfam01576 97 EKKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1866 TSISKEEL--EKVHSQLEQSEAKCEDALKTQKVLTADLENMHSEL-ENVTRSKSLVDE---QLYRLQFERADLLKRIDED 1939
Cdd:pfam01576 176 KSLSKLKNkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLqEQIAELQAQIAElraQLAKKEEELQAALARLEEE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1940 QGDLNDLMQKHKDLIAQsaadigqIQELQLQLE-----ETKKEKQK--LREQLH---------------MAQLRIQY-LE 1996
Cdd:pfam01576 256 TAQKNNALKKIRELEAQ-------ISELQEDLEseraaRNKAEKQRrdLGEELEalkteledtldttaaQQELRSKReQE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1997 QSTVERAI---VSRQEAIICDLENK--------TEfQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQ 2065
Cdd:pfam01576 329 VTELKKALeeeTRSHEAQLQEMRQKhtqaleelTE-QLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 2066 QRLEelkAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTES 2136
Cdd:pfam01576 408 KKLE---GQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1918-2232 |
9.57e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1918 VDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLhMAQLRIQYLEQ 1997
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1998 STveraiVSRQEAIIcDLENKTEFqkvqIKRFEvLVIRLRDSMIKMGEELSRAVKAEAQQRENsqyYQQRLEELKAEMQE 2077
Cdd:COG3883 100 GS-----VSYLDVLL-GSESFSDF----LDRLS-ALSKIADADADLLEELKADKAELEAKKAE---LEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2078 LAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQTAVDCSSRSGKEGDNVSVI 2157
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 2158 SSQPEGSLQSWMSCSLSLATDSVRIPSGQSVVSSSFHSPRVSEEAGDSERLRTASSALSGAWDAARDASKAGSAS 2232
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAG 320
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1870-2128 |
1.62e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1870 KEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQK 1949
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1950 HKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIICDLENKTEFQKVQIKR- 2028
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2029 FEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQT 2108
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260
....*....|....*....|
gi 291327510 2109 DLETSIRRIADLQAALEEVV 2128
Cdd:COG4372 291 AALELKLLALLLNLAALSLI 310
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
120-468 |
2.35e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 56.70 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 120 TSTSGERPQESGPTGtpakRTLPFKRGVRR-GDVLLMVAKLDPELAKADQKVQPRDVPVDKTPAPAKDSGGTKKGVTTGT 198
Cdd:pfam03154 16 TLRSGRKKQTASPDG----RASPTNEDLRSsGRNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 199 SSaPQPSMPEKTRTRGVgDTGQSTKGGKCQGTEGK-----GSRDPQTIGQKEGES-------QSTEEQGTRSQAQEAGNK 266
Cdd:pfam03154 92 EE-PERATAKKSKTQEI-SRPNSPSEGEGESSDGRsvndeGSSDPKDIDQDNRSTspsipspQDNESDSDSSAQQQILQT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 267 EQLGTAEKEGGGPPKKMEKEDEPKVAGAEVRPVEPPVPLRkwggflGWRSKWDSPQSKDRVTESHRKDEKTGDLQSPavd 346
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQ------GSPATSQPPNQTQSTAAPHTLIQQTPTLHPQ--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 347 rscgQLAEPTgQPSGPTGQPSGPTGQLSESTGQPSGPTGQPAGPTGQPAGPT-------GQPAGPT---GQPAGPTGQQQ 416
Cdd:pfam03154 241 ----RLPSPH-PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvpPQPFPLTpqsSQSQVPPGPSP 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 291327510 417 EAPVKMEGKVGRP--QKKLVTPRKPRELPGVAAKTQNPEesCKAPdriPTTGIS 468
Cdd:pfam03154 316 AAPGQSQQRIHTPpsQSQLQSQQPPREQPLPPAPLSMPH--IKPP---PTTPIP 364
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1589-2126 |
4.24e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1589 ARTELEQKLGELQSAYEEAKKMAHQLKRKCHH-------LTWDLEDTRVLLENQQSRNH---ELEKRQKKFDLQLAQALG 1658
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDResdrnqeLQKRIRLLEKREAEAEEALReqaELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1659 ESM-FEKSLREKVSQENNGVRwelgQLQQQLEQKEQEASKLKQEVERLQGQKRELlscasvgDQGVASLKERVWELETna 1737
Cdd:pfam05557 94 EKEsQLADAREVISCLKNELS----ELRRQIQRAELELQSTNSELEELQERLDLL-------KAKASEAEQLRQNLEK-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1738 leQQKIHSQQENTIKQLEQLRQRFELEIERMKQMhqKDREDQEEELEdvrqSCQKRLRQLEMQLEQEYEEKQVALHEKHD 1817
Cdd:pfam05557 161 --QQSSLAEAEQRIKELEFEIQSQEQDSEIVKNS--KSELARIPELE----KELERLREHNKHLNENIENKLLLKEEVED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1818 LEgliGTLCDQIGHRD----FDVEK-RLRRDLRRTHALLSDVQLLLATIEDSKTSIS---------KEELEKVHSQLEQS 1883
Cdd:pfam05557 233 LK---RKLEREEKYREeaatLELEKeKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEqlqqreivlKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1884 EAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERaDLLKRI----DEDQGDLNDLMQKHKDLiaQSAA 1959
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKER-DGYRAIlesyDKELTMSNYSPQLLERI--EEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1960 DIgqIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQS-TVERAIVSRQEAIICDLENKTEFQKVQIKRFEVLviRLRD 2038
Cdd:pfam05557 387 DM--TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERElQALRQQESLADPSYSKEEVDSLRRKLETLELERQ--RLRE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2039 SMIKMGEELSRAVKAE---------AQQREN--SQYYQQRleelkAEMQELAQREEEASRRcmELEKYVEELATVRQTLQ 2107
Cdd:pfam05557 463 QKNELEMELERRCLQGdydpkktkvLHLSMNpaAEAYQQR-----KNQLEKLQAEIERLKR--LLKKLEDDLEQVLRLPE 535
|
570
....*....|....*....
gi 291327510 2108 TDLETSIRRIADLQAALEE 2126
Cdd:pfam05557 536 TTSTMNFKEVLDLRKELES 554
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1442-2127 |
6.35e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTL----LRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKgdVACQALESER--AERLQALR-EV 1514
Cdd:PRK04863 445 EEFQAKEQEATEellsLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAR--ELLRRLREQRhlAEQLQQLRmRL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1515 QELKTKYQQVQDAlgevQKQLEEAQQR-IQGANLEEKPAGGADEWQMRLDCAQMEndflrkrLQQCEERldsemkaRTEL 1593
Cdd:PRK04863 523 SELEQRLRQQQRA----ERLLAEFCKRlGKNLDDEDELEQLQEELEARLESLSES-------VSEARER-------RMAL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1594 EQKLGELQSAYEEAKKMAHQlkrkchhltWdledtrvlLENQQSrnheLEKRQKKFDLQLA--QALGESMFEKSLREKVS 1671
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPA---------W--------LAAQDA----LARLREQSGEEFEdsQDVTEYMQQLLEREREL 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1672 QENNgvrwelgqlqqqleqkeqeaSKLKQEVERLQGQKRELLSCASVGDQGVASLKER-----VWEL----------ETN 1736
Cdd:PRK04863 644 TVER--------------------DELAARKQALDEEIERLSQPGGSEDPRLNALAERfggvlLSEIyddvsledapYFS 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1737 ALEQQKIH----SQQENTIKQLEQLRQRFE--LEIERMKQMHQKDREDQEEELEDV------RQSCQKRLRQL------- 1797
Cdd:PRK04863 704 ALYGPARHaivvPDLSDAAEQLAGLEDCPEdlYLIEGDPDSFDDSVFSVEELEKAVvvkiadRQWRYSRFPEVplfgraa 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1798 -EMQLEQEYEEKQvALHEKHDlegligtlcdqigHRDFDVEKrlrrdLRRTHALLSD---VQLLLATIEDsktsiSKEEL 1873
Cdd:PRK04863 784 rEKRIEQLRAERE-ELAERYA-------------TLSFDVQK-----LQRLHQAFSRfigSHLAVAFEAD-----PEAEL 839
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1874 EKVHSQLEQSEAKCEDalktqkvLTADLENMHSELENVTRSKSLVDEQLYRLQ-FERADLLKRIDEDQGDLNDL------ 1946
Cdd:PRK04863 840 RQLNRRRVELERALAD-------HESQEQQQRSQLEQAKEGLSALNRLLPRLNlLADETLADRVEEIREQLDEAeeakrf 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1947 MQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIicDLENKTefqkvqi 2026
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAA--EMLAKN------- 983
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2027 krfEVLVIRLRDSMIKMGEELSRA----VKAEAQQRENSQYY----------QQRLEELKAEMQELAQR-----EEEASR 2087
Cdd:PRK04863 984 ---SDLNEKLRQRLEQAEQERTRAreqlRQAQAQLAQYNQVLaslkssydakRQMLQELKQELQDLGVPadsgaEERARA 1060
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 291327510 2088 RCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEV 2127
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL 1100
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1442-2117 |
6.98e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTL----LRQKLQKSENSRSELRQNTDLLESKITDLTSELAderfkGDVACQALESER-----AERLQALR 1512
Cdd:COG3096 444 AAFRAKEQQATEevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQA-----WQTARELLRRYRsqqalAQRLQQLR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1513 -EVQELKTKYQQVQDAlgevQKQLEEAQQRIqganleekpaGGADEWQMRLDCAQMEndfLRKRLQQCEERLDSEMKART 1591
Cdd:COG3096 519 aQLAELEQRLRQQQNA----ERLLEEFCQRI----------GQQLDAAEELEELLAE---LEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1592 ELEQKLGELQSAYEEAKKMA---HQLKRKCHHLTwdlEDTRVLLENQQSRNHELEkrqkkfdlQLAQALGESMFEKSlre 1668
Cdd:COG3096 582 ELRQQLEQLRARIKELAARApawLAAQDALERLR---EQSGEALADSQEVTAAMQ--------QLLEREREATVERD--- 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1669 kvsqenngvrwelgqlqqqleqkeqeasKLKQEVERLQGQKRELLSCASVGDQGVASLKERV-WELETNALEQQKIH--- 1744
Cdd:COG3096 648 ----------------------------ELAARKQALESQIERLSQPGGAEDPRLLALAERLgGVLLSEIYDDVTLEdap 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1745 ---------------SQQENTIKQLEQLRQRFE--LEIERMKQMHQKD-REDQEEELEDVRQSCQKRLR----------- 1795
Cdd:COG3096 700 yfsalygparhaivvPDLSAVKEQLAGLEDCPEdlYLIEGDPDSFDDSvFDAEELEDAVVVKLSDRQWRysrfpevplfg 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1796 --QLEMQLEQeyeekqvaLHEKHDlegligTLCDQIGHRDFDVEKrlrrdLRRTHALLSDV---QLLLATIEDSKTSIsk 1870
Cdd:COG3096 780 raAREKRLEE--------LRAERD------ELAEQYAKASFDVQK-----LQRLHQAFSQFvggHLAVAFAPDPEAEL-- 838
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1871 EELEKVHSQLEQSEAKCEDALKTQKvltadlenmhSELENVTRSKSLVDEQLYRLQ-FERADLLKRIDEDQGDLNDL--- 1946
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLR----------QQLDQLKEQLQLLNKLLPQANlLADETLADRLEELREELDAAqea 908
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1947 ---MQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIICDLENKTefqk 2023
Cdd:COG3096 909 qafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD---- 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2024 vqikrfevLVIRLRDSMIKMGEELSRA-VKAEAQQRENSQYYQ-------------QRLEELKAEMQEL-----AQREEE 2084
Cdd:COG3096 985 --------LNEKLRARLEQAEEARREArEQLRQAQAQYSQYNQvlaslkssrdakqQTLQELEQELEELgvqadAEAEER 1056
|
730 740 750
....*....|....*....|....*....|...
gi 291327510 2085 ASRRCMELEkyvEELATVRQTLqTDLETSIRRI 2117
Cdd:COG3096 1057 ARIRRDELH---EELSQNRSRR-SQLEKQLTRC 1085
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1858-2099 |
8.48e-07 |
|
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: 52.72 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1858 LATIEDsKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELEnvtRSKSLVDEQLYRLQferaDLLKRID 1937
Cdd:pfam00261 3 MQQIKE-ELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELE---RTEERLAEALEKLE----EAEKAAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1938 EDQgdlndlmQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQStVERAI--VSRQEAIICDL 2015
Cdd:pfam00261 75 ESE-------RGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD-LERAEerAELAESKIVEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2016 ENKTEFQKVQIKRFEVLVirlrdsmikmgeelsravkAEAQQRENSqyYQQRLEELKAEMQELAQREEEASRRCMELEKY 2095
Cdd:pfam00261 147 EEELKVVGNNLKSLEASE-------------------EKASEREDK--YEEQIRFLTEKLKEAETRAEFAERSVQKLEKE 205
|
....
gi 291327510 2096 VEEL 2099
Cdd:pfam00261 206 VDRL 209
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1948-2140 |
1.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1948 QKHKDLiaQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIqyleqstvERAIVSRQEaiicdLENKTEFQKVQIK 2027
Cdd:COG1196 213 ERYREL--KEELKELEAELLLLKLRELEAELEELEAELEELEAEL--------EELEAELAE-----LEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2028 RFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQR-----------EEEASRRCMELEKYV 2096
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEleeleeeleelEEELEEAEEELEEAE 357
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 291327510 2097 EELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQTA 2140
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1523-2126 |
1.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1523 QVQDALGEVQKQLEEaqqrIQGANLEEKPAG---GADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTE---LEQK 1596
Cdd:PRK02224 184 DQRGSLDQLKAQIEE----KEEKDLHERLNGlesELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1597 LGELQSAYEEAKKMAHQLKRKchhltwdledtrvlLENQQSRNHELEKRqkkfdlqLAQALGESMFEKSLREKVSQENNG 1676
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE--------------VRDLRERLEELEEE-------RDDLLAEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1677 VRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCAsvgdqgvASLKERVWELETNALEQQKIHSQQENTI----K 1752
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA-------EELREEAAELESELEEAREAVEDRREEIeeleE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1753 QLEQLRQRFELEIErmkqmhqkDREDQEEELEDVRQScQKRLRQLEMQLEQEYEEKQVALHEKHDL--EGLIGTlCDQig 1830
Cdd:PRK02224 392 EIEELRERFGDAPV--------DLGNAEDFLEELREE-RDELREREAELEATLRTARERVEEAEALleAGKCPE-CGQ-- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1831 hrdfDVEKrlrrdlrRTHAllsdvqlllATIEDSKTSIskEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELEN 1910
Cdd:PRK02224 460 ----PVEG-------SPHV---------ETIEEDRERV--EELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1911 VTRSKSLVDEQLYRLQfERADLLKRIDEDQGDLNDLMQKHKDliaqsaadigQIQELQLQLEETKKEKQKLREQLHMAQL 1990
Cdd:PRK02224 518 REDLEELIAERRETIE-EKRERAEELRERAAELEAEAEEKRE----------AAAEAEEEAEEAREEVAELNSKLAELKE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1991 RIQYLEQStveRAIVSRQEAIICDLENKTE----FQKVQIKRFEVLVIRlRDSMIKMGEELSRAVKAEAQQ-RENSQYYQ 2065
Cdd:PRK02224 587 RIESLERI---RTLLAAIADAEDEIERLREkreaLAELNDERRERLAEK-RERKRELEAEFDEARIEEAREdKERAEEYL 662
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 2066 QRLEElkaEMQELAQREEEASRRCMELEKYVEELATVRQTLqTDLETSIRRIADLQAALEE 2126
Cdd:PRK02224 663 EQVEE---KLDELREERDDLQAEIGAVENELEELEELRERR-EALENRVEALEALYDEAEE 719
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1942-2232 |
1.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1942 DLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQ--STVERAIVSRQEAiicdLENKT 2019
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiAEAEAEIEERREE----LGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2020 EFQKVQIKRFEVLVIRLRDSMIkmGEELSRAVKAEAQqrenSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEEL 2099
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESF--SDFLDRLSALSKI----ADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2100 ATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQTAVDcSSRSGKEGDNVSVISSQPEGSLQSWMSCSLSLATDS 2179
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE-AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 291327510 2180 VRIPSGQSVVSSSFHSPRVSEEAGDSERLRTASSALSGAWDAARDASKAGSAS 2232
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGA 298
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1566-2012 |
1.39e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.81 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1566 QMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCH------HLTWDLEDTRVLLENQQSRN 1639
Cdd:COG5185 145 EIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAepsgtvNSIKESETGNLGSESTLLEK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1640 HE----LEKRQKKFDLQLAQALGESMFEKSLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKREL--- 1712
Cdd:COG5185 225 AKeiinIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYtks 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1713 LSCASVGDQGVASLKErvWELETNaLEQQKIHSQQENTiKQLEQLRQRFELEIERMKQMhqKDREDQEEELEDVRQScQK 1792
Cdd:COG5185 305 IDIKKATESLEEQLAA--AEAEQE-LEESKRETETGIQ-NLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKS-SE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1793 RLRQLEMQLE---QEYEEKQVALHEKHDlEGLIgTLCDQIGHRDFDVEkRLRRDLRRTHALLSDVQLLLATIEDSKTSIS 1869
Cdd:COG5185 378 ELDSFKDTIEstkESLDEIPQNQRGYAQ-EILA-TLEDTLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVM 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1870 KEELEKVHSQLEQSEAKCEDALKTQKvltADLENMHSELENVTRSKSLVDEQLY-RLQFERADLLKRIDEDQGDLNDLMQ 1948
Cdd:COG5185 455 READEESQSRLEEAYDEINRSVRSKK---EDLNEELTQIESRVSTLKATLEKLRaKLERQLEGVRSKLDQVAESLKDFMR 531
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1949 KHKDLIAQSAADIGQIQELQLQLEETKKEKQklrEQLHMAQLRIQYLEQSTVERAIVSRQEAII 2012
Cdd:COG5185 532 ARGYAHILALENLIPASELIQASNAKTDGQA---ANLRTAVIDELTQYLSTIESQQAREDPIPD 592
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1454-2126 |
2.04e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1454 LRQKLQKSENSRSELrqntDLLESKI--------TDLTSELADERfkgdvacqALESERAERLQALRE--------VQEL 1517
Cdd:pfam10174 5 LRDLQRENELLRREL----DIKESKLgssmnsikTFWSPELKKER--------ALRKEEAARISVLKEqyrvtqeeNQHL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1518 KTKYQQVQDALgEVQKQL------EEAQQRIQGANLEEKPAGGADEW---QMRLDCAQMENDFLRKRLQQCEERLDSE-- 1586
Cdd:pfam10174 73 QLTIQALQDEL-RAQRDLnqllqqDFTTSPVDGEDKFSTPELTEENFrrlQSEHERQAKELFLLRKTLEEMELRIETQkq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1587 -MKARTELEQKLGEL-------QSAYEEAKKMAHQL---KRKCHHLTWDLEDTRV----LLENQQSRNHELEKRQKKFDL 1651
Cdd:pfam10174 152 tLGARDESIKKLLEMlqskglpKKSGEEDWERTRRIaeaEMQLGHLEVLLDQKEKenihLREELHRRNQLQPDPAKTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1652 QLAQALGESmfekslreKVSQENNGVRwelgqlqqqleqkeqeasKLKQEVERLQgqkrellscasvgDQGVASLKERvw 1731
Cdd:pfam10174 232 QTVIEMKDT--------KISSLERNIR------------------DLEDEVQMLK-------------TNGLLHTEDR-- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1732 ELETNALEQQKIHSQ-QENTIKQLEQLRQRFELEIERMKQM------HQKDREDQEEELEDVRQSCQKRLRQLEMQ---L 1801
Cdd:pfam10174 271 EEEIKQMEVYKSHSKfMKNKIDQLKQELSKKESELLALQTKletltnQNSDCKQHIEVLKESLTAKEQRAAILQTEvdaL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1802 EQEYEEKQVALHEK----HDLEGLIGTLCDQIGH-RD-FDVEKRlrrdlrRTHALLSDVQLLLATIEDSKTSISkeELEK 1875
Cdd:pfam10174 351 RLRLEEKESFLNKKtkqlQDLTEEKSTLAGEIRDlKDmLDVKER------KINVLQKKIENLQEQLRDKDKQLA--GLKE 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1876 VHSQLEQSEAKCEDALKTQKVLTADLENMHSEL-ENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDL------MQ 1948
Cdd:pfam10174 423 RVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKesslidLK 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1949 KHKDLIAQSAADI-GQIQELQLQLEETKKEKQKLREQLHMAQ-------------LRIQYLEQ--------STVERAIVS 2006
Cdd:pfam10174 503 EHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHnaeeavrtnpeinDRIRLLEQevarykeeSGKAQAEVE 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2007 RQEAIICDLENKTEFQKVQIKRFEVLVirlrdsmikmgeelSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEAS 2086
Cdd:pfam10174 583 RLLGILREVENEKNDKDKKIAELESLT--------------LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNL 648
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 291327510 2087 RRC---MELEKYVEELATVRQtlqtDLETSIRRIADLQAALEE 2126
Cdd:pfam10174 649 ADNsqqLQLEELMGALEKTRQ----ELDATKARLSSTQQSLAE 687
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1448-1617 |
2.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1448 EEELTLLRQKLQKSENSRSELRQNTDL----------------LESKITDLTSELADERFKGDVACQALESERAE--RLQ 1509
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLvdlseeaklllqqlseLESQLAEARAELAEAEARLAALRAQLGSGPDAlpELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1510 ALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGAN--LEEKPAGGADEWQMRLDCAQMENDFLRKR---LQQCEERLD 1584
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRaqIAALRAQLQQEAQRILASLEAELEALQAReasLQAQLAQLE 340
|
170 180 190
....*....|....*....|....*....|...
gi 291327510 1585 SEMKARTELEQKLGELQSAYEEAKKMAHQLKRK 1617
Cdd:COG3206 341 ARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1536-1918 |
2.98e-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: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1536 EEAQQRIQGANLEEKPAGGADEWQMRLDCAQM-ENDFLRKRLQQCEERldsemKARTELEQKlgelqsayEEAKKMAHQ- 1613
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEYTVRYNGQTMtENEFLNQLLHIVQHQ-----KAVSERQQQ--------EKFEKMEQEr 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1614 LKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALG-ESMFEKSLREKVSQENNGVRwelgqlqqqLEQKE 1692
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErERELERIRQEERKRELERIR---------QEEIA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1693 QEASKLKqEVERLQGQKREllSCASVGDQGVASLKERVWELEtnalEQQKIHSQQentiKQLEQLRQrfELEIERMKQMh 1772
Cdd:pfam17380 372 MEISRMR-ELERLQMERQQ--KNERVRQELEAARKVKILEEE----RQRKIQQQK----VEMEQIRA--EQEEARQREV- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1773 QKDREDQEEELEDVRQSCQKRLRQLEM--QLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHAL 1850
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291327510 1851 LSDvqlllaTIEDSKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENmHSELENVTRSKSLV 1918
Cdd:pfam17380 518 LEK------EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMM 578
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1698-2002 |
3.10e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.90 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1698 LKQEVERLQGQKREllscasvGDQGVASLKERVWELETNAleqqkihSQQENTIKQLEQLRQRFELEIERMKqmHQKDRE 1777
Cdd:pfam10174 399 LQKKIENLQEQLRD-------KDKQLAGLKERVKSLQTDS-------SNTDTALTTLEEALSEKERIIERLK--EQRERE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1778 DQE--EELEDVRQsCQKRLRQLEMQLEQEYEEKQVALHekhDLEGLIGTLCDQIGHRDFDVeKRLRRDLRRTHALLSDVQ 1855
Cdd:pfam10174 463 DRErlEELESLKK-ENKDLKEKVSALQPELTEKESSLI---DLKEHASSLASSGLKKDSKL-KSLEIAVEQKKEECSKLE 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1856 LLLATIEDSK-TSISKEELEKVHSQLEQSEA-KCEDALKTQkvltADLENMHSELENVTRSKSLVDEQLYRLQFERADLL 1933
Cdd:pfam10174 538 NQLKKAHNAEeAVRTNPEINDRIRLLEQEVArYKEESGKAQ----AEVERLLGILREVENEKNDKDKKIAELESLTLRQM 613
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 1934 KRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQE------LQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVER 2002
Cdd:pfam10174 614 KEQNKKVANIKHGQQEMKKKGAQLLEEARRREDnladnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEK 688
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1572-1977 |
3.23e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1572 LRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMahqlkrkchhltwdledtrvlLENQQSRNHELEKRQKKFDL 1651
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---------------------IGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1652 QLAQalgesmfeksLREKVSqenngvrwelgqlqqqleQKEQEASKLKQEVERLQGQKRELlscasvgdqgvaslkervw 1731
Cdd:TIGR02169 738 RLEE----------LEEDLS------------------SLEQEIENVKSELKELEARIEEL------------------- 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1732 eletnaleQQKIHSQQEntikQLEqlrqrfelEIERMKQMHQKDREDQE-EELEDVRQSCQKRLRQLEMQLEQEYEEKQV 1810
Cdd:TIGR02169 771 --------EEDLHKLEE----ALN--------DLEARLSHSRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1811 ALHEKHDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLATIEDSKTSISKE------ELEKVHSQLEQSE 1884
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaQLRELERKIEELE 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1885 AKCEDALKTQKVLTADLENMHSEL----ENVTRSKSLVDEQLY--RLQFERADLLKRI--------------DEDQGDLN 1944
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELseieDPKGEDEEIPEEELSleDVQAELQRVEEEIralepvnmlaiqeyEEVLKRLD 989
|
410 420 430
....*....|....*....|....*....|...
gi 291327510 1945 DLMQKHKDLIAQSAAdigqIQELQLQLEETKKE 1977
Cdd:TIGR02169 990 ELKEKRAKLEEERKA----ILERIEEYEKKKRE 1018
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
191-439 |
3.85e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.90 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 191 KKGVTTGTSSAPQPSMPEKT--RTRGVGDTGQSTKGGKCQGTEGKGSRDPQTIGQKeGESQSTEEQGTRSQAQEAGNKEQ 268
Cdd:PHA03169 35 RRRGTAARAAKPAPPAPTTSgpQVRAVAEQGHRQTESDTETAEESRHGEKEERGQG-GPSGSGSESVGSPTPSPSGSAEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 269 LGTA---EKEGGGPPKKMEKEDEPKVAGAEVRPVEPPVPlrkwggflgwrskwdspqskdrvtESHRKDEktGDLQSPAV 345
Cdd:PHA03169 114 LASGlspENTSGSSPESPASHSPPPSPPSHPGPHEPAPP------------------------ESHNPSP--NQQPSSFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 346 DRSCGQLAEPtgqPSGPTGQPSgptgqlSESTGQPSGPTGQPAGPTGQPAGPTGQPAGPTGQPA-GPTGQQQEAPVKMEG 424
Cdd:PHA03169 168 QPSHEDSPEE---PEPPTSEPE------PDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQApSPNTQQAVEHEDEPT 238
|
250
....*....|....*
gi 291327510 425 KVGRPQKKLVTPRKP 439
Cdd:PHA03169 239 EPEREGPPFPGHRSH 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1736-2131 |
4.53e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1736 NALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVrQSCQKRLRQLEMQLEQEYEEKQVALHEK 1815
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAI-QELQFENEKVSLKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1816 HDLEGLIGTLCDQIGhRDFDVEKRLRRDLRRTHALLSDvqlLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKTQK 1895
Cdd:pfam05483 151 NATRHLCNLLKETCA-RSAEKTKKYEYEREETRQVYMD---LNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1896 VLtadlENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHK-------DLIAQSAADIGQIQELQ 1968
Cdd:pfam05483 227 LE----EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1969 LQLEETKKEKQKLREQLHMAQLRIQYL--------EQSTVERA----IVSRQEAIICDLEN--KTEFQKVQIKRFEVLVI 2034
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIATKTICQLteekeaqmEELNKAKAahsfVVTEFEATTCSLEEllRTEQQRLEKNEDQLKII 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2035 RLRdsMIKMGEELSRAVKAeaqqRENSQYYQQRLEELKAEMQELAQREEEasrrcmeLEKYVEELATVRQTLQTDLETSI 2114
Cdd:pfam05483 383 TME--LQKKSSELEEMTKF----KNNKEVELEELKKILAEDEKLLDEKKQ-------FEKIAEELKGKEQELIFLLQARE 449
|
410
....*....|....*..
gi 291327510 2115 RRIADLQAALEEVVSSD 2131
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSE 466
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1745-2127 |
4.86e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1745 SQQENTIKQLE-QLRQRFELEI-ERMKQMHQKDREDQE--EELEDVRQSCQKRLRQLEMQLEqEYEEKQVALHE-KHDLE 1819
Cdd:PRK02224 183 SDQRGSLDQLKaQIEEKEEKDLhERLNGLESELAELDEeiERYEEQREQARETRDEADEVLE-EHEERREELETlEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1820 GLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLATIEdsKTSISKEELEKVHSQLEQSEAKCEDALKTQKVlta 1899
Cdd:PRK02224 262 DLRETIAETERERE-ELAEEVRDLRERLEELEEERDDLLAEAG--LDDADAEAVEARREELEDRDEELRDRLEECRV--- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1900 DLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQ 1979
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1980 KLREQLHMAQLRIQYLEQS--TVERAIVSRQE-----------------AIICDLENKTEfqkvQIKRFEVLVIRLRDSM 2040
Cdd:PRK02224 416 ELREERDELREREAELEATlrTARERVEEAEAlleagkcpecgqpvegsPHVETIEEDRE----RVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2041 IKMGEELSRA---VKAEAQ---QRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSI 2114
Cdd:PRK02224 492 EEVEERLERAedlVEAEDRierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410
....*....|...
gi 291327510 2115 RRIADLQAALEEV 2127
Cdd:PRK02224 572 EEVAELNSKLAEL 584
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1698-2106 |
4.94e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.00 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1698 LKQEVERLQGQKRELLSCAsvgdQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQL----RQRFELEIERMKQMHQ 1773
Cdd:pfam05622 92 LEKEVLELQHRNEELTSLA----EEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrRQVKLLEERNAEYMQR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1774 KdrEDQEEELedvrqscqKRLRQLEMQLEQeYEEKQVALHEKHDLEGLigtLCDQIGHRDFDVEKRLRRDLRRTHALLSD 1853
Cdd:pfam05622 168 T--LQLEEEL--------KKANALRGQLET-YKRQVQELHGKLSEESK---KADKLEFEYKKLEEKLEALQKEKERLIIE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1854 VQLLLATIEDSKTSiskeelekvhsQLEQSEAKCEDALKTQKVLTADleNMHSELENVTrskslVDEQLYRLQFERadll 1933
Cdd:pfam05622 234 RDTLRETNEELRCA-----------QLQQAELSQADALLSPSSDPGD--NLAAEIMPAE-----IREKLIRLQHEN---- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1934 KRIDEDQGdlndlmqkhkdliaqsAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQStVERAIVSRQEAiic 2013
Cdd:pfam05622 292 KMLRLGQE----------------GSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ-VEELQKALQEQ--- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2014 dlENKTEFQKVQIKRFEVLVIRLRdsmiKMGEELSRAVKA--EAQQRENSQyYQQRLEELkaeMQELAQREEEAsrRCME 2091
Cdd:pfam05622 352 --GSKAEDSSLLKQKLEEHLEKLH----EAQSELQKKKEQieELEPKQDSN-LAQKIDEL---QEALRKKDEDM--KAME 419
|
410
....*....|....*..
gi 291327510 2092 --LEKYVEELATVRQTL 2106
Cdd:pfam05622 420 erYKKYVEKAKSVIKTL 436
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
99-419 |
6.56e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.10 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 99 NSADIPGKEPPG------AGDKDSTPVTSTSGERP----QESGPTGTPAKRTLPFKRGVRRGDVLLMVAKLDPELAKADQ 168
Cdd:PHA03307 63 DRFEPPTGPPPGpgteapANESRSTPTWSLSTLAPaspaREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 169 KVQPRDVPVDKtPAPAKDSGGTKKGVTTGTSSAPQPSMPEKTRTrgvGDTGQSTKGGKCQGTEGKG--SRDPQTIGQKEG 246
Cdd:PHA03307 143 SPGPPPAASPP-AAGASPAAVASDAASSRQAALPLSSPEETARA---PSSPPAEPPPSTPPAAASPrpPRRSSPISASAS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 247 ESQSTeeqGTRSQAQEAGNK-------EQLGTAEKEGGGPPKKMEKE-DEPKVAGAEVRPVEP---PVPLRKWGGFLGWR 315
Cdd:PHA03307 219 SPAPA---PGRSAADDAGASssdssssESSGCGWGPENECPLPRPAPiTLPTRIWEASGWNGPssrPGPASSSSSPRERS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 316 SKWDSPQSKDRVTESHRKDEKTGDLQSPAVDRScgqlAEPTGQPSGPTGQPSGPTGQLSESTGQPSGPTGQPAGPT-GQP 394
Cdd:PHA03307 296 PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS----TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKrPRP 371
|
330 340
....*....|....*....|....*
gi 291327510 395 AGPTGQPAGPTGQPAGPTGQQQEAP 419
Cdd:PHA03307 372 SRAPSSPAASAGRPTRRRARAAVAG 396
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1498-2126 |
7.02e-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: 51.66 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1498 QALESERAERLQALrevqelktkYQQVQDalgEVQKQLEEAQQRIQGanLEEKPAGG---ADEWQMRLDCAQmendflrk 1574
Cdd:pfam15921 248 EALKSESQNKIELL---------LQQHQD---RIEQLISEHEVEITG--LTEKASSArsqANSIQSQLEIIQ-------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1575 rlQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMahqlkrkchhltwdledtrvllenQQSRNHELEKrqkkfdlQLA 1654
Cdd:pfam15921 306 --EQARNQNSMYMRQLSDLESTVSQLRSELREAKRM------------------------YEDKIEELEK-------QLV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1655 QALGESMFEKSLREKVSQENNGVRwelgqlqqqleqkeqeaSKLKQEVERLQGQKRELlscasvgdqgvaSLK----ERV 1730
Cdd:pfam15921 353 LANSELTEARTERDQFSQESGNLD-----------------DQLQKLLADLHKREKEL------------SLEkeqnKRL 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1731 WELET-NALEQQkiHSQQENTIKQLEQlrQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrLRQLEMQLEQEYEEKQ 1809
Cdd:pfam15921 404 WDRDTgNSITID--HLRRELDDRNMEV--QRLEALLKAMKSECQGQMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLR 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1810 VALHE----KHDLEGLIGTLCdqighrdfDVEKRLRRDLRRTHALLSDVQLLlatieDSKTSISKEELEKVHSQ---LEQ 1882
Cdd:pfam15921 479 KVVEEltakKMTLESSERTVS--------DLTASLQEKERAIEATNAEITKL-----RSRVDLKLQELQHLKNEgdhLRN 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1883 SEAKCEdALKTQKVLTAD-LENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDL--MQKHKDliaqsaa 1959
Cdd:pfam15921 546 VQTECE-ALKLQMAEKDKvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFkiLKDKKD------- 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1960 diGQIQELQLQLEETKKEK--------QKLREQLHMAQLRIQYLEQSTVER----AIVSRQEAIICDLENKTEFQ----- 2022
Cdd:pfam15921 618 --AKIRELEARVSDLELEKvklvnagsERLRAVKDIKQERDQLLNEVKTSRnelnSLSEDYEVLKRNFRNKSEEMetttn 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2023 --KVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCM----ELEKYV 2096
Cdd:pfam15921 696 klKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHflkeEKNKLS 775
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 291327510 2097 EELATV---RQTLQTDLE---TSIRR----IADLQAALEE 2126
Cdd:pfam15921 776 QELSTVateKNKMAGELEvlrSQERRlkekVANMEVALDK 815
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1888-2138 |
7.35e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1888 EDALKTQKVLTADLE-----NMHSELENVTRSKSLVDEQLYRLQferadllKRIDEDQGDLNDLMQKHK--------DLI 1954
Cdd:COG3206 145 PDPELAAAVANALAEayleqNLELRREEARKALEFLEEQLPELR-------KELEEAEAALEEFRQKNGlvdlseeaKLL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1955 AQSAADI-GQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIvsrqeaiicdlenKTEFQKVQIKRFEVL- 2032
Cdd:COG3206 218 LQQLSELeSQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL-------------RAQLAELEAELAELSa 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2033 --------VIRLRDSMikmgEELSRAVKAEAqqrensqyyQQRLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQ 2104
Cdd:COG3206 285 rytpnhpdVIALRAQI----AALRAQLQQEA---------QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA 351
|
250 260 270
....*....|....*....|....*....|....*...
gi 291327510 2105 T---LQTDLETSIRRIADLQAALEEV-VSSDSDTESVQ 2138
Cdd:COG3206 352 ElrrLEREVEVARELYESLLQRLEEArLAEALTVGNVR 389
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1442-1812 |
9.64e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITD-------LTSELADERFKGDVAcQALESERAERLQAL--- 1511
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEK-ESFLNKKTKQLQDLtee 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1512 -------------------REVQELKTKYQQVQDALGEVQKQLEEAQQRIQGAnleEKPAGGADEWQMRLDCAQMENDFL 1572
Cdd:pfam10174 375 kstlageirdlkdmldvkeRKINVLQKKIENLQEQLRDKDKQLAGLKERVKSL---QTDSSNTDTALTTLEEALSEKERI 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1573 RKRLQQCEERLDSEM--------KARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLtwdleDTRVLLENQQSRNHELEK 1644
Cdd:pfam10174 452 IERLKEQREREDRERleeleslkKENKDLKEKVSALQPELTEKESSLIDLKEHASSL-----ASSGLKKDSKLKSLEIAV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1645 RQKKFDLQLAQALGESMFEKSLREKVSQE-NNGVRwelgQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGV 1723
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVRTNPEiNDRIR----LLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKI 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1724 ASLKERVWEL--ETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQ----------SCQ 1791
Cdd:pfam10174 603 AELESLTLRQmkEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQeldatkarlsSTQ 682
|
410 420 430
....*....|....*....|....*....|..
gi 291327510 1792 KRLRQLE-----------MQLEQEYEEKQVAL 1812
Cdd:pfam10174 683 QSLAEKDghltnlraerrKQLEEILEMKQEAL 714
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1466-1883 |
9.98e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1466 SELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGA 1545
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1546 NLEEKPAGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKART--ELEQKLGELQSAYEEAKKMAhQLKRKChhltw 1623
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqQVNQEKQEKQHELDTVVSKI-ELNRKL----- 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1624 dLEDTRVLLENQQSRNHEL--EKRQKKFDLQLAQALGESMFEK-----SLREKVSQENNGVRWELGQLQQQLEQKEQEAS 1696
Cdd:TIGR00606 852 -IQDQQEQIQHLKSKTNELksEKLQIGTNLQRRQQFEEQLVELstevqSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1697 K--------------LKQEVERLQGQKRELLScaSVGDQGVASLKERVWELETNALEQQKIHSQQENTIKQLEQLRQRFE 1762
Cdd:TIGR00606 931 SketsnkkaqdkvndIKEKVKNIHGYMKDIEN--KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1763 LEIERMK----QMHQKDREDQEEELEDVRQSCQKRLRQLE-MQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVE 1837
Cdd:TIGR00606 1009 TQKIQERwlqdNLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 291327510 1838 KRLR-RDLRRTHALLSDVQLLLATiedskTSISKEELEKVHSQLEQS 1883
Cdd:TIGR00606 1089 KELRePQFRDAEEKYREMMIVMRT-----TELVNKDLDIYYKTLDQA 1130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1918-2127 |
1.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1918 VDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLI-AQSAADI-GQIQELQLQLEETKKEKQKLREQLHMAQLRIQYL 1995
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEdAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1996 EQSTVERAIVSRQEAIIcDLENKTEFQKVQIKRFEVLVIRLRDSMIKMG--------EELSRAVKAEAQQRENSQYYQQR 2067
Cdd:COG4913 289 RLELLEAELEELRAELA-RLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2068 LEELKAEMQELAQREEEASRRCMELekyVEELATVRQTLQTDLETSIRRIADLQAALEEV 2127
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1393-1876 |
1.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1393 RQEYKKLKiRRLATLCIQKNLavflkvkdWPWWGLLASLRpllsstlgtEQLRAKEEELTLLRQKLQksenSRSELRQNT 1472
Cdd:COG4717 108 EAELEELR-EELEKLEKLLQL--------LPLYQELEALE---------AELAELPERLEELEERLE----ELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1473 DLLESKITDLTSELADERfkgdvacqaleseRAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQgaNLEEKpa 1552
Cdd:COG4717 166 EELEAELAELQEELEELL-------------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEEE-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1553 ggADEWQmrldcAQMENDFLRKRLQQCEERLDSeMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLL 1632
Cdd:COG4717 229 --LEQLE-----NELEAAALEERLKEARLLLLI-AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1633 ENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLrekvsqENNGVRWELGQLQQQLEQKEQEASKLKQ-EVERLQGQKRE 1711
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1712 LLSCASVGDqgvaslkervwelETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQ-MHQKDREDQEEELEDVRQsc 1790
Cdd:COG4717 375 LLAEAGVED-------------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEE-- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1791 qkRLRQLEMQLEQEYEEKQVALHEKHDLEGliGTLCDQIGHRDFDVEKRLRRDLRRTHALlsdvQLLLATIEDSKTSISK 1870
Cdd:COG4717 440 --ELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYRE 511
|
....*.
gi 291327510 1871 EELEKV 1876
Cdd:COG4717 512 ERLPPV 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1448-1876 |
1.72e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1448 EEELTLLRQKLQKSENSRSELRQntdlLESKITDLTSELadERFKGDVacQALESERA--ERLQALR------EVQELKT 1519
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE----LKKKLKELEKRL--EELEERH--ELYEEAKAkkEELERLKkrltglTPEKLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1520 KYQQVQDALGEVQKQLEEAQQRIQGANLEEKpaggadewqmRLDCAQMENDFLRKRLQQCEERLDSEMKAR--TELEQKL 1597
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIK----------ELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1598 GELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNH--ELEKRQKKFDLQLAQALGESmFEKSLRE--KVSQE 1673
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNLEELEKKAEE-YEKLKEKliKLKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1674 NNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELLScasVGDQGVASLKERVWELE---------TNAL------ 1738
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE---LGFESVEELEERLKELEpfyneylelKDAEkelere 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1739 --EQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVAlheKH 1816
Cdd:PRK03918 618 ekELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KK 694
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1817 DLEGLigtlcdqigHRDFDVEKRLRRDLRRTHALLSDVQLLLATIEDSKTSISKEELEKV 1876
Cdd:PRK03918 695 TLEKL---------KEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKV 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1846-2149 |
2.12e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1846 RTHALLSDVQLLLATIEDSKTSISKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRskslvdeQLYRL 1925
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1926 QFERADLLKRidedqgdlndlmqkhkdliaqsaadigqIQELQLQLEETKKEKQKLREQLhMAQLRIQYLEQSTVERAIV 2005
Cdd:COG4942 75 EQELAALEAE----------------------------LAELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLALL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2006 SRQEAIicdlenktefqkVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEA 2085
Cdd:COG4942 126 LSPEDF------------LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 2086 SRrcmELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQTAVDCSSRSGK 2149
Cdd:COG4942 194 KA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1749-2138 |
2.25e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.22 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1749 NTIKQLEQLRQRFELEIERMKQMHQKDR----------EDQEEELEDVRQ------SCQKRLRQLEMQLEQEYEEKQVAL 1812
Cdd:PTZ00440 536 NEIEGLIELIKYYLQSIETLIKDEKLKRsmkndiknkiKYIEENVDHIKDiislndEIDNIIQQIEELINEALFNKEKFI 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1813 HEKHDLEGLIGTLCDQIGHRDFDvekrlrrdlrrthALLSDvqlLLATIEDSKTSI----SKEELEKVHSQLEQSEAKCE 1888
Cdd:PTZ00440 616 NEKNDLQEKVKYILNKFYKGDLQ-------------ELLDE---LSHFLDDHKYLYheakSKEDLQTLLNTSKNEYEKLE 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1889 DalKTQKVLTADLENMHSELENV-TRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKdliaqsaADIGQIQEL 1967
Cdd:PTZ00440 680 F--MKSDNIDNIIKNLKKELQNLlSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK-------EEEEKLEVY 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1968 QLQLEETKKE--------KQKLREQLHMAQLRIQYLEQSTVERAIVSRQeaiICDLENKTEFQKVQIKRFEVLVIRLrds 2039
Cdd:PTZ00440 751 KHQIINRKNEfilhlyenDKDLPDGKNTYEEFLQYKDTILNKENKISND---INILKENKKNNQDLLNSYNILIQKL--- 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2040 mikmgeelsravkaEAQQRENSqyyqqrlEELKAEMQELAQREEEASRRcmELEKYVEELATVRQTLQTDLETSIRRIAD 2119
Cdd:PTZ00440 825 --------------EAHTEKND-------EELKQLLQKFPTEDENLNLK--ELEKEFNENNQIVDNIIKDIENMNKNINI 881
|
410
....*....|....*....
gi 291327510 2120 LQAALEEVVSSDSDTESVQ 2138
Cdd:PTZ00440 882 IKTLNIAINRSNSNKQLVE 900
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1864-2141 |
2.32e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1864 SKTSISKEELEKVHSQLEQSEAKCEdalKTQKVLTADLENMHSELENVtRSKSLVDEQLYRLQFERADLLKRIDEDQGDL 1943
Cdd:pfam05557 34 KKASALKRQLDRESDRNQELQKRIR---LLEKREAEAEEALREQAELN-RLKKKYLEALNKKLNEKESQLADAREVISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1944 NDLMQKHKDliaqsaadigQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQ--STVERAIVSRQEAI--ICDLENKT 2019
Cdd:pfam05557 110 KNELSELRR----------QIQRAELELQSTNSELEELQERLDLLKAKASEAEQlrQNLEKQQSSLAEAEqrIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2020 EFQK-------------VQIKRFEVLVIRLRDsMIKMGEELSRAVKAEAQQRENsqyYQQRLEELKAEMQELAQREEEAS 2086
Cdd:pfam05557 180 QSQEqdseivknskselARIPELEKELERLRE-HNKHLNENIENKLLLKEEVED---LKRKLEREEKYREEAATLELEKE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 2087 RRCMELEKYVEELATVRQTLQTDLETSiRRIADLQ----AALEEVVSSDSDTESVQTAV 2141
Cdd:pfam05557 256 KLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQqreiVLKEENSSLTSSARQLEKAR 313
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1456-1668 |
2.33e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1456 QKLQKSENSRSELRQNTDLLeskITDLTSELADERFKGDVACQALESERAERLQALREVQELKTKYQQVQDALGEVQKQL 1535
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1536 EEAQQRIQGANLEEKPAggadewQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLK 1615
Cdd:COG4372 83 EELNEQLQAAQAELAQA------QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 291327510 1616 RKCHHLTWDLEDTRvllenQQSRNHELEKRQKKFDLQLAQALGESMFEKSLRE 1668
Cdd:COG4372 157 EQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1441-1672 |
3.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1441 TEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLEskitdltseladerfkgdvacqalesERAERLQALREVQELKTK 1520
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------------------------ERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1521 YQQVQDALGEVQKQLEEAQqriqganleekpAGGADewqmrLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGEL 1600
Cdd:COG4913 663 VASAEREIAELEAELERLD------------ASSDD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA 725
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291327510 1601 QSAYEEAKKMAHQL-KRKCHHLTWDLEDTR--VLLENQQSRNHE-LEKRQKKFDLQLAQAlgesmfEKSLREKVSQ 1672
Cdd:COG4913 726 EEELDELQDRLEAAeDLARLELRALLEERFaaALGDAVERELREnLEERIDALRARLNRA------EEELERAMRA 795
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1758-2091 |
3.13e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1758 RQRFELEIERMKQMHQKDRED----QEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLcdqighrd 1833
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINIL-------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1834 fdvEKRLRRdlrrthallSDVQLLLATIEDSKTSISKEELEKVHSQLEQ---SEAKCE-------DALKTQKV-LTADLE 1902
Cdd:PLN02939 176 ---EMRLSE---------TDARIKLAAQEKIHVEILEEQLEKLRNELLIrgaTEGLCVhslskelDVLKEENMlLKDDIQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1903 NMHSELENVTRSkslvDEQLYRLQFERADLlkridedQGDLNDLMQKhkdLIAqSAADIGQIQELQLQLEETKKEkqKLR 1982
Cdd:PLN02939 244 FLKAELIEVAET----EERVFKLEKERSLL-------DASLRELESK---FIV-AQEDVSKLSPLQYDCWWEKVE--NLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1983 EQLHMAQLRiqyleqstVERAIVSRQEAIicDLENKTE-----FQKVQIKRFEVLVIRLRDSMIKMGEElsRAVKAEAQQ 2057
Cdd:PLN02939 307 DLLDRATNQ--------VEKAALVLDQNQ--DLRDKVDkleasLKEANVSKFSSYKVELLQQKLKLLEE--RLQASDHEI 374
|
330 340 350
....*....|....*....|....*....|....
gi 291327510 2058 RENSQYYQQRLEELKAEMQELaqrEEEASRRCME 2091
Cdd:PLN02939 375 HSYIQLYQESIKEFQDTLSKL---KEESKKRSLE 405
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1435-1669 |
4.04e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1435 LSSTLGT-EQLRAKEEELTLLRQKLQKSENsrsELRQNTDLLEsKITDLTSELADERFkGDVACQALESERAERLQALRE 1513
Cdd:PRK11281 65 LEQTLALlDKIDRQKEETEQLKQQLAQAPA---KLRQAQAELE-ALKDDNDEETRETL-STLSLRQLESRLAQTLDQLQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1514 VQE-----------LKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKP--AGGADEWQMRLDCAQMENDFLRKRLQQCE 1580
Cdd:PRK11281 140 AQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKAlrPSQRVLLQAEQALLNAQNDLQRKSLEGNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1581 ERLD------SEMKARTE-LEQKLGELQSA-----YEEAKKMAHQLkrkchhltwdledtRVLLENQQSRNHELEKRQKK 1648
Cdd:PRK11281 220 QLQDllqkqrDYLTARIQrLEHQLQLLQEAinskrLTLSEKTVQEA--------------QSQDEAARIQANPLVAQELE 285
|
250 260
....*....|....*....|....*..
gi 291327510 1649 FDLQLAQAL------GESMFEKSLREK 1669
Cdd:PRK11281 286 INLQLSQRLlkatekLNTLTQQNLRVK 312
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1740-2127 |
4.74e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.06 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1740 QQKIHSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSCQKRL-----RQLEMQLEQ--EYEEKQval 1812
Cdd:PTZ00440 896 KQLVEHLLNNKIDLKNKLEQHMK-IINTDNIIQKNEKLNLLNNLNKEKEKIEKQLsdtkiNNLKMQIEKtlEYYDKS--- 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1813 heKHDLEGLIGTLCDQighrdFDVEKRLRRDLRRT-HALLSDVQLLLATIEDsktsISKEELEKV--HSQLEQSEAKCED 1889
Cdd:PTZ00440 972 --KENINGNDGTHLEK-----LDKEKDEWEHFKSEiDKLNVNYNILNKKIDD----LIKKQHDDIieLIDKLIKEKGKEI 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1890 ALKTQKVLTAdLENMHSEL------ENVTRSKS-LVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQS----- 1957
Cdd:PTZ00440 1041 EEKVDQYISL-LEKMKTKLssfhfnIDIKKYKNpKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdkekn 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1958 ---------AADIG----QIQELQLQLEETKKEKQKLREqlhMAQLRIQYleqstvERAIVsrqEAIICDLENKTEFQKV 2024
Cdd:PTZ00440 1120 kqtehynkkKKSLEkiykQMEKTLKELENMNLEDITLNE---VNEIEIEY------ERILI---DHIVEQINNEAKKSKT 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2025 QIKRFEVLVIRLRDSMIKMGEElsraVKAEAQQRENSQYYQQrLEELKAEMQELAQ----REEEASRrcmelEKYVEELA 2100
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSKE----RNDHLTTFEYNAYYDK-ATASYENIEELTTeakgLKGEANR-----STNVDELK 1257
|
410 420
....*....|....*....|....*..
gi 291327510 2101 TVRQTLQTDLETSIRRIADLQAALEEV 2127
Cdd:PTZ00440 1258 EIKLQVFSYLQQVIKENNKMENALHEI 1284
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1443-1811 |
4.76e-05 |
|
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: 49.20 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1443 QLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADErfKGDVACQALESERAERLQALREVQELKTKYQ 1522
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT--KELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1523 QVQDALGEVQKQLEEAQQRIQGANLEEkpaggADEWQMRLDCAQMENDFLRkrlqqcEERLDSEMKARTELEQKLGELQS 1602
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEA-----QDKINEELKLLKQKIDEEE------EEEEKSRLKKEEKEEEKSELSLK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1603 AYEEAKKMAHQLKRKchhltWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESMFEKSLREKVSQENNGVRWELG 1682
Cdd:pfam02463 773 EKELAEEREKTEKLK-----VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1683 QLQQQLEQKEQEASKLKQEVERLQ--GQKRELLSCASVGDQGVASLKER-------VWELETNALEQQKIHSQQENTIKQ 1753
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQEllLKEEELEEQKLKDELESKEEKEKeekkeleEESQKLNLLEEKENEIEERIKEEA 927
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291327510 1754 LEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLE----QEYEEKQVA 1811
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNlmaiEEFEEKEER 989
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1427-1679 |
5.65e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1427 LLASLRPLLSSTLGTEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERfkgdvacQALESERAE 1506
Cdd:COG4942 5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-------RRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1507 RLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKP-----AGGADEWQMRLDCAQMENDFLRKRLQQCEE 1581
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1582 RLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGESM 1661
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*...
gi 291327510 1662 FEKSLREKVSQENNGVRW 1679
Cdd:COG4942 238 AAAERTPAAGFAALKGKL 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1570-2125 |
7.17e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1570 DFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKf 1649
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1650 dlqLAQALGESMFEKSLREKVSQ-ENNGVrwelgqlqQQLEQKEQEASKLKQEVerlqGQKRELLSCAsvgDQGVASLKE 1728
Cdd:PRK01156 265 ---LSMELEKNNYYKELEERHMKiINDPV--------YKNRNYINDYFKYKNDI----ENKKQILSNI---DAEINKYHA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1729 RVWELEtnalEQQKIHSQQENTIKQLEQL-RQRFELEIERMK--------QMHQKDREDQEEELEDVRQSCQKRLRQLEM 1799
Cdd:PRK01156 327 IIKKLS----VLQKDYNDYIKKKSRYDDLnNQILELEGYEMDynsylksiESLKKKIEEYSKNIERMSAFISEILKIQEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1800 ---QLEQEYEEKQVALhekHDLEGLIGTLCDQIghrdfDVEKRLRRDLRRTHALLSD---VQLLLATIEDSKTSISKEEL 1873
Cdd:PRK01156 403 dpdAIKKELNEINVKL---QDISSKVSSLNQRI-----RALRENLDELSRNMEMLNGqsvCPVCGTTLGEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1874 EKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLyrLQFERADLlkriDEDQGDLNDLMQKHkdl 1953
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK--IESARADL----EDIKIKINELKDKH--- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1954 iAQSAADIGQIQELQLQLEETKKEK----QKLREQLHMAQLRIQYLEQSTVERAIVSRQEAIICDLENKTEFQKVQIKRF 2029
Cdd:PRK01156 546 -DKYEEIKNRYKSLKLEDLDSKRTSwlnaLAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2030 EVLVIRLRDSmIKMGEELSRAVKaeaQQRENSQYYQQRLeelkAEMQELAQREEEASRRCMELE---KYVE--------- 2097
Cdd:PRK01156 625 ENEANNLNNK-YNEIQENKILIE---KLRGKIDNYKKQI----AEIDSIIPDLKEITSRINDIEdnlKKSRkalddakan 696
|
570 580 590
....*....|....*....|....*....|
gi 291327510 2098 --ELATVRQTLQTDLETSIRRIADLQAALE 2125
Cdd:PRK01156 697 raRLESTIEILRTRINELSDRINDINETLE 726
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
208-424 |
8.28e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 47.66 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 208 EKTRTRGVGDTGQSTKGGKCQGTEGKGSRDPQTIGQKEGESQSTEEQGTRSQAQEAGNKEQLGTAEKEGGGPPKKMEKED 287
Cdd:PHA03169 31 EQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 288 EPKVAGAevrpveppvplrkwggfLGWRSKWDSPQSKDRVTESHRKDEKTGDLQSPAVDRSCGQlaEPTGQPSG---PTG 364
Cdd:PHA03169 111 AEELASG-----------------LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNP--SPNQQPSSflqPSH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 365 QPSGPTGQLSESTGQPSGPtGQPAGPTGQPAGPTGQPAGPTGQPAGPTGQQQEAPVKMEG 424
Cdd:PHA03169 172 EDSPEEPEPPTSEPEPDSP-GPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1329-1613 |
8.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1329 EELDERKVVEELLKTLDlEKKAVAVGHSQVFLKAGVVSRLERQREKLVSRNIVLFQAACRGFLSRQEYKKLKIRRLATLc 1408
Cdd:COG4717 230 EQLENELEAAALEERLK-EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1409 iqKNLAVFLKVKDWPWWGLLASLRplLSSTLGTEQLRAKEEELTLLRQKLQKSENSRSELRQNtDLLESKITDLTSELAD 1488
Cdd:COG4717 308 --QALPALEELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1489 ErfkgdvacqalESERAERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKpaggADEWQMRLDCAQME 1568
Cdd:COG4717 383 D-----------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE----LEELEEELEELEEE 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 291327510 1569 NDFLRKRLQQCEERLdSEMKARTELEQKLGELQSAYEEAKKMAHQ 1613
Cdd:COG4717 448 LEELREELAELEAEL-EQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1441-1807 |
8.44e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1441 TEQLRAKEEELtllrQKLQKSENSRSELRQNtdlLESKITDLTSELADErfkgdvacQALESERAERLQALRevQELKTK 1520
Cdd:TIGR04523 362 QRELEEKQNEI----EKLKKENQSYKQEIKN---LESQINDLESKIQNQ--------EKLNQQKDEQIKKLQ--QEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1521 YQQVQDALGEVQKQLEEAQqriqgaNLEEKPAggadewqmRLDCAQMENDFLRKRL-QQCEERLDSEMKARTELEQKLGE 1599
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIK------DLTNQDS--------VKELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1600 LQSAYEEAKKMAHQLKrkchhltwDLEDTRVLLENQQS------RNHELEKRQKKFDL-QLAQALGESMFE--KSLREKV 1670
Cdd:TIGR04523 491 LKSKEKELKKLNEEKK--------ELEEKVKDLTKKISslkekiEKLESEKKEKESKIsDLEDELNKDDFElkKENLEKE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1671 SQENNgvrwelgqlqqqleqkeQEASKLKQEVERLQGQKREllscasvgdqgvasLKERVWELETnalEQQKIHSQQENT 1750
Cdd:TIGR04523 563 IDEKN-----------------KEIEELKQTQKSLKKKQEE--------------KQELIDQKEK---EKKDLIKEIEEK 608
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 1751 IKQLEQLrqrfELEIERMKQMHqkdredqeEELEDVRQSCQKRLRQLEMQLEQEYEE 1807
Cdd:TIGR04523 609 EKKISSL----EKELEKAKKEN--------EKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1498-1609 |
8.82e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1498 QALESERAE---RLQAL-REVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAGG-ADEWQMRL---------D 1563
Cdd:COG1579 13 QELDSELDRlehRLKELpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArIKKYEEQLgnvrnnkeyE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 291327510 1564 CAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKK 1609
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1501-1814 |
1.09e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1501 ESERAERLQALREVQELKtKYQQVQDALGEVQKQLEEAQQRIQGANLEEKP--AGGADEWQMRLDCAQMENDFLRKRLQQ 1578
Cdd:pfam02029 3 DEEEAARERRRRAREERR-RQKEEEEPSGQVTESVEPNEHNSYEEDSELKPsgQGGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1579 CEERLDSEMKARTELEQKLGE--LQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKfdlqlaqa 1656
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAErkENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAE-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1657 lgESMFEKSLREKVSQENNGVRWELGQLQQQLEQKEQeasKLKQEVERLQGQKRELLSCAS-VGDQGVASLK---ERVWE 1732
Cdd:pfam02029 154 --EEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEK---KVKYESKVFLDQKRGHPEVKSqNGEEEVTKLKvttKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1733 LETNALEQQKIHSQQENTIKQLEQLRQRF-ELEIERMKQMHQKDRE-DQE-EELEDVRQSCQKRLRQLEMQLEQEYEEKQ 1809
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEaELElEELKKKREERRKLLEEEEQRRKQEEAERK 308
|
....*
gi 291327510 1810 VALHE 1814
Cdd:pfam02029 309 LREEE 313
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1442-1615 |
1.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKTKY 1521
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLEEAQQRIQganleekpaggadEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKArtELEQKLGELQ 1601
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIA-------------EREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDELL 189
|
170
....*....|....
gi 291327510 1602 SAYEEAKKMAHQLK 1615
Cdd:COG4372 190 KEANRNAEKEEELA 203
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1748-2130 |
1.26e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1748 ENTIKQLEQLRQRFELEIERMKQMHQKDREdQEEELEDVRQSCQKRL-----------RQLEMQLEQEYEEKQ--VALHE 1814
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNRE-EVEQLKDLYRELRKSLlanrfsfgpalDELEKQLENLEEEFSqfVELTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1815 KHD-LEGligtlcdqighrdFDVEKRLRRDLRRTHALLSDVQLLLATIEDsktsiskeeleKVHSQLEQSEAKCEDaLKT 1893
Cdd:PRK04778 190 SGDyVEA-------------REILDQLEEELAALEQIMEEIPELLKELQT-----------ELPDQLQELKAGYRE-LVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1894 QK-VLTADleNMHSELENVTRSKSLVDEQLYRLQFERA-DLLKRIDEDQGDLNDLMQKhkDLIAQsaadigqiQELQLQL 1971
Cdd:PRK04778 245 EGyHLDHL--DIEKEIQDLKEQIDENLALLEELDLDEAeEKNEEIQERIDQLYDILER--EVKAR--------KYVEKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1972 EETKKEKQKLREQLHMAQLRIQYLEQS---------TVeRAIVSRQEAIICDLENKTEFQKVQIKRFEVLVIRLRDSM-- 2040
Cdd:PRK04778 313 DTLPDFLEHAKEQNKELKEEIDRVKQSytlneseleSV-RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILkq 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2041 --------IKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEM---------QELAQREEEASrrcMELEKYVEELATVR 2103
Cdd:PRK04778 392 leeiekeqEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLeksnlpglpEDYLEMFFEVS---DEIEALAEELEEKP 468
|
410 420 430
....*....|....*....|....*....|
gi 291327510 2104 ---QTLQTDLETSIRRIADLQAALEEVVSS 2130
Cdd:PRK04778 469 inmEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
1443-1543 |
1.36e-04 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 43.69 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1443 QLRAKEEELTLLRQKLQKSENSRSELRQntdllesKITDLTSEladerfkgdvaCQALESERAERLQALREVQELKTKYQ 1522
Cdd:pfam12325 20 TIRRLEGELASLKEELARLEAQRDEARQ-------EIVKLMKE-----------NEELKELKKELEELEKELKELEQRYE 81
|
90 100
....*....|....*....|.
gi 291327510 1523 QVQDALGEVQKQLEEAQQRIQ 1543
Cdd:pfam12325 82 TTLELLGEKSEEVEELKADVE 102
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
739-1015 |
1.39e-04 |
|
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: 47.43 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 739 VLRAFGCVSTGHSRRATRFAMVMSLDFnATG------RVTAAQLQTVLLENSRVARQ------PQGEGNFEVFSQLLAGM 806
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQV-AFGlhpwefQICGCHISPFLLEKSRVTSErgresgDQNELNFHILYAMVAGV 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 807 DVD-----LRTELNLH--------QMAESSAFGMGLWSKPEDKQKAATAFSQLRGAMELLGISEGEQQAIWRVLAAIYHL 873
Cdd:cd14894 334 NAFpfmrlLAKELHLDgidcsaltYLGRSDHKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 874 G--AAGACKVGRKQFMRFEWANHAAEALgcdYEELNTATFKHHLRQIieqMTSGPQRQGLQDNEACSGLKMTGVECVEGM 951
Cdd:cd14894 414 GniELDYREVSGKLVMSSTGALNAPQKV---VELLELGSVEKLERML---MTKSVSLQSTSETFEVTLEKGQVNHVRDTL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 952 ASGLYQELFVAVVSLINRSFSSHHLS-----------------MASIMVVDTPGFQNPRHQgkdraaTFEELCYNYAQER 1014
Cdd:cd14894 488 ARLLYQLAFNYVVFVMNEATKMSALStdgnkhqmdsnasapeaVSLLKIVDVFGFEDLTHN------SLDQLCINYLSEK 561
|
.
gi 291327510 1015 L 1015
Cdd:cd14894 562 L 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1773-2055 |
1.66e-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: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1773 QKDREDQEEELEDVrqscQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIgtlcdqighrdfdveKRLRRDLRRTHALLS 1852
Cdd:COG4942 19 ADAAAEAEAELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRI---------------AALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1853 DVQLLLAtiedsktsiskeELEKVHSQLEQSEAKCEDALKTQkVLTADLENMHSELENVTRSKSLvdEQLYRlqfeRADL 1932
Cdd:COG4942 80 ALEAELA------------ELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDF--LDAVR----RLQY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1933 LKRIdedqgdlndlMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQyleqstverAIVSRQEAII 2012
Cdd:COG4942 141 LKYL----------APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE---------ALKAERQKLL 201
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 291327510 2013 CDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEA 2055
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1427-1667 |
1.67e-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: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1427 LLASLRpllSSTLGTEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLL----ESKITDLTSELaDERFKGDVAcQAlES 1502
Cdd:COG3096 925 LVAVLQ---SDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFsyedAVGLLGENSDL-NEKLRARLE-QA-EE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1503 ERAERLQALREVQELKTKYQQVQDAL----GEVQKQLEEAQQRIQG------ANLEEKPAGGADEWQMRLDCAQMENDFL 1572
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLkssrDAKQQTLQELEQELEElgvqadAEAEERARIRRDELHEELSQNRSRRSQL 1078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1573 RKRLQQCEerldSEMKartELEQKLGELQSAYEEAKKMAHQLKRkchhlTWDledtRVLlenQQSRNHELEKRQKKFDL- 1651
Cdd:COG3096 1079 EKQLTRCE----AEMD---SLQKRLRKAERDYKQEREQVVQAKA-----GWC----AVL---RLARDNDVERRLHRRELa 1139
|
250
....*....|....*..
gi 291327510 1652 -QLAQALgESMFEKSLR 1667
Cdd:COG3096 1140 yLSADEL-RSMSDKALG 1155
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1442-1844 |
1.80e-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: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLL-------RQKLQKSENSRSELrqntdlleskitdLTSELADErFKGDVAcQALESERAERLQALREV 1514
Cdd:COG3096 788 EELRAERDELAEQyakasfdVQKLQRLHQAFSQF-------------VGGHLAVA-FAPDPE-AELAALRQRRSELEREL 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1515 QELKTKYQQVQDALGEVQKQLEEAQQRIQGANL--EEKPAGGADEWQMRLDCAQMENDFLR---KRLQQCEERLDSemkA 1589
Cdd:COG3096 853 AQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLlaDETLADRLEELREELDAAQEAQAFIQqhgKALAQLEPLVAV---L 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1590 RTELEQkLGELQSAYEEAKKMAHQLKRKC----------HHLTWdlEDTRVLLENQQSRNHELEKRQKKFDLQLAQAlGE 1659
Cdd:COG3096 930 QSDPEQ-FEQLQADYLQAKEQQRRLKQQIfalsevvqrrPHFSY--EDAVGLLGENSDLNEKLRARLEQAEEARREA-RE 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1660 SMfeKSLREKVSQENngvrwelgqlqqqlEQKEQEASKLKQEVERLQGQKRELlscASVGDQGVASLKERVwELETNALE 1739
Cdd:COG3096 1006 QL--RQAQAQYSQYN--------------QVLASLKSSRDAKQQTLQELEQEL---EELGVQADAEAEERA-RIRRDELH 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1740 QQKIHSQQENTikQLEQLRQRFELEIErmkqmhqkdredqeeeledvrqSCQKRLRQLEMQLEQEYEEKQVALHEKHDLE 1819
Cdd:COG3096 1066 EELSQNRSRRS--QLEKQLTRCEAEMD----------------------SLQKRLRKAERDYKQEREQVVQAKAGWCAVL 1121
|
410 420
....*....|....*....|....*.
gi 291327510 1820 GLIgtlcdqighRDFDVEKRL-RRDL 1844
Cdd:COG3096 1122 RLA---------RDNDVERRLhRREL 1138
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1448-1932 |
2.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1448 EEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADerfkgdvacqaLESERAERLQALREVQElktkyqqvqdA 1527
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE-----------LESELEEAREAVEDRRE----------E 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1528 LGEVQKQLEEAQQRIQGANLEekpaggadewqmrLDCAQMENDFLRKRLQQCEERLdsemkarTELEQKLGELQSAYEEA 1607
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVD-------------LGNAEDFLEELREERDELRERE-------AELEATLRTARERVEEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1608 KKMahQLKRKCHHLTWDLEDTRVLlenqqSRNHELEKRQKKFDLQLAQAlgesmfeKSLREKVSQENNgvrwelgqlqqq 1687
Cdd:PRK02224 446 EAL--LEAGKCPECGQPVEGSPHV-----ETIEEDRERVEELEAELEDL-------EEEVEEVEERLE------------ 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1688 leqKEQEASKLKQEVERLQgQKRELLS------CASVGDQ--GVASLKERVWELETNALEQ----QKIHSQQEN---TIK 1752
Cdd:PRK02224 500 ---RAEDLVEAEDRIERLE-ERREDLEeliaerRETIEEKreRAEELRERAAELEAEAEEKreaaAEAEEEAEEareEVA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1753 QLEQLRQRFELEIERMKQMhqkdrEDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQvALHEKHD----LEGligtlcdq 1828
Cdd:PRK02224 576 ELNSKLAELKERIESLERI-----RTLLAAIADAEDEIERLREKREALAELNDERRE-RLAEKRErkreLEA-------- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1829 ighrDFDVEK--RLRRDLRRTHALLSDVQLLLATIEDSKTSISK---------EELEKVHSQLEQSEAKCEdALKTQKVL 1897
Cdd:PRK02224 642 ----EFDEARieEAREDKERAEEYLEQVEEKLDELREERDDLQAeigavenelEELEELRERREALENRVE-ALEALYDE 716
|
490 500 510
....*....|....*....|....*....|....*
gi 291327510 1898 TADLENMHSELENVTRSKSLvdEQLYRLQFERADL 1932
Cdd:PRK02224 717 AEELESMYGDLRAELRQRNV--ETLERMLNETFDL 749
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1871-2081 |
2.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1871 EELEKVHSQLEqseakceDALKTQKVLTaDLENMHSELENVTRSKSLVDE-----QLYRLQFERADLLKRIDEDQGDLND 1945
Cdd:COG4913 235 DDLERAHEALE-------DAREQIELLE-PIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1946 LMQKHKDLIAQSAADIGQIQELQLQLEETK-KEKQKLREQLHMAQLRIQYLEQstvERAIVSRQeAIICDLENKTEfqkv 2024
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER---RRARLEAL-LAALGLPLPAS---- 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 2025 qIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQR 2081
Cdd:COG4913 379 -AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
100-508 |
2.55e-04 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 46.21 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 100 SADIPGKEPPGAGDKDSTPVTSTSGERPQESGPTGTPAKRTL----PFKRGVRRGDVLLMVAKLDPELAKADQKVQPRDV 175
Cdd:COG5180 92 SPDTPEEQLGAPAGDLLVLPAAKTPELAAGALPAPAAAAALPkakvTREATSASAGVALAAALLQRSDPILAKDPDGDSA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 176 PVDKTPAPAKDSGGTKKGVTTGTSsapqpsmPEKTRTRGVGdTGQSTKGGKCQGTEGKGsrdpqtigqkegesqsteeqG 255
Cdd:COG5180 172 STLPPPAEKLDKVLTEPRDALKDS-------PEKLDRPKVE-VKDEAQEEPPDLTGGAD--------------------H 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 256 TRSQAQEAGNKEQLGTAEKEGGGPPKKMEKEDEPKVAGAEVRPVEPPVPLRKWGGFLGWRSKWDSPQSKDRVTESHRKDE 335
Cdd:COG5180 224 PRPEAASSPKVDPPSTSEARSRPATVDAQPEMRPPADAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPID 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 336 KTGDLQSPAVDRScgqlaeptGQPSGPTGQPSGPtgQLSESTGQPSG--PTGQPAG--PTGQPAGPTGQPAGPTGQPAGP 411
Cdd:COG5180 304 VKGVASAPPATRP--------VRPPGGARDPGTP--RPGQPTERPAGvpEAASDAGqpPSAYPPAEEAVPGKPLEQGAPR 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 412 TGQQQEAPVKMEGKVGRPQKKLVTPRKPRELPGVAAKTQNPEEsckAPDRiPTTGISAEAAKRDGQPESRVQGAGEPRVC 491
Cdd:COG5180 374 PGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALD---GGGR-ETASLGGAAGGAGQGPKADFVPGDAESVS 449
|
410
....*....|....*..
gi 291327510 492 TEEEVDvVKPQAEGHVE 508
Cdd:COG5180 450 GPAGLA-DQAGAAASTA 465
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1442-1785 |
2.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRaKEEELTLLRQKLQKSENSRSELRQNTDL--LESKITDLTSELADERFKgdVACQALESERAERLQA--LREVQEL 1517
Cdd:PTZ00121 1555 EELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYEEEKK--MKAEEAKKAEEAKIKAeeLKKAEEE 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1518 KTKYQQVQDALGEVQKQLE-----EAQQRIQGANLEEKP---------AGGADEWQMRLDCAQMENDFLRKRLQQCEERL 1583
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEelkkaEEENKIKAAEEAKKAeedkkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1584 DSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDledtrvllENQQSRNHELEKRQKKFDLQLAQALgesmfE 1663
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD--------EEEKKKIAHLKKEEEKKAEEIRKEK-----E 1778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1664 KSLREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASvgdQGVASLKERVWElETNALEQQKI 1743
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI---KEVADSKNMQLE-EADAFEKHKF 1854
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 291327510 1744 HSQQENT--------IKQLEQLRQRFELEIERMKQMHQKDREDQEEELED 1785
Cdd:PTZ00121 1855 NKNNENGedgnkeadFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1445-1821 |
2.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1445 RAKE--EELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKTKYQ 1522
Cdd:PRK02224 357 RAEElrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1523 QVQDALgevqkqlEEAQQRIQ-------GANLEEKP-AGGADEWqmrldcaqmendflRKRLQQCEERLDSEMKARTELE 1594
Cdd:PRK02224 437 TARERV-------EEAEALLEagkcpecGQPVEGSPhVETIEED--------------RERVEELEAELEDLEEEVEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1595 QKLGELQSAyEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRqkkfdlqlAQALGESMFEKslrEKVSQEn 1674
Cdd:PRK02224 496 ERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER--------AAELEAEAEEK---REAAAE- 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1675 ngVRWELGQLQQQLEQKEQEASKLKQEVERLqGQKRELLSCASVGDQGVASLKERVWEL-ETNALEQQKIHSQ------- 1746
Cdd:PRK02224 563 --AEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaELNDERRERLAEKrerkrel 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1747 ----QENTIKQLEQLRQRFELEIERMkqmhqkdrEDQEEELEDVRQSCQKRLRQLEMQLEQ--EYEEKQVALHEKHD-LE 1819
Cdd:PRK02224 640 eaefDEARIEEAREDKERAEEYLEQV--------EEKLDELREERDDLQAEIGAVENELEEleELRERREALENRVEaLE 711
|
..
gi 291327510 1820 GL 1821
Cdd:PRK02224 712 AL 713
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1512-2136 |
2.79e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1512 REVQELKTKYQQVQDALGEV-QKQLEEAQQRIQG-----ANLEEKPAGGADEWQMrldcAQMENDFLRKRLQQCEERLDS 1585
Cdd:pfam07111 140 RELEEIQRLHQEQLSSLTQAhEEALSSLTSKAEGlekslNSLETKRAGEAKQLAE----AQKEAELLRKQLSKTQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1586 EMKARTELEQKLGElqsayeeakkmahQLKRKCHHLTWDLEDTRVLlenqQSRNHELEKRQkkfDLQLAQALGESMFEKS 1665
Cdd:pfam07111 216 QVTLVESLRKYVGE-------------QVPPEVHSQTWELERQELL----DTMQHLQEDRA---DLQATVELLQVRVQSL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1666 LREKVSQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELetnaleQQKIHS 1745
Cdd:pfam07111 276 THMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL------QEQVTS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1746 Q-QENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEEledVRQSCQKRLRQLEMQLE---QEYEEKQVALHEKHdlegl 1821
Cdd:pfam07111 350 QsQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQE---ARRRQQQQTASAEEQLKfvvNAMSSTQIWLETTM----- 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1822 igTLCDQIGHRDFDVEKRLRRDLRRTHAllsdVQLLLAtiedSKTSISKEELEkvhsqleqSEAKCEDALKTQKVLTADL 1901
Cdd:pfam07111 422 --TRVEQAVARIPSLSNRLSYAVRKVHT----IKGLMA----RKVALAQLRQE--------SCPPPPPAPPVDADLSLEL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1902 ENMHselenvtrskslvdEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAadigqiQELQLQLEETKKEKQKL 1981
Cdd:pfam07111 484 EQLR--------------EERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVA------QQLEQELQRAQESLASV 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1982 REQLHMAQLRiqylEQSTVERAIVSRQEaiicdLENKTEF--QKVQIKRFEVLViRLRDSMIKMGEELSRAVKAEAQQRE 2059
Cdd:pfam07111 544 GQQLEVARQG----QQESTEEAASLRQE-----LTQQQEIygQALQEKVAEVET-RLREQLSDTKRRLNEARREQAKAVV 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2060 NSQYYQQRLEELKAEMQELAQREEEA--------SRRCMELEKYVE-ELATVRQTLQTDLETSIRRIADLQAALEE--VV 2128
Cdd:pfam07111 614 SLRQIQHRATQEKERNQELRRLQDEArkeegqrlARRVQELERDKNlMLATLQQEGLLSRYKQQRLLAVLPSGLDKksVV 693
|
....*...
gi 291327510 2129 SSDSDTES 2136
Cdd:pfam07111 694 SSPRPECS 701
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1441-1995 |
3.96e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1441 TEQLRAKEEELTLLRQKLQKSENSRSELrqntDLLESKITDLTSELADERFKG---DVACQALESERAERLQALREVQEL 1517
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRAR----IELEKKASALKRQLDRESDRNqelQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1518 KTKYQQVQDALGEVQK----QLEEAQQRIQGANLEekpaggADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTEL 1593
Cdd:pfam05557 78 NRLKKKYLEALNKKLNekesQLADAREVISCLKNE------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1594 EQKLGELQSAYEEAKKMAHQLKRKCHHLTwDLEDTRVLLENQQS---RNHELEKRQKKFDLQLAQaLGESMFEKSLrekV 1670
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIKELEFEIQ-SQEQDSEIVKNSKSelaRIPELEKELERLREHNKH-LNENIENKLL---L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1671 SQENNGVRwelgQLQQQLEQKEQEASKLKQEVERLQgqkRELLSCASVGDQGVASLkeRVWELETNALEQ----QKIHSQ 1746
Cdd:pfam05557 227 KEEVEDLK----RKLEREEKYREEAATLELEKEKLE---QELQSWVKLAQDTGLNL--RSPEDLSRRIEQlqqrEIVLKE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1747 QENTI-KQLEQLR-QRFELEIErmKQMHQKDREDQEEELEdvRQSCQKRLRQlemqleqeyeeKQVAL--HEKHDLEGLI 1822
Cdd:pfam05557 298 ENSSLtSSARQLEkARRELEQE--LAQYLKKIEDLNKKLK--RHKALVRRLQ-----------RRVLLltKERDGYRAIL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1823 GTLCDQIGHRDFDVEKRLRrdLRRTHALLSDVQLLLatiEDSKTSISK-EELEKVHSQLEQSEAKCEDALKTQkvltADL 1901
Cdd:pfam05557 363 ESYDKELTMSNYSPQLLER--IEEAEDMTQKMQAHN---EEMEAQLSVaEEELGGYKQQAQTLERELQALRQQ----ESL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1902 ENMHSELENVTRSKSLVDEqlyrLQFERADLLKRIDEdqgdLNDLMQKHKdliAQSAADIGQIQELQLQLEETKKEKQKL 1981
Cdd:pfam05557 434 ADPSYSKEEVDSLRRKLET----LELERQRLREQKNE----LEMELERRC---LQGDYDPKKTKVLHLSMNPAAEAYQQR 502
|
570
....*....|....
gi 291327510 1982 REQLHMAQLRIQYL 1995
Cdd:pfam05557 503 KNQLEKLQAEIERL 516
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1964-2124 |
4.82e-04 |
|
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: 45.40 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1964 IQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQSTVERAIV----------SRQEAIICDLEN-KTEFQKVQiKRFEVL 2032
Cdd:pfam05701 79 IEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVaakaqlevakARHAAAVAELKSvKEELESLR-KEYASL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2033 VIRlRDSMIKMGEElsraVKAEAQQREnsqyyqQRLEELKAE----MQEL-----AQREEEASRRCM------------- 2090
Cdd:pfam05701 158 VSE-RDIAIKRAEE----AVSASKEIE------KTVEELTIEliatKESLesahaAHLEAEEHRIGAalareqdklnwek 226
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 291327510 2091 ELEKYVEELATVRQT------LQTDLETSIRRIADLQAAL 2124
Cdd:pfam05701 227 ELKQAEEELQRLNQQllsakdLKSKLETASALLLDLKAEL 266
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1309-1803 |
4.84e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1309 FRRRFQvldpALLKKLDLTSEELDERKVVEEL--LKTLDLekkavaVGHSQVFLKagvvsRLERQREKLVSRNI-----V 1381
Cdd:PRK04778 23 LRKRNY----KRIDELEERKQELENLPVNDELekVKKLNL------TGQSEEKFE-----EWRQKWDEIVTNSLpdieeQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1382 LFQAAcrGFLSRQEYKKLK--IRRLATLC--IQKNLAVflkvkdwpwwgLLASLRPLLSSTlgtEQLRAKEEELTLLRQK 1457
Cdd:PRK04778 88 LFEAE--ELNDKFRFRKAKheINEIESLLdlIEEDIEQ-----------ILEELQELLESE---EKNREEVEQLKDLYRE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1458 LQKSENSRSELRQNT-DLLESKITDLTSELadERFK-----GDVAcQALE--SERAERLQALR----------------- 1512
Cdd:PRK04778 152 LRKSLLANRFSFGPAlDELEKQLENLEEEF--SQFVeltesGDYV-EAREilDQLEEELAALEqimeeipellkelqtel 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1513 --EVQELKTKYQQVQDA---LGEVQ--KQLEEAQQRIQG--ANLEEkpaggadewqMRLDCAQMENDFLRKRLQQCEERL 1583
Cdd:PRK04778 229 pdQLQELKAGYRELVEEgyhLDHLDieKEIQDLKEQIDEnlALLEE----------LDLDEAEEKNEEIQERIDQLYDIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1584 DSEMKARTELEQKLGELQSAYEEAKKMAHQLKrkchhltwdLEDTRVllenQQSR--NHELEKRQKKFDLQLAQAlgESM 1661
Cdd:PRK04778 299 EREVKARKYVEKNSDTLPDFLEHAKEQNKELK---------EEIDRV----KQSYtlNESELESVRQLEKQLESL--EKQ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1662 FEKSLREKVSQEnngvrwelgqlqqqleqkeQEASKLKQEVERLQGQkrellscasvgdqgvaslkervweletnaLEQq 1741
Cdd:PRK04778 364 YDEITERIAEQE-------------------IAYSELQEELEEILKQ-----------------------------LEE- 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 1742 kIHSQQENTIKQLEQLR----------QRFELEIERMKQMHQKDR-----EDQEEELEDVrqscQKRLRQLEMQLEQ 1803
Cdd:PRK04778 395 -IEKEQEKLSEMLQGLRkdeleareklERYRNKLHEIKRYLEKSNlpglpEDYLEMFFEV----SDEIEALAEELEE 466
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1925-2126 |
5.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1925 LQFERADLLKRIDEDQGDLndlmqkHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREqlhmAQLRIQYLEQStverai 2004
Cdd:COG4717 40 LAFIRAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2005 VSRQEAIICDLENKTEFQKVQIKRFEVLvirlrdsmikmgeelSRAVKAEAQQREnsqyYQQRLEELKAEMQELAQREEE 2084
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLY---------------QELEALEAELAE----LPERLEELEERLEELRELEEE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 291327510 2085 ASRRCMELEKYVEELATVRQTLQT----DLETSIRRIADLQAALEE 2126
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAE 210
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1432-1814 |
5.71e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1432 RPLLSSTLGTEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADErfkgdvacqaleSERAERLQal 1511
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL------------KEQMQEIQ-- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1512 REVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLEEKPAGGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKART 1591
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1592 ELEQKLgeLQSAYEEAKKMAHQLK-----------RKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQalgES 1660
Cdd:TIGR00618 650 ALQLTL--TQERVREHALSIRVLPkellasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE---IE 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1661 MFEKSLREKVSQENngvrwelgqlqqqleqkeqeaSKLKQEVERLQGQKRELLsCASVGDQGVASLKERVwELETNALEQ 1740
Cdd:TIGR00618 725 NASSSLGSDLAARE---------------------DALNQSLKELMHQARTVL-KARTEAHFNNNEEVTA-ALQTGAELS 781
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1741 QKIhSQQENTIKQLEQLRQrfelEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLeqeyEEKQVALHE 1814
Cdd:TIGR00618 782 HLA-AEIQFFNRLREEDTH----LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL----EEKSATLGE 846
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1442-1656 |
6.14e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.83 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVAcQALESERAERLQALREVQELKTKY 1521
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEELE-QRLLQTSAQLQELQNQLAQLNSQL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1522 QQVQDALGEVQKQLEEAQQRIQ--GANLEEKPAGGADEWQMRLDCAQMENDFLRKRLQQceerLDSEMKARTELeQKLGE 1599
Cdd:pfam12795 109 IELQTRPERAQQQLSEARQRLQqiRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDM----LEQELLSNNNR-QDLLK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 1600 LQSAYEEAKKmahqlkrkchhltWDLEDTRVLLENQQSrnhelEKRQKKFDLQLAQA 1656
Cdd:pfam12795 184 ARRDLLTLRI-------------QRLEQQLQALQELLN-----EKRLQEAEQAVAQT 222
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1874-2139 |
6.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1874 EKVHSQLEQSeAKCEDALKTQKVLTADLENMHSELENVTRSKSlvDEQLYRLQFERADllKRIDEDQGDLNDLMQKHKDL 1953
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKE--ETEQLKQQLAQAP--AKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1954 IAQSAADIGqIQELQLQLEETKKEKQKLREQLhmAQLRIQYLEQSTV-ERAivsrQEAIicdLENKTEFQkvQIkrfevl 2032
Cdd:PRK11281 114 TRETLSTLS-LRQLESRLAQTLDQLQNAQNDL--AEYNSQLVSLQTQpERA----QAAL---YANSQRLQ--QI------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2033 virlrDSMIKMGEELSRAVKAEAQQRENSQY--------YQQRLEELKAEMQELAQ-REEEASRRCMELEKYVeelatvr 2103
Cdd:PRK11281 176 -----RNLLKGGKVGGKALRPSQRVLLQAEQallnaqndLQRKSLEGNTQLQDLLQkQRDYLTARIQRLEHQL------- 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 291327510 2104 QTLQTDLetSIRRIADLQAALEEVVSSDsDTESVQT 2139
Cdd:PRK11281 244 QLLQEAI--NSKRLTLSEKTVQEAQSQD-EAARIQA 276
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
357-511 |
7.09e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 357 GQPSGPTGQPSGPTGQLSESTGQPSGPTGQPAGPTGQPAGPTGQPAGPTGQPAGPTGQQQEAPVKMEGKVGRPQKKLVTP 436
Cdd:PRK07764 596 GGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 437 RKPRELPGVAAKTQNPEESCKAP----DRIPTTGISAEAAKRDGQPESRVQGAGEPRvctEEEVDVVKPQAEGHVESIP 511
Cdd:PRK07764 676 AAPAAPPPAPAPAAPAAPAGAAPaqpaPAPAATPPAGQADDPAAQPPQAAQGASAPS---PAADDPVPLPPEPDDPPDP 751
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1588-1825 |
7.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1588 KARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQKKFDLQLAQALGEsmfEKSLR 1667
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1668 EKVSQENNgvrwelgqlqqqleqkeqeasKLKQEVERLQGQKRE-----LLSCASVGDqgvasLKERVWELETNALEQQK 1742
Cdd:COG4942 97 AELEAQKE---------------------ELAELLRALYRLGRQpplalLLSPEDFLD-----AVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1743 IHSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLI 1822
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
...
gi 291327510 1823 GTL 1825
Cdd:COG4942 230 ARL 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1442-1609 |
7.80e-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: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERfkgdvacQALESERAER-LQAL-REVQELKT 1519
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------EQLGNVRNNKeYEALqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1520 KYQQVQDALGEVQKQLEEAQQRIQGANLE-EKPAGGADEWQMRLDcaqmendflrKRLQQCEERLDSEMKARTELEQKLG 1598
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAElAELEAELEEKKAELD----------EELAELEAELEELEAEREELAAKIP 173
|
170
....*....|..
gi 291327510 1599 E-LQSAYEEAKK 1609
Cdd:COG1579 174 PeLLALYERIRK 185
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1507-1617 |
9.30e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.44 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1507 RLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGanLEEKpAGGADEWQMRLDCAQMENDFLRKRLQQCEERldsE 1586
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEE--LEEE-RRQAEEEAERLEQKRQEAEEEKERLEESAEM---E 74
|
90 100 110
....*....|....*....|....*....|.
gi 291327510 1587 MKARTELEQKLGELQsayEEAKKMAHQLKRK 1617
Cdd:pfam20492 75 AEEKEQLEAELAEAQ---EEIARLEEEVERK 102
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1442-1770 |
9.54e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSRSELRQNTDL-------------LESKITDLTSELADERFKGDVACQALE------S 1502
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEeaaeqlA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1503 ERAERLQALR-EVQELKTKYQQVQDALGEVQ----------KQLEEAQQRIQGANLEEKpagGADEWQMRLdcaQMENDF 1571
Cdd:COG3096 379 EAEARLEAAEeEVDSLKSQLADYQQALDVQQtraiqyqqavQALEKARALCGLPDLTPE---NAEDYLAAF---RAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1572 LRKRLQQCEERLDSEMKARTELEQKLGELQS---------AYEEAKKMAHQLKRKCHH------LTWDLEDTRVLLENQQ 1636
Cdd:COG3096 453 ATEEVLELEQKLSVADAARRQFEKAYELVCKiageversqAWQTARELLRRYRSQQALaqrlqqLRAQLAELEQRLRQQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1637 SRNHELEKRQKKFDLQLAQA--LGESMFE-KSLREKVSQENNGVRwelgqlqqqleqkeQEASKLKQEVERLQGQKRELL 1713
Cdd:COG3096 533 NAERLLEEFCQRIGQQLDAAeeLEELLAElEAQLEELEEQAAEAV--------------EQRSELRQQLEQLRARIKELA 598
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1714 SCASV---GDQGVASLKERVWELETNA----------LEQQKIHSQQENtikQLEQLRQRFELEIERMKQ 1770
Cdd:COG3096 599 ARAPAwlaAQDALERLREQSGEALADSqevtaamqqlLEREREATVERD---ELAARKQALESQIERLSQ 665
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1839-1984 |
9.61e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1839 RLRRDLRRTHALLSDVQLLLATIEDSKTSIsKEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHS--ELENVTRSKS 1916
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAA-KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291327510 1917 LVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAAdigQIQELQLQLEETKKEKQKLREQ 1984
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAE 164
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1929-2141 |
1.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1929 RADLLK-RIDEDQGDLNDLMQKHKDLIAQSAADI-----------GQIQELQLQLEETKKEKQKLRE---QLHMAQLRIQ 1993
Cdd:pfam07888 28 RAELLQnRLEECLQERAELLQAQEAANRQREKEKerykrdreqweRQRRELESRVAELKEELRQSREkheELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1994 YL-EQSTVERAIVSRQ----EAIICDLEN--KTEFQKVQIKrfEVLVIRLRDSMIKMGEELsravKAEAQQRENsqyYQQ 2066
Cdd:pfam07888 108 ASsEELSEEKDALLAQraahEARIRELEEdiKTLTQRVLER--ETELERMKERAKKAGAQR----KEEEAERKQ---LQA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 2067 RLEELKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTESVQTAV 2141
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1442-1608 |
1.11e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 42.73 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1442 EQLRAKEEELTLLRQKLQKSENSrseLRQNTDLLESKITDLtseladERFKGDVACQ--ALESERAERLQAL-REVQELK 1518
Cdd:pfam15665 39 LQYKSKIGEELDLKRRIQTLEES---LEQHERMKRQALTEF------EQYKRRVEERelKAEAEHRQRVVELsREVEEAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1519 TKYQQVQDALGEVQKQLEEAQQriqgANLEEKPAGGADEWQMRLD-CAQMENDFLRKR-------------LQQCEERLD 1584
Cdd:pfam15665 110 RAFEEKLESFEQLQAQFEQEKR----KALEELRAKHRQEIQELLTtQRAQSASSLAEQekleelhkaelesLRKEVEDLR 185
|
170 180
....*....|....*....|....*
gi 291327510 1585 SEMKART-ELEQKLGELQSAYEEAK 1608
Cdd:pfam15665 186 KEKKKLAeEYEQKLSKAQAFYEREL 210
|
|
| DUF4472 |
pfam14739 |
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ... |
1906-2009 |
1.13e-03 |
|
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.
Pssm-ID: 464291 [Multi-domain] Cd Length: 107 Bit Score: 40.75 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1906 SELENVTRSKSLVDeqlyrLQFERADLLKRIDEDQGDLNDLMQKHK----DLIAQSAADIGQIQELQLQLEETKKEKQKL 1981
Cdd:pfam14739 1 SEEEKLQISKALVD-----LQIENNKLREQYEAEKFELKNKLLNLEnrvlELELRLEKAAEEIQDLRERLRELEDDRREL 75
|
90 100
....*....|....*....|....*...
gi 291327510 1982 REQLHMaqLRIQYLEQSTVERAIVSRQE 2009
Cdd:pfam14739 76 AEEFVA--LKKNYQALSKELEAEVAKNQ 101
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
673-763 |
1.20e-03 |
|
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: 41.95 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 673 PAHVTSLAQRAYWALLSQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGR--------------VSVEKLRATFT 738
Cdd:cd01363 32 QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgetegwvylteitvTLEDQILQANP 111
|
90 100
....*....|....*....|....*
gi 291327510 739 VLRAFGCVSTGHSRRATRFAMVMSL 763
Cdd:cd01363 112 ILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1739-2127 |
1.53e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1739 EQQKIHSQQENTIKQLEQLRQrfelEIERMKQMHQKDREdQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEkhdL 1818
Cdd:pfam06160 87 ALDEIEELLDDIEEDIKQILE----ELDELLESEEKNRE-EVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAE---I 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1819 EGLIGTLCDQIGHRDF----DVEKRLRRDLRRTHALLSDVQLLLATIEDsktsiskeELEKvhsQLEQSEAKCEDALKTQ 1894
Cdd:pfam06160 159 EEEFSQFEELTESGDYlearEVLEKLEEETDALEELMEDIPPLYEELKT--------ELPD---QLEELKEGYREMEEEG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1895 KVLTADleNMHSELENVTRSKSLVDEQLYRLQFERA-DLLKRIDEDQGDLNDLMQKHKDliAQsaadigqiQELQLQLEE 1973
Cdd:pfam06160 228 YALEHL--NVDKEIQQLEEQLEENLALLENLELDEAeEALEEIEERIDQLYDLLEKEVD--AK--------KYVEKNLPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1974 TKKEKQKLREQLHMAQLRIQYLEQS------TVERA---------IVSRQEAIICDLENKT-------EFQKVQIKRFEV 2031
Cdd:pfam06160 296 IEDYLEHAEEQNKELKEELERVQQSytlnenELERVrglekqleeLEKRYDEIVERLEEKEvayselqEELEEILEQLEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2032 LvirlRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKaemqelaqREEEASRrcmelekyveeLATVRQTLQTDLE 2111
Cdd:pfam06160 376 I----EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIK--------RLVEKSN-----------LPGLPESYLDYFF 432
|
410
....*....|....*.
gi 291327510 2112 TSIRRIADLQAALEEV 2127
Cdd:pfam06160 433 DVSDEIEDLADELNEV 448
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1733-1816 |
1.72e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1733 LETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQ-------KRLRQLEMQL---- 1801
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeadeiiKELRQLQKGGyasv 604
|
90
....*....|....*.
gi 291327510 1802 -EQEYEEKQVALHEKH 1816
Cdd:PRK00409 605 kAHELIEARKRLNKAN 620
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1920-2098 |
1.75e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1920 EQLYRLQferaDLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQLRIQYLEQst 1999
Cdd:COG1579 7 RALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2000 veraivsRQEAI-----ICDLENKTEFQKVQIKRFEvlvIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEELKAE 2074
Cdd:COG1579 81 -------QLGNVrnnkeYEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....
gi 291327510 2075 MQELAQREEEASRRCMELEKYVEE 2098
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1748-1939 |
1.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1748 ENTIKQLEQLrQRFELEIERMKqmhqKDREDQEEELEDVrqscQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCD 1827
Cdd:COG1579 3 PEDLRALLDL-QELDSELDRLE----HRLKELPAELAEL----EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1828 QIGhrdfDVEKRLR--RDLRRTHALLSDvqllLATIEDSKTSISKEELEkVHSQLEQSEAKCEDALKTQKVLTADLENMH 1905
Cdd:COG1579 74 RIK----KYEEQLGnvRNNKEYEALQKE----IESLKRRISDLEDEILE-LMERIEELEEELAELEAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|....
gi 291327510 1906 SELENVTRSkslVDEQLYRLQFERADLLKRIDED 1939
Cdd:COG1579 145 AELDEELAE---LEAELEELEAEREELAAKIPPE 175
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
260-488 |
2.01e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 260 AQEAGNKEQLGTAEKEGGGPPKKMEKEDEPKVAGAEVRPVEPPVPlrkwGGFLGWRSKWDSPQSKDRVTESHRKDEktgd 339
Cdd:PRK07764 586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPA----GAAAAPAEASAAPAPGVAAPEHHPKHV---- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 340 lQSPAVDRSCGQLAEPTGQPsGPTGQPSGPTgqlSESTGQPSGPTGQPAGPTGQPAGPTGQPAGPTGQPAGPTGQQQEAP 419
Cdd:PRK07764 658 -AVPDASDGGDGWPAKAGGA-APAAPPPAPA---PAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPS 732
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327510 420 VKMEGKVGRPQKKLVTPRKPRELPGVAAKTQNPEESCKAPDRIPTTGISAEAAKRDGQPESRVQGAGEP 488
Cdd:PRK07764 733 PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA 801
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1504-1814 |
2.01e-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: 42.98 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1504 RAERLQALREVQELKT-KYQQVQDALGEVQKQLEEAQQRIQGANLEEKpaggaDEWQMRLDCAQMENDflrkrlqqcEER 1582
Cdd:pfam13868 50 EEERERALEEEEEKEEeRKEERKRYRQELEEQIEEREQKRQEEYEEKL-----QEREQMDEIVERIQE---------EDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1583 LDSEMKARtELEQKLGELQSAYEEAKKMAHQLKRKChhltwDLEDTRVL--LENQQSRNHELEKRQKKfdlqlaqalges 1660
Cdd:pfam13868 116 AEAEEKLE-KQRQLREEIDEFNEEQAEWKELEKEEE-----REEDERILeyLKEKAEREEEREAEREE------------ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1661 mfEKSLREKVSQenngvrwelgqlqqqleqkeqeasKLKQEVERLQGQKRELlscasvgDQgvasLKERVWELETNALEQ 1740
Cdd:pfam13868 178 --IEEEKEREIA------------------------RLRAQQEKAQDEKAER-------DE----LRAKLYQEEQERKER 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291327510 1741 QKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQScQKRLRQLEMQLEQEYEEKQVALHE 1814
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRK-QAEDEEIEQEEAEKRRMKRLEHRR 293
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1505-1714 |
2.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1505 AERLQALREVQELKTKYQQVQDALGEVQKQLEEAQQRIQGANLeekpaggadewqmRLDCAQMENDFLRKRLQQCEERLD 1584
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEA-------------RLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1585 SEMKARTELEQKLGELQSAyEEAKKMAHQlkrkchhltwdledtrvlLENQQSRNHELEKRQKKFDLQLAQALGESMFEK 1664
Cdd:COG1579 70 EVEARIKKYEEQLGNVRNN-KEYEALQKE------------------IESLKRRISDLEDEILELMERIEELEEELAELE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 291327510 1665 SLREKVSQENNGVRwelgqlqqqlEQKEQEASKLKQEVERLQGQKRELLS 1714
Cdd:COG1579 131 AELAELEAELEEKK----------AELDEELAELEAELEELEAEREELAA 170
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1733-2080 |
2.25e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1733 LETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEY------E 1806
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAsseelsE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1807 EKQVALHEKHD-------LEGLIGTLCDQIGHRDFDVEkRLRRDLRRTHALLSDV-------QLLLATIEDSKTSISKEE 1872
Cdd:pfam07888 116 EKDALLAQRAAhearireLEEDIKTLTQRVLERETELE-RMKERAKKAGAQRKEEeaerkqlQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1873 LEKVHS---------QLEQSEAKCEDALKTQKVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDL 1943
Cdd:pfam07888 195 QELRNSlaqrdtqvlQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1944 ndlmqkHKDLIaQSAADIGQIQELQLQLEETK----KEKQKLREQLHMAQLRIQYLEqstveRAIVSRQEAIicdLENKT 2019
Cdd:pfam07888 275 ------HQARL-QAAQLTLQLADASLALREGRarwaQERETLQQSAEADKDRIEKLS-----AELQRLEERL---QEERM 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 2020 EFQKvqikrFEVLVIRLRDSMIKMGEELSRAVKaeaQQRENSQYYQQRLEELKAEMQELAQ 2080
Cdd:pfam07888 340 EREK-----LEVELGREKDCNRVQLSESRRELQ---ELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1565-1808 |
2.32e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1565 AQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEK 1644
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1645 RQKKFDLQLAQALGeSMFEKSLREKV-----SQENNGVRWELGQLQQQLEQKEQEASKLKQEVERLQGQKRellscasvg 1719
Cdd:COG4942 98 ELEAQKEELAELLR-ALYRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1720 dqgvaslkervwELETNALEQQKIHSQQENTIKQLEQLRQRFELEIERMkqmhQKDREDQEEELEDVRQScQKRLRQLEM 1799
Cdd:COG4942 168 ------------ELEAERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQE-AEELEALIA 230
|
....*....
gi 291327510 1800 QLEQEYEEK 1808
Cdd:COG4942 231 RLEAEAAAA 239
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1836-2125 |
2.43e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1836 VEKRLRRDLRRTHALLSDVQLLLATIEDSKTSIS--KEELEKVHSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTR 1913
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEqlEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1914 SKSLVDEQLYRLQFERADL---LKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEETKKEKQKLREQLHMAQL 1990
Cdd:COG4372 109 EAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1991 RIQYLEQSTVERAIVSRQEAIicDLENKTEFQKVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQRLEE 2070
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLI--ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 2071 LKAEMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLETSIRRIADLQAALE 2125
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1968-2126 |
2.46e-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: 43.19 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1968 QLQLEETKKEKQKLR-EQLHMAQLRIQYLEQSTVERAivSRQEAIICDLENKtefQKVQIKRFEvlviRLRdsmiKMGEE 2046
Cdd:pfam17380 352 RIRQEERKRELERIRqEEIAMEISRMRELERLQMERQ--QKNERVRQELEAA---RKVKILEEE----RQR----KIQQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2047 LSRAVKAEAQQRENSQYYQQRLEELKA---------------EMQELAQREEEASRRCMELEKYVEELATVRQTLQTDLE 2111
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAremervrleeqerqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
|
170
....*....|....*
gi 291327510 2112 TSIRriADLQAALEE 2126
Cdd:pfam17380 499 KELE--ERKQAMIEE 511
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1441-1543 |
2.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1441 TEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKTK 1520
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
|
90 100
....*....|....*....|...
gi 291327510 1521 YQQVQDALGEVQKQLEEAQQRIQ 1543
Cdd:COG4372 138 IAELQSEIAEREEELKELEEQLE 160
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1553-1672 |
2.67e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.38 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1553 GGADEWQMRLDCAQMENDFLRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKChhltwDLEDTRVLL 1632
Cdd:pfam15294 126 GGSALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEIS-----DLEEKMAAL 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 291327510 1633 ENQQSRN-HELEKRQKKFDLQLAQALGE--------SMFEKSLREKVSQ 1672
Cdd:pfam15294 201 KSDLEKTlNASTALQKSLEEDLASTKHEllkvqeqlEMAEKELEKKFQQ 249
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1869-1978 |
3.85e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1869 SKEELEKVHSQ---LEQSEAKCEDALKTQKVLTADLE----NMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQG 1941
Cdd:pfam05911 686 LKEEFEQLKSEkenLEVELASCTENLESTKSQLQESEqliaELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEA 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 291327510 1942 DLNDLMQK--------------HKDLIAQSaadigqiQELQLQLEETKKEK 1978
Cdd:pfam05911 766 ELNELRQKfealeveleeekncHEELEAKC-------LELQEQLERNEKKE 809
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1498-1648 |
3.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1498 QALESERAERLQALREVQELKtkyQQVQDALGEVQKQLEEAQQRIQGANLEEKpaggaDEWQMRLDCAQMENDFLRKRLQ 1577
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL---KEAEKLKEELEEKKEKLQEEEDKLLEEAE-----KEAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327510 1578 QCEERLDSEMKARtELEQKLGELQSAYEEAKKMAHQLKRKCHHLTwdlEDTRVLLENQQSRNHELEKRQKK 1648
Cdd:PRK00409 595 QLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELK---VGDEVKYLSLGQKGEVLSIPDDK 661
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1572-1652 |
3.90e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1572 LRKRLQQCEERLDSEMKARTELEQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVLLENQQSRNHELEKRQ--KKF 1649
Cdd:COG4026 133 LREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRllEVF 212
|
...
gi 291327510 1650 DLQ 1652
Cdd:COG4026 213 SLE 215
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1454-1670 |
4.01e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1454 LRQKLQKSENSRSELRQN--TDLLESKITDLTSELADerfKGDVACQalESERAerlqalREVQELKTKYQQVQDalgEV 1531
Cdd:PRK10929 84 LRQQLNNERDEPRSVPPNmsTDALEQEILQVSSQLLE---KSRQAQQ--EQDRA------REISDSLSQLPQQQT---EA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1532 QKQLEEAQQRIQGANLEEKPAGGA----------------DEWQM-------RLDCAQMENDFLRKRlqqcEERLDSEMK 1588
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQAqltalqaesaalkalvDELELaqlsannRQELARLRSELAKKR----SQQLDAYLQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1589 A-RTEL-EQKLGELQSAYEEAKKMAHQLKRKCHHLTWDLEDTRVL--LENQQSRNHEL---EKRQKKFD-LQLAQALGes 1660
Cdd:PRK10929 226 AlRNQLnSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELsqALNQQAQRMDLiasQQRQAASQtLQVRQALN-- 303
|
250
....*....|
gi 291327510 1661 mfekSLREKV 1670
Cdd:PRK10929 304 ----TLREQS 309
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1436-1803 |
4.56e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1436 SSTLGTEqLRAKEEELTLLRQKLQ---KSENSRSELRQNTDLLESKiTDLTSELADERFKGDVACQALESER-------A 1505
Cdd:COG3096 322 ESDLEQD-YQAASDHLNLVQTALRqqeKIERYQEDLEELTERLEEQ-EEVVEEAAEQLAEAEARLEAAEEEVdslksqlA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1506 ERLQALREVQELKTKYQQVQDAlgevqkqLEEAQQRIQGANLEEKpagGADEWQMRLdcaQMENDFLRKRLQQCEERLDS 1585
Cdd:COG3096 400 DYQQALDVQQTRAIQYQQAVQA-------LEKARALCGLPDLTPE---NAEDYLAAF---RAKEQQATEEVLELEQKLSV 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1586 EMKARTELEQklgelqsAYEEAKKMAHQLKRKCHHLTwdledTRVLLENQQSRNHELEKRQkkfdlQLAQALGEsmfeks 1665
Cdd:COG3096 467 ADAARRQFEK-------AYELVCKIAGEVERSQAWQT-----ARELLRRYRSQQALAQRLQ-----QLRAQLAE------ 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1666 LREKVSQENNGVRWELG------QLQQQLEQKEQEASKLKQEVERLQGQKRELLSCASVGDQGVASLKERVWELETNALE 1739
Cdd:COG3096 524 LEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPA 603
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291327510 1740 QQKIHSQQEntikQL-EQLRQRFELEIERMKQMHQKdrEDQEEELEDVRQSCQKRLRQLEMQLEQ 1803
Cdd:COG3096 604 WLAAQDALE----RLrEQSGEALADSQEVTAAMQQL--LEREREATVERDELAARKQALESQIER 662
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1932-2136 |
5.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1932 LLK-RIDEDQGDLNDL-MQK---------HKDLIAQSAADIGQ-IQELQLQLEETKKEKQKLREQLhmAQLRIQYLEqst 1999
Cdd:PHA02562 171 LNKdKIRELNQQIQTLdMKIdhiqqqiktYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEI--EELTDELLN--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2000 VERAIVSRQEAIiCDLENKTEFQKVQIKRFevlvirlrDSMIKMGEE----------LSRAVKAEAQQRENSQYYQQRLE 2069
Cdd:PHA02562 246 LVMDIEDPSAAL-NKLNTAAAKIKSKIEQF--------QKVIKMYEKggvcptctqqISEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 2070 ELKAEMQELAQREEEASrrcmELEKYVEELATVRQTLQTDLETSIRRIADLQAALEEVVSSDSDTES 2136
Cdd:PHA02562 317 KLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1509-1994 |
5.52e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1509 QALREVQELKTKYQQVQDA-LGEVQKQLEEAqqriqganleekpAGGADewQMRLDCAQMENDFLRKRLQQCEERLDSEM 1587
Cdd:PRK04778 61 QSEEKFEEWRQKWDEIVTNsLPDIEEQLFEA-------------EELND--KFRFRKAKHEINEIESLLDLIEEDIEQIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1588 KARTELEQKLGELQSAYEEAKKMAHQLKRKchhltwdledtrvLLENqqsrNHELEKRQKKFDLQLAQAlgESMFEKslr 1667
Cdd:PRK04778 126 EELQELLESEEKNREEVEQLKDLYRELRKS-------------LLAN----RFSFGPALDELEKQLENL--EEEFSQ--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1668 ekvsqenngvrwelgqlqqqleqkeqeASKLKQEVERLQGqkRELLScasvgdqgvaSLKErvwelETNALEQQ-----K 1742
Cdd:PRK04778 184 ---------------------------FVELTESGDYVEA--REILD----------QLEE-----ELAALEQImeeipE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1743 IHSQQENTIK-QLEQLRQ---------------RFELEIERMKQMHQKDREDQEE-ELEDVR---QSCQKRLRQLEMQLE 1802
Cdd:PRK04778 220 LLKELQTELPdQLQELKAgyrelveegyhldhlDIEKEIQDLKEQIDENLALLEElDLDEAEeknEEIQERIDQLYDILE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1803 QEYEEKQVALHEKHDLEGLIGTLCDQ----------------IGHRDFDVEKRLRRDLrrtHALLSDVQLLLATIEDSKT 1866
Cdd:PRK04778 300 REVKARKYVEKNSDTLPDFLEHAKEQnkelkeeidrvkqsytLNESELESVRQLEKQL---ESLEKQYDEITERIAEQEI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1867 SIS--KEELEKVHSQLEQSEAKCEDALKTQKVLTAD-------LENMHSELENVTR--SKS----LVDEqlYRLQFERAD 1931
Cdd:PRK04778 377 AYSelQEELEEILKQLEEIEKEQEKLSEMLQGLRKDelearekLERYRNKLHEIKRylEKSnlpgLPED--YLEMFFEVS 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291327510 1932 llKRIDEdqgdLNDLMQKHKdliaqsaADIGQIQEL----QLQLEETKKEKQKLREQLHMAQLRIQY 1994
Cdd:PRK04778 455 --DEIEA----LAEELEEKP-------INMEAVNRLleeaTEDVETLEEETEELVENATLTEQLIQY 508
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1743-1993 |
5.90e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1743 IHSQQEntikQLEQLRQRFELEI-----------ERMKQMHQKDREdQEEELEDVRQSCQKRLRQLEMqLEQEYEE-KQV 1810
Cdd:COG0497 128 IHGQHE----HQSLLDPDAQRELldafagleellEEYREAYRAWRA-LKKELEELRADEAERARELDL-LRFQLEElEAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1811 AL--HEKHDLEGLIGTLcdqighrdFDVEKrLRRDLRRTHALLSDVQL-LLATIEDSKTSISK-----EELEKVHSQLEQ 1882
Cdd:COG0497 202 ALqpGEEEELEEERRRL--------SNAEK-LREALQEALEALSGGEGgALDLLGQALRALERlaeydPSLAELAERLES 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1883 SEAKCEDAlktqkvlTADLENMHSELEnvtrskslVDEQlyRLQferadllkRIDEDQGDLNDLMQKHK----DLIA--- 1955
Cdd:COG0497 273 ALIELEEA-------ASELRRYLDSLE--------FDPE--RLE--------EVEERLALLRRLARKYGvtveELLAyae 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 291327510 1956 QSAADI-------GQIQELQLQLEETKKEKQKLREQLHmaQLRIQ 1993
Cdd:COG0497 328 ELRAELaelensdERLEELEAELAEAEAELLEAAEKLS--AARKK 370
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1763-2081 |
6.04e-03 |
|
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: 41.34 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1763 LEIERMKQMHQKDREDQEEELEDVRQSCQ------KRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLcdqighrdfdv 1836
Cdd:pfam15905 59 LELKKKSQKNLKESKDQKELEKEIRALVQergeqdKRLQALEEELEKVEAKLNAAVREKTSLSASVASL----------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1837 eKRLRRDLRRTHALLSdvQLLLATIEDSKTSISKEELEKVHSQLEqseakcedalKTQKVLTADLENMHSelenvtrsks 1916
Cdd:pfam15905 128 -EKQLLELTRVNELLK--AKFSEDGTQKKMSSLSMELMKLRNKLE----------AKMKEVMAKQEGMEG---------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1917 lvdeQLYRLQferadllKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQelqlQLEETKKEKQKLREQLHMAQLRIQYLE 1996
Cdd:pfam15905 185 ----KLQVTQ-------KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE----KLLEYITELSCVSEQVEKYKLDIAQLE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1997 Q--STVERAIVSRQ---EAIICDLENKTEFQKVQIKRFEvlviRLRDSMIKMGEELSRAVKAEAQQrensqyYQQRLEEL 2071
Cdd:pfam15905 250 EllKEKNDEIESLKqslEEKEQELSKQIKDLNEKCKLLE----SEKEELLREYEEKEQTLNAELEE------LKEKLTLE 319
|
330
....*....|
gi 291327510 2072 KAEMQELAQR 2081
Cdd:pfam15905 320 EQEHQKLQQK 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1443-1617 |
6.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1443 QLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADerfkgdvacqaLESERAERLQALREVQELKTKYQ 1522
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-----------LEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1523 QVQDA------LGEVQKQLEEAQQRIQgaNLEEkpaggadewqmRLDCAQMENDFLRKRLQQCEERLDsemKARTELEQK 1596
Cdd:COG1579 80 EQLGNvrnnkeYEALQKEIESLKRRIS--DLED-----------EILELMERIEELEEELAELEAELA---ELEAELEEK 143
|
170 180
....*....|....*....|.
gi 291327510 1597 LGELQSAYEEAKKMAHQLKRK 1617
Cdd:COG1579 144 KAELDEELAELEAELEELEAE 164
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2046-2130 |
6.87e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2046 ELSRAVKAEAQQRENSQYYQQRLEELKAEMQEL-AQREEEASRRCMELEKYVEELATVRQTLQtDLETSIRRI-ADLQAA 2123
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQLATERSARR-EAEAELERLqEELRYL 126
|
....*..
gi 291327510 2124 LEEVVSS 2130
Cdd:pfam09787 127 EEELRRS 133
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
338-440 |
6.91e-03 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 40.02 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 338 GDLQSPAVDRSCGQLAEPTGQPSGPTGQPSGPTGQLSESTGQPSGPTGQPAGPTGQ----------PAGPTGQPAGPTGQ 407
Cdd:pfam15240 52 GGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQggnqqqgpppPGKPQGPPPQGGGP 131
|
90 100 110
....*....|....*....|....*....|...
gi 291327510 408 PAGPTGQQQEAPVKMEGKVGRPQKKLVTPRKPR 440
Cdd:pfam15240 132 PPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQG 164
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1963-2126 |
7.06e-03 |
|
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: 40.27 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1963 QIQELQLQLEETKKEKQKLREQLHmaqlriqyleqstveraivsRQEAIICDLENK-TEFQKVQIKRFE---VLVIRLRD 2038
Cdd:pfam15619 19 ELAELQSKLEELRKENRLLKRLQK--------------------RQEKALGKYEGTeSELPQLIARHNEevrVLRERLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2039 SMIKmGEELSRAVKAEAQQRENSQYYQQRL------------EELKAEMQELAQREEEASRRCMELEKYVE--------- 2097
Cdd:pfam15619 79 LQEK-ERDLERKLKEKEAELLRLRDQLKRLeklsedknlaerEELQKKLEQLEAKLEDKDEKIQDLERKLElenksfrrq 157
|
170 180 190
....*....|....*....|....*....|.
gi 291327510 2098 ELATVRQTLQTDLETSI--RRIADLQAALEE 2126
Cdd:pfam15619 158 LAAEKKKHKEAQEEVKIlqEEIERLQQKLKE 188
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1696-2020 |
7.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1696 SKLKQEVERLQ---GQKRELLSCASVGDQGVASLKERVWElETNALEQQKIHSQQ-----ENTIKQLEQLRQRFELEIER 1767
Cdd:pfam07888 76 RELESRVAELKeelRQSREKHEELEEKYKELSASSEELSE-EKDALLAQRAAHEArirelEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1768 MKQmHQKDREDQEEELEDVRQSCQKRLRQLEMQLEQEYEEKQVALHEKHDLEGLIGTLCDQIGHRDFDVEKRLRR--DLR 1845
Cdd:pfam07888 155 MKE-RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaENE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1846 RTHALLSDVQLLLATIEdSKTSISKEELEKV-----HSQLEQSEAKCEDALKTQKVLTADLE------NMHSELENVTRS 1914
Cdd:pfam07888 234 ALLEELRSLQERLNASE-RKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1915 KSLVDEQLYRLQFERADLLKRIDEDQgdlndlMQKHKdliaqSAADIGQIQELQL-QLEETKKEKQKLREQLHMAQlriQ 1993
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEER------MEREK-----LEVELGREKDCNRvQLSESRRELQELKASLRVAQ---K 378
|
330 340
....*....|....*....|....*....
gi 291327510 1994 YLEQSTVEraivsRQEAI--ICDLENKTE 2020
Cdd:pfam07888 379 EKEQLQAE-----KQELLeyIRQLEQRLE 402
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1966-2123 |
7.43e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1966 ELQLQLEETKKEKQKLREQLH-----MAQLR--IQYLEQSTVERAIVSRQEaiICDLENKTEFQKVQIKRFEVLVIRLRD 2038
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQklrgqIQQLRteLQELEAQQQEEAESSREQ--LQELEEQLATERSARREAEAELERLQE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2039 SMIKMGEELSRAvKAEAQQRENSQyyQQRLEELKAEM----------QELAQREEEASRRCMELEKYVEELATVRQTLQT 2108
Cdd:pfam09787 122 ELRYLEEELRRS-KATLQSRIKDR--EAEIEKLRNQLtsksqssssqSELENRLHQLTETLIQKQTMLEALSTEKNSLVL 198
|
170
....*....|....*
gi 291327510 2109 DLETSIRRIADLQAA 2123
Cdd:pfam09787 199 QLERMEQQIKELQGE 213
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1895-2099 |
7.99e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1895 KVLTADLENMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQKHKDLIAQSAADIGQIQELQLQLEET 1974
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1975 KKEKQKLREQLHMAQLRIQYLEQSTVERAIVSRQeaiICDLENKTEFQKVQIKRFEVLVIRLRdsmiKMGEELSRAVKAE 2054
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGSIDKLRKE---IERLEWRQQTEVLSPEEEKELVEKIK----ELEKELEKAKKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 291327510 2055 AQQRENSQYYQQ------RLEELKAEMQELAQREEEASRRCMELEKYVEEL 2099
Cdd:COG1340 157 EKNEKLKELRAElkelrkEAEEIHKKIKELAEEAQELHEEMIELYKEADEL 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1870-2135 |
8.85e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1870 KEELEKVHSQLEQSEAKcedalktqkvltadleNMHSELENVTRSKSLVDEQLYRLQFERADLLKRIDEDQGDLNDLMQK 1949
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEK----------------DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1950 HKDLIAQSAAdigqIQELQLQLEETKKEKQKLREQLHMAQLRIQYLE--------QSTVERAIVSRQEAIICDLENktef 2021
Cdd:PRK02224 250 REELETLEAE----IEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaEAGLDDADAEAVEARREELED---- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 2022 QKVQIKRfEVLVIRLRDSMIKmgEELSRAVKAEAQQRENSQYYQQRLEELKAEMQELAQREEEASRRCMELEKYVEELAT 2101
Cdd:PRK02224 322 RDEELRD-RLEECRVAAQAHN--EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270
....*....|....*....|....*....|....
gi 291327510 2102 VRQTLQTDLETSIRRIADLQAALEEVVSSDSDTE 2135
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1367-1613 |
9.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1367 RLERQREKLVSRnivLFQAAcrgflsrQEYKKLKiRRLATLCIQKNLAVFLKVKDWP---WWGL---LASLRPLLSS-TL 1439
Cdd:COG4913 614 ALEAELAELEEE---LAEAE-------ERLEALE-AELDALQERREALQRLAEYSWDeidVASAereIAELEAELERlDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1440 GTEQLRAKEEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKT 1519
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1520 KYQQVQDALGEVQKQLEEAQQRIQGAnLEEKPAGGADEWQMRLD---------------CAQMENDFLRKRLQQCEERLD 1584
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEE-LERAMRAFNREWPAETAdldadleslpeylalLDRLEEDGLPEYEERFKELLN 841
|
250 260
....*....|....*....|....*....
gi 291327510 1585 SEMkartelEQKLGELQSAYEEAKKMAHQ 1613
Cdd:COG4913 842 ENS------IEFVADLLSKLRRAIREIKE 864
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1448-1702 |
9.43e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 41.38 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1448 EEELTLLRQKLQKSENSRSELRQNTDLLESKITDLTSELADERFKGDVACQALESERAERLQALREVQELKTKYQQVQDA 1527
Cdd:pfam09726 401 EQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEA 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1528 LGEVQKQLEEAQQRiqgANLEEKPA--GGADEWQMRLDCAqmenDFLRKRLQQCE---ERLDSEMKARTE----LEQKLG 1598
Cdd:pfam09726 481 RASAEKQLAEEKKR---KKEEEATAarAVALAAASRGECT----ESLKQRKRELEseiKKLTHDIKLKEEqireLEIKVQ 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1599 ELqSAYEEAKKmahqlkrkchhltwdleDTRVL---LENQQSRNHELEKR---QKKFDLQLAQALGES-----MFEKSLR 1667
Cdd:pfam09726 554 EL-RKYKESEK-----------------DTEVLmsaLSAMQDKNQHLENSlsaETRIKLDLFSALGDAkrqleIAQGQIY 615
|
250 260 270
....*....|....*....|....*....|....*
gi 291327510 1668 EKvSQEnngvrwelgqlqqqleqkeqeASKLKQEV 1702
Cdd:pfam09726 616 QK-DQE---------------------IKDLKQKI 628
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1851-2108 |
9.53e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1851 LSDVQLLLATIEDSKtsiskeelekvhSQLEQSEAKCEDALKTQKVLTADLENMHSELENVTRS--KSLVDEQLYRLQFE 1928
Cdd:PRK11281 65 LEQTLALLDKIDRQK------------EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlSTLSLRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1929 RADLLKRIDEDQGDLNDLmqkhkdLI--------AQSA--ADIGQIQELQLQLEETKKEKQKLR-EQLHMAQLRIQYLEQ 1997
Cdd:PRK11281 133 TLDQLQNAQNDLAEYNSQ------LVslqtqperAQAAlyANSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327510 1998 STVERaivsRQEaiicdLENKTEFQ----------KVQIKRFEVLVIRLRDSMIKMGEELSRAVKAEAQQRENSQYYQQR 2067
Cdd:PRK11281 207 QNDLQ----RKS-----LEGNTQLQdllqkqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 291327510 2068 lEELKAEMQ---ELAQREEEASRRCMELekyveelatVRQTLQT 2108
Cdd:PRK11281 278 -PLVAQELEinlQLSQRLLKATEKLNTL---------TQQNLRV 311
|
|
| |
