|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
378-642 |
2.11e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.19 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 378 LIATCSLDHSVRIWNFE-LNMLELYKEFQEEAYSVALHPTGLFILVGFCDK-LRLMNLLIDD-IRTFKEFTvRGCRECAF 454
Cdd:COG2319 134 TLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTGHT-GAVRSVAF 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 455 SYGGHLFA-AVNGNVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNTLTSKRESESVLKTCMYT 533
Cdd:COG2319 213 SPDGKLLAsGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 534 NVTISPDAKIIFAVGTDCTLK--EIQDCQIVKEVPSNDVTYTAVALSHLGRVLFIGTSAGTVRAlkYPLPIQNEWIEYQG 611
Cdd:COG2319 293 SVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTLTG 370
|
250 260 270
....*....|....*....|....*....|.
gi 2064967944 612 HAAPITKMAVTFDDQFLLTVSEDNCLLIWKI 642
Cdd:COG2319 371 HTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
363-641 |
5.24e-29 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 118.21 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 363 HSGIITGLSICIRKPLIATCSLDHSVRIWNFELNMLEL-YKEFQEEAYSVALHPTGLFILVGFCDK-LRLMNL-LIDDIR 439
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLeTGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 440 TFKEFTvRGCRECAFSYGGHLFAAVNG-NVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNTlt 518
Cdd:cd00200 88 TLTGHT-SYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 519 skrESESVLKTCM-----YTNVTISPDAKIIFAVGTDCTLK--EIQDCQIVKEVPSNDVTYTAVALSHLGRVLFIGTSAG 591
Cdd:cd00200 165 ---RTGKCVATLTghtgeVNSVAFSPDGEKLLSSSSDGTIKlwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2064967944 592 TVRAlkYPLPIQNEWIEYQGHAAPITKMAVTFDDQFLLTVSEDNCLLIWK 641
Cdd:cd00200 242 TIRV--WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
315-594 |
5.80e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 102.68 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 315 IMCMCISPLEETLATSTDRGqlySITLTSAEMGKEGEEayfefLSDsfHSGIITGLSICirkP---LIATCSLDHSVRIW 391
Cdd:COG2319 123 VRSVAFSPDGKTLASGSADG---TVRLWDLATGKLLRT-----LTG--HSGAVTSVAFS---PdgkLLASGSDDGTVRLW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 392 NFE-LNMLELYKEFQEEAYSVALHPTGLFILVGFCDK-LRLMNLliDD---IRTFK--EFTVRGCrecAFSYGGHLFAAV 464
Cdd:COG2319 190 DLAtGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGtVRLWDL--ATgklLRTLTghSGSVRSV---AFSPDGRLLASG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 465 -NGNVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNTLTSKRESESVLKTCMYTNVTISPDAKI 543
Cdd:COG2319 265 sADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKT 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 544 IFAVGTDCTLK--EIQDCQIVKEVPSNDVTYTAVALSHLGRVLFIGTSAGTVR 594
Cdd:COG2319 345 LASGSDDGTVRlwDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVR 397
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
315-554 |
2.58e-22 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 98.56 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 315 IMCMCISPLEETLATSTDRGQLYSITLTSAEMGKEGEEayfeflsdsfHSGIITGLSICIRKPLIATCSLDHSVRIWNFE 394
Cdd:cd00200 12 VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG----------HTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 395 LN-MLELYKEFQEEAYSVALHPTGLFILVGFCDKlrlmNLLIDDIRTFK-EFTVRGCRE--------------------- 451
Cdd:cd00200 82 TGeCVRTLTGHTSYVSSVAFSPDGRILSSSSRDK----TIKVWDVETGKcLTTLRGHTDwvnsvafspdgtfvasssqdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 452 -------------------------CAFSY-GGHLFAAVNGNVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSC 505
Cdd:cd00200 158 tiklwdlrtgkcvatltghtgevnsVAFSPdGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2064967944 506 GMDGAVYEWNTltskrESESVLKTC-MYTN----VTISPDAKIIFAVGTDCTLK 554
Cdd:cd00200 238 SEDGTIRVWDL-----RTGECVQTLsGHTNsvtsLAWSPDGKRLASGSADGTIR 286
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
438-642 |
8.20e-20 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 91.24 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 438 IRTFKEFTVrGCRECAFSYGGHLFAAVNG-NVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNt 516
Cdd:cd00200 2 RRTLKGHTG-GVTCVAFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 517 lTSKRESESVLK--TCMYTNVTISPDAKIIFAVGTDCTLK--EIQDCQIVKEVPSNDVTYTAVALSHLGRVLFIGTSAGT 592
Cdd:cd00200 80 -LETGECVRTLTghTSYVSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2064967944 593 VRA--LKYPLPIQNewieYQGHAAPITKMAVTFDDQFLLTVSEDNCLLIWKI 642
Cdd:cd00200 159 IKLwdLRTGKCVAT----LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
312-515 |
1.13e-19 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 90.86 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 312 QQEIMCMCISPLEETLATStdrGQLYSITLTSAEMGKEGeeayFEFLSdsfHSGIITGLSICIRKPLIATCSLDHSVRIW 391
Cdd:cd00200 93 TSYVSSVAFSPDGRILSSS---SRDKTIKVWDVETGKCL----TTLRG---HTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 392 NFELNML-ELYKEFQEEAYSVALHPTGLFILVGFCDKlrlmNLLIDDIRTFKEFTV-----RGCRECAFSYGGHLFAAVN 465
Cdd:cd00200 163 DLRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKCLGTlrgheNGVNSVAFSPDGYLLASGS 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 466 G-NVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWN 515
Cdd:cd00200 239 EdGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
659-1096 |
1.13e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 92.01 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 659 SEEILVTKSDLEEKNQLMLELKTRVDELKMeneyQLRLRDMNYNEKLKELTEKFiQEIDSLKTKNQVLKTEKEKLELDHK 738
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEK----QKKENKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 739 ALMDEMMEKhskeQRDLESTNNQKLMLEY---------EKYLELQMKSQHMQEDFeRQLHSSEQSKTEALEELTLQYES- 808
Cdd:TIGR04523 177 LLEKEKLNI----QKNIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNt 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 ----------------KLQEKV-------RKLKECEDKSQQQKREYEEMIKIMEED-----------ADREILDIR---V 851
Cdd:TIGR04523 252 qtqlnqlkdeqnkikkQLSEKQkeleqnnKKIKELEKQLNQLKSEISDLNNQKEQDwnkelkselknQEKKLEEIQnqiS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 852 KFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKE 931
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 932 KRIYDLRKKNTELEKfkfvldyKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNL---KLKATD 1008
Cdd:TIGR04523 412 EQIKKLQQEKELLEK-------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinKIKQNL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1009 KDRRREM-QRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQLYSCYVQKSDvvDIDGVDADIQK-EYNRQREHLEKT 1086
Cdd:TIGR04523 485 EQKQKELkSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES--KISDLEDELNKdDFELKKENLEKE 562
|
490
....*....|
gi 2064967944 1087 VASLKKKLAK 1096
Cdd:TIGR04523 563 IDEKNKEIEE 572
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
452-640 |
5.61e-18 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 87.66 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 452 CAFSYGGHLFA-AVNGNVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNTLTSKRESESVLKTC 530
Cdd:COG2319 84 VAFSPDGRLLAsASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 531 MYTNVTISPDAKIIFAVGTDCTLK--EIQDCQIVKEVPSNDVTYTAVALSHLGRVLFIGTSAGTVRAlkYPLPIQNEWIE 608
Cdd:COG2319 164 AVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL--WDLATGKLLRT 241
|
170 180 190
....*....|....*....|....*....|..
gi 2064967944 609 YQGHAAPITKMAVTFDDQFLLTVSEDNCLLIW 640
Cdd:COG2319 242 LTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
670-999 |
3.92e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 670 EEKNQLML-ELKTRVDELKMENE----YQ---LRLRDMNYNEKLKEL--TEKFIQEIDSlktKNQVLKTEKEKLELDHKA 739
Cdd:TIGR02169 186 IERLDLIIdEKRQQLERLRREREkaerYQallKEKREYEGYELLKEKeaLERQKEAIER---QLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 740 LMDEMMEKhskeQRDLESTNNQKLMLEYEKYLELQmksqhmqedfeRQLHS--SEQSKTEALEELTLQYESKLQEKVRKL 817
Cdd:TIGR02169 263 LEKRLEEI----EQLLEELNKKIKDLGEEEQLRVK-----------EKIGEleAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 818 KECEDKSQQQKREYEEMI--------KIMEEDADREilDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKN 889
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIeeerkrrdKLTEEYAELK--EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 890 METEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIydlrKKNTElekfkfvldyKIKELKKQIEPRENNI 969
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI----KKQEW----------KLEQLAADLSKYEQEL 471
|
330 340 350
....*....|....*....|....*....|
gi 2064967944 970 KEMREQIQKMEGELEQFQRrntqmELNIAE 999
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQR-----ELAEAE 496
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
453-640 |
2.16e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 79.57 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 453 AFSYGGHLFAAVNGNVIHIYSTTTFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNTLTSKRESESVLKTCMY 532
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 533 TNVTISPDAKIIFAVGTDCTLK--EIQDCQIVKEVPSNDVTYTAVALSHLGRVLFIGTSAGTVRAlkYPLPIQNEWIEYQ 610
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRlwDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL--WDLATGKLLRTLT 201
|
170 180 190
....*....|....*....|....*....|
gi 2064967944 611 GHAAPITKMAVTFDDQFLLTVSEDNCLLIW 640
Cdd:COG2319 202 GHTGAVRSVAFSPDGKLLASGSADGTVRLW 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
718-1000 |
5.63e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.11 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 718 SLKTKNQVLKTEKEKLELDHKALMDEM--MEKHSKEQRDLESTNNQK---LMLEYEKYLELQMKSQHMQEDFERQLHSSE 792
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELrrIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 793 QSKTEALEELTlQYESKLQEKVRKLKECEDKSQQQKREY-EEMIKIMEEDAdREILDIRVKFEKMLTE-EKETN-VHLKD 869
Cdd:TIGR02169 751 QEIENVKSELK-ELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAEL-SKLEEEVSRIEARLREiEQKLNrLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 870 EtgIMRKKFSSLQREIDDknmeteklkVELQKlhgviKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKF 949
Cdd:TIGR02169 829 E--YLEKEIQELQEQRID---------LKEQI-----KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 950 VLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAEL 1000
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
660-974 |
1.14e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.91 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 660 EEILVTKSDLEEKNQLMLELKTRVDELKMEneyqLRLRDMNYNEKLKELTEKfIQEIDSLKTKNQVLKTEKEKLELDHKA 739
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 740 LMDEMMEKHSKEQ------RDLEStNNQKLMLEYEKYLELQMKSQHMQEDFERQ----------LHSSEQSKTEALEELT 803
Cdd:TIGR04523 396 LESKIQNQEKLNQqkdeqiKKLQQ-EKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRESLETQLKVLS 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 804 LQYESKLQEKVRKLKECEDKSQQ------QKREYEEMIKimeeDADREILDIRVKFEKMLTEEKETNVHLKD-ETGIMRK 876
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKElkklneEKKELEEKVK----DLTKKISSLKEKIEKLESEKKEKESKISDlEDELNKD 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 877 KF----SSLQREIDDKNMETEKLKVELQKL-------HGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELE 945
Cdd:TIGR04523 551 DFelkkENLEKEIDEKNKEIEELKQTQKSLkkkqeekQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
330 340
....*....|....*....|....*....
gi 2064967944 946 KFKFVLDYKIKELKKQIEPRENNIKEMRE 974
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
682-1030 |
1.58e-14 |
|
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: 78.24 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 682 RVDELKMENEYQLRLRDMNYNEKLKELTEKFIQEIDslktKNQVLKTEKEKLELDHKALMDEMMEKHSKeqRDLESTNNQ 761
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----RQAAIYAEQERMAMERERELERIRQEERK--RELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 762 KLMLEYEKYLEL---QMKSQHMQEDFERQLhsseqsktEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIM 838
Cdd:pfam17380 369 EIAMEISRMRELerlQMERQQKNERVRQEL--------EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 839 EEDADREILdiRVKFEKMlTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKV---ELQKLHGVIKSLEKDILS 915
Cdd:pfam17380 441 EEERAREME--RVRLEEQ-ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlekELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 916 LKKEIQERDETIQDKEKR--IYDLRKKNTELEKfkfvldykikelKKQIEPRENNIKEMREQIQKMEGELEQFQR----R 989
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRreAEEERRKQQEMEE------------RRRIQEQMRKATEERSRLEAMEREREMMRQivesE 585
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2064967944 990 NTQMELNIAELNLKLKATDKDRRREMQRvHDIEALVRRFKT 1030
Cdd:pfam17380 586 KARAEYEATTPITTIKPIYRPRISEYQP-PDVESHMIRFTT 625
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
658-1108 |
6.13e-14 |
|
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: 76.70 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 658 YSEEILVTKSDLEEKNQL-----------MLELKTRVDELKMENE--YQLRLRDMNYNEKLKELTEKFIQEIDSLKT-KN 723
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELhekqkfylrqsVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKClKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 724 QVLKTEKEKLE------LDHKALM---------------------DEMMEKH--------SKEQRDL------------- 755
Cdd:pfam15921 163 DMLEDSNTQIEqlrkmmLSHEGVLqeirsilvdfeeasgkkiyehDSMSTMHfrslgsaiSKILRELdteisylkgrifp 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 756 ----------ESTNNQKLMLEYEKYLELQMKSQHMQE--------DFERQLHSSEQSKTEALEE-------LTLQYESKL 810
Cdd:pfam15921 243 vedqlealksESQNKIELLLQQHQDRIEQLISEHEVEitgltekaSSARSQANSIQSQLEIIQEqarnqnsMYMRQLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 811 QEKVRKLKEcedKSQQQKREYEEMIKIMEED---ADREILDIRV------------------------KFEKMLTEEKET 863
Cdd:pfam15921 323 ESTVSQLRS---ELREAKRMYEDKIEELEKQlvlANSELTEARTerdqfsqesgnlddqlqklladlhKREKELSLEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 864 NVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKL---------------HGVIKSLEKdILSLKKEIQERDE--- 925
Cdd:pfam15921 400 NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecqgqmerqmaaiQGKNESLEK-VSSLTAQLESTKEmlr 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 926 -----------TIQDKEKRIYDL-----------RKKNTELEKFKFVLDYKIKE--------------------LKKQIE 963
Cdd:pfam15921 479 kvveeltakkmTLESSERTVSDLtaslqekeraiEATNAEITKLRSRVDLKLQElqhlknegdhlrnvqteceaLKLQMA 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 964 PRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLkatdKDRRREMQ-----------RVHDIEALVRRFKTDL 1032
Cdd:pfam15921 559 EKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI----NDRRLELQefkilkdkkdaKIRELEARVSDLELEK 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1033 HRCVSFIQEPKKLKDSIRQ-----LYSCYVQKSDVVDIDGVDADIQKEYNRQREHLEKTVASLKKKL--AKDTLASTKSA 1105
Cdd:pfam15921 635 VKLVNAGSERLRAVKDIKQerdqlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLksAQSELEQTRNT 714
|
...
gi 2064967944 1106 PSS 1108
Cdd:pfam15921 715 LKS 717
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
669-1096 |
6.25e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 669 LEEKNQLMLELKTRVDELKmENEYQLRLRDMNYNEKLKELTEKfIQEIDS-------LKTKNQVLKTEKEKLELDHKALM 741
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEkeerleeLKKKLKELEKRLEELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 742 D-----EMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEELTlqyESKLQEKV-- 814
Cdd:PRK03918 366 EakakkEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVcg 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 815 RKLKEcEDKSQQQKREYEEMIKIMEE-----DADREILDIRVKFEKMLTEEKE--TNVHLKDETGIMRKKFSSLQRE-ID 886
Cdd:PRK03918 443 RELTE-EHRKELLEEYTAELKRIEKElkeieEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEeLE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 887 DKNMETEKLKVELQKLHGVIKSLEKDILS---LKKEIQERDETIQDKEKRIYDLrkkNTELEKFKFVLDYKIKELKKQIE 963
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL---LKELEELGFESVEELEERLKELE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 964 PRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRRemqrvhdIEALVRRFKTDLHRcvsfiqEPK 1043
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-------LEELEKKYSEEEYE------ELR 665
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 1044 KLKDSIRQLYScyvqksdvvdidGVDADIqKEYNRQREHLEKTVASLKKKLAK 1096
Cdd:PRK03918 666 EEYLELSRELA------------GLRAEL-EELEKRREEIKKTLEKLKEELEE 705
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
670-1157 |
9.94e-14 |
|
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: 76.31 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 670 EEKNQLMLELKTRVDELKMENEYQLRLRDMNYNEKL------KELTEKFIqEIDSLKTKNQVLKTE-KEKLELDHKALM- 741
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSItidhlrRELDDRNM-EVQRLEALLKAMKSEcQGQMERQMAAIQg 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 742 -DEMMEKHSKEQRDLESTnnqKLMLEyeKYLELQMKSQHMQEDFER---QLHSSEQSKTEALE-------ELTLQYESKL 810
Cdd:pfam15921 456 kNESLEKVSSLTAQLEST---KEMLR--KVVEELTAKKMTLESSERtvsDLTASLQEKERAIEatnaeitKLRSRVDLKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 811 QEkVRKLKECEDKSQQQKREYEEM-IKIMEEDADREILdiRVKFEKMLteeKETNVHLKdETGIMRKKFSSLQREIDDKN 889
Cdd:pfam15921 531 QE-LQHLKNEGDHLRNVQTECEALkLQMAEKDKVIEIL--RQQIENMT---QLVGQHGR-TAGAMQVEKAQLEKEINDRR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 890 METEKLKVelqklhgvikslekdilsLKkeiQERDETIQDKEKRIYDLrkkntELEKFKFVLD-----YKIKELKKQIEP 964
Cdd:pfam15921 604 LELQEFKI------------------LK---DKKDAKIRELEARVSDL-----ELEKVKLVNAgserlRAVKDIKQERDQ 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 965 RENNIKEMREQIQKMEGELE----QFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEA----------------L 1024
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGsdghamkvamgmqkqiT 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1025 VRRFKTD-LHRCVSFIQE----PKKLKDSIRQLYSCYVQKSDVVDIDGVDADIQKEYNRQREHlektvaSLKKKLAKDTL 1099
Cdd:pfam15921 738 AKRGQIDaLQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER------RLKEKVANMEV 811
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 1100 ASTKSApsspvsrLNFdGESERIIQLQRVEIGRLRneiLIHG-DTHLVQTPSTVNLPSV 1157
Cdd:pfam15921 812 ALDKAS-------LQF-AECQDIIQRQEQESVRLK---LQHTlDVKELQGPGYTSNSSM 859
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
667-1005 |
1.58e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.06 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 667 SDLEEKNQLMLELKTRVDELKMENEYQLRLRDMNYNEKLKELTE--------------KFIQEIDSLKTKNQVLKTEKEK 732
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkleeiqnqisQNNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 733 LELDHKALMDEMMEKHS---KEQRDLESTNNQKLMLEYEKY-LELQMKSQHMQE-DFERQLHSSEQSKTEALEELTLQYE 807
Cdd:TIGR04523 354 SESENSEKQRELEEKQNeieKLKKENQSYKQEIKNLESQINdLESKIQNQEKLNqQKDEQIKKLQQEKELLEKEIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 808 SKLQEKvRKLKECEDKSQQQKREYEEMIKIME------EDADREILDIRVKFEKMLTEEKETN---VHLKDETGIMRKKF 878
Cdd:TIGR04523 434 TIIKNN-SEIKDLTNQDSVKELIIKNLDNTREsletqlKVLSRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 SSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEI--QERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIK 956
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2064967944 957 ELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLK 1005
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
682-1018 |
5.95e-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: 73.22 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 682 RVDELKMENEYQLRLRD--MNYNEKLKELTEKFIQEidslktknqvLKTEKEKLELDhkalmdemMEKHSKEQRDLESTN 759
Cdd:pfam05483 89 KIKKWKVSIEAELKQKEnkLQENRKIIEAQRKAIQE----------LQFENEKVSLK--------LEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 760 NQ-----KLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSKTE----ALEELTLQYESKLQEKVRKLKECEDKSQQQKRE 830
Cdd:pfam05483 151 NAtrhlcNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEkmilAFEELRVQAENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 831 YEEMIKIMEEDADREILDIRVKFEKM------LTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHG 904
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 905 VIKSLEKDILSLKKEIQERDEtiqDKEKRIYDLRKKN-------TELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQ 977
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTE---EKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2064967944 978 KMEGELEQFQRRNTQMELNIAELNLKLKATDK--DRRREMQRV 1018
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKllDEKKQFEKI 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
766-1027 |
1.09e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 766 EYEKYLELQmksqHMQEDFERQLhSSEQSKTEALEELTLQYESKLQEKVRKLKECEdKSQQQKREYEEMIKIMEEDADRE 845
Cdd:TIGR02169 672 EPAELQRLR----ERLEGLKREL-SSLQSELRRIENRLDELSQELSDASRKIGEIE-KEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 846 ILDIRVKfekmLTEEKETNVHLKDETGIMRKKFSSLQREIDD------------KNMETEKLKVELQKLHGVIKSLEKDI 913
Cdd:TIGR02169 746 LSSLEQE----IENVKSELKELEARIEELEEDLHKLEEALNDlearlshsripeIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 914 -------LSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQF 986
Cdd:TIGR02169 822 nrltlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2064967944 987 QRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRR 1027
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
782-1054 |
1.81e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 782 EDFERQLHSSEQSKTEALEELtlqyeSKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREildirvkfEKMLTEEK 861
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKEL-----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--------EERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 862 ETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKN 941
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 942 TELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDI 1021
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270
....*....|....*....|....*....|....*..
gi 2064967944 1022 EALVRRFKTDLH----RCVSFIQEPKKLKDSIRQLYS 1054
Cdd:TIGR02168 914 RRELEELREKLAqlelRLEGLEVRIDNLQERLSEEYS 950
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
687-1052 |
4.20e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 687 KMENEYQLRLRDMNYNEKLKELTEKFIQEIDSLKtkNQVLKTEKEKLELDHKalMDEMMEKHSKEQRDLEstnnqKLMLE 766
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE--ELIKEKEKELEEVLRE--INEISSELPELREELE-----KLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 767 YEKYLELQMKSqhmqEDFERQLHSSEQSKtEALEELTLQYESKLQEKVRKLKECEDKsqqqkreyEEMIKIMEEDADREI 846
Cdd:PRK03918 230 VKELEELKEEI----EELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEK--------VKELKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 847 ldirvKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDdknmETEKLKVELQKLHGVIKSLEKDILSLKKEIQERdET 926
Cdd:PRK03918 297 -----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELY-EE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 927 IQDKEKRIYDLRKKNTELEkfkfvldykIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNlKLKA 1006
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLT---------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK-KAKG 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2064967944 1007 TDKDRRREMQRVHDIEaLVRRFKTDLHRCVSfiqEPKKLKDSIRQL 1052
Cdd:PRK03918 437 KCPVCGRELTEEHRKE-LLEEYTAELKRIEK---ELKEIEEKERKL 478
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
639-1094 |
1.05e-11 |
|
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: 69.37 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 639 IWKIIDKERHGMKRDNEICYSEEILVTKSdleEKNQLMLELKTRVDELKME-NEYQLRLRDMNYNEKLKELtekfiQEID 717
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVVTEF---EATTCSLEELLRTEQQRLEkNEDQLKIITMELQKKSSEL-----EEMT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 718 SLKTKNQVLKTEKEKLELDHKALMDEMmEKHSKEQRDLESTNNQKLMLeyekyLELQMKSQHmqeDFERQL---HSSEQS 794
Cdd:pfam05483 398 KFKNNKEVELEELKKILAEDEKLLDEK-KQFEKIAEELKGKEQELIFL-----LQAREKEIH---DLEIQLtaiKTSEEH 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 795 KTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEE--DADREILDIRVKFEKMLT-----EEKETNvhL 867
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKqienlEEKEMN--L 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 868 KDETGIMRKKFSSLQREID---DKNMETEK-LKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTE 943
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKcklDKSEENARsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 944 LEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKmEGELEQFQRRNTQMELNIAELNLKlKATDKDRRREMQRVHDIEA 1023
Cdd:pfam05483 627 ENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLLEEVEKAKAIAD-EAVKLQKEIDKRCQHKIAE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 1024 LVRRFKTDLHRCVSFIQEpkklKDSIRQLYscyvqKSDVVDIDGVDADIQKEYNRQREHLektvASLKKKL 1094
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEE----RDSELGLY-----KNKEQEQSSAKAALEIELSNIKAEL----LSLKKQL 762
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-1068 |
2.91e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 703 EKLKELTEKFIQEIDSLKTKNQVLKTEKEKLElDHKALmdemmekhSKEQRDLESTnnqKLMLEYEKyLELQMksqhmqE 782
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQAL--------LKEKREYEGY---ELLKEKEA-LERQK------E 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 783 DFERQLhsseQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYE-EMIKIMEEdadreILDIRVKFEKMLTEEK 861
Cdd:TIGR02169 241 AIERQL----ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEK-----IGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 862 ETNVHLKDETGIMRKKFS---SLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLR 938
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 939 KK----NTELEKFKFVLDYKIKELKKQIEPREnnikEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRRE 1014
Cdd:TIGR02169 392 EKleklKREINELKRELDRLQEELQRLSEELA----DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 1015 MQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQLYSCYVQKSDVV--DIDGV 1068
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLkaSIQGV 523
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
592-1095 |
3.63e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 67.69 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 592 TVRALKYPLPIQNEWIEYQGHAAPITKMAvtfddQFLLTVSEDNCLLIWKIIDKERhgmKRDNEICYSEEILVTKSDLEE 671
Cdd:TIGR00618 271 ELRAQEAVLEETQERINRARKAAPLAAHI-----KAVTQIEQQAQRIHTELQSKMR---SRAKLLMKRAAHVKQQSSIEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 672 KNQLMLELKTRVDELKMENEYQLRLRDmnYNEKLKELTEKfiqeidsLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKE 751
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIRE--ISCQQHTLTQH-------IHTLQQQKTTLTQKLQSLCKELDILQREQATID 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 752 QRDLESTNNQKLMLEYEKYLELQMKSQHMQedferQLHSSEQSKTEALEELTLQ-YESKLQEKVRKLKECEDKSQQQKRE 830
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELC-----AAAITCTAQCEKLEKIHLQeSAQSLKEREQQLQTKEQIHLQETRK 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 831 YEEMIKIMEEDADREILdirvkFEKmltEEKETNVHLKDeTGIMRKKFSSLQREIDdknmETEKLKVELQKLHGVIKSLE 910
Cdd:TIGR00618 489 KAVVLARLLELQEEPCP-----LCG---SCIHPNPARQD-IDNPGPLTRRMQRGEQ----TYAQLETSEEDVYHQLTSER 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 911 KDILSLKKEIQERDETIQDKEKRIYDLRKkntELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRN 990
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKE---DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 991 T--QMELNIAELNLKLKATDKDRRREMQRVHdiEALVRRFKTDLHRCVSfiQEPKKLKDSIRQLYScyvQKSDVVDIDGV 1068
Cdd:TIGR00618 633 HlqQCSQELALKLTALHALQLTLTQERVREH--ALSIRVLPKELLASRQ--LALQKMQSEKEQLTY---WKEMLAQCQTL 705
|
490 500 510
....*....|....*....|....*....|
gi 2064967944 1069 DADIQ---KEYNRQREHLEKTVASLKKKLA 1095
Cdd:TIGR00618 706 LRELEthiEEYDREFNEIENASSSLGSDLA 735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
713-1137 |
7.89e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.68 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 713 IQEIDSLKTKNQVLKTEKEKLELDH---------KALMDEMMEKHSKEQRDLESTNNQKLML-EYEKY------LELQMK 776
Cdd:pfam15921 39 IENTSSTGTFTQIPIFPKYEVELDSprkiiaypgKEHIERVLEEYSHQVKDLQRRLNESNELhEKQKFylrqsvIDLQTK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 777 SQHMQedFERQ-LHSSEQSKTEALEELTLQYESKLQE--KVRKLKEceDKSQQQKREYEEMIKIM--EEDADREILDIRV 851
Cdd:pfam15921 119 LQEMQ--MERDaMADIRRRESQSQEDLRNQLQNTVHEleAAKCLKE--DMLEDSNTQIEQLRKMMlsHEGVLQEIRSILV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 852 KFE-----KMLTEEKETNVHLKDETGIMRKKFSSLQREID---------DKNMETEKL----KVEL------QKLHGVIK 907
Cdd:pfam15921 195 DFEeasgkKIYEHDSMSTMHFRSLGSAISKILRELDTEISylkgrifpvEDQLEALKSesqnKIELllqqhqDRIEQLIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 908 SLEKDILSLKKE----------IQERDETIQDKEK--------RIYDLRKK----NTELEKFKFVLDYKIKELKKQIEPR 965
Cdd:pfam15921 275 EHEVEITGLTEKassarsqansIQSQLEIIQEQARnqnsmymrQLSDLESTvsqlRSELREAKRMYEDKIEELEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 966 ENNIKEMR--------------EQIQKM-------EGEL----EQFQR---RNTQMELNIAELNLKLkatdKDRRREMQR 1017
Cdd:pfam15921 355 NSELTEARterdqfsqesgnldDQLQKLladlhkrEKELslekEQNKRlwdRDTGNSITIDHLRREL----DDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1018 vhdIEALVRRFKTDlhrCVSFIQepkklkdsiRQLYSCYVQKSDVVDIDGVDADIQKeynrQREHLEKTVASLKKKlaKD 1097
Cdd:pfam15921 431 ---LEALLKAMKSE---CQGQME---------RQMAAIQGKNESLEKVSSLTAQLES----TKEMLRKVVEELTAK--KM 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2064967944 1098 TLASTKSAPSSPVSRLNfdgESERIIQLQRVEIGRLRNEI 1137
Cdd:pfam15921 490 TLESSERTVSDLTASLQ---EKERAIEATNAEITKLRSRV 526
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
678-1094 |
2.17e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEYQLRlrdmNYNEKLKELTEKFIQEIDSLKTKNQVL---KTEKEKLELDHKALMDEmmekhskeQRD 754
Cdd:pfam05483 201 ELRVQAENARLEMHFKLK----EDHEKIQHLEEEYKKEINDKEKQVSLLliqITEKENKMKDLTFLLEE--------SRD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 755 LESTNNQKLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSKT--EALEElTLQYESKLQEKVRKLKECEDKSQQQKREYE 832
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqKALEE-DLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 833 EMIkIMEEDADREILDIRVKFEKMLTEEKETnvHLKDETGIMRKKFSSLQ---REIDDKNMETEKLKV---ELQKLHGVI 906
Cdd:pfam05483 348 SFV-VTEFEATTCSLEELLRTEQQRLEKNED--QLKIITMELQKKSSELEemtKFKNNKEVELEELKKilaEDEKLLDEK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 907 KSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQF 986
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 987 QRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKTDLHrcvSFIQEPKKLKDSIRqlysCYVQKSDVVDID 1066
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE---SVREEFIQKGDEVK----CKLDKSEENARS 577
|
410 420
....*....|....*....|....*...
gi 2064967944 1067 GVDADIQKEynRQREHLEKTVASLKKKL 1094
Cdd:pfam05483 578 IEYEVLKKE--KQMKILENKCNNLKKQI 603
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
660-1096 |
2.55e-10 |
|
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: 64.99 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 660 EEILVTKSDLEEKNQLmlelktrvDELKMENEYQLRLRDMNYNEKLKELTEKfIQEIDSLKTKNQVLKTEKEKLELDHKA 739
Cdd:pfam02463 160 EEAAGSRLKRKKKEAL--------KKLIEETENLAELIIDLEELKLQELKLK-EQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 740 LmdemmEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSK---TEALEELTLQYESKLQEKVRK 816
Cdd:pfam02463 231 Y-----LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKklqEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 817 LKECEDKSQQQKREYEEMIKI-MEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKL 895
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 896 KVELQKLHGV---IKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKntELEKFKfvldyKIKELKKQIEPRENNIKEM 972
Cdd:pfam02463 386 LSSAAKLKEEeleLKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE--EEEESI-----ELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 973 REQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQL 1052
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2064967944 1053 YSCYVQKSDVVDIDGVDADIQKEynrQREHLEKTVASLKKKLAK 1096
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVE---ERQKLVRALTELPLGARK 579
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
636-1021 |
3.13e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 636 CLLIWKIIDKERHGMKRDNEIcySEEILVTKSDLEEKNQLMLELKTRVDELK------------MENEYQLRLRDmNYNE 703
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEI--EEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLE-EYTA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 704 KLKELtEKFIQEIDSLKTKNQVLKTEKEKLELDHKAL--MDEMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQ 781
Cdd:PRK03918 460 ELKRI-EKELKEIEEKERKLRKELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 782 EDFerqlhSSEQSKTEALEELtlqyESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTeek 861
Cdd:PRK03918 539 GEI-----KSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE--- 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 862 etnvhLKDetgimrkkfssLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRiyDLRKKN 941
Cdd:PRK03918 607 -----LKD-----------AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEY 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 942 TELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEG---ELEQFQRRNTQMElNIAELNLKLKAtdKDRRREMQRV 1018
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakkELEKLEKALERVE-ELREKVKKYKA--LLKERALSKV 745
|
...
gi 2064967944 1019 HDI 1021
Cdd:PRK03918 746 GEI 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
823-1033 |
4.66e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 823 KSQQQKREYEEMIKIMEEDADReILDIRVKFEKML----------TEEKETNVHLKD-ETGIMRKKFSSLQREIDDKNME 891
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDR-LEDILNELERQLkslerqaekaERYKELKAELRElELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 892 TEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKE 971
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064967944 972 MREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKTDLH 1033
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
650-1008 |
5.18e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 650 MKRDNEICYSEEILVTKSDLEEKNQLMLELKtRVDELKMENEYQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTE 729
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 730 KEKLELDHKALMDEMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEAleeltlqYESK 809
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 810 LQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETN--VHLKDE-----TGIMRKKFSSLQ 882
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEeekkaEEIRKEKEAVIE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 883 REIDDKNmetEKLKVELQKLHGVIKSLEKDILSLKKE----IQERDETIQDKEKRIYDlrKKNTELEKFKFVLDYKIKEL 958
Cdd:PTZ00121 1783 EELDEED---EKRRMEVDKKIKDIFDNFANIIEGGKEgnlvINDSKEMEDSAIKEVAD--SKNMQLEEADAFEKHKFNKN 1857
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 959 KKQIEPRENNIKEMREQ------IQKMEGELEQFQRRNTQMELNIAELNLKLKATD 1008
Cdd:PTZ00121 1858 NENGEDGNKEADFNKEKdlkeddEEEIEEADEIEKIDKDDIEREIPNNNMAGKNND 1913
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
925-1137 |
1.07e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 925 ETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKL 1004
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1005 KAtdkdRRREMQRVhdieaLVRRFKTDLHRCVSFIQEPKKLKDSIRQL-YSCYVQKSDVVDIDGVDADiQKEYNRQREHL 1083
Cdd:COG4942 100 EA----QKEELAEL-----LRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRAD-LAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 1084 EKTVASLKKKLA-----KDTLASTKSAPSSPVSRLN--FDGESERIIQLQRvEIGRLRNEI 1137
Cdd:COG4942 170 EAERAELEALLAeleeeRAALEALKAERQKLLARLEkeLAELAAELAELQQ-EAEELEALI 229
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
772-1032 |
1.16e-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: 62.89 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 772 ELQmKSQHMQEDFERQLHSSEQSKTEALEEltlqyESKLQEKVRKLKECedksqqqKREYEEMiKIMEEDADREILDIRV 851
Cdd:pfam01576 13 ELQ-KVKERQQKAESELKELEKKHQQLCEE-----KNALQEQLQAETEL-------CAEAEEM-RARLAARKQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 852 KFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSL----------KKEIQ 921
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLedqnsklskeRKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 922 ER-------------------------DETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQI 976
Cdd:pfam01576 159 ERiseftsnlaeeeekakslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 977 QKMEGELE--------------QFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKTDL 1032
Cdd:pfam01576 239 AKKEEELQaalarleeetaqknNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
700-1011 |
2.34e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 700 NYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDH---KALMDEM--MEKHSKEQRDLESTNNQKL--MLEYEKYLE 772
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEekiNNSNNKIkiLEQQIKDLNDKLKKNKDKInkLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 773 LQMKSQHMQED-FERQLHSSEQSKTEALEELTLQYE--SKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDAD---REI 846
Cdd:TIGR04523 110 SEIKNDKEQKNkLEVELNKLEKQKKENKKNIDKFLTeiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniqKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 847 LDIRVKFEKM------LTEEKETNVHLKDETGIMRKKFSSLQREIddknmetEKLKVELQKLHGVIKSLEKDILSLKKEI 920
Cdd:TIGR04523 190 DKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNI-------EKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 921 QERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEprENNIKEMREQIQKMEGELEQFQRRNTQMELNIAEL 1000
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
330
....*....|.
gi 2064967944 1001 NLKLKATDKDR 1011
Cdd:TIGR04523 341 NEQISQLKKEL 351
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
897-1082 |
3.18e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.78 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 897 VELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRiydLRKKNTELEKfkfvLDYKIKELKKQIEPRENNIKEMREQI 976
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEAR---LEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 977 ---------QKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKTDLHRCVSFIQ-EPKKLK 1046
Cdd:COG1579 83 gnvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEaELEELE 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 2064967944 1047 DSIRQLyscyvqksdvvdIDGVDADIQKEYNRQREH 1082
Cdd:COG1579 163 AEREEL------------AAKIPPELLALYERIRKR 186
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
677-975 |
5.70e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 677 LELKTRVDELKMEnEYQLRLRDMNYN-EKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQ--- 752
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYell 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 753 RDLESTNNQKLMLEyEKYLELQMKSQHMQEDfERQLHSSEQSKTEALEELTLQYEsKLQEKVRKLKECEDKSQQQKREYE 832
Cdd:COG1196 295 AELARLEQDIARLE-ERRRELEERLEELEEE-LAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 833 EMikimEEDADREILDIRvkfEKMLTEEKETNVHLKDETGIMRKKfSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKD 912
Cdd:COG1196 372 AE----LAEAEEELEELA---EELLEALRAAAELAAQLEELEEAE-EALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 913 ILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvLDYKIKELKKQIEPRENNIKEMREQ 975
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEA----ALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
624-1000 |
7.83e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 59.99 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 624 DDQFLLTVSEDNCLLIWKIIDKERHGMKRDNEICYSEEILVTKSDLEEKNQLMLELKTRVDELKMENEYQLRlrdmnyNE 703
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV------KA 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 704 KLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQED 783
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 784 FERQlhSSEQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKET 863
Cdd:pfam02463 747 EEEE--EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 864 NVHLKDETGIMRKK-------FSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYD 936
Cdd:pfam02463 825 EQEEKIKEEELEELalelkeeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064967944 937 LRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQI----QKMEGELEQFQRRNTQMELNIAEL 1000
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEadekEKEENNKEEEEERNKRLLLAKEEL 972
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-223 |
9.24e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 59.15 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 26 DEQTVIFPSGNNCVR-YNID-QKWQRFIPGTekSQSIQALALSPNRRYLAVSerGEKGTITVYDLQNDQIkkRKVLSGGE 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLASG--SADGTVRLWDLATGEL--LRTLTGHS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 104 IPVQefvCMAFSPDSKYLIgqSGTPDFILFYWMWEKQKVIATVN-TGGPTHQVSFNPrDNTQI-CACGIGVFKLFRYAEG 181
Cdd:COG2319 289 GGVN---SVAFSPDGKLLA--SGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSP-DGKTLaSGSDDGTVRLWDLATG 362
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2064967944 182 VLkqfsAQKLESHNflshDWVSEkrlIAGTDKGRLLVIESGD 223
Cdd:COG2319 363 EL----LRTLTGHT----GAVTS---VAFSPDGRTLASGSAD 393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
659-1019 |
1.07e-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: 59.68 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 659 SEEILVTKSDLEEKNQLMLELKTRVDELKMENEyQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHK 738
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELE-SKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 739 -ALMDEMMEKHSKE--------QRDLEStnnQKLMLEYEKYLELQMKS-QHMQEDFERQLHSSEQSKTEALEELTLQyES 808
Cdd:TIGR00606 662 tAVYSQFITQLTDEnqsccpvcQRVFQT---EAELQEFISDLQSKLRLaPDKLKSTESELKKKEKRRDEMLGLAPGR-QS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 KLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDadreildiRVKFEKMLTEEKETNVHLKDETGIMRkkfssLQREIDDK 888
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ--------ETLLGTIMPEEESAKVCLTDVTIMER-----FQMELKDV 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 889 NMETEKLKVELQKLhgvikSLEKDILSLKKEIQERDET--------------IQDKEKRIYDLRKKNTELEKFKF----- 949
Cdd:TIGR00606 805 ERKIAQQAAKLQGS-----DLDRTVQQVNQEKQEKQHEldtvvskielnrklIQDQQEQIQHLKSKTNELKSEKLqigtn 879
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064967944 950 -----VLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVH 1019
Cdd:TIGR00606 880 lqrrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
867-1147 |
1.51e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 867 LKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEK 946
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 947 FKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRrnTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVR 1026
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1027 RFKTDLHRCVSFIQEPKKLK------DSIRQLYSCYVQKSDVVDIDGVDADIQKEYNRQREHLEKTVASLKKKLAKDTLA 1100
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLeaklglALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2064967944 1101 STKSAPSSPVSRLNFDGESERIIQLQRVEIGRLRNEILIHGDTHLVQ 1147
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
750-1003 |
2.19e-08 |
|
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: 57.51 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 750 KEQRDLESTNNQKlMLEYEKYLELQMKS------QHMQEDFER---QLHSSEQSKTEALEELTlQYESKLQEKVR----- 815
Cdd:pfam15905 64 KSQKNLKESKDQK-ELEKEIRALVQERGeqdkrlQALEEELEKveaKLNAAVREKTSLSASVA-SLEKQLLELTRvnell 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 816 KLKECEDKSQqqKREYEEMIKIME-----EDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNM 890
Cdd:pfam15905 142 KAKFSEDGTQ--KKMSSLSMELMKlrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 891 ETEKLKVELQKLHGVIKSLEKdilsLKKEIQERDETiqdkekriydLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIK 970
Cdd:pfam15905 220 ETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
250 260 270
....*....|....*....|....*....|....
gi 2064967944 971 EMREQIQKMEGEL-EQFQRRNTQMELNIAELNLK 1003
Cdd:pfam15905 286 LLESEKEELLREYeEKEQTLNAELEELKEKLTLE 319
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
483-646 |
3.66e-08 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 56.19 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 483 LKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWNTltskrESESVLKTCM-----YTNVTISPDAKIIFAVGTDCTLKeIQ 557
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL-----ETGELLRTLKghtgpVRDVAASADGTYLASGSSDKTIR-LW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 558 DcqivkeVPSNDVTYTavalshlgrvlfigtsagtvralkyplpiqnewieYQGHAAPITKMAVTFDDQFLLTVSEDNCL 637
Cdd:cd00200 79 D------LETGECVRT-----------------------------------LTGHTSYVSSVAFSPDGRILSSSSRDKTI 117
|
....*....
gi 2064967944 638 LIWKIIDKE 646
Cdd:cd00200 118 KVWDVETGK 126
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
875-1052 |
4.23e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 875 RKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyK 954
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-------E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 955 IKELKKQIEPRENNI--------------------------------KEMREQIQKMEGELEQFQRRNTQMELNIAELNL 1002
Cdd:COG4942 99 LEAQKEELAELLRALyrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1003 KLKATDKDRRREMQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQL 1052
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
678-1031 |
5.14e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEyqlrlrdmNYNEKLKELtEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLES 757
Cdd:COG4717 75 ELEEELKEAEEKEE--------EYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 758 TNNQKLMLEYEKYLELQMKsqhmQEDFERQLHSSEQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEE-MIK 836
Cdd:COG4717 146 ERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 837 IMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGI-----------------------------------------MR 875
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgllallflllarekasLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 876 KKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEK-----RIYDLRKKNTELEKFKFV 950
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 951 LD----YKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELN--IAELNLKLKATDKDRRREMQRVHDIEAL 1024
Cdd:COG4717 382 EDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEeeLEELEEELEELEEELEELREELAELEAE 461
|
....*..
gi 2064967944 1025 VRRFKTD 1031
Cdd:COG4717 462 LEQLEED 468
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
678-945 |
5.39e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEYQLRLRDMNYNEKLKELTekfiQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLES 757
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELN----GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 758 TNNQklMLEYEKYLELQM-KSQHMQEDFE-RQLHSSEQSKTEaLEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMI 835
Cdd:pfam12128 352 WQSE--LENLEERLKALTgKHQDVTAKYNrRRSKIKEQNNRD-IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 836 kimeEDADREILDIRVKFEKMLTEEKetnVHLKDETGIMRKKfssLQREIDDKnmETEKLKVELQKLHGVIKSLEKDILS 915
Cdd:pfam12128 429 ----EAGKLEFNEEEYRLKSRLGELK---LRLNQATATPELL---LQLENFDE--RIERAREEQEAANAEVERLQSELRQ 496
|
250 260 270
....*....|....*....|....*....|
gi 2064967944 916 LKKEIQERDETIQDKEKRIYDLRKKNTELE 945
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
681-1114 |
5.73e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 681 TRVDELKMENEYQLRLRDMNYNEkLKELTEKFIQEIDSL-------KTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQR 753
Cdd:pfam02463 98 RRRVYRGGDSEYYINGKNVTKKE-VAELLESQGISPEAYnflvqggKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 754 DLESTNNQKLMLEYEKyLELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKLQEkvrkLKECEDKSQQQKREYEE 833
Cdd:pfam02463 177 KLIEETENLAELIIDL-EELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL----NEERIDLLQELLRDEQE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 834 MIKIMEEDADREildirvkfEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDI 913
Cdd:pfam02463 252 EIESSKQEIEKE--------EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 914 LSLKKEIQERDETIQDKEKriydlrkkntelekfkfvldykikELKKQIEPRENNIKEMREQIQKM------EGELEQFQ 987
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEK------------------------ELKELEIKREAEEEEEEELEKLQekleqlEEELLAKK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 988 RRNTQM---ELNIAELNLKLKATDKDRRR-EMQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQLYSCYVQKSDVV 1063
Cdd:pfam02463 380 KLESERlssAAKLKEEELELKSEEEKEAQlLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 1064 DIDGVDADIQKEYNRQREHLEKTVASLKKKLAKDTLASTKSAPSSPVSRLN 1114
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
826-1027 |
6.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 826 QQKREYEEMIKIMEEDADReILDIRvkfekmltEEKETNV-HLKDEtgimR---KKFSSLQREIDDKNMET-----EKLK 896
Cdd:COG1196 172 ERKEEAERKLEATEENLER-LEDIL--------GELERQLePLERQ----AekaERYRELKEELKELEAELlllklRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 897 VELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQI 976
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 977 QKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRR 1027
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
667-996 |
7.47e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.30 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 667 SDLEEKNQLMLELKTRVDELKMENEyQLRLRDMNYNEKLKELTEKfiqeidsLKTKNQVLKTEKEKLElDHKALMDEMME 746
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIE-ELKEKRDELNEELKELAEK-------RDELNAQVKELREEAQ-ELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 747 K--HSKEQRDLESTNNQKLMLEYEKYLELQMKsqhmqedfERQLHSSEQSKTEALEELtlqyESKLQEKVRKLKEcEDKS 824
Cdd:COG1340 72 KvkELKEERDELNEKLNELREELDELRKELAE--------LNKAGGSIDKLRKEIERL----EWRQQTEVLSPEE-EKEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 825 QQQKREYEEMIKIMEEdadreildirvkfekmlteEKETNVHLKDetgiMRKKFSSLQREIDDKNMETEKLKVELQKLHG 904
Cdd:COG1340 139 VEKIKELEKELEKAKK-------------------ALEKNEKLKE----LRAELKELRKEAEEIHKKIKELAEEAQELHE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 905 VIKSLEKDILSLKKEIQERDETIQDKEKriydlrkkntelekfkfvldyKIKELKKQIEPRENNIKEMREQIQKMEGELE 984
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEIVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQR 254
|
330
....*....|..
gi 2064967944 985 QFQRRNTQMELN 996
Cdd:COG1340 255 ALKREKEKEELE 266
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
666-1052 |
7.86e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 666 KSDLEEKNQLMlELKTRVDELKMENEYQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMM 745
Cdd:PTZ00121 1450 KKKAEEAKKAE-EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 746 EKHSKEQRD-LESTNNQKLMLEYEKYLELQMKSQHMQEDFERQlhsSEQSKTEALE--ELTLQYESKLQEKVRKLKECED 822
Cdd:PTZ00121 1529 KAEEAKKADeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---AEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEK 1605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 823 --KSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVElq 900
Cdd:PTZ00121 1606 kmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA-- 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 901 klhgvikslEKDilslKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKELKKQIEPRENNIKEMREQIQKME 980
Cdd:PTZ00121 1684 ---------EED----EKKAAEALKKEAEEAKKAEELKKKEAEEKK-------KAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064967944 981 GELEQFqRRNTQMELNIAELNLKLKATDKDRRREMQRVhdiealvrrfktdlhrcvsfIQEPKKLKDSIRQL 1052
Cdd:PTZ00121 1744 KKAEEA-KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--------------------IEEELDEEDEKRRM 1794
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
646-1002 |
9.20e-08 |
|
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: 56.29 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 646 ERHGMKRDNEICYSEEILVTKSDLEEKNQLMLELKTRVDELKMENEYQlrlrDMNYNEKLKELtEKFIQEIDSLKTKNQV 725
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----ELELQSTNSEL-EELQERLDLLKAKASE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 726 LKTEKEKLELDHKALMDEmmEKHSKE-QRDLESTNNQKLMLEYEKylELQMKSQHMQEDFERQLHSSEQSKT-----EAL 799
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEA--EQRIKElEFEIQSQEQDSEIVKNSK--SELARIPELEKELERLREHNKHLNEnienkLLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 800 EELTLQYESKL------QEKVRKLKECEDKSQQQKREYEEMIKIMEEDAdREILDIRVKFEKMLTEE---KETNVHLKDE 870
Cdd:pfam05557 227 KEEVEDLKRKLereekyREEAATLELEKEKLEQELQSWVKLAQDTGLNL-RSPEDLSRRIEQLQQREivlKEENSSLTSS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 871 TGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEI--------------------QERDETIQDK 930
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrailesydkeltmsnysPQLLERIEEA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 931 EKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQ-------------------IQKMEGELEQFQRRNT 991
Cdd:pfam05557 386 EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQesladpsyskeevdslrrkLETLELERQRLREQKN 465
|
410
....*....|.
gi 2064967944 992 QMELNIAELNL 1002
Cdd:pfam05557 466 ELEMELERRCL 476
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
678-1021 |
9.91e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 55.88 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEYQLRLR---DMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEkleldhkalmdemmekhskeqrD 754
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKqqlEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQV----------------------E 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 755 LESTNNQklmleyekylelQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKLQEKVRKLKE--CEDKSQQQKREYE 832
Cdd:pfam03528 63 LDALQNQ------------LALARAEMENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKEtvREYEVQFHRRLEQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 833 EMIKIME--EDADREILDIRvkfeKMLTEEKEtnvhlkdetgimrkkfsslqreidDKNMETE--KLKVELQKLHGVIKS 908
Cdd:pfam03528 131 ERAQWNQyrESAEREIADLR----RRLSEGQE------------------------EENLEDEmkKAQEDAEKLRSVVMP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 909 LEKDILSLKKEIQERDETIqdKEKRIYDLRKKNTELEKFKFV---LDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQ 985
Cdd:pfam03528 183 MEKEIAALKAKLTEAEDKI--KELEASKMKELNHYLEAEKSCrtdLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQ 260
|
330 340 350
....*....|....*....|....*....|....*.
gi 2064967944 986 FQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDI 1021
Cdd:pfam03528 261 ERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESV 296
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
875-1013 |
1.08e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 875 RKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKR----------------IYDLR 938
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyealqkeIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064967944 939 KKNTELEKfkfvldyKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNtqmELNIAELNLKLKATDKDRRR 1013
Cdd:COG1579 103 RRISDLED-------EILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
57-218 |
1.66e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 54.92 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 57 SQSIQALALSPNRRYLAVSerGEKGTITVYDLQNDQIkkRKVLSGGEIPVQefvCMAFSPDSKYLIgqSGTPDFILFYWM 136
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASG--SADGTVRLWDLATGKL--LRTLTGHSGSVR---SVAFSPDGRLLA--SGSADGTVRLWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 137 WEKQKVIATVNT-GGPTHQVSFNPrDNTQI-CACGIGVFKLFRYAEGVLkqfsAQKLESHnflsHDWVSE-------KRL 207
Cdd:COG2319 275 LATGELLRTLTGhSGGVNSVAFSP-DGKLLaSGSDDGTVRLWDLATGKL----LRTLTGH----TGAVRSvafspdgKTL 345
|
170
....*....|.
gi 2064967944 208 IAGTDKGRLLV 218
Cdd:COG2319 346 ASGSDDGTVRL 356
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
843-1092 |
2.40e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 843 DREILDIRVKFEKMLTEEKETNVHLKDetgimrkkfssLQREIDDKNMETEKLKVELQklhgvikSLEKDILSLKKEIQE 922
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAE-----------LRKELEELEEELEQLRKELE-------ELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 923 RDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRR--NTQME---LNI 997
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldELRAEltlLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 998 AELNLKLKATDKDRRREMQRVHdIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQLYSCYVQKSDVVdidgvdADIQKEYN 1077
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERR-LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER------ASLEEALA 890
|
250
....*....|....*
gi 2064967944 1078 RQREHLEKTVASLKK 1092
Cdd:TIGR02168 891 LLRSELEELSEELRE 905
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
726-1023 |
2.61e-07 |
|
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: 55.18 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 726 LKTEKEKLELDHKALMdEMMEKHSKEQRDLE---STNNQKLMlEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEEL 802
Cdd:pfam01576 487 LSTRLRQLEDERNSLQ-EQLEEEEEAKRNVErqlSTLQAQLS-DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEK 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 803 TLQYEsklqekvrKLKECEDKSQQqkrEYEEMikIMEEDADREILDI----RVKFEKMLTEEKETNVHLKDEtgimRKKF 878
Cdd:pfam01576 565 AAAYD--------KLEKTKNRLQQ---ELDDL--LVDLDHQRQLVSNlekkQKKFDQMLAEEKAISARYAEE----RDRA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 SSLQREIDDKNMeteKLKVELQKLHGVIKSLEKDILSLKKEIqerDETIQDKEkriyDLRKKNTELEKFKfvldykiKEL 958
Cdd:pfam01576 628 EAEAREKETRAL---SLARALEEALEAKEELERTNKQLRAEM---EDLVSSKD----DVGKNVHELERSK-------RAL 690
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 959 KKQIEprennikEMREQIQKMEGELEQFQRRNTQMELNIA--------ELNLKLKATDKDRRREMQRVHDIEA 1023
Cdd:pfam01576 691 EQQVE-------EMKTQLEELEDELQATEDAKLRLEVNMQalkaqferDLQARDEQGEEKRRQLVKQVRELEA 756
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
842-1023 |
2.84e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 842 ADREILDIRVKFEKMLTEEKETNvhlkdetgimrKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQ 921
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ-----------AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 922 ERDETIqdkEKRIYDLRKKNTELEKFKFVL------DY-------------------KIKELKKQIEPRENNIKEMREQI 976
Cdd:COG3883 83 ERREEL---GERARALYRSGGSVSYLDVLLgsesfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2064967944 977 QKMEGELEQFQRrntQMELNIAELNLKLKATDKDRRREMQRVHDIEA 1023
Cdd:COG3883 160 EALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
786-1026 |
3.22e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 786 RQLHSSEQSKTEA-LEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADR---------EILDIRVKFEK 855
Cdd:PRK02224 190 DQLKAQIEEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERreeletleaEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 856 MLTEEKEtnvhLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEK--- 932
Cdd:PRK02224 270 TEREREE----LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEeae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 933 ----RIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEqfqrrNTQMELNIAELNLKLKATD 1008
Cdd:PRK02224 346 slreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG-----DAPVDLGNAEDFLEELREE 420
|
250
....*....|....*...
gi 2064967944 1009 KDRRREmqRVHDIEALVR 1026
Cdd:PRK02224 421 RDELRE--REAELEATLR 436
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
476-515 |
3.88e-07 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 47.31 E-value: 3.88e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2064967944 476 TFENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWN 515
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
677-1004 |
5.18e-07 |
|
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: 54.03 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 677 LELKTRVDELKMENEYQLRLRDMNYNEKLKELTEK---FIQEIDSLKTKNQVLKTEKEKLELDHKALMDEM--------- 744
Cdd:pfam01576 716 LRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQvreLEAELEDERKQRAQAVAAKKKLELDLKELEAQIdaankgree 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 745 -------MEKHSKE-QRDLESTN-NQKLML----EYEKYLE-LQMKSQHMQEDF---ERQLHSSEQSKTEALEELTLQYE 807
Cdd:pfam01576 796 avkqlkkLQAQMKDlQRELEEARaSRDEILaqskESEKKLKnLEAELLQLQEDLaasERARRQAQQERDELADEIASGAS 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 808 SK--LQEKVRKLkecEDKSQQQKREYEEmikimeEDADREILDIRVKFEKMLTEEkeTNVHLKDETGIMRKKFSSLQrEI 885
Cdd:pfam01576 876 GKsaLQDEKRRL---EARIAQLEEELEE------EQSNTELLNDRLRKSTLQVEQ--LTTELAAERSTSQKSESARQ-QL 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 886 DDKNMEtekLKVELQKLHGVIKS--------LEKDILS----LKKEIQER---DETIQDKEKRIYDL------RKKNTE- 943
Cdd:pfam01576 944 ERQNKE---LKAKLQEMEGTVKSkfkssiaaLEAKIAQleeqLEQESRERqaaNKLVRRTEKKLKEVllqvedERRHADq 1020
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064967944 944 ----LEKfkfvLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKL 1004
Cdd:pfam01576 1021 ykdqAEK----GNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
638-1030 |
6.38e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 638 LIWKIIDKERHGMKRDNEICYSEEILVTKSDLEEKNQLMLELKTRVDELKMENEyQLRLRDMNYNEKLKELtEKFIQEID 717
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQIL-ELEGYEMDYNSYLKSI-ESLKKKIE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 718 SLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLESTN------NQKL--MLEYEKYLELQMK-----------SQ 778
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISskvsslNQRIraLRENLDELSRNMEmlngqsvcpvcGT 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 779 HMQEDFERQLHSSEQSKTEALEELTLQYE---SKLQEKVRKLKECEDKSQQQK-REYEEMIKIMeEDADREILDIRVKF- 853
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKKSRLEEKIREIEievKDIDEKIVDLKKRKEYLESEEiNKSINEYNKI-ESARADLEDIKIKIn 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 854 ---EKMLTEEKETNVHLKDETGIMRKKFSS---------------LQREIDDKNMETEKLKVELQKLHGVIKSLEKDILS 915
Cdd:PRK01156 540 elkDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalavislidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 916 LKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKELKKQI---EPRENNIKEMREQIQKMEGELEQFQRRNTQ 992
Cdd:PRK01156 620 SIREIENEANNLNNKYNEIQENKILIEKLRG-------KIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLKKSRKALDD 692
|
410 420 430
....*....|....*....|....*....|....*...
gi 2064967944 993 MELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKT 1030
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
800-1000 |
7.80e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 800 EELTLQYESKLQEKVRKLKECEDKSQQQKREYEEmikimeEDADREILDIRVK-FEKMLTEEKETNVHLKDETGIMRKKF 878
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKER------YKRDREQWERQRReLESRVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 SSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERD---ETIQDKEKRIYDLRKKN-TELEKFKFVLDYK 954
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelERMKERAKKAGAQRKEEeAERKQLQAKLQQT 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 955 IKE----------LKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAEL 1000
Cdd:pfam07888 184 EEElrslskefqeLRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
678-1031 |
8.53e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKmenEYQLRLRDMNYNEKlKEL--TEKFIQEIdslkTKNQVLKTEKEKLE--LDHKALmDEMMEK--HSKE 751
Cdd:TIGR01612 1359 KIKKIIDEVK---EYTKEIEENNKNIK-DELdkSEKLIKKI----KDDINLEECKSKIEstLDDKDI-DECIKKikELKN 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 752 QRDLESTNNQ---KLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEELTLqyeSKLQEKVRKLKECEDKSQQQK 828
Cdd:TIGR01612 1430 HILSEESNIDtyfKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNI---NELKEHIDKSKGCKDEADKNA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 829 REYEEMiKIMEEDADREI---------LDIRVKFEK-------MLTEEKETNVHLKDETGIMRKKFSSLQRE---IDD-- 887
Cdd:TIGR01612 1507 KAIEKN-KELFEQYKKDVtellnkysaLAIKNKFAKtkkdseiIIKEIKDAHKKFILEAEKSEQKIKEIKKEkfrIEDda 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 888 -KNMETEKLKVELQKlhgVIKSLEKDIL---SLKKEIQERDETIQDKEKRI--YDLRKKNTELEKFKFVLDY------KI 955
Cdd:TIGR01612 1586 aKNDKSNKAAIDIQL---SLENFENKFLkisDIKKKINDCLKETESIEKKIssFSIDSQDTELKENGDNLNSlqefleSL 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 956 KELKKQIEPRENNIKEMREQIQKMEGELEQFQRrntQMELNIAElnlKLKATDKDRRREMQRVHD-----IEALVRRFKT 1030
Cdd:TIGR01612 1663 KDQKKNIEDKKKELDELDSEIEKIEIDVDQHKK---NYEIGIIE---KIKEIAIANKEEIESIKElieptIENLISSFNT 1736
|
.
gi 2064967944 1031 D 1031
Cdd:TIGR01612 1737 N 1737
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
669-1096 |
1.09e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 669 LEEKNQLMLELKTRVDELKMENEyqlRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKH 748
Cdd:PRK01156 217 LKEIERLSIEYNNAMDDYNNLKS---ALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 749 SKEQRDLESTNNQ----KLML-----EYEKYLELQMKSQHMQEDFERQLhsSEQSKTEALEELTLQYESKLQEKVRKLKE 819
Cdd:PRK01156 294 RNYINDYFKYKNDienkKQILsnidaEINKYHAIIKKLSVLQKDYNDYI--KKKSRYDDLNNQILELEGYEMDYNSYLKS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 820 CEDKsQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGimrkKFSSLQREIDDKNMETEKLKVEL 899
Cdd:PRK01156 372 IESL-KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISS----KVSSLNQRIRALRENLDELSRNM 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 900 QKLHG------------------VIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKF----VLDYKIKE 957
Cdd:PRK01156 447 EMLNGqsvcpvcgttlgeeksnhIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEInksiNEYNKIES 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 958 LKKQIEPRENNIKEMREQIQKMEGELEQFQrrntQMELNIaelnLKLKATDKDRRREMQRVHDIEALVRRFKtdlhrcvs 1037
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYK----SLKLED----LDSKRTSWLNALAVISLIDIETNRSRSN-------- 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 1038 fiQEPKKLKDSIRQLYSCYVQKSDVVD-IDGVDADIQKEYN-------------RQREHLEKTVASLKKKLAK 1096
Cdd:PRK01156 591 --EIKKQLNDLESRLQEIEIGFPDDKSyIDKSIREIENEANnlnnkyneiqenkILIEKLRGKIDNYKKQIAE 661
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
898-1096 |
1.20e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 898 ELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKELKKQIEPRENNIKEMREQIQ 977
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 978 KMEGELEQFQRRNTQMEL-----NIAELnlklkatdkdrrreMQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQl 1052
Cdd:COG3883 90 ERARALYRSGGSVSYLDVllgseSFSDF--------------LDRLSALSKIADADADLLEELKADKAELEAKKAELEA- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2064967944 1053 yscyvQKSDVVDIDGVDADIQKEYNRQREHLEKTVASLKKKLAK 1096
Cdd:COG3883 155 -----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
639-1098 |
1.29e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.91 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 639 IWKIIDKERHGMKRDNEICYSEEILVTKSDLEEKNQLMLELKTRVDELKMeNEYQlrlrdMNYNEKLKELTEKFIQE--- 715
Cdd:PTZ00440 392 IETLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEI-IEIK-----KKYDEKINELKKSINQLktl 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 716 IDSLKTKNQVLKTEKEKleldhkalMDEMMEKHSKEQRDLESTNNQKLMLEYEKYlelqmKSQHMQEDFERQLHSSEQSK 795
Cdd:PTZ00440 466 ISIMKSFYDLIISEKDS--------MDSKEKKESSDSNYQEKVDELLQIINSIKE-----KNNIVNNNFKNIEDYYITIE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 796 TEALE-ELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADreildirvKFEKMLTEEKETNVHLKDETGIM 874
Cdd:PTZ00440 533 GLKNEiEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVD--------HIKDIISLNDEIDNIIQQIEELI 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 875 RKKFSSLQREIDDKNMETEKLKVELQKLH-GVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKF---- 949
Cdd:PTZ00440 605 NEALFNKEKFINEKNDLQEKVKYILNKFYkGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFmksd 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 950 ----VLDYKIKELKKQIEPRENNIKEMREQI-QKMEGELEQFQRRNTqmelniaELNLKLKATDKDRRREMQRVHDIEAL 1024
Cdd:PTZ00440 685 nidnIIKNLKKELQNLLSLKENIIKKQLNNIeQDISNSLNQYTIKYN-------DLKSSIEEYKEEEEKLEVYKHQIINR 757
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064967944 1025 VRRFKTDLHrcvsfiQEPKKLKDSiRQLYSCYVQKSDVVDID----GVDADIQKEYNRQREHLEKTVASLKKKLAKDT 1098
Cdd:PTZ00440 758 KNEFILHLY------ENDKDLPDG-KNTYEEFLQYKDTILNKenkiSNDINILKENKKNNQDLLNSYNILIQKLEAHT 828
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
701-840 |
1.54e-06 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 48.84 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 701 YNEKLKELTEKFI---QEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKeqrdleSTNNQKlmleyekyleLQMKS 777
Cdd:pfam12718 19 LEEKVKELEQENLekeQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKL------KTNNEN----------LTRKI 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 778 QHMQEDFERqlhsSEQSKTEALEELTlQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEE 840
Cdd:pfam12718 83 QLLEEELEE----SDKRLKETTEKLR-ETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
742-1034 |
1.84e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.79 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 742 DEMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMksQHMQEdfERQLHSSEQSKTEALEELTLQYESKLQEKVRKLKECE 821
Cdd:pfam02029 35 SVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRT--AKREE--RRQKRLQEALERQKEFDPTIADEKESVAERKENNEEE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 822 DKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNvhlkdETGIMRKKFSSLQREIDDKNMETEKLKVELQK 901
Cdd:pfam02029 111 ENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAE-----EEGEEEEDKSEEAEEVPTENFAKEEVKDEKIK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 902 LHGVIKSLEKDILSLKKEIQERdeTIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPrENNIKEMREQIQKMEG 981
Cdd:pfam02029 186 KEKKVKYESKVFLDQKRGHPEV--KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA-EQKLEELRRRRQEKES 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064967944 982 -ELEQFQRRNTQMELNIAELNLKLKATDK-----DRRR---EMQRVHDIEALVRRFKTDLHR 1034
Cdd:pfam02029 263 eEFEKLRQKQQEAELELEELKKKREERRKlleeeEQRRkqeEAERKLREEEEKRRMKEEIER 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
660-911 |
2.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 660 EEILVTKSDLEEKNQLMLELKTRVDELKMENEyQLRLRDMNYNEKLKELTEKF---IQEIDSLKTKNQVLKTEKEKLELD 736
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 737 HKALMDEMMEKHSKEQRDLESTNNQKlmleyEKYLELQMKSQHMQEDFER------QLHSSEQSKTEALE-------ELT 803
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELE-----EKLEELKEELESLEAELEEleaeleELESRLEELEEQLEtlrskvaQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 804 LQYES---KLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREIldirvkfEKMLTEEKETNVHLKDETGIMRKKFSS 880
Cdd:TIGR02168 393 LQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-------QAELEELEEELEELQEELERLEEALEE 465
|
250 260 270
....*....|....*....|....*....|.
gi 2064967944 881 LQREIDDKNMETEKLKVELQKLHGVIKSLEK 911
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
26-135 |
2.35e-06 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 50.80 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 26 DEQTVIFPSGNNCVR-YNID-QKWQRFIPGteKSQSIQALALSPNRRYLAVSerGEKGTITVYDLQNDQIKKrkVLSGGE 103
Cdd:cd00200 188 DGEKLLSSSSDGTIKlWDLStGKCLGTLRG--HENGVNSVAFSPDGYLLASG--SEDGTIRVWDLRTGECVQ--TLSGHT 261
|
90 100 110
....*....|....*....|....*....|..
gi 2064967944 104 IPVQefvCMAFSPDSKYLIgqSGTPDFILFYW 135
Cdd:cd00200 262 NSVT---SLAWSPDGKRLA--SGSADGTIRIW 288
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
881-1032 |
2.70e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 881 LQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKK------NTELEkfkfVLDYK 954
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYE----ALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 955 IKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVH-DIEALVRRFKTDL 1032
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
678-1002 |
2.88e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEYqlrlrdMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEK-LELDHKALMDEMMEKHSKEQRDLE 756
Cdd:TIGR00606 170 ALKQKFDEIFSATRY------IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKaCEIRDQITSKEAQLESSREIVKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 757 STNNQKLMlEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEemik 836
Cdd:TIGR00606 244 ENELDPLK-NRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 837 imeedadREILDIRVKFEKMLTEEKETN---VHLKDETGIMRKKFSSLQREIDDKNMETEKL--KVELQKL-HGVIKSLE 910
Cdd:TIGR00606 319 -------RELVDCQRELEKLNKERRLLNqekTELLVEQGRLQLQADRHQEHIRARDSLIQSLatRLELDGFeRGPFSERQ 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 911 -KDILSLKKEIQERD-----ETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELE 984
Cdd:TIGR00606 392 iKNFHTLVIERQEDEaktaaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
330
....*....|....*...
gi 2064967944 985 QFQRRNTQMELNIAELNL 1002
Cdd:TIGR00606 472 RILELDQELRKAERELSK 489
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
807-1074 |
3.73e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 807 ESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILD-----IRVKFEKMLTE-EKETNVH-----LKDETGIMR 875
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNddpeeIEKKIENIVTKiDKKKNIYdeikkLLNEIAEIE 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 876 KKFSSLQrEIDDKNME---------TEKLKVELQKLHGVIKSLE---KDILSLKKEIQERDETI---------------- 927
Cdd:TIGR01612 1204 KDKTSLE-EVKGINLSygknlgklfLEKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMgiemdikaemetfnis 1282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 928 QDKEKRIYDLRKKNTElekfkFVLDYKIKELK-KQIEPRENNIKEMREQIQKmegELEQFQRRNTQMELNIAELN----- 1001
Cdd:TIGR01612 1283 HDDDKDHHIISKKHDE-----NISDIREKSLKiIEDFSEESDINDIKKELQK---NLLDAQKHNSDINLYLNEIAniyni 1354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 1002 LKLKATDKDRRREMQRVHDIEALVRRFKTDLHRCVSFIqepKKLKDSIrQLYSCYVQKSDVVDIDGVDADIQK 1074
Cdd:TIGR01612 1355 LKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI---KKIKDDI-NLEECKSKIESTLDDKDIDECIKK 1423
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
907-1026 |
3.85e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 907 KSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQ----------I 976
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEerreirkdreI 467
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2064967944 977 QKMEGELEQFQRRNTQMELNIAELNLKL----KATDKDRRREMQRVHDIEALVR 1026
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELKRKLerlkELWKLEHSGELVPVKVVEKFTK 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
651-900 |
3.94e-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: 51.28 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 651 KRDNEICYSEEILVTKSDLEEKNQLMLELKTRVDELKMENEYQlrlrdmnynEKLKELTEKFIQEIDSLKTKNQVLKTEK 730
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAA---------RKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 731 EkleldhKALMDEMMEKHSKEQRDLESTNNQKlmLEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKL 810
Cdd:pfam17380 430 E------EARQREVRRLEEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 811 QEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGiMRKKFSSL--QREIDDK 888
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE-ERSRLEAMerEREMMRQ 580
|
250
....*....|..
gi 2064967944 889 NMETEKLKVELQ 900
Cdd:pfam17380 581 IVESEKARAEYE 592
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
730-1051 |
4.77e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 730 KEKLELDHKALMDEMmekhskeqRDLESTNNQ--KLMLEYEKY---LELQMKSQHMQ-EDFERQLHSSEQSKTE---ALE 800
Cdd:pfam01576 652 KEELERTNKQLRAEM--------EDLVSSKDDvgKNVHELERSkraLEQQVEEMKTQlEELEDELQATEDAKLRlevNMQ 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 801 ELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMikiMEEDADREILDIRVKfEKMLTEEKETNVHL------KDETGIM 874
Cdd:pfam01576 724 ALKAQFERDLQARDEQGEEKRRQLVKQVRELEAE---LEDERKQRAQAVAAK-KKLELDLKELEAQIdaankgREEAVKQ 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 875 RKK----FSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEI-----------QERDE-------------- 925
Cdd:pfam01576 800 LKKlqaqMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLaaserarrqaqQERDEladeiasgasgksa 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 926 TIQDK---EKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNL 1002
Cdd:pfam01576 880 LQDEKrrlEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 1003 KLKATDKD-------RRREMQRVHDIEALVRRFKTDLHRcvsfiQEPKKLKDSIRQ 1051
Cdd:pfam01576 960 TVKSKFKSsiaaleaKIAQLEEQLEQESRERQAANKLVR-----RTEKKLKEVLLQ 1010
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
832-960 |
5.28e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.63 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 832 EEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLhgviKSLEK 911
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA----RSEER 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2064967944 912 DILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKELKK 960
Cdd:COG2433 459 REIRKDREISRLDREIERLERELEEERERIEELKR-------KLERLKE 500
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
687-1006 |
5.39e-06 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 50.83 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 687 KMENEYQLRLRDMNYNEKLKElteKFIQEIDSLKTKNQVLKTEkEKLELDHKALMDEMMEKHSK---EQRDLESTNN--- 760
Cdd:pfam13166 144 KKNSALSEALNGFKYEANFKS---RLLREIEKDNFNAGVLLSD-EDRKAALATVFSDNKPEIAPltfNVIDFDALEKaei 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 761 --QKLMLEYEKYLELQmKSQHMQEDFERQLHSSEQSKT-----------EALEELTLQYESKLQEKVRKLKECEDKSQQQ 827
Cdd:pfam13166 220 liQKVIGKSSAIEELI-KNPDLADWVEQGLELHKAHLDtcpfcgqplpaERKAALEAHFDDEFTEFQNRLQKLIEKVESA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 828 KREYEEMIKIMEEDADREILDIRVKFEkmlteeketnvhLKDETGIMRKKFSSLQREIDDKNMETEKlKVELQKLHGVIK 907
Cdd:pfam13166 299 ISSLLAQLPAVSDLASLLSAFELDVED------------IESEAEVLNSQLDGLRRALEAKRKDPFK-SIELDSVDAKIE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 908 SLEKDILSLKKEIQERDETIQDKEKRIYDLRKKnteLEKFKFV--------LDYKIKELKKQIEPRENNIKEMREQIQKM 979
Cdd:pfam13166 366 SINDLVASINELIAKHNEITDNFEEEKNKAKKK---LRLHLVEefkseideYKDKYAGLEKAINSLEKEIKNLEAEIKKL 442
|
330 340
....*....|....*....|....*..
gi 2064967944 980 EGELEQFQRRNTQMELNIAELNLKLKA 1006
Cdd:pfam13166 443 REEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
888-998 |
6.34e-06 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 49.59 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 888 KNMETEKLKVELQKLhgviKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTEL-EKFKFVL--------------- 951
Cdd:pfam17060 135 PQESPETPRRINRKY----KSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLkDKYDFLSrefefykqhhehggn 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 952 ---------DYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIA 998
Cdd:pfam17060 211 nsiktatkhEFIISELKRKLQEQNRLIRILQEQIQFDPGALHDNGPKNLVLNGAIA 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
746-967 |
6.61e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 746 EKHSKEQRDLESTNNQklMLEYEKYLELQMKSQhmqEDFERQLHSSEQ---SKTEALEELTLQY---ESKLQEKVRKLKE 819
Cdd:COG4942 20 DAAAEAEAELEQLQQE--IAELEKELAALKKEE---KALLKQLAALERriaALARRIRALEQELaalEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 820 CEDKSQQQKREYEEMIKIMEEDADREILDIRVK------FEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETE 893
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSpedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064967944 894 KLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFkfvldykIKELKKQIEPREN 967
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL-------IARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
668-994 |
8.85e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 668 DLEEKNQLMLELKTRVDE-LKMENEY-----QLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALm 741
Cdd:pfam01576 30 ELEKKHQQLCEEKNALQEqLQAETELcaeaeEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 742 demmekhsKEQRDLESTNNQKLMLEyEKYLELQMKSqhMQED---FERQlHSSEQSKTEALEELTLQYESKLQEKVRKLK 818
Cdd:pfam01576 109 --------EEQLDEEEAARQKLQLE-KVTTEAKIKK--LEEDillLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEKAK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 819 ECedksQQQKREYEEMIKIMEEDADREildirvkfEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVE 898
Cdd:pfam01576 177 SL----SKLKNKHEAMISDLEERLKKE--------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 899 LQKLHG--------------VIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKK----NTELE----------KFKFV 950
Cdd:pfam01576 245 LQAALArleeetaqknnalkKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElealKTELEdtldttaaqqELRSK 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2064967944 951 LDYKIKELKKQIEPR----ENNIKEMRE----QIQKMEGELEQFQRRNTQME 994
Cdd:pfam01576 325 REQEVTELKKALEEEtrshEAQLQEMRQkhtqALEELTEQLEQAKRNKANLE 376
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
24-332 |
9.00e-06 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 48.87 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 24 FYDEQTVIFPSGNNCVR-YNIDQKWQRFIpGTEKSQSIQALALSPNRRYLAVSerGEKGTITVYDLQNDqiKKRKVLSGG 102
Cdd:cd00200 18 SPDGKLLATGSGDGTIKvWDLETGELLRT-LKGHTGPVRDVAASADGTYLASG--SSDKTIRLWDLETG--ECVRTLTGH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 103 EIPVQefvCMAFSPDSKYLIgqSGTPDFILFYWMWEKQKVIATVNT-GGPTHQVSFNPRDNTQICACGIGVFKLFRYAEG 181
Cdd:cd00200 93 TSYVS---SVAFSPDGRILS--SSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 182 VLKqfsaqklesHNFLSH-DWVSEkrlIAGTDKGRLLVIESGD--LR-WEMnvvmkpsaqdperseDRKKQEESAPAQLP 257
Cdd:cd00200 168 KCV---------ATLTGHtGEVNS---VAFSPDGEKLLSSSSDgtIKlWDL---------------STGKCLGTLRGHEN 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 258 RVTAIAAYSKGFFCSAGpgmvclfekmeDKDhyrKSREIWipaDPCSNDPSQT---EQQEIMCMCISPLEETLAT-STD 332
Cdd:cd00200 221 GVNSVAFSPDGYLLASG-----------SED---GTIRVW---DLRTGECVQTlsgHTNSVTSLAWSPDGKRLASgSAD 282
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
760-1017 |
9.31e-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: 49.74 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 760 NQKLMLEYEKYLELQMKSQHMQEDFERQlhssEQSKTEALEeltlqyesklQEKVRKLKECEDKSQQQKREYE------- 832
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQ----QQEKFEKME----------QERLRQEKEEKAREVERRRKLEeaekarq 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 833 ----------------------EMIKIMEEDADREILDIRVK-----------FEKMLTEEKETNVHLKDETGIMRKKF- 878
Cdd:pfam17380 327 aemdrqaaiyaeqermamererELERIRQEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKi 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 --SSLQREIDDKNMETEKLKVELQ-----KLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFK--- 948
Cdd:pfam17380 407 leEERQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKrdr 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 949 --------FVLDYKIKE--------------LKKQIEPRENNI---KEMREQIQKMEGELEQFQRRNTQMELNIA-ELNL 1002
Cdd:pfam17380 487 kraeeqrrKILEKELEErkqamieeerkrklLEKEMEERQKAIyeeERRREAEEERRKQQEMEERRRIQEQMRKAtEERS 566
|
330
....*....|....*
gi 2064967944 1003 KLKATDKDrrREMQR 1017
Cdd:pfam17380 567 RLEAMERE--REMMR 579
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
727-1027 |
1.26e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 727 KTEKEKLELDHKALMDEMME----KHSKEQRDLESTNNQKlMLEYEKYLELQM--KSQHMQEDFERQLHSSEQ--SKTEA 798
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEeereRALEEEEEKEEERKEE-RKRYRQELEEQIeeREQKRQEEYEEKLQEREQmdEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 799 LEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDirvkFEKMLTEEKETnvhlkdetgIMRKKf 878
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE----YLKEKAEREEE---------REAER- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 sslQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSL---KKEIQERDETIQDKEKRIYDLRK-KNTELEKFKFVLDYK 954
Cdd:pfam13868 176 ---EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQElQQAREEQIELKERRL 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 955 IKELKKQIEPRENNIKEMREQIQKmegELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRR 1027
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEI---EQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLRE 322
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
477-515 |
1.75e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.72 E-value: 1.75e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2064967944 477 FENILNLKGHNGKVRSIMWSEDDRRLVSCGMDGAVYEWN 515
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
728-984 |
1.76e-05 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 48.67 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 728 TEKEKLELDHKALMDEMMEKHSKE----QRDLEstnNQKLmleyEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEELT 803
Cdd:cd23695 1 TEYEQERRAYKQLFKEYRKKHKKDywesQTIVE---NEFI----DKYNKEELKKQRKDLDKWRTSIITISKATQNHIKLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 804 LQYESKLQEKVRKLKECEDKSQQQKReyeEMIKIMEEDADREI--LDIRVKF-EKML---TEEKETNVHLK-DETGIMRK 876
Cdd:cd23695 74 EKKSVKKEENERKYLLEQDVKAMNKK---IILDVMNEESKNWInlQNMNEKInPNLIlpdTILDETSYYLKlQELAFLFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 877 --KFSSLQrEIDDKNMETEKLKVELQKLHGVIKSLEKDILSlkKEIQERDETIQDKEKRIYDLRKKNTE-----LEKFKF 949
Cdd:cd23695 151 qgDHEEMD-KLLDENEEIEYKNSLLMPIYQDLKSLIKHLKY--TELFKLLKEYQDAKAIIIEDFRESSEegaekLEKLEK 227
|
250 260 270
....*....|....*....|....*....|....*
gi 2064967944 950 VLDYKIKELKKQIEPRENNIKEMREQIQKMEGELE 984
Cdd:cd23695 228 AFATLLKNYKEELEEPEKQLEFMQKRLLDLYNLLR 262
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
658-1021 |
2.42e-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: 48.58 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 658 YSEEILVTKSDLEEKNQLMLELKTRVDELKmENEYQLRLRDMNYNEKLKELTEK------FIQEIDSLKTKNQVLKTEKE 731
Cdd:pfam05557 116 LRRQIQRAELELQSTNSELEELQERLDLLK-AKASEAEQLRQNLEKQQSSLAEAeqrikeLEFEIQSQEQDSEIVKNSKS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 732 KLEldHKALMDEMMEKHSKEQRDLESTNNQKLMLE------------YEKYLE----LQMKSQHMQEDFER-----QLHS 790
Cdd:pfam05557 195 ELA--RIPELEKELERLREHNKHLNENIENKLLLKeevedlkrklerEEKYREeaatLELEKEKLEQELQSwvklaQDTG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 791 SEQSKTEAL---------EELTLQ-----YESKLQEKVRKLKECEDK-SQQQKREYEEMIKIMEEDADREILDIRV---- 851
Cdd:pfam05557 273 LNLRSPEDLsrrieqlqqREIVLKeenssLTSSARQLEKARRELEQElAQYLKKIEDLNKKLKRHKALVRRLQRRVlllt 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 852 -----------KFEKMLTEEKET---------------NVHLKDETgiMRKKFSSLQREIDDKNMETEKLKVELQKL--- 902
Cdd:pfam05557 353 kerdgyraileSYDKELTMSNYSpqllerieeaedmtqKMQAHNEE--MEAQLSVAEEELGGYKQQAQTLERELQALrqq 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 903 --HGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRkknTELEKFKFVLDYKIKELK-----------------KQIE 963
Cdd:pfam05557 431 esLADPSYSKEEVDSLRRKLETLELERQRLREQKNELE---MELERRCLQGDYDPKKTKvlhlsmnpaaeayqqrkNQLE 507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 964 PRENNIKEMREQIQKMEGELEQFQRRN-TQMELNIAELNlKLKATDKDRRREMQRVHDI 1021
Cdd:pfam05557 508 KLQAEIERLKRLLKKLEDDLEQVLRLPeTTSTMNFKEVL-DLRKELESAELKNQRLKEV 565
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
641-845 |
2.44e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 641 KIIDKERHGMKRDNEIcyseEILVTKSDLEEKNQLMLElktRVDELKMENEYQLRLRDMNYNEKLKELTEkfiQEIDSLK 720
Cdd:pfam17380 405 KILEEERQRKIQQQKV----EMEQIRAEQEEARQREVR---RLEEERAREMERVRLEEQERQQQVERLRQ---QEEERKR 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 721 TKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLESTNNQKLMleyEKylELQMKSQHMQEDFERQLHSSEQSKTEALE 800
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL---EK--EMEERQKAIYEEERRREAEEERRKQQEME 549
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2064967944 801 EltlqyESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADRE 845
Cdd:pfam17380 550 E-----RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
649-1050 |
2.57e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 649 GMKRDNEIC--YSEEILVTKSDLEEKNQLMLELKTRVDELKmeNEYqLRLRDMN-YNEKLK-ELTEKfiqeIDSLKTKNQ 724
Cdd:TIGR01612 545 GLKESYELAknWKKLIHEIKKELEEENEDSIHLEKEIKDLF--DKY-LEIDDEIiYINKLKlELKEK----IKNISDKNE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 725 VLK--TEKEKLELDHKALMDEMME-------KHSKEQRDLESTNNQKLmleyekylelqmkSQHMQEDFERqLHSSEQSK 795
Cdd:TIGR01612 618 YIKkaIDLKKIIENNNAYIDELAKispyqvpEHLKNKDKIYSTIKSEL-------------SKIYEDDIDA-LYNELSSI 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 796 TEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEE--KETNVHLKDetgi 873
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEinKDLNKILED---- 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 874 MRKKFSSLQREIDDKNMETEKLKVELQKLhGVIKSLEKDILSLkkeiqerDETIQDKEKRIYDLRKKNT------ELEKF 947
Cdd:TIGR01612 760 FKNKEKELSNKINDYAKEKDELNKYKSKI-SEIKNHYNDQINI-------DNIKDEDAKQNYDKSKEYIktisikEDEIF 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 948 KFVldYKIKELKKQIEPR-------ENNIKEmreqiqKMEGELEQFqrrntqmelniAELNLKLKATDKDRRREM--QRV 1018
Cdd:TIGR01612 832 KII--NEMKFMKDDFLNKvdkfinfENNCKE------KIDSEHEQF-----------AELTNKIKAEISDDKLNDyeKKF 892
|
410 420 430
....*....|....*....|....*....|..
gi 2064967944 1019 HDIEALVRRFKTDLHRCVSFIQEPKKLKDSIR 1050
Cdd:TIGR01612 893 NDSKSLINEINKSIEEEYQNINTLKKVDEYIK 924
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1097 |
2.68e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEYQLRLrdmnynEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLES 757
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 758 TNNQKlmleyEKYLELQMKSQhmqedferqlhssEQSKTEALEEltlqyesKLQEKVRKLKECEdKSQQQKREYEEMIKI 837
Cdd:PTZ00121 1373 KEEAK-----KKADAAKKKAE-------------EKKKADEAKK-------KAEEDKKKADELK-KAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 838 MEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLK 917
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 918 KEIQERDETIQDKEKRIYDLRKKNTELEKFKFVldYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNtqMELNI 997
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN--MALRK 1582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 998 AELnlkLKATDKDRRREMQRVHDIEALVR----------RFKTDLHRCVsfiQEPKKLKDSIRQLYSCYVQKSDVVDIDG 1067
Cdd:PTZ00121 1583 AEE---AKKAEEARIEEVMKLYEEEKKMKaeeakkaeeaKIKAEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
410 420 430
....*....|....*....|....*....|
gi 2064967944 1068 VDADIQKEYNRQREHLEKTVASLKKKLAKD 1097
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
668-984 |
2.97e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 668 DLEE--------KNQLMLELKTRVDELKMENEYQLRLRDMNYN-EKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHK 738
Cdd:pfam01576 107 DLEEqldeeeaaRQKLQLEKVTTEAKIKKLEEDILLLEDQNSKlSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 739 ALMDEMMEKHSKEQR------------DLESTNNQKLMLEYEKYL-ELQMKSQHMQEDFERQLHSSEQS---KTEALE-- 800
Cdd:pfam01576 187 AMISDLEERLKKEEKgrqelekakrklEGESTDLQEQIAELQAQIaELRAQLAKKEEELQAALARLEEEtaqKNNALKki 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 801 -ELTLQYeSKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADrEILD-------IRVKFEKMLTE-----EKETNVHl 867
Cdd:pfam01576 267 rELEAQI-SELQEDLESERAARNKAEKQRRDLGEELEALKTELE-DTLDttaaqqeLRSKREQEVTElkkalEEETRSH- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 868 KDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHgviKSLEKDILSLKKEIQERDETIQDKEKRiydlRKKntelekf 947
Cdd:pfam01576 344 EAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAK---QALESENAELQAELRTLQQAKQDSEHK----RKK------- 409
|
330 340 350
....*....|....*....|....*....|....*..
gi 2064967944 948 kfvLDYKIKELKKQIEPRENNIKEMREQIQKMEGELE 984
Cdd:pfam01576 410 ---LEGQLQELQARLSESERQRAELAEKLSKLQSELE 443
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
797-922 |
3.67e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 797 EALEELTLQYESKLQEKVRKLKECEDKSQQQKRE----YEEMIKIME----------EDADREILDIRVKFEKMLTEEKE 862
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEeirrLEEQVERLEaeveeleaelEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 863 tNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQE 922
Cdd:COG2433 460 -EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEK 518
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
874-1093 |
3.67e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 874 MRKKFSSLQREIddkNMETEKLKVELQKLHGVIKSLEKDILSLKKEiqeRDETIQDKEKRIYDLRKKNTELEKFKFVLDY 953
Cdd:PHA02562 168 MDKLNKDKIREL---NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKK---NGENIARKQNKYDELVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 954 KIKELKKQIEPRENNIKEMREQIQKMEGELEQFQR-----------------------RNTQMELNIAELNLKLKATDKD 1010
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1011 RRREMQRVHDIEALVRRF---KTDLHRC----VSFIQEPKKLKDSIRQLyscyvqKSDVVDIDGVDADIQKEYnrqrEHL 1083
Cdd:PHA02562 322 IDELEEIMDEFNEQSKKLlelKNKISTNkqslITLVDKAKKVKAAIEEL------QAEFVDNAEELAKLQDEL----DKI 391
|
250
....*....|
gi 2064967944 1084 EKTVASLKKK 1093
Cdd:PHA02562 392 VKTKSELVKE 401
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
772-992 |
4.38e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 772 ELQMKSQHMQEDFERQLHSSEQSKTEALEELTlQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDadreildirv 851
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELE-QLREELEQAREELEQLEEELEQARSELEQLEEELEEL---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 852 kfEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKE 931
Cdd:COG4372 86 --NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 932 KRIYDLRKKNTELEKFKfvLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQ 992
Cdd:COG4372 164 EELAALEQELQALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
666-1018 |
4.61e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 666 KSDLEEKNQLMLELKTRVDELKMENEyqlrlRDMNYNEKLKEltekfiqeidSLKTKNQ---VLKTEKE--KLELDHKAl 740
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS-----DCKQHIEVLKE----------SLTAKEQraaILQTEVDalRLRLEEKE- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 741 mdEMMEKHSKEQRDL---EST-----NNQKLMLEYE--KYLELQMKSQHMQE---DFERQLhSSEQSKTEALEE------ 801
Cdd:pfam10174 359 --SFLNKKTKQLQDLteeKSTlageiRDLKDMLDVKerKINVLQKKIENLQEqlrDKDKQL-AGLKERVKSLQTdssntd 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 802 ---LTLqyESKLQEKVR---KLKECEDKSQQQKRE----YEEMIKIMEEDADREILDIRVKfEKMLTEEKETNVHLKDET 871
Cdd:pfam10174 436 talTTL--EEALSEKERiieRLKEQREREDRERLEelesLKKENKDLKEKVSALQPELTEK-ESSLIDLKEHASSLASSG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 872 GIMRKKFSSLQREIDDKNMETEKLKVELQKLHGV-------------IKSLEKDILSLKKE--------------IQERD 924
Cdd:pfam10174 513 LKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAeeavrtnpeindrIRLLEQEVARYKEEsgkaqaeverllgiLREVE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 925 ETIQDKEKRIYDLRK--------KNTELEKFKFVLDYKIKELKKQIE------------PRENNIKEMREQIQKMEGELE 984
Cdd:pfam10174 593 NEKNDKDKKIAELESltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEearrrednladnSQQLQLEELMGALEKTRQELD 672
|
410 420 430
....*....|....*....|....*....|....
gi 2064967944 985 QFQRRNTQMELNIAELNLKLKATDKDRRREMQRV 1018
Cdd:pfam10174 673 ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEI 706
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
798-1018 |
4.81e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 798 ALEELTLQYESKLQEKVRKLKECEDKSQQQKREyeemikimEEDADREILDIRVKFEKMLTEEKETNVHLKDetgiMRKK 877
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKE--------EKALLKQLAALERRIAALARRIRALEQELAA----LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 878 FSSLQREIDDKNMETEKLKVELQKLHGVI-----KSLEKDILS-------------LKKEIQERDETIQDKEKRIYDLRK 939
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALyrlgrQPPLALLLSpedfldavrrlqyLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 940 KNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRV 1018
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
625-1052 |
4.83e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 625 DQFLLTVSEDNCLLIWKIIDKERHGMKRDNEICYSEEiLVTKSDLEEKNQLMLELKTRvdelKMENEYQLRLRdmNYNEK 704
Cdd:TIGR00618 155 AQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKS-LHGKAELLTLRSQLLTLCTP----CMPDTYHERKQ--VLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 705 LKELTEKFIQEIDSLK--TKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQE 782
Cdd:TIGR00618 228 LKHLREALQQTQQSHAylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 783 DFERqLHSSEQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKE 862
Cdd:TIGR00618 308 QAQR-IHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 863 TNVHLKDETGIMRKKFSSLQRE---IDDKNMETEKLKVELQKLHGVIKsLEKDILSLKKEIQERDETIQDKEKRI----- 934
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAITCTAQCEKLEKIHlqesa 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 935 YDLRKKnTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQ----------FQRRNTQMELNIAELNLKL 1004
Cdd:TIGR00618 466 QSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNParqdidnpgpLTRRMQRGEQTYAQLETSE 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2064967944 1005 KATDKDRRREMQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQL 1052
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI 592
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
781-948 |
4.84e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 781 QEDFERQLHSSEQSKTEA------LEELTLQYES---KLQEKVRKLKECEDKS-QQQKREYEEMIKIMEEDADREILDIR 850
Cdd:PRK00409 515 KEKLNELIASLEELERELeqkaeeAEALLKEAEKlkeELEEKKEKLQEEEDKLlEEAEKEAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 851 VKFEKMLTEEKEtnvhlkdetgimrKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEK----------DILSL--KK 918
Cdd:PRK00409 595 QLQKGGYASVKA-------------HELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkylslgqkgEVLSIpdDK 661
|
170 180 190
....*....|....*....|....*....|.
gi 2064967944 919 EIQERDETIQDKEKrIYDLRK-KNTELEKFK 948
Cdd:PRK00409 662 EAIVQAGIMKMKVP-LSDLEKiQKPKKKKKK 691
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
873-1022 |
5.05e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 873 IMRKKFSSLQRE----IDDKNMETEKLKVEL-----QKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRiydLRKKNTE 943
Cdd:PRK12704 28 IAEAKIKEAEEEakriLEEAKKEAEAIKKEAlleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN---LDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 944 LEKfkfvldykikeLKKQIEPRENNIKEMREQIQKMEGELEQF-QRRNTQMElNIAEL------NLKLKATDKDRRREMQ 1016
Cdd:PRK12704 105 LEK-----------REEELEKKEKELEQKQQELEKKEEELEELiEEQLQELE-RISGLtaeeakEILLEKVEEEARHEAA 172
|
....*..
gi 2064967944 1017 R-VHDIE 1022
Cdd:PRK12704 173 VlIKEIE 179
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
659-850 |
5.64e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 659 SEEILVTKSDLEEKNQLMLELKTRVDELK-MENEYQLRLRDM-NYNEKLKELTEKFIQEIDSLKTK-NQVLKTEKEKLEL 735
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNELNsLSEDYEVLKRNFrNKSEEMETTTNKLKMQLKSAQSElEQTRNTLKSMEGS 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 736 DHKALMDEM-MEKHSKEQRDLESTNNQKLmleyeKYLELQM----KSQHMQEDFERQLH------SSEQSKTEALEELTL 804
Cdd:pfam15921 722 DGHAMKVAMgMQKQITAKRGQIDALQSKI-----QFLEEAMtnanKEKHFLKEEKNKLSqelstvATEKNKMAGELEVLR 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2064967944 805 QYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADR----EILDIR 850
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRlklqHTLDVK 846
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
662-934 |
7.20e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 662 ILVTKSDLEEKNQLMLELKTRVDELKMENEYQLRLRDMNYNEKlkeltekfiqeiDSLKTKNQVLKTEKEKLELDHKALM 741
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER------------KQLQAKLQQTEEELRSLSKEFQELR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 742 DEMMEKHSKEQ--RDLESTNNQKLMLEYEKYLELQMKSQHMQEDFERqLHSSEQSKT---EALEELTLQ--------YES 808
Cdd:pfam07888 199 NSLAQRDTQVLqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQER-LNASERKVEglgEELSSMAAQrdrtqaelHQA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 KLQ--EKVRKLKEC-----EDKSQQQKrEYEEMIKIMEEDADR------EILdirvKFEKMLTEEKETNVHLKDETGimr 875
Cdd:pfam07888 278 RLQaaQLTLQLADAslalrEGRARWAQ-ERETLQQSAEADKDRieklsaELQ----RLEERLQEERMEREKLEVELG--- 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 876 kkfsslqREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRI 934
Cdd:pfam07888 350 -------REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
903-1052 |
7.39e-05 |
|
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: 46.97 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 903 HGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKELKKQIEPRENNIKEMREQIQKMEGE 982
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE-------ELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064967944 983 LEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVH----DIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQL 1052
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeaeaEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
671-985 |
7.49e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 671 EKNQLMLELKTRVDELKMENEYQLRLRD---MNYnEKLKELTEKFIQEIDSLKTKnqvlktEKEKleldhkalmdEMMEK 747
Cdd:PTZ00440 799 DINILKENKKNNQDLLNSYNILIQKLEAhteKND-EELKQLLQKFPTEDENLNLK------ELEK----------EFNEN 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 748 HSKEQRDLESTNNQKLMLEYEKYLELQMKSQhmqedferqlhSSEQSKTEALEELTLQYESKLQEKVRKLK-----ECED 822
Cdd:PTZ00440 862 NQIVDNIIKDIENMNKNINIIKTLNIAINRS-----------NSNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiQKNE 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 823 KSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQ-- 900
Cdd:PTZ00440 931 KLNLLNNLNKEKEKIEKQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNil 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 901 --KLHGVIKSLEKDILSL-KKEIQERDETIQDK-EKRIYDLRKKNTELEKFKFVLDYK----------IKELKKQIEPRE 966
Cdd:PTZ00440 1011 nkKIDDLIKKQHDDIIELiDKLIKEKGKEIEEKvDQYISLLEKMKTKLSSFHFNIDIKkyknpkikeeIKLLEEKVEALL 1090
|
330
....*....|....*....
gi 2064967944 967 NNIKEMREQIQKMEGELEQ 985
Cdd:PTZ00440 1091 KKIDENKNKLIEIKNKSHE 1109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
854-1029 |
7.67e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 854 EKMLTEEKETN--VHLKDETGIMRKKFSSLQREIddknmetEKLKVELQKLHGVIKSLEKDILSLKKEIQE--RDETIQD 929
Cdd:COG3206 195 EAALEEFRQKNglVDLSEEAKLLLQQLSELESQL-------AEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 930 KEKRIYDLRKKNTELEKfKFVLDY-KIKELKKQIEPRENNIK-EMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKAT 1007
Cdd:COG3206 268 LRAQLAELEAELAELSA-RYTPNHpDVIALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
170 180
....*....|....*....|....*....
gi 2064967944 1008 DKDRR--REMQRVHDI-----EALVRRFK 1029
Cdd:COG3206 347 PELEAelRRLEREVEVarelyESLLQRLE 375
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
3-165 |
1.03e-04 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 45.07 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 3 TVVAQSHFIFGLRTGVTNNIVFYDEQTVIFPSGNNCVRYNIDQKWQRFIPGTEKSQSIQALALSPNRRYLAVSERGEkGT 82
Cdd:COG3391 55 ALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGN-GR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 83 ITVYDLQNDQIKKRkvLSGGEIPVqefvCMAFSPDSKYL-IGQSGTPD-FILFYWM-WEKQKVIATVNTGGPTHQVSFNP 159
Cdd:COG3391 134 VSVIDTATGKVVAT--IPVGAGPH----GIAVDPDGKRLyVANSGSNTvSVIVSVIdTATGKVVATIPVGGGPVGVAVSP 207
|
....*.
gi 2064967944 160 rDNTQI 165
Cdd:COG3391 208 -DGRRL 212
|
|
| F-BAR_PACSIN1 |
cd07680 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
673-869 |
1.11e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153364 [Multi-domain] Cd Length: 258 Bit Score: 45.42 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 673 NQLMLELKTRVdelKMENEYQLRLRDmnYNEKLKELTEKFIQeIDSLKTKNQVLKTEKEKLELDHK----ALMDEMMEK- 747
Cdd:cd07680 22 NDLMNCVQERA---KIEKAYGQQLTD--WAKRWRQLIEKGPQ-YGSLERAWGAIMTEADKVSELHQevknNLLNEDLEKv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 748 --------HS------KEQRDLES--TNNQKLMLEYEKYLELQMKSQHMQEDfERQLHSSEQSKTEALEELTLQYESKLQ 811
Cdd:cd07680 96 knwqkdayHKqimggfKETKEAEDgfRKAQKPWAKKMKELEAAKKAYHLACK-EEKLAMTREANSKAEQSVTPEQQKKLQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2064967944 812 EKVRKlkeCEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKD 869
Cdd:cd07680 175 DKVDK---CKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKE 229
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
661-1097 |
1.15e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 661 EILVTKSDLEEKNQLMLELKTRVDELKMENEYQLRLRDMNYNEKLKELTEKFIQEI-----DSLKTKNQVLKTEKEKLEL 735
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVierqeDEAKTAAQLCADLQSKERL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 736 DHKALmDEMMEKHSKEQRDLEstnNQKLMLEyEKYLELQMKSQHMQ--EDFERQLHSSEQSKTEALEELTLQYESKLQEK 813
Cdd:TIGR00606 424 KQEQA-DEIRDEKKGLGRTIE---LKKEILE-KKQEELKFVIKELQqlEGSSDRILELDQELRKAERELSKAEKNSLTET 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 814 V---------------RKLKECEDKSQQQKREYE-----EMIKIMEEDADREILDIRVKFEKMLTEE----------KET 863
Cdd:TIGR00606 499 LkkevkslqnekadldRKLRKLDQEMEQLNHHTTtrtqmEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqlEDW 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 864 NVHLKDETGIMRKKFSSLQREI-------DDKNMETEKLKVELQKLHGVI------KSLEKDILSLKKEIQE--RDETIQ 928
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELasleqnkNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKssKQRAML 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 929 DKEKRIYD-----LRKKN------------TELEKFKFVLDY---------KIKELKKQIEPRENNIKEM-------REQ 975
Cdd:TIGR00606 659 AGATAVYSqfitqLTDENqsccpvcqrvfqTEAELQEFISDLqsklrlapdKLKSTESELKKKEKRRDEMlglapgrQSI 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 976 IQKMEGELEQFQRRNTQMELNIAELNLKLKATDKdrrrEMQRVHDIEALVRRFKTDLHRCVSFIQEPKKLKDSIRQLysc 1055
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQ--- 811
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2064967944 1056 yVQKSDVVDIDGVDADIQKEYNRQREHLEKTVA--SLKKKLAKD 1097
Cdd:TIGR00606 812 -AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSkiELNRKLIQD 854
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
718-940 |
1.22e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 45.40 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 718 SLKTKNQVLKTEKEKLEldhkalmdemmekhskEQrdLESTNNQKLMLEYEKYLE---LQMKSQHMQEDFERQLHSSEQS 794
Cdd:pfam04849 91 SLLKQNSVLTERNEALE----------------EQ--LGSAREEILQLRHELSKKddlLQIYSNDAEESETESSCSTPLR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 795 KTEALEELT--LQYESkLQEKVRKLkecEDKSQQQKREYEEMIKIMEEDADRE---ILDIRVKFE------KMLTEE--- 860
Cdd:pfam04849 153 RNESFSSLHgcVQLDA-LQEKLRGL---EEENLKLRSEASHLKTETDTYEEKEqqlMSDCVEQLSeanqqmAELSEElar 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 861 -KETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRK 939
Cdd:pfam04849 229 kMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRK 308
|
.
gi 2064967944 940 K 940
Cdd:pfam04849 309 K 309
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
750-1014 |
1.46e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 750 KEQRDLESTNNQ-KLMLEYEKYL------ELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKLQEKVRKLKEced 822
Cdd:COG5022 810 KEYRSYLACIIKlQKTIKREKKLreteevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQE--- 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 823 kSQQQKREYEEMIKIMEEDaDREILDIRVKFEKMLTEEKE-TNVHLKDETGIMRKKFSSLQREIDdknMETEKlkvELQK 901
Cdd:COG5022 887 -LKIDVKSISSLKLVNLEL-ESEIIELKKSLSSDLIENLEfKTELIARLKKLLNNIDLEEGPSIE---YVKLP---ELNK 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 902 LHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELekFKFVLDYK-IKELKKQIEPRENNIKEMREQIQKME 980
Cdd:COG5022 959 LHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL--AELSKQYGaLQESTKQLKELPVEVAELQSASKIIS 1036
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2064967944 981 GELEQFQRRN------TQMELNIAELNLKLKATDKDRRRE 1014
Cdd:COG5022 1037 SESTELSILKplqklkGLLLLENNQLQARYKALKLRRENS 1076
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
674-971 |
1.56e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 674 QLMLELKTRVDELKMENEYQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQR 753
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEK 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 754 DLESTNNQKLMLEYEKY------LELQMKSQHMQEDFER-----QLHSSEQSKTEALEELTLQYESKLQEKVRKlkecED 822
Cdd:TIGR01612 580 EIKDLFDKYLEIDDEIIyinklkLELKEKIKNISDKNEYikkaiDLKKIIENNNAYIDELAKISPYQVPEHLKN----KD 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 823 KSQQQKREyeEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQreiddkNMETEKLKVEL--- 899
Cdd:TIGR01612 656 KIYSTIKS--ELSKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ------NMETATVELHLsni 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 900 ----QKLHGVIKSLEKDILS-LKKEIQERDETIQDKEK----RIYDLRKKNTELEKFKfvldYKIKELKKQIEPREN--N 968
Cdd:TIGR01612 728 enkkNELLDIIVEIKKHIHGeINKDLNKILEDFKNKEKelsnKINDYAKEKDELNKYK----SKISEIKNHYNDQINidN 803
|
...
gi 2064967944 969 IKE 971
Cdd:TIGR01612 804 IKD 806
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
893-1096 |
1.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 893 EKLKVELQKLHGVIKSLEKDILSLKKEIQeRDETIqdkEKRIYDLRKKNTELEKfkfvldyKIKELKKQIEPRENNIKEM 972
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIK-RTENI---EELIKEKEKELEEVLR-------EINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 973 REQIQKME---GELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRVHDIEALVRRFKTdlhrcvsfIQEPKKLKDSI 1049
Cdd:PRK03918 227 EKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKL 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2064967944 1050 RQLYSCYVQKSDVVD---------IDGVDADIQK--EYNRQREHLEKTVASLKKKLAK 1096
Cdd:PRK03918 299 SEFYEEYLDELREIEkrlsrleeeINGIEERIKEleEKEERLEELKKKLKELEKRLEE 356
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
678-1015 |
1.79e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 678 ELKTRVDELKMENEYQLRLRDMNYNEKLKELTEKFI----QEIDSLKTKNQVLKTEKEKLELDHKALMD-EMMEKHSKEQ 752
Cdd:COG5185 150 EASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTlgllKGISELKKAEPSGTVNSIKESETGNLGSEsTLLEKAKEII 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 753 rdlESTNNQKLMLEYEKYLELqmkSQHMQEDFERQLHSSEQSKTEALEElTLQYESKLQEKVRKLKECEDKSQQQKREYE 832
Cdd:COG5185 230 ---NIEEALKGFQDPESELED---LAQTSDKLEKLVEQNTDLRLEKLGE-NAESSKRLNENANNLIKQFENTKEKIAEYT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 833 EMIKIMEEDADREILDIRVKFEKMLTE-EKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKL--KVELQKLHGVIKSL 909
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEEsKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 910 EKDILSLKKEIQERDETIQDKEKRIYDlrkkntELEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRR 989
Cdd:COG5185 383 KDTIESTKESLDEIPQNQRGYAQEILA------TLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMRE 456
|
330 340 350
....*....|....*....|....*....|...
gi 2064967944 990 -------NTQMELNIAELNLKLKATDKDRRREM 1015
Cdd:COG5185 457 adeesqsRLEEAYDEINRSVRSKKEDLNEELTQ 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1096 |
1.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 875 RKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKeIQERDETIQD---KEKRIYDLRKKNTELEKFkfvl 951
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDvasAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 952 DYKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLkatdkDRRREMQRVHDIEALVRRFKTd 1031
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-----EAAEDLARLELRALLEERFAA- 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064967944 1032 lhrcvsfiqepkklkdsirqlyscyvqksdvVDIDGVDADIQKEYNRQREHLEKTVASLKKKLAK 1096
Cdd:COG4913 758 -------------------------------ALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
659-988 |
1.90e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 659 SEEILVTKSDLEEKNQLmleLKTRVDELKMENEYQLRLRDMN-YNEKLKELTEKFIQ---EIDSLKTKNQVLKTEKEKLE 734
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETL---LGTIMPEEESAKVCLTDVTIMErFQMELKDVERKIAQqaaKLQGSDLDRTVQQVNQEKQE 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 735 LDHKalMDEMMEKHSKEQRDLESTNNQKLMLEyEKYLELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYE-SKLQEK 813
Cdd:TIGR00606 834 KQHE--LDTVVSKIELNRKLIQDQQEQIQHLK-SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREiKDAKEQ 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 814 VRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFekmlteeKETNVHLKDetgIMRKKFSSLQREIDDKNMETE 893
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV-------KNIHGYMKD---IENKIQDGKDDYLKQKETELN 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 894 KLKVELQKLHGVIKSLEKDILSLKKEI---QERDETIQDKekriYDLRKKNTElekfkfvldykIKELKKQI-----EPR 965
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDIdtqKIQERWLQDN----LTLRKRENE-----------LKEVEEELkqhlkEMG 1045
|
330 340
....*....|....*....|...
gi 2064967944 966 ENNIKEMREQIQKMEGELEQFQR 988
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENIDLIKR 1068
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
775-1102 |
2.37e-04 |
|
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: 45.23 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 775 MKSQHMQEDFER--QLHSSEQSKTEaLEELTLQYEsKLQEKvrKLKECED---------------KSQQQKREYEEMIKI 837
Cdd:pfam06160 22 LMNLPVQEELSKvkKLNLTGETQEK-FEEWRKKWD-DIVTK--SLPDIEEllfeaeelndkyrfkKAKKALDEIEELLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 838 MEEDADreilDIRVKFEKMLTEEKETnvhlKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKlhgVIKSLEKDILSLK 917
Cdd:pfam06160 98 IEEDIK----QILEELDELLESEEKN----REEVEELKDKYRELRKTLLANRFSYGPAIDELEK---QLAEIEEEFSQFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 918 KEIQERD-----ETIQDKEKRIYDLRKKnteLEKF-KFVLDYKiKELKKQIEPRENNIKEMREQ-----IQKMEGELEQF 986
Cdd:pfam06160 167 ELTESGDylearEVLEKLEEETDALEEL---MEDIpPLYEELK-TELPDQLEELKEGYREMEEEgyaleHLNVDKEIQQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 987 QRRNTQMELNIAELNLklkatdKDRRREMQRVHD-IEALV----------RRFKTDLHRCVSFIQEPKKLKDSIRQLYSc 1055
Cdd:pfam06160 243 EEQLEENLALLENLEL------DEAEEALEEIEErIDQLYdllekevdakKYVEKNLPEIEDYLEHAEEQNKELKEELE- 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2064967944 1056 YVQKSDVVDIDgvDADIQKEYNRQREHLEKTVASLKKKLAKDTLAST 1102
Cdd:pfam06160 316 RVQQSYTLNEN--ELERVRGLEKQLEELEKRYDEIVERLEEKEVAYS 360
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
645-985 |
2.50e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.59 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 645 KERHGMKRDNEICYSEEILVTKSDLEEKNqlmLELKTRVDELKMENEYQLRLRDM------NYNEK---LKELTEKFIQE 715
Cdd:PTZ00440 1122 TEHYNKKKKSLEKIYKQMEKTLKELENMN---LEDITLNEVNEIEIEYERILIDHiveqinNEAKKsktIMEEIESYKKD 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 716 IDSlkTKNQVLKTEKEKL-ELDHKALMDEMMEKH-------------------SKEQRDLESTNNQ------KLMLEYEK 769
Cdd:PTZ00440 1199 IDQ--VKKNMSKERNDHLtTFEYNAYYDKATASYenieeltteakglkgeanrSTNVDELKEIKLQvfsylqQVIKENNK 1276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 770 yLELQMKSQHMQEDFERQLHSSEQSK-----TEALEELTLQYESKLQEKVRKLKECEDKSQQQKrEYEEMIKIMEEDA-- 842
Cdd:PTZ00440 1277 -MENALHEIKNMYEFLISIDSEKILKeilnsTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAK-EHKNKIYGSLEDKqi 1354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 843 DREILDIRVKFEKMLTEEKETNVHLKD---------------ETGIMRKKFSSLQREIDDKNMEteklKVELQKLHGVI- 906
Cdd:PTZ00440 1355 DDEIKKIEQIKEEISNKRKEINKYLSNiksnkekcdlhvrnaSRGKDKIDFLNKHEAIEPSNSK----EVNIIKITDNIn 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 907 --KSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELE 984
Cdd:PTZ00440 1431 kcKQYSNEAMETENKADENNDSIIKYEKEITNILNNSSILGK-KTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLN 1509
|
.
gi 2064967944 985 Q 985
Cdd:PTZ00440 1510 Q 1510
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
888-1018 |
2.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 888 KNMETEKLKVELQKLHGVIKSLEKDILSLKKEI--QERDETIQDKEKRIYDLRKKNTELEKfkfvldykikeLKKQIEPR 965
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQK-----------LEKRLLQK 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 966 ENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRV 1018
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
729-1017 |
3.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 729 EKEKLELDHKAlmdEMMEKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQEDFERQLHSSEQSKTEaleELTLQYES 808
Cdd:PTZ00121 1222 DAKKAEAVKKA---EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE---EKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 KLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETnvhlKDETGIMRKKFSSLQREIDDK 888
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA----EAEAAADEAEAAEEKAEAAEK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 889 NMETEKLKVELQKLhgviKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfKFVLDYKIKELKKQIEP--RE 966
Cdd:PTZ00121 1372 KKEEAKKKADAAKK----KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEakKA 1446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 967 NNIKEMREQIQKMEGELEQFQRRNTQMElniaelnLKLKATDKDRRREMQR 1017
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADE-------AKKKAEEAKKADEAKK 1490
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
713-948 |
3.36e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 713 IQEIDSL-KTKNQVLKTEKEKL--ELDHKALMDEMMEKHSKEQRDLESTNNQKLMLEYEKYLELqmksqhmqedfERQLH 789
Cdd:PHA02562 165 LSEMDKLnKDKIRELNQQIQTLdmKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE-----------AKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 790 SSEQSKTEALEELTLQYESkLQEKVRKLKECEDKSQQQKREYEEMIKIMEE------------DADREILDIRVKFEKML 857
Cdd:PHA02562 234 AEIEELTDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 858 TEEKETNVHLKDETGIMrkkfsslqREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDL 937
Cdd:PHA02562 313 HSLEKLDTAIDELEEIM--------DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
250
....*....|.
gi 2064967944 938 RKKNTELEKFK 948
Cdd:PHA02562 385 QDELDKIVKTK 395
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
667-962 |
3.37e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 667 SDLEEKNQLMLELKTRVDELKMENEYQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQvlKTEKEKLELdhkalmDEMME 746
Cdd:pfam15964 431 SQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQ--EIEKLGLEL------SESKQ 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 747 KHSKEQRDLESTNNQKLMLEyekylELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKLQEKVRKLKECEdkSQQ 826
Cdd:pfam15964 503 RLEQAQQDAARAREECLKLT-----ELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQME--AQH 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 827 QKREYEEmikimeedadreildirvkfEKMLTEEKETNVHLKDETGIMRKKFSSL----QREIDDKNMETEKLKVELQKL 902
Cdd:pfam15964 576 DKTVNEQ--------------------YSLLTSQNTFIAKLKEECCTLAKKLEEItqksRSEVEQLSQEKEYLQDRLEKL 635
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064967944 903 HGVIKSLEKDIL-------SLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQI 962
Cdd:pfam15964 636 QKRNEELEEQCVqhgrmheRMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
670-835 |
3.51e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 670 EEKNQLMLELKTRVDELKMENEYQLRLRdmnyNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALmdemmekhS 749
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRER----RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL--------E 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 750 KEQRDLEstnnqklmleyEKYLELQMKSQHMQEDFER--QLhSSEQSKTEALEELtlqyESKLQ-EKVRKLKECEDKSQQ 826
Cdd:PRK12704 121 QKQQELE-----------KKEEELEELIEEQLQELERisGL-TAEEAKEILLEKV----EEEARhEAAVLIKEIEEEAKE 184
|
170
....*....|
gi 2064967944 827 Q-KREYEEMI 835
Cdd:PRK12704 185 EaDKKAKEIL 194
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
363-392 |
3.82e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.83 E-value: 3.82e-04
10 20 30
....*....|....*....|....*....|
gi 2064967944 363 HSGIITGLSICIRKPLIATCSLDHSVRIWN 392
Cdd:smart00320 11 HTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
874-1052 |
3.84e-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: 44.37 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 874 MRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRK----------KNTE 943
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 944 LEKFKFVLD-------YKIKELKKQIEP-RENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREM 1015
Cdd:COG4942 119 QPPLALLLSpedfldaVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 2064967944 1016 QRVHDIEalvRRFKTDLHRCVSFIQEPKKLKDSIRQL 1052
Cdd:COG4942 199 KLLARLE---KELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
703-984 |
4.20e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 703 EKLKELTEKFIQEIDSLKTKNQvlktekeklelDHKALMDEMMEKHSKEQRDLESTNNQklmleY---EKYLELQMKSqh 779
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEE-----------KNREEVEQLKDLYRELRKSLLANRFS-----FgpaLDELEKQLEN-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 780 MQEDFER--QLHSS----EQSKT-EALEELTLQYESKLqEKVRKL-KECEDKSQQQKRE----YEEMIK----IMEEDAD 843
Cdd:PRK04778 177 LEEEFSQfvELTESgdyvEAREIlDQLEEELAALEQIM-EEIPELlKELQTELPDQLQElkagYRELVEegyhLDHLDIE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 844 REILDIRVKFEKM--------LTEEKETNVHLKDETGIMrkkFSSLQREIDDKNM---ETEKLKVELQKLHGVIKSLEKD 912
Cdd:PRK04778 256 KEIQDLKEQIDENlalleeldLDEAEEKNEEIQERIDQL---YDILEREVKARKYvekNSDTLPDFLEHAKEQNKELKEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 913 ILSLKK--EIQERD-ETIQDKEKRIYDLRKKNTELEK--------FKFVLDyKIKELKKQIEPRENNIKEMREQIQKME- 980
Cdd:PRK04778 333 IDRVKQsyTLNESElESVRQLEKQLESLEKQYDEITEriaeqeiaYSELQE-ELEEILKQLEEIEKEQEKLSEMLQGLRk 411
|
....
gi 2064967944 981 GELE 984
Cdd:PRK04778 412 DELE 415
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
701-1090 |
4.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 701 YNEKLKELTEkFIQEIDSLKTKnqVLKTEKEKLEL-----DHKALMDEMMEK--HSKEQRDLESTNNQKLMLEYEkylEL 773
Cdd:PRK02224 246 HEERREELET-LEAEIEDLRET--IAETEREREELaeevrDLRERLEELEEErdDLLAEAGLDDADAEAVEARRE---EL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 774 QMKSQHMQEDFERQLHSSEQSKTEA--LEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEdADREILDIRV 851
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAesLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-LEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 852 KFE-------------KMLTEEK--------ETNVHLKDETGIMRK-----------------KFSSLQREIDDKNMETE 893
Cdd:PRK02224 399 RFGdapvdlgnaedflEELREERdelrereaELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 894 KLKVELQKLHGVIKSLEKDILSLK--------------------KEIQERDETIQDKEKRIYDLRKKNTELE-------- 945
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEdlveaedrierleerredleELIAERRETIEEKRERAEELRERAAELEaeaeekre 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 946 --------------KFKfVLDYKIKELKKQIEPREN------NIKEMREQIQKMEGELEQFQRRNTQMELNIAELNlklk 1005
Cdd:PRK02224 559 aaaeaeeeaeeareEVA-ELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKR---- 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1006 atdkDRRREMQRVHDiEALVRRFKTDLHRCVSFIQepkKLKDSIRQLYScyvQKSDVV-DIDGVDADIQ--KEYNRQREH 1082
Cdd:PRK02224 634 ----ERKRELEAEFD-EARIEEAREDKERAEEYLE---QVEEKLDELRE---ERDDLQaEIGAVENELEelEELRERREA 702
|
....*...
gi 2064967944 1083 LEKTVASL 1090
Cdd:PRK02224 703 LENRVEAL 710
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
646-956 |
4.69e-04 |
|
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: 44.29 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 646 ERHGMKRDNEICYSEEI---LVTKSDLEEKNQLMLELKTRVDELKMENEyQLRLRDMNYNEKLKELT---EKFIQEIDSL 719
Cdd:pfam05622 159 ERNAEYMQRTLQLEEELkkaNALRGQLETYKRQVQELHGKLSEESKKAD-KLEFEYKKLEEKLEALQkekERLIIERDTL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 720 KTKNQVLKTEKekLELDHKALMDEMMEKHSKEqrdLESTNNQKLMLEY-EKYLELQ-----MKSQHMQEDFER------Q 787
Cdd:pfam05622 238 RETNEELRCAQ--LQQAELSQADALLSPSSDP---GDNLAAEIMPAEIrEKLIRLQhenkmLRLGQEGSYRERltelqqL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 788 LHSSEQSKTEALEELTLQYE--SKLQEKVRKLKEC--------EDKSQQQKREYEEMIKIMEEDADREILdirvkfeKML 857
Cdd:pfam05622 313 LEDANRRKNELETQNRLANQriLELQQQVEELQKAlqeqgskaEDSSLLKQKLEEHLEKLHEAQSELQKK-------KEQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 858 TEEKE----TNVHLKDET--GIMRKKfsslqrEIDDKNMEtEKLKVELQKLHGVIKSLE-KDILSLKKEIQERDETIQDK 930
Cdd:pfam05622 386 IEELEpkqdSNLAQKIDElqEALRKK------DEDMKAME-ERYKKYVEKAKSVIKTLDpKQNPASPPEIQALKNQLLEK 458
|
330 340
....*....|....*....|....*.
gi 2064967944 931 EKRIYDLRKkntELEKFKFVLDYKIK 956
Cdd:pfam05622 459 DKKIEHLER---DFEKSKLQREQEEK 481
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
746-1071 |
5.08e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 746 EKHSKEQRDLESTNNQKLMLEYEKYLELQMKSQHMQEDFERQLHSSEQskteaLEELTLQYEsKLQEKVRKLKECEDKSQ 825
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK-----IESARADLE-DIKIKINELKDKHDKYE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 826 QQKREYEEM-IKIMEE--------DADREILDIrvkfEKMLTEEKETNVHLKDETGIMRKKFSSLQ----------REID 886
Cdd:PRK01156 550 EIKNRYKSLkLEDLDSkrtswlnaLAVISLIDI----ETNRSRSNEIKKQLNDLESRLQEIEIGFPddksyidksiREIE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 887 DKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDykikELKKQIEPRE 966
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD----DAKANRARLE 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 967 NNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNlklkatDKDRRREMQRVHDIEALVRrfktdlhrcvsfiqepKKLK 1046
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIG------DLKRLREAFDKSGVPAMIR----------------KSAS 759
|
330 340
....*....|....*....|....*
gi 2064967944 1047 DSIRQLYSCYVQKSDvVDIDGVDAD 1071
Cdd:PRK01156 760 QAMTSLTRKYLFEFN-LDFDDIDVD 783
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
363-392 |
5.20e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 5.20e-04
10 20 30
....*....|....*....|....*....|
gi 2064967944 363 HSGIITGLSICIRKPLIATCSLDHSVRIWN 392
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
685-994 |
5.47e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 685 ELKMENEYQLRlrdMNYNEKLKE--LTEKFIQEIDS-LKTKNQVLKTEKEKLeldhKALMdEMMEKHSKEQRDLESTNNQ 761
Cdd:pfam10174 112 ELTEENFRRLQ---SEHERQAKElfLLRKTLEEMELrIETQKQTLGARDESI----KKLL-EMLQSKGLPKKSGEEDWER 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 762 KL-MLEYEKYL--------ELQMKSQHMQEDFERQLH-SSEQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKR-- 829
Cdd:pfam10174 184 TRrIAEAEMQLghlevlldQKEKENIHLREELHRRNQlQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTng 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 830 -----EYEEMIKIME--------------------EDADREILDIRVKFEKMLTEEKETNVH---LKDETGIMRKKFSSL 881
Cdd:pfam10174 264 llhteDREEEIKQMEvykshskfmknkidqlkqelSKKESELLALQTKLETLTNQNSDCKQHievLKESLTAKEQRAAIL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 882 QREID---------------------DKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKK 940
Cdd:pfam10174 344 QTEVDalrlrleekesflnkktkqlqDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 941 NTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQI-----QKMEgELEQFQRRNTQME 994
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQReredrERLE-ELESLKKENKDLK 481
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
791-948 |
6.05e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 42.36 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 791 SEQSKTEALEELTLQYESKlQEKVRKLKeceDKSQQQKREYEEMIKIME----------EDADREILDIRVKFEKMLTEE 860
Cdd:pfam05010 2 SQKDMDAALEKARNEIEEK-ELEINELK---AKYEELRRENLEMRKIVAefektiaqmiEEKQKQKELEHAEIQKVLEEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 861 KETNVHLKDetgiMRKKFSSLQREIddknmetEKLKvelqklhGVIKSLEKDILSLKKEIQERDETIQDKEKRiYDLRKK 940
Cdd:pfam05010 78 DQALADLNS----VEKSFSDLFKRY-------EKQK-------EVISGYKKNEESLKKCAQDYLARIKKEEQR-YQALKA 138
|
....*...
gi 2064967944 941 NTElEKFK 948
Cdd:pfam05010 139 HAE-EKLD 145
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
608-641 |
7.75e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.06 E-value: 7.75e-04
10 20 30
....*....|....*....|....*....|....
gi 2064967944 608 EYQGHAAPITKMAVTFDDQFLLTVSEDNCLLIWK 641
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
809-1017 |
8.45e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 KLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDAD------REILDIRVKFEKmLTEEKETNVHLKDETGIMRKKFSSLQ 882
Cdd:COG1340 68 ELNEKVKELKEERDELNEKLNELREELDELRKELAelnkagGSIDKLRKEIER-LEWRQQTEVLSPEEEKELVEKIKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 883 REIDDKNMEtEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKntelekfkfvldykIKELKKQI 962
Cdd:COG1340 147 KELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE--------------ADELRKEA 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2064967944 963 EPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQR 1017
Cdd:COG1340 212 DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
744-1085 |
8.48e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.10 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 744 MMEKHSKEQRDLE--------------STNNQKLMLEYEKYLELQMKSQHMQEDFERQ---LHSSEQSKTEALEELTLQY 806
Cdd:pfam15558 13 MLARHKEEQRMRElqqqaalaweelrrRDQKRQETLERERRLLLQQSQEQWQAEKEQRkarLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 807 ESKL------QEKVR--KLKECEDKSQQQKREYEEMIKIMEEdadrEILDIRVKFEKMLTEEKETNVHLKdetgimRKKF 878
Cdd:pfam15558 93 ESRWreqaedQENQRqeKLERARQEAEQRKQCQEQRLKEKEE----ELQALREQNSLQLQERLEEACHKR------QLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 SSLQREIDDKNMeTEKLKVELqklhgvikslekdilsLKKEI--QERDETIqdkekriydLRKKNTELEKFKFVLDYKik 956
Cdd:pfam15558 163 REEQKKVQENNL-SELLNHQA----------------RKVLVdcQAKAEEL---------LRRLSLEQSLQRSQENYE-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 957 elkKQIEPREnniKEMREQIQKMEGELEQFQRRNTQMElniAELNLKLKATDKDRRREMQRVHDIEALVRRFKTDLhrcv 1036
Cdd:pfam15558 215 ---QLVEERH---RELREKAQKEEEQFQRAKWRAEEKE---EERQEHKEALAELADRKIQQARQVAHKTVQDKAQR---- 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1037 sfIQEPKKLKDSIRQLYSCYVQKSDVVDIDGVDADI-QKEYNRQREHLEK 1085
Cdd:pfam15558 282 --ARELNLEREKNHHILKLKVEKEEKCHREGIKEAIkKKEQRSEQISREK 329
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
748-1092 |
1.05e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 748 HSKEQRDLESTN-NQKLmleYEKYL----------ELQMKSQHMQEDFERQLHSSEQskteaLEELTL---QYESKLQ-E 812
Cdd:TIGR01612 1973 HKKEQDTLNIIFeNQQL---YEKIQasnelkdtlsDLKYKKEKILNDVKLLLHKFDE-----LNKLSCdsqNYDTILElS 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 813 KVRKLKECEDKSQQQKREY--EEMIKIMEEDADREILDIRvKFEKML----------TEEKETNVHLKDETGIMRKKFSS 880
Cdd:TIGR01612 2045 KQDKIKEKIDNYEKEKEKFgiDFDVKAMEEKFDNDIKDIE-KFENNYkhsekdnhdfSEEKDNIIQSKKKLKELTEAFNT 2123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 881 LQREIDDKNMETEKLKVELQKLHG--VIKSLEKDILSLKKEIQERDETIQDKEKRIYDLrkkntelekFKFV------LD 952
Cdd:TIGR01612 2124 EIKIIEDKIIEKNDLIDKLIEMRKecLLFSYATLVETLKSKVINHSEFITSAAKFSKDF---------FEFIedisdsLN 2194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 953 YKIKELKKQIEPRENN--IKEMREQIQKMEGELEQFQRRNTQMELNIAEL-NLKLKATDKDrrremqRVHDIEALVRRFK 1029
Cdd:TIGR01612 2195 DDIDALQIKYNLNQTKkhMISILADATKDHNNLIEKEKEATKIINNLTELfTIDFNNADAD------ILHNNKIQIIYFN 2268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064967944 1030 TDLHRCVsfiqepkklkDSIRQLYSCY--VQKSDVVDIDGVDADIQKEYNR----QREHLEKTVASLKK 1092
Cdd:TIGR01612 2269 SELHKSI----------ESIKKLYKKInaFKLLNISHINEKYFDISKEFDNiiqlQKHKLTENLNDLKE 2327
|
|
| PEARLI-4 |
pfam05278 |
Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several ... |
888-1004 |
1.08e-03 |
|
Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several phospholipase-like proteins from Arabidopsis thaliana which are homologous to PEARLI 4.
Pssm-ID: 253129 [Multi-domain] Cd Length: 234 Bit Score: 42.13 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 888 KNMETEKLKVelqklhGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKELKKqiepREN 967
Cdd:pfam05278 124 KDLESVKIRV------GWLRSVLEEFAEAVEYFDQQETAVVEKERHERDVLLKKQEMEK-------QEAELVR----KEK 186
|
90 100 110
....*....|....*....|....*....|....*..
gi 2064967944 968 NIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKL 1004
Cdd:pfam05278 187 EVKEFREKVEEMAGRLGELEMKRLRLEKRLDFLGSKV 223
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
872-1032 |
1.12e-03 |
|
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: 43.29 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 872 GIM--RKKFSSLQREIDdknmETEKLKVELQKLHGVIKSLEKDILSlkkEIQERDETIQDKEKRIYDLRK----KNTELE 945
Cdd:pfam12128 235 GIMkiRPEFTKLQQEFN----TLESAELRLSHLHFGYKSDETLIAS---RQEERQETSAELNQLLRTLDDqwkeKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 946 KFKFVLDYKIKELKKQIEPRENNIKE-MREQIQKMEGELEQFQRRNTQMELNIAELNLKL----KATDKDRRREMQRVHD 1020
Cdd:pfam12128 308 GELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTgkhqDVTAKYNRRRSKIKEQ 387
|
170
....*....|..
gi 2064967944 1021 IEALVRRFKTDL 1032
Cdd:pfam12128 388 NNRDIAGIKDKL 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
809-1018 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 KLQEKVRKLKEcedkSQQQKREYEEMIKIMEEdADREILDIRVKFEKMLTEEKETNVHLKDETgiMRKKFSSLQREIDDK 888
Cdd:COG4717 72 ELKELEEELKE----AEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 889 NMETEKLKVELQKLHgvikslekdilSLKKEIQERDETIQDKEKRIYDLRKKNTElekfkfvldykikELKKQIEPRENN 968
Cdd:COG4717 145 PERLEELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSL-------------ATEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2064967944 969 IKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQRV 1018
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
816-985 |
1.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 816 KLKECEDKSQQQ----KREYEEMIKIMEEDADREILDIRVKFEKmltEEKETNVHLKD-ETGIMRKKfsslqREIDDKNM 890
Cdd:PRK12704 32 KIKEAEEEAKRIleeaKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKlEKRLLQKE-----ENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 891 ETEKLKVELQKLhgvikslEKDILSLKKEIQERDETIQDKEKriydlrKKNTELEKfkfVLDYKIKELKKQIepRENNIK 970
Cdd:PRK12704 104 LLEKREEELEKK-------EKELEQKQQELEKKEEELEELIE------EQLQELER---ISGLTAEEAKEIL--LEKVEE 165
|
170
....*....|....*
gi 2064967944 971 EMREQIQKMEGELEQ 985
Cdd:PRK12704 166 EARHEAAVLIKEIEE 180
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
659-984 |
1.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 659 SEEILVTKSDLEEKNQLMLELKTRVDELKMENEyqlrlrdmNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLElDHK 738
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELE--------QLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 739 ALMDEMMEKHSKEQRDLESTNNQKLMLEYE--KYLELQMKSQHMQEDFERQLHSSEQSKTEALEELTLQYESKLQEKVRK 816
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 817 LKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLK 896
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 897 VELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQI 976
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
....*...
gi 2064967944 977 QKMEGELE 984
Cdd:COG4372 341 DLLQLLLV 348
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
673-993 |
1.54e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 673 NQLMLELKTRVDELKMENEYQLRLRDM-----NYNEKLKELT---------------------------------EKFIQ 714
Cdd:TIGR01612 599 NKLKLELKEKIKNISDKNEYIKKAIDLkkiieNNNAYIDELAkispyqvpehlknkdkiystikselskiyeddiDALYN 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 715 EIDSLKTKNQVLKTE-KEKLElDHKALMDEMMEK-HSKEQRDLES------TNNQKL---MLEYEKYL--ELQMKSQHMQ 781
Cdd:TIGR01612 679 ELSSIVKENAIDNTEdKAKLD-DLKSKIDKEYDKiQNMETATVELhlsnieNKKNELldiIVEIKKHIhgEINKDLNKIL 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 782 EDF---ERQLHSSEQSKTEALEELTlQYESKLQE---------KVRKLKECEDKSQ-QQKREYEEMIKIMEEDADREILD 848
Cdd:TIGR01612 758 EDFknkEKELSNKINDYAKEKDELN-KYKSKISEiknhyndqiNIDNIKDEDAKQNyDKSKEYIKTISIKEDEIFKIINE 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 849 IRVKFEKMLTE-EKETNV--HLKDETGIMRKKFSSL----QREIDDKNMETEKLKVELQK--LHGVIKSLEKD---ILSL 916
Cdd:TIGR01612 837 MKFMKDDFLNKvDKFINFenNCKEKIDSEHEQFAELtnkiKAEISDDKLNDYEKKFNDSKslINEINKSIEEEyqnINTL 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 917 KKeIQERDETIQDKEKRIYDLRKKNTELEKfkfVLDYKIKELKKQ--IEPR-----ENNIKEMREQIQKM--EGELEQFQ 987
Cdd:TIGR01612 917 KK-VDEYIKICENTKESIEKFHNKQNILKE---ILNKNIDTIKESnlIEKSykdkfDNTLIDKINELDKAfkDASLNDYE 992
|
....*.
gi 2064967944 988 RRNTQM 993
Cdd:TIGR01612 993 AKNNEL 998
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
608-640 |
1.57e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|...
gi 2064967944 608 EYQGHAAPITKMAVTFDDQFLLTVSEDNCLLIW 640
Cdd:pfam00400 6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
883-1034 |
1.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 883 REIDDKNMETEKLKVELQKLHGVIKSL-----EKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfvldyKIKE 957
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALRE-------ELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 958 LKKQIepREN---NIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKD----RRREMQRVHDIEALVRRFKT 1030
Cdd:COG4913 328 LEAQI--RGNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEE 405
|
....
gi 2064967944 1031 DLHR 1034
Cdd:COG4913 406 ALAE 409
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
710-989 |
1.61e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 41.84 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 710 EKFIQEIDSLKTKNQVLKTEKEKLeLDHKALMDEMM-EKHSKEQRDLES-TNNQKLMLEYEKYLELQMKSQHMQEDFERQ 787
Cdd:pfam13949 23 EKSLDDLPKLKQRNREILDEAEKL-LDEEESEDEQLrAKYGTRWTRPPSsELTATLRAEIRKYREILEQASESDSQVRSK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 788 LHSSEqsktEALEELTLQYES---------------KLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREilDIRVK 852
Cdd:pfam13949 102 FREHE----EDLELLSGPDEDleaflpssrraknspSVEEQVAKLRELLNKLNELKREREQLLKDLKEKARND--DISPK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 853 fekmLTEEKETNVHLKDETGIMR---KKFSSLQREIDDKNMETEKLKVELQKLHgvikslekdilslkkeiqerDETIQD 929
Cdd:pfam13949 176 ----LLLEKARLIAPNQEEQLFEeelEKYDPLQNRLEQNLHKQEELLKEITEAN--------------------NEFLQD 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 930 KEKRIYDLRKKNTELEKFKFVLDyKIKELKkqiepreNNIKEMREQIQKMEGELEQFQRR 989
Cdd:pfam13949 232 KRVDSEKQRQREEALQKLENAYD-KYKELV-------SNLQEGLKFYNDLTEILEKLLKK 283
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
660-941 |
1.81e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 660 EEILVTKSDLEEKNQLMLELKTRVDELKmeneyQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKA 739
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELE-----AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 740 LMDEMMEKH-SKEQRDLESTNNQKLMLEYEKYL-ELQMKSQHMQEDF---ERQLHSSEQSKTEALEELtLQYESKLQEKV 814
Cdd:TIGR02168 836 TERRLEDLEeQIEELSEDIESLAAEIEELEELIeELESELEALLNERaslEEALALLRSELEELSEEL-RELESKRSELR 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 815 RKLKECEDKSQQQKREYEEMikimEEDADREILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQREID---DKNM- 890
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGL----EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgPVNLa 990
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2064967944 891 ---ETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKN 941
Cdd:TIGR02168 991 aieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
702-1016 |
1.89e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 702 NEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEM---MEKHSKEQRDLESTNN---QKLMLEYEKYLELQM 775
Cdd:PTZ00440 2250 KKKLLDNKNKINNIKDKINDKEKELINVDSSFTLESIKTFNEIyddIKSNIGDLYKLEDTNNdelKKVKLYIENITHLLN 2329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 776 KSQHMQEDFERQLHSSEQSKTEA-LEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEM-----IKIMEEDADREILDI 849
Cdd:PTZ00440 2330 RINTLINDLDNYQDENYGKDKNIeLNNENNSYIIKTKEKINNLKEEFSKLLKNIKRNNTLcnnnnIKDFISNIGKSVETI 2409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 850 RVKFEKMLTEEK---ETNVHLKDETGIM----RKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQE 922
Cdd:PTZ00440 2410 KQRFSSNLPEKEklhQIEENLNEIKNIMnetkRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDLIENVTSHNEKIKS 2489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 923 RDETIQDKEKRIYDLRKK-------------NTELEKFKFVLD--YKIKELKKQIEPRENNIKEMREQIQKMEGELEQFQ 987
Cdd:PTZ00440 2490 ELLIINDALRRVKEKKDEmnklfnsltennnNNNNSAKNIVDNstYIINELESHVSKLNELLSYIDNEIKELENEKLKLL 2569
|
330 340
....*....|....*....|....*....
gi 2064967944 988 RRNTQmELNIAELNLKLKATDKDRRREMQ 1016
Cdd:PTZ00440 2570 EKAKI-EESRKERERIESETQEDNTDEEQ 2597
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
879-994 |
1.89e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 879 SSLQREIDDknmetekLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKrIYDLRKKNTEL--------EKFKFV 950
Cdd:pfam05667 338 EELQEQLED-------LESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEK-QYKVKKKTLDLlpdaeeniAKLQAL 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 951 LDY---------------------KIKELKKQIEPRENN-------IKEMREQIQKMEGEL----EQFQRRNTQME 994
Cdd:pfam05667 410 VDAsaqrlvelagqwekhrvplieEYRALKEAKSNKEDEsqrkleeIKELREKIKEVAEEAkqkeELYKQLVAEYE 485
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
679-912 |
2.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 679 LKTRVDELKMEN---EYQLRLrdmnYNEKLKeLTEKFIQEIDSLKTKNQVLKTEK----EKLELDHKALMDEMMEKHSKE 751
Cdd:PHA02562 172 NKDKIRELNQQIqtlDMKIDH----IQQQIK-TYNKNIEEQRKKNGENIARKQNKydelVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 752 QRDLESTNN--QKLMLEYEKylelqMKSQHMQEDFERQLHSSEQ---SKTEALEEltlqYESKLQEKVRKLKECEDKSQQ 826
Cdd:PHA02562 247 VMDIEDPSAalNKLNTAAAK-----IKSKIEQFQKVIKMYEKGGvcpTCTQQISE----GPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 827 QKREYEEMIKIMEE--DADREILDIRVKFEKmlteEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKL-- 902
Cdd:PHA02562 318 LDTAIDELEEIMDEfnEQSKKLLELKNKIST----NKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIvk 393
|
250 260
....*....|....*....|.
gi 2064967944 903 -----------HGVIKSLEKD 912
Cdd:PHA02562 394 tkselvkekyhRGIVTDLLKD 414
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
714-976 |
2.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 714 QEIDSLKTKNQVLktekEKLE-----LDHKALMDEMMEKHskEQRDlESTNNQKLMLEYEKYLELqmksqhmqedFERQL 788
Cdd:PRK04863 865 SQLEQAKEGLSAL----NRLLprlnlLADETLADRVEEIR--EQLD-EAEEAKRFVQQHGNALAQ----------LEPIV 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 789 hSSEQSKTEALEELTLQYE------SKLQEKVRKLKECedksqQQKRE---YEEMIKIMEEDADREILdIRVKFEKMLTE 859
Cdd:PRK04863 928 -SVLQSDPEQFEQLKQDYQqaqqtqRDAKQQAFALTEV-----VQRRAhfsYEDAAEMLAKNSDLNEK-LRQRLEQAEQE 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 860 EKETNVHLKDETGIMRKK---FSSLQREIDDKNMETEKLKVELQKLhGVikslEKDILSLKKEIQERDETiqdkEKRIYD 936
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQYnqvLASLKSSYDAKRQMLQELKQELQDL-GV----PADSGAEERARARRDEL----HARLSA 1071
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2064967944 937 LRKKNTELEKFKFVLDYKIKELKKQIEPRENNIKEMREQI 976
Cdd:PRK04863 1072 NRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
702-1013 |
2.17e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 702 NEKLKELtEKFIQEIDSLKTKNQVLKTEKEKLELDHKALmdemmekhskeQRDLESTNNQKLmlEYEKYLELQMKSQHMQ 781
Cdd:pfam10174 271 EEEIKQM-EVYKSHSKFMKNKIDQLKQELSKKESELLAL-----------QTKLETLTNQNS--DCKQHIEVLKESLTAK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 782 EdferQLHSSEQSKTEALEELTLQYESKLQEKVRKLKECEDKSQQQKREYEEMiKIMEEDADREILDIRVKFE------- 854
Cdd:pfam10174 337 E----QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDL-KDMLDVKERKINVLQKKIEnlqeqlr 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 855 ---KMLTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHgviKSLEKDILSLKKEIQERDETI---- 927
Cdd:pfam10174 412 dkdKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRERED---RERLEELESLKKENKDLKEKVsalq 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 928 ---QDKEKRIYDLRKKNTELEKFKFVLDYKIKELkkqieprENNIKEMREQIQKMEGELEQFQrrntQMELNI---AELN 1001
Cdd:pfam10174 489 pelTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH----NAEEAVrtnPEIN 557
|
330
....*....|..
gi 2064967944 1002 LKLKATDKDRRR 1013
Cdd:pfam10174 558 DRIRLLEQEVAR 569
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
881-1017 |
2.60e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 881 LQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKriydlrKKNTELEKFKfvldYKIKELKK 960
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELED------CDPTELDRAK----EKLKKLLQ 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2064967944 961 QIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDKDRRREMQR 1017
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEK 275
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
756-987 |
2.72e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.09 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 756 ESTNNQKLMLEYEKYLELQMKsqhmqedfERQLHSSEQSKTEALEEltlQYESKLQEKVRKLKECEDKSQQQKREYEEMI 835
Cdd:pfam09728 33 EMKRLQKDLKKLKKKQDQLQK--------EKDQLQSELSKAILAKS---KLEKLCRELQKQNKKLKEESKKLAKEEEEKR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 836 KIMEEDADREILDIrvkfEKMLTEEKETNVHLKDETGIMRKKFSSLqreiddknmeteklkvelqklhgvIKSLEKDILS 915
Cdd:pfam09728 102 KELSEKFQSTLKDI----QDKMEEKSEKNNKLREENEELREKLKSL------------------------IEQYELRELH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064967944 916 LKKEIQERDETIQDKEKRiydLRKKNTELEKFKFVLDY-KIKELKKQIEPRENNIKEMREQIQKMEGELEQFQ 987
Cdd:pfam09728 154 FEKLLKTKELEVQLAEAK---LQQATEEEEKKAQEKEVaKARELKAQVQTLSETEKELREQLNLYVEKFEEFQ 223
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
880-977 |
2.91e-03 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 39.39 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 880 SLQREIDDKNMETEKLKVELQKLHGVIKSlekDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELK 959
Cdd:pfam06009 3 ELAREANETAKEVLEQLAPLSQNLENTSE---KLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLK 79
|
90 100
....*....|....*....|.
gi 2064967944 960 KQIEPREN---NIKEMREQIQ 977
Cdd:pfam06009 80 QLEVNSSSlsdNISRIKELIA 100
|
|
| FAM76 |
pfam16046 |
FAM76 protein; This family of proteins is functionally uncharacterized. This family of ... |
905-1001 |
3.73e-03 |
|
FAM76 protein; This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 233 and 341 amino acids in length.
Pssm-ID: 464993 [Multi-domain] Cd Length: 303 Bit Score: 40.93 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 905 VIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKfkfVLDYKIKELKKQieprennikemreqiqkMEGELE 984
Cdd:pfam16046 223 AITQLKEQIASLQKQLAQKDQQLLEKDKQITELKAKHFTKER---ELRNKMKTMEKE-----------------HEDKVE 282
|
90
....*....|....*..
gi 2064967944 985 QFQRRNTQMELNIAELN 1001
Cdd:pfam16046 283 QLQIKIRSLLKEVATLS 299
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
315-392 |
4.47e-03 |
|
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.
Pssm-ID: 439303 [Multi-domain] Cd Length: 325 Bit Score: 40.67 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 315 IMCMCISPLEETLATSTDRGQLYSITLTsaeMGKegeeayfefLSDSFH---SGIITGLSICIRKPLIATCSLDHSVRIW 391
Cdd:cd22857 226 IKAVAEDPDGHTVYVGDTSGDLASIDLR---TGK---------LLGCFKgkcGGSIRSIARHPELPLIASCGLDRYLRIW 293
|
.
gi 2064967944 392 N 392
Cdd:cd22857 294 D 294
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
573-648 |
4.61e-03 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 40.40 E-value: 4.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064967944 573 TAVALSHLGRVLFIGTSAGTVRalKYPLPIQNEWIEYQGHAAPITKMAVTFDDQFLLTVSEDNCLLIWKIIDKERH 648
Cdd:cd00200 13 TCVAFSPDGKLLATGSGDGTIK--VWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV 86
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
857-1094 |
4.89e-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: 40.56 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 857 LTEEKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKkeiqerdETIQDKEKRIYD 936
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLS-------ASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 937 LRKKNtELEKFKFVLDYKIK-------ELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQMELNIAELNLKLKATDK 1009
Cdd:pfam15905 134 LTRVN-ELLKAKFSEDGTQKkmsslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 1010 DRRREMQRVHDIEALVRRFKtdlhrCVSfiQEPKKLKDSIRQLYSCYVQKSDVVDIdgvdadIQKEYNRQREHLEKTVAS 1089
Cdd:pfam15905 213 EKIEEKSETEKLLEYITELS-----CVS--EQVEKYKLDIAQLEELLKEKNDEIES------LKQSLEEKEQELSKQIKD 279
|
....*
gi 2064967944 1090 LKKKL 1094
Cdd:pfam15905 280 LNEKC 284
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
890-988 |
5.21e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 890 METEKLKVELQKLHGVIKSLEKDILSLKKE----IQERDETIQDKEKriyDLRKKNTEL----EKFKFVLDyKIKELKKQ 961
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELA---ELEEELEALkarwEAEKELIE-EIQELKEE 479
|
90 100
....*....|....*....|....*..
gi 2064967944 962 IEPRENNIKEMREQIQKMEGELEQFQR 988
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAP 506
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
62-122 |
5.54e-03 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 40.27 E-value: 5.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064967944 62 ALALSPNRRYLAVSERGEkGTITVYDLQNDQIKKRKV---LSGGEIPvqefVCMAFSPDSKYLI 122
Cdd:COG2706 255 DIHISPDGRFLYVSNRGH-NSIAVFAIDADGGKLTLVghvPTGGKWP----RDFAIDPDGRFLL 313
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
62-121 |
6.11e-03 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 40.79 E-value: 6.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 62 ALALSPNRRYLAVSERgeKGTITVYDLQNDQIkkRKVLSGGE-IPVQEFvcmAFSPDSKYL 121
Cdd:COG4946 393 NPVWSPDGKKIAFTDN--RGRLWVVDLASGKV--RKVDTDGYgDGISDL---AWSPDSKWL 446
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
673-923 |
6.13e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 673 NQLMLELKTRVDElkmenEYQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKL--ELDHK--------ALMD 742
Cdd:PLN03229 461 NEMIEKLKKEIDL-----EYTEAVIAMGLQERLENLREEFSKANSQDQLMHPVLMEKIEKLkdEFNKRlsrapnylSLKY 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 743 --EMMEKHSKEQRDLESTNN-QKLMLEYEKYLELQMKSQHMQEDFE---RQLHSSEQSKTEALEEltlqyesKLQEKVRK 816
Cdd:PLN03229 536 klDMLNEFSRAKALSEKKSKaEKLKAEINKKFKEVMDRPEIKEKMEalkAEVASSGASSGDELDD-------DLKEKVEK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 817 LKecedksqqqKREYEEMIKIMEEdADREILDIRVKfeKMLTEEKETNVHLKDETGIMR----KKFSSLQREIDDKNMeT 892
Cdd:PLN03229 609 MK---------KEIELELAGVLKS-MGLEVIGVTKK--NKDTAEQTPPPNLQEKIESLNeeinKKIERVIRSSDLKSK-I 675
|
250 260 270
....*....|....*....|....*....|..
gi 2064967944 893 EKLKVELQKLHGVIKSLEKD-ILSLKKEIQER 923
Cdd:PLN03229 676 ELLKLEVAKASKTPDVTEKEkIEALEQQIKQK 707
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
64-127 |
6.21e-03 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 40.02 E-value: 6.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064967944 64 ALSPNRRYLAVSERgEKGTITVYDlqndqIKKRKVLsgGEIPVQ-EFVCMAFSPDSKYLIGQSGT 127
Cdd:TIGR03866 89 ALHPNGKILYIANE-DDALVTVID-----IETRKVL--AQIDVGvEPEGMAVSPDGKIVVNTSET 145
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
797-940 |
6.29e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 797 EALEELTLQYEsKLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADReildirvkFEKMLTE---EKETNvHLKDETGI 873
Cdd:COG1579 31 AELAELEDELA-ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--------YEEQLGNvrnNKEYE-ALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064967944 874 MRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKK 940
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
828-949 |
6.46e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 828 KREYEEMIKIMEEdADREILDIRVKFEKMLTE-------EKETNVHLKDETGIMRKKFSSLQREIDDKNMETEKLKVELQ 900
Cdd:smart00787 157 KEDYKLLMKELEL-LNSIKPKLRDRKDALEEElrqlkqlEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQ 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2064967944 901 KLHGVIKSLEKDILSLKKEIQERDETIqdKEKRIYDLRKKNTELEKFKF 949
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEIAEAEKKL--EQCRGFTFKEIEKLKEQLKL 282
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
791-1009 |
6.62e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 791 SEQSKTEALEELtLQYESKLQEKVRKLKE--------CEDKSQQQKREYEEMIKIMEEDADrEILD-IRVKFEKM--LTE 859
Cdd:PRK05771 37 KEELSNERLRKL-RSLLTKLSEALDKLRSylpklnplREEKKKVSVKSLEELIKDVEEELE-KIEKeIKELEEEIseLEN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 860 EKETNVHLKDETgimrKKFSSLqrEIDDKNMETEK-LKVELQKLHGVIKSLEKDILSLKKEIqerdETIQDKEKRIY--- 935
Cdd:PRK05771 115 EIKELEQEIERL----EPWGNF--DLDLSLLLGFKyVSVFVGTVPEDKLEELKLESDVENVE----YISTDKGYVYVvvv 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 936 ----DLRKKNTELEKF---KFVLDYK------IKELKKQIEPRENNIKEMREQIQKMEGELEQFQRRNTQ---MELNIAE 999
Cdd:PRK05771 185 vlkeLSDEVEEELKKLgfeRLELEEEgtpselIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEyleIELERAE 264
|
250
....*....|
gi 2064967944 1000 LNLKLKATDK 1009
Cdd:PRK05771 265 ALSKFLKTDK 274
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
669-1011 |
6.63e-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: 40.26 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 669 LEEKNQLMLELKTRVDELKMENEYQLRLRDmNYNEKLKELTEKfiqeIDSLKTknqVLKTEKEKLEldhkalmdEMMEKH 748
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDRE-QWERQRRELESR----VAELKE---ELRQSREKHE--------ELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 749 SKEQRDLESTNNQKLMLeyekyLELQMKSQHMQEDFERQLHSSEQSKTEALEELtlqyeSKLQEKVRKLKECEDKSQQQK 828
Cdd:pfam07888 104 KELSASSEELSEEKDAL-----LAQRAAHEARIRELEEDIKTLTQRVLERETEL-----ERMKERAKKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 829 REYEEMIKIMEEDADREILDIRVKfeKMLTEEKETNV-HLKDETGIMRKKFSSLQReiddKNMETEKLKVELQKLHGVIK 907
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQEL--RNSLAQRDTQVlQLQDTITTLTQKLTTAHR----KEAENEALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 908 SLEKDILSLKKEIQE----RDETIQDKEK----------RIYDLR-----------------KKNTELEKfkfvldYKIK 956
Cdd:pfam07888 248 ASERKVEGLGEELSSmaaqRDRTQAELHQarlqaaqltlQLADASlalregrarwaqeretlQQSAEADK------DRIE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 957 ELKKQIEPRENNIKEMREQIQKMEGELEQ------FQRRNTQMELNiaELNLKLKATDKDR 1011
Cdd:pfam07888 322 KLSAELQRLEERLQEERMEREKLEVELGRekdcnrVQLSESRRELQ--ELKASLRVAQKEK 380
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
674-1004 |
7.09e-03 |
|
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: 40.72 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 674 QLMLELKTR-VDELKMENEYQLRLRDMNYNEKLKELTEKFIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQ 752
Cdd:TIGR00618 550 QLTSERKQRaSLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 753 RDLESTNNQKLMLEYEKYLElQMKSQHMQEDFERQLHSSEQSKTEALE--ELTLQYESKLQEKVRKLKECEDKSQQQKRE 830
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALH-ALQLTLTQERVREHALSIRVLPKELLAsrQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 831 YEEmiKIMEEDADR-EILDIRVKFEKMLTEEKETNVHLKDEtgIMRKKFSSLQREIDDKNMETEKLKVELQKLHGvIKSL 909
Cdd:TIGR00618 709 LET--HIEEYDREFnEIENASSSLGSDLAAREDALNQSLKE--LMHQARTVLKARTEAHFNNNEEVTAALQTGAE-LSHL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 910 EKDILSLKKEIQERDETIQDKEKRIYDLRKKN---TELEKFKFVLDYkiKELKKQIEPRENNIKEMREQIQKMEGELEQF 986
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDediLNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLKYEECSKQL 861
|
330
....*....|....*...
gi 2064967944 987 QRRnTQMELNIAELNLKL 1004
Cdd:TIGR00618 862 AQL-TQEQAKIIQLSDKL 878
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
667-1011 |
7.48e-03 |
|
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: 40.54 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 667 SDLEEKnqlMLELKTRVDELKM-----ENEYQ---LRLRD--MNYNEKLKELTEKFIQeIDSLKTKNQVLKTEKEKLELD 736
Cdd:pfam01576 218 TDLQEQ---IAELQAQIAELRAqlakkEEELQaalARLEEetAQKNNALKKIRELEAQ-ISELQEDLESERAARNKAEKQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 737 HKALMDEMMEKHSKEQRDLESTNNQKlMLEYEKYLELQMKSQHMQED---FERQLHSSEQSKTEALEELTLQYEsklqeK 813
Cdd:pfam01576 294 RRDLGEELEALKTELEDTLDTTAAQQ-ELRSKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLE-----Q 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 814 VRKLKECEDKSQQQ-KREYEEMIKIME--EDADREILDIRVKFEKMLTEeketnvhlkdetgiMRKKFSSLQREIDDKNM 890
Cdd:pfam01576 368 AKRNKANLEKAKQAlESENAELQAELRtlQQAKQDSEHKRKKLEGQLQE--------------LQARLSESERQRAELAE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 891 ETEKLKVELQKLHGVIKSLE-------KDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKE------ 957
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEgkniklsKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEeeeakr 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2064967944 958 -LKKQIEPRENNIKEMREQIQKMEGELEQFQ--RRNTQMELNIAELNLKLKATDKDR 1011
Cdd:pfam01576 514 nVERQLSTLQAQLSDMKKKLEEDAGTLEALEegKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
896-1003 |
7.57e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 896 KVELQKLHGVIKSLEKDILSLKKEIQERDETIQDKEKRIYDLRKKNTELEKFKFVLDYKIKELKKQIE--------PREN 967
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVAtlgendfaLPSS 118
|
90 100 110
....*....|....*....|....*....|....*.
gi 2064967944 968 NIKEMREQIQKMegeLEQFQRRNTQMELNIAELNLK 1003
Cdd:pfam06008 119 DLSRMLAEAQRM---LGEIRSRDFGTQLQNAEAELK 151
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
831-984 |
7.73e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.66 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 831 YEEMIKIMEEDADR----EILDIRVKFEKMLTEEKETNVHLKDETGIMRKKFSSLQR--EIDDKNMET--EKLKVELQKL 902
Cdd:cd22656 93 YAEILELIDDLADAtddeELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENqtEKDQTALETleKALKDLLTDE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 903 HGVIKSleKDILSLKKEI-QERDETIQDKEKRIYDLRKKNTELE-----KFKFVLDYK-----IKELKKQIEPRENNIKE 971
Cdd:cd22656 173 GGAIAR--KEIKDLQKELeKLNEEYAAKLKAKIDELKALIADDEaklaaALRLIADLTaadtdLDNLLALIGPAIPALEK 250
|
170
....*....|...
gi 2064967944 972 MREQIQKMEGELE 984
Cdd:cd22656 251 LQGAWQAIATDLD 263
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
712-976 |
7.83e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 40.17 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 712 FIQEIDSLKTKNQVLKTEKEKLELDHKALMDEMMEKHSKEQRDLESTNNqklmLEYEKYLELQmksqHMQEDFERQLHSS 791
Cdd:COG5391 256 LSSFIENRKSVPTPLSLDLTSTTQELDMERKELNESTSKAIHNILSIFS----LFEKILIQLE----SEEESLTRLLESL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 792 ---EQSKTEALEELT----LQYESKLQEKVRK-------LKECEDKSQQQKREYEEMIKIMEE---DADREILDIRVKFE 854
Cdd:COG5391 328 nnlLLLVLNFSGVFAkrleQNQNSILNEGVVQaetlrssLKELLTQLQDEIKSRESLILTDSNlekLTDQNLEDVEELSR 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 855 KMLTEEKETNVhlKDETGIMRKKFSSLQREIDDKNMETEKLKVelqklhgvIKSLEKDILSLKKEIQERDETIQDKEKRI 934
Cdd:COG5391 408 SLRKNSSQRAV--VSQQPEGLTSFSKLSYKLRDFVQEKSRSKS--------IESLQQDKEKLEEQLAIAEKDAQEINEEL 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2064967944 935 YDlrkkntELEKFKFVLDYKIKELKKQ-----IEPRENNIK---EMREQI 976
Cdd:COG5391 478 KN------ELKFFFSVRNSDLEKILKSvadshIEWAEENLEiwkSVKEQL 521
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
658-980 |
7.91e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 658 YSEEILVTKSDLEE-KNQLmlELKTRVDELKMENEYQlrlrdmNYnEKLKELTEKF-IQEIDSLKTKNQVlktekeklel 735
Cdd:TIGR01612 777 EKDELNKYKSKISEiKNHY--NDQINIDNIKDEDAKQ------NY-DKSKEYIKTIsIKEDEIFKIINEM---------- 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 736 dhKALMDEMMEKHSKeQRDLESTNNQKLMLEYEKYLELQMK-----SQHMQEDFERQLHSSEQSKTEALEELTLQYES-- 808
Cdd:TIGR01612 838 --KFMKDDFLNKVDK-FINFENNCKEKIDSEHEQFAELTNKikaeiSDDKLNDYEKKFNDSKSLINEINKSIEEEYQNin 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 809 --------------------KLQEKVRKLKECEDKSQQQKREYEEMIKIMEEDADREILDIRVKFEKMLTE------EKE 862
Cdd:TIGR01612 915 tlkkvdeyikicentkesieKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDaslndyEAK 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 863 TNV------HLKDETGimRKKFSSLQREIDDKNMETEKLKVELQKLHGVIKSLE-------------------KDILSLK 917
Cdd:TIGR01612 995 NNElikyfnDLKANLG--KNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEiaihtsiyniideiekeigKNIELLN 1072
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 918 KEIQERDETI-----QDKEK-RIYDLR--------KKNTELEKFK-------FVLDYKIKELKKQIEPRENNIKEMREQI 976
Cdd:TIGR01612 1073 KEILEEAEINitnfnEIKEKlKHYNFDdfgkeeniKYADEINKIKddiknldQKIDHHIKALEEIKKKSENYIDEIKAQI 1152
|
....
gi 2064967944 977 QKME 980
Cdd:TIGR01612 1153 NDLE 1156
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
696-840 |
8.51e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 38.76 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 696 LRDMN-YNEKLKELTEKFIQEIDSLKTKNQVLKTEKEkleldHKALMDEMMEKHSKEQRDLEStnnqklMLEYEKYLELQ 774
Cdd:pfam06391 40 LREYNdYLEEVEDIVFNLTNGIDVEETEKKIEQYEKE-----NKDLILKNKMKLSQEEEELEE------LLELEKREKEE 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064967944 775 MKSQHMQEDfERQLHSSEQSKTEALEELTLQYE--SKLQEKVRKLKecEDKSQQQKREYEEMIKIMEE 840
Cdd:pfam06391 109 RRKEEKQEE-EEEKEKKEKAKQELIDELMTSNKdaEEIIAQHKKTA--KKRKSERRRKLEELNRVLEQ 173
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
855-985 |
9.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064967944 855 KMLTEEKEtnvhlkdETGIMRKKFSSLQREIDDKNMETEKLKVELQKLHgviKSLEKDILSLKkeiQERDETIQDKEKRI 934
Cdd:PRK00409 509 KLIGEDKE-------KLNELIASLEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQ---EEEDKLLEEAEKEA 575
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2064967944 935 YDLRKKNTElEKFKFVLDYKIKELKKQIEPRENNIKEMREQIQKMEGELEQ 985
Cdd:PRK00409 576 QQAIKEAKK-EADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK 625
|
|
| |
