|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
340-606 |
3.21e-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: 92.40 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 340 VLCLCFSPSEETLI-ASTNKnqlysiTMSLTEISKGEAAHFeyllYPLHSASITGLDTCIRKPLIATCSLDRSVRIWNYE 418
Cdd:cd00200 12 VTCVAFSPDGKLLAtGSGDG------TIKVWDLETGELLRT----LKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 419 SN-TLELYKEYQEEAYTVSLHPSGHYIVVGFADKlrlmNLLIDDIRPFK-EYSVRGCKE----CSFS-NGGHLFAAVNGN 491
Cdd:cd00200 82 TGeCVRTLTGHTSYVSSVAFSPDGRILSSSSRDK----TIKVWDVETGKcLTTLRGHTDwvnsVAFSpDGTFVASSSQDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 492 VIHIFTTTSLENINILKGHTGKIlreipafdviyTSITISHSGRMIFVGTSVGTIRamKYPLSLQKEYNEYQAHAGPVMK 571
Cdd:cd00200 158 TIKLWDLRTGKCVATLTGHTGEV-----------NSVAFSPDGEKLLSSSSDGTIK--LWDLSTGKCLGTLRGHENGVNS 224
|
250 260 270
....*....|....*....|....*....|....*
gi 568929692 572 MLLTFDDQFLLTVGEDGclfTWKVFDKDGRGIKRE 606
Cdd:cd00200 225 VAFSPDGYLLASGSEDG---TIRVWDLRTGECVQT 256
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
340-595 |
1.22e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 83.81 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 340 VLCLCFSPSEETLiASTNKNQlysiTMSLTEISKGEAAHfeylLYPLHSASITGLDTCIRKPLIATCSLDRSVRIWNYES 419
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLR----TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 420 NT-LELYKEYQEEAYTVSLHPSGHYIVVGFADK-LRLMNLLIDDIRPFKEYSVRGCKECSFS-NGGHLFAAVNGNVIHIF 496
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 497 TTTSLENINILKGHTGKIlreipafdviyTSITISHSGRMIFVGTSVGTIRAmkYPLSLQKEYNEYQAHAGPVMKMLLTF 576
Cdd:COG2319 316 DLATGKLLRTLTGHTGAV-----------RSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTLTGHTGAVTSVAFSP 382
|
250
....*....|....*....
gi 568929692 577 DDQFLLTVGEDGCLFTWKV 595
Cdd:COG2319 383 DGRTLASGSADGTVRLWDL 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
757-1094 |
1.36e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 757 EFYEAKLQEKTGLLEEA------QEDVRQQLREFEETKKQIEEDED--REI---------QDIKTKYERKLRDEKEsNLR 819
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilNELerqlkslerQAEKAERYKELKAELR-ELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 820 LkgetGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEK 899
Cdd:TIGR02168 227 L----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 900 FKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVR 979
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 980 RFKTDLHncvayiqepgLLKEKIRGLfEKYVQRADmVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYV 1059
Cdd:TIGR02168 383 TLRSKVA----------QLELQIASL-NNEIERLE-ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
330 340 350
....*....|....*....|....*....|....*
gi 568929692 1060 RIMQENVSLIKEINELRRELKLTRSQIYDLESALK 1094
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
624-965 |
9.62e-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: 82.81 E-value: 9.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 624 EKAQIMLELKTRVEELkmenEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELvDKQTR 703
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL-NKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 704 ELQDLECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTGLLEEAQEDVRQQLRE 783
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 784 FEEtkkqieededrEIQDIKTKYERKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQgiirsle 863
Cdd:TIGR02169 355 LTE-----------EYAELKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ------- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 864 kdiqglkREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQN 943
Cdd:TIGR02169 413 -------EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340
....*....|....*....|..
gi 568929692 944 TQLELNITELLQKLRATDQEMR 965
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVR 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
692-975 |
1.03e-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: 82.81 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 692 ERLEELVDKQTRELQDLECCNNQKllleyEKYQELQLKSQ-RMQEEYEKQLRDNDETKSQALEELTEFyEAKLQEKTGLL 770
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKA-----ERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASL-EEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 771 EEAQEDVRQQLREFEETKKQIE---EDEDREIQ----DIKTKYERKLRDEKESNLRLKGETGIMRKKFS---SLQKEIEE 840
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKdlgEEEQLRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 841 RTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQ-------DKEKRIYDLKKKNQELEKFKFVLDYKIKELKK 913
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 914 QIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLE 975
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
748-1094 |
1.99e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 748 KSQALEELTEFYEaKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNlRLKGETGIM 827
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYK 907
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 908 IKELKKQIEPRENEIKVMKEQIQ--------------EMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERD 973
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIEslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 974 LEALVRRFKTDLHNCVAYIQEpglLKEKIRGLFEK----YVQRADMVEIAGLNSDLQQEYARQRehlernLATLKKKVIK 1049
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEG---LEVRIDNLQERlseeYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568929692 1050 EGELhrtdyvrimqeNVSLIKEINELRRELKLTRSQIYDLESALK 1094
Cdd:TIGR02168 984 LGPV-----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
604-996 |
3.54e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 604 KREREVGFAEEvLVTKTDMEEKAQimlELKTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEK 683
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 684 EKQDISHRERLEELVD-KQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 762
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 763 LQEKTGLLEEAQEDVRQQLREFEETKKQIE-----EDEDREIQDIKTKYERKLRdeKESNLRlKGETGIMRKKFSSLQKE 837
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkaEEEKKKVEQLKKKEAEEKK--KAEELK-KAEEENKIKAAEEAKKA 1670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 838 IEERTNDIELLKSEQMKlqgiirslEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELEKFKFVLDYKIKELKKQiep 917
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDE--------KKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKE--- 1738
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929692 918 rENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEalVRRFKTDLHNCVAYIQEPG 996
Cdd:PTZ00121 1739 -AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIEGG 1814
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
668-966 |
1.64e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 668 EMESLKTKNQVLKTEKEKQdISHRERLEELVDKQTRELQDLEccnnqKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDET 747
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSL-QSELRRIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 748 KSQALEEltefYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIM 827
Cdd:TIGR02169 749 LEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYK 907
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929692 908 IKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQL------ELNITELLQKLRATDQEMRK 966
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRA 969
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
620-933 |
3.21e-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: 77.37 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 620 TDMEEKAQIMLELKTRVEELKMENEyQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKT-EKEKQDISHR-ERLEEL 697
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQ-SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKlQQEKELLEKEiERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 698 VDKQTRELQDLECCNNQKLLL-----EYEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTGLLEE 772
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIiknldNTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKELEE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 773 AQEDVRQQLREFEETKKQIEededREIQDIKTKYERKLRDEKESNLRLKGETgiMRKKFSSLQKEIEERTNDIELLKSEQ 852
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLE----SEKKEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 853 MKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEM 932
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
.
gi 568929692 933 E 933
Cdd:TIGR04523 665 I 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
792-1091 |
3.42e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.80 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 792 EEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKR 871
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 872 EIQERDETIQDKEKRIYDLKKKNQELEK-----FKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQL 946
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 947 ELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEpglLKEKIRGLFEkyvQRADMVEIAGLNSDLQ 1026
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD---LESRLGDLKK---ERDELEAQLRELERKI 905
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929692 1027 QEYARQREHLERNLATLK-KKVIKEGEL-HRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLES 1091
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKaKLEALEEELsEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
654-984 |
3.81e-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: 77.37 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 654 YTEKIKELTDkfiqEMESLKTKNQVLKTEKEKQDishrerlEELVDKQTrELQDleccNNQKLLLEYEKYQELQLKSQRM 733
Cdd:TIGR04523 209 KIQKNKSLES----QISELKKQNNQLKDNIEKKQ-------QEINEKTT-EISN----TQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 734 QEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDE------DREIQDIK---- 803
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisqlNEQISQLKkelt 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 804 -------------TKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLK 870
Cdd:TIGR04523 353 nsesensekqrelEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 871 REIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNI 950
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
330 340 350
....*....|....*....|....*....|....*...
gi 568929692 951 TELLQK---LRATDQEMRKEQ-QKERDLEALVRRFKTD 984
Cdd:TIGR04523 513 KDLTKKissLKEKIEKLESEKkEKESKISDLEDELNKD 550
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
721-1046 |
1.38e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 721 EKYQELQLKsqrmQEEYEKQLRdndetkSQALEELtefyEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEdedreiq 800
Cdd:COG1196 213 ERYRELKEE----LKELEAELL------LLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEE------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 801 diktkyerklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETI 880
Cdd:COG1196 272 --------------------------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 881 QDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRAT 960
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 961 DQEM-RKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLERN 1039
Cdd:COG1196 406 EEAEeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
....*..
gi 568929692 1040 LATLKKK 1046
Cdd:COG1196 486 LAEAAAR 492
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
631-1099 |
1.95e-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: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 631 ELKTRVEELKMENEYQLRLKD-MNYTEKIKELTDKFI-----------QEMESLKTKNQVLKTEKEKQDISHRERLEELV 698
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 699 DKQtrelQDLECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTGL 769
Cdd:TIGR04523 184 NIQ----KNIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 770 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYErKLRDEKESNL--RLKGETGIMRKKFSSLQKEIEERTND 844
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEIS-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQISQNNKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 845 IELLKSEqmklqgiIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKV 924
Cdd:TIGR04523 337 ISQLNEQ-------ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ-------EIKNLESQINDLESKIQN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 925 MKEQIQEMEAELERFHKQNTQLELNITELLQklratdqEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEpglLKEKIrg 1004
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKE-------TIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---LETQL-- 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1005 lfekyvqradmveiaglnSDLQQEYARQREHLERNLATLKKKVikegelhrtdyvrimqenvsliKEINELRRELKLTRS 1084
Cdd:TIGR04523 471 ------------------KVLSRSINKIKQNLEQKQKELKSKE----------------------KELKKLNEEKKELEE 510
|
490
....*....|....*
gi 568929692 1085 QIYDLESALKVSKKT 1099
Cdd:TIGR04523 511 KVKDLTKKISSLKEK 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
613-1080 |
4.06e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 613 EEVLVTKTDMEEKAQIMLELKTRVEELKmENEYQLRLKDMNYTEKIKELTDKfIQEMESLKTKNQVLKTEKE--KQDISH 690
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 691 RERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEA--KLQEKTG 768
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 769 --------LLEEAQEDV----RQQLREFEETKKQIEEDEdREIQDIKTKYERKLRDEKE--SNLRLKGETGIMRKKFSSL 834
Cdd:PRK03918 437 kcpvcgreLTEEHRKELleeyTAELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 835 QKE-IEERTNDIELLKSEQMKLQGIIRSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKknqELEKFKFVLDYKIKE 910
Cdd:PRK03918 516 NLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLK---ELEELGFESVEELEE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 911 LKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLElNITELLQKLRATDQEMRKEqqkerdLEALVRRFKtdlhncva 990
Cdd:PRK03918 593 RLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKE------LEELEKKYS-------- 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 991 yiqepgllKEKIRGLFEKYVQRADmvEIAGLNSDLqQEYARQREHLERNLATLK--KKVIKEGELHRTDYVRIMQENVSL 1068
Cdd:PRK03918 658 --------EEEYEELREEYLELSR--ELAGLRAEL-EELEKRREEIKKTLEKLKeeLEEREKAKKELEKLEKALERVEEL 726
|
490
....*....|..
gi 568929692 1069 IKEINELRRELK 1080
Cdd:PRK03918 727 REKVKKYKALLK 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
745-1102 |
6.78e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 745 DETKSQALEELTEfyeakLQEKTGLLEEAQEDVRQQLrefeetkkqieededreiqdiktkyeRKLRDEKESNLRlkget 824
Cdd:TIGR02169 169 DRKKEKALEELEE-----VEENIERLDLIIDEKRQQL--------------------------ERLRREREKAER----- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 825 gimrkkFSSLQKEIEERTNDIELLKSEQMKLQgiIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL-EKFKFV 903
Cdd:TIGR02169 213 ------YQALLKEKREYEGYELLKEKEALERQ--KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 904 LDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKT 983
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 984 DLHNCVAYIQEpglLKEKIRGLFEKYVQRADMVEiaglnsdlqqEYARQREHLERNLATL---KKKVIKEGELHRTDYVR 1060
Cdd:TIGR02169 365 ELEDLRAELEE---VDKEFAETRDELKDYREKLE----------KLKREINELKRELDRLqeeLQRLSEELADLNAAIAG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568929692 1061 IMQENVSLIKEINELRRELKLTRSQiydLESALKVSKKTRSQ 1102
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWK---LEQLAADLSKYEQE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
618-1151 |
7.73e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 618 TKTDMEEKAQIMLELKTRVEELKMENEYQLRLKDmnYTEKIKELtdkfiqEMESLKTKNQVLKTEKEKQDiSHRERLEEL 697
Cdd:TIGR02168 184 TRENLDRLEDILNELERQLKSLERQAEKAERYKE--LKAELREL------ELALLVLRLEELREELEELQ-EELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 698 VDKQTRELQDLEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKS--QALEELTEFYEAKLQEKTGLLEEAQE 775
Cdd:TIGR02168 255 LEELTAELQELE-----------EKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 776 DVRQQLREFEETKKQIEEDEDrEIQDIKTKYErklrDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKL 855
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEE-KLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 856 QGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKnqelekfkfvldykikELKKQIEPRENEIKVMKEQIQEMEAE 935
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----------------ELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 936 LERFHKQntqlelnITELLQKLRATDQEMRKEQQKERDLEALVRRFKtDLHNCVAYIQEP--------GLLKEKIRglFE 1007
Cdd:TIGR02168 463 LEELREE-------LEEAEQALDAAERELAQLQARLDSLERLQENLE-GFSEGVKALLKNqsglsgilGVLSELIS--VD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1008 KYVQRAdmVEIAgLNSDLQQEYARQREHLERNLATLKKK-----------VIKEGELHRTDYVRIMQEN------VSLIK 1070
Cdd:TIGR02168 533 EGYEAA--IEAA-LGGRLQAVVVENLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGNDREILKNIEgflgvaKDLVK 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1071 EINELRRELKLTRSQIY---DLESALKVSKKTRSQEvpeSVISKD--VVGSTSTMRLNEQEETGRIIEmQRLEIRRLRDQ 1145
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLvvdDLDNALELAKKLRPGY---RIVTLDgdLVRPGGVITGGSAKTNSSILE-RRREIEELEEK 685
|
....*.
gi 568929692 1146 IQEQEQ 1151
Cdd:TIGR02168 686 IEELEE 691
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
337-547 |
8.09e-13 |
|
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: 70.44 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 337 KQDVLCLCFSPSEETLIASTNKNqlysiTMSLTEISKGEAAHfeylLYPLHSASITGLDTCIRKPLIATCSLDRSVRIWN 416
Cdd:cd00200 93 TSYVSSVAFSPDGRILSSSSRDK-----TIKVWDVETGKCLT----TLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 417 YESNTL-ELYKEYQEEAYTVSLHPSGHYIVVGFADKlrlmNLLIDDIRPFKE-YSVRGCKE----CSFSNGGHLFAAVNG 490
Cdd:cd00200 164 LRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKClGTLRGHENgvnsVAFSPDGYLLASGSE 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 491 -NVIHIFTTTSLENINILKGHTGKIlreipafdviyTSITISHSGRMIFVGTSVGTIR 547
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSV-----------TSLAWSPDGKRLASGSADGTIR 286
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
640-1094 |
4.87e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 640 KMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKtkNQVLKTEKEKQDISHR-ERLEELVDKQTRELQDLEccnnqKLLL 718
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE--ELIKEKEKELEEVLREiNEISSELPELREELEKLE-----KEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 719 EYEKYQELQLKSQRMQEEYEKQLRdndetksqaleeltefyeaKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEdedre 798
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKR-------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE----- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 799 IQDIKTKYER--KLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTND---IELLKSEQMKLQGIIRSLEKDIQGLK-- 870
Cdd:PRK03918 288 LKEKAEEYIKlsEFYEEYLDELReIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYEea 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 871 REIQERDETIQDKEK--RIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEME----------AELER 938
Cdd:PRK03918 368 KAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 939 FHKQNTqlelnITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEkIRGLFEKyvqradmveI 1018
Cdd:PRK03918 448 EHRKEL-----LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEK---------L 512
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929692 1019 AGLNSDLQQEYARQREHLERNLATLKKKVIkegelhrtdyvRIMQEnvslIKEINELRRELKLTRSQIYDLESALK 1094
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIK-----------SLKKE----LEKLEELKKKLAELEKKLDELEEELA 573
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
618-987 |
6.76e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 618 TKTDMEEKAQIMLELKTRVEELKME-NEYQLRLKDMNyTEKIKELTDKFIQEMESLKTKNQVLKTE--KEKQDIShreRL 694
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisQNNKIIS---QL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 695 EELVDKQTRELQDLECCNNQKLLLEYEKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTGLLEEAQ 774
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 775 EDVRQQLREFEETKKQIEEDED------REIQDIKTKYER--KLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDI 845
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSeikdltNQDSVKELIIKNldNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 846 ELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKK---------KNQELEKFKFVLDYKIKELKKQI- 915
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQk 578
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 916 ------EPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHN 987
Cdd:TIGR04523 579 slkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
668-1161 |
7.32e-12 |
|
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: 69.77 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 668 EMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQDLEccnnqkllLEYEKYQELQLKSQRMQEEYEKQlrdndet 747
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLD--------RESDRNQELQKRIRLLEKREAEA------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 748 ksqaleeltefyEAKLQEKTglleeaqEDVRQQLREFEETKKQIEEDEDreiqdiktkyerKLRDEKESNLRLKGETgim 827
Cdd:pfam05557 68 ------------EEALREQA-------ELNRLKKKYLEALNKKLNEKES------------QLADAREVISCLKNEL--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 rkkfSSLQKEIEErtNDIELlkseqmklqgiiRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEkfkfVLDYK 907
Cdd:pfam05557 114 ----SELRRQIQR--AELEL------------QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLA----EAEQR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 908 IKELKKQIEPREN---EIKVMKE---QIQEMEAELERFHKQNTQLELNI------TELLQKLRATDQEMRKEQQKERDLE 975
Cdd:pfam05557 172 IKELEFEIQSQEQdseIVKNSKSelaRIPELEKELERLREHNKHLNENIenklllKEEVEDLKRKLEREEKYREEAATLE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 976 ALVRRFKTDLHNCVAYIQEPGL---LKEKIRGLFEKYVQR--ADMVEIAGLNSDLQQEYARQREhLERNLATLKKKVIKE 1050
Cdd:pfam05557 252 LEKEKLEQELQSWVKLAQDTGLnlrSPEDLSRRIEQLQQReiVLKEENSSLTSSARQLEKARRE-LEQELAQYLKKIEDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1051 G-ELHRTD-YVRIMQENVSLI-KEINELRRELKLTRSQIYDLESALKVSKKTRSQE---------VPESVISKDVVGSTS 1118
Cdd:pfam05557 331 NkKLKRHKaLVRRLQRRVLLLtKERDGYRAILESYDKELTMSNYSPQLLERIEEAEdmtqkmqahNEEMEAQLSVAEEEL 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929692 1119 T---------------MRLNEQ-----------EETGRIIEMQRLEIRRLRDQIQEQEQVPGFHTIAGV 1161
Cdd:pfam05557 411 GgykqqaqtlerelqaLRQQESladpsyskeevDSLRRKLETLELERQRLREQKNELEMELERRCLQGD 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
641-979 |
8.36e-12 |
|
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: 69.77 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 641 MENEYQLRLKDMNYTEKikELTDKFIQEMESLKTKNQvlKTEKEKQDISHRERLEELVDKQTRELQdleccnNQKLLLEY 720
Cdd:pfam17380 252 MTPEYTVRYNGQTMTEN--EFLNQLLHIVQHQKAVSE--RQQQEKFEKMEQERLRQEKEEKAREVE------RRRKLEEA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 721 EKYQELQLKSQ--------RMQEEYEKQL-RDNDETKSQALEELTEFYEAKLQEKTGLLEEAQ-------EDVRQQLrEF 784
Cdd:pfam17380 322 EKARQAEMDRQaaiyaeqeRMAMERERELeRIRQEERKRELERIRQEEIAMEISRMRELERLQmerqqknERVRQEL-EA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 785 EETKKQIEEDEDREIQDIKTKYErKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIELLKSEQMKLQGIIRSLEK 864
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEME-QIRAEQEEARQRE------------VRRLEEERAREMERVRLEEQERQQQVERLRQ 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 865 DIQGLKREIQERDETiQDKEKRIYDLKKK--NQELEKFKFVL---DYKIKELKKQIEPRENEIKvmkEQIQEMEAELERf 939
Cdd:pfam17380 468 QEEERKRKKLELEKE-KRDRKRAEEQRRKilEKELEERKQAMieeERKRKLLEKEMEERQKAIY---EEERRREAEEER- 542
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568929692 940 hkqNTQLELnitellQKLRATDQEMRKEQQKERDLEALVR 979
Cdd:pfam17380 543 ---RKQQEM------EERRRIQEQMRKATEERSRLEAMER 573
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
619-1151 |
3.47e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.07 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 619 KTDMEEKAQIMLELKTRVEELK--MENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDI------SH 690
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 691 RERLEELVDKQTRELQDLECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLL 770
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 771 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIELLKS 850
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 851 EQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVM--KEQ 928
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 929 IQEMEAELERFHKQNTQL-ELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDL-HNCVAYIQEPGLLKEKIRGLF 1006
Cdd:pfam02463 462 KDELELKKSEDLLKETQLvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1007 EKYVQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRImQENVSLIKEINELRRELKLTRSQI 1086
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929692 1087 YDLESALKVSKKTRSQEVPESVISKDVVGSTSTMRLNEQEETGRIIEMQRLEIRRLRDQIQEQEQ 1151
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-977 |
3.47e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 623 EEKAQIMLELKTRVEELKMENEyQLRLKDMNYTEKIKELTDKFiQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQT 702
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIE-ELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 703 RELQDLEccNNQKLLLEYEKYqelqlksqrmQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTGLLEEAQEDVRQQLR 782
Cdd:TIGR02168 744 QLEERIA--QLSKELTELEAE----------IEELEERLEEAEEELAEAEAEI-----EELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 783 EFEETKKQiEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSL 862
Cdd:TIGR02168 807 ELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 863 EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELekfkfvldykiKELKKQIEPRENEIKVMKEQIQEMEAELErfhkq 942
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEEL-----------REKLAQLELRLEGLEVRIDNLQERLSEEY----- 949
|
330 340 350
....*....|....*....|....*....|....*..
gi 568929692 943 ntQLELNITELLQKLRATDQEMRKEQQK--ERDLEAL 977
Cdd:TIGR02168 950 --SLTLEEAEALENKIEDDEEEARRRLKrlENKIKEL 984
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
630-1071 |
1.20e-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: 65.90 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 630 LELKTRVEELKME-NEYQLRLKDMNYTEKIKELtdkfiQEMESLKTKNQVlKTEKEKQDISHRERL---EELVDKQTREL 705
Cdd:pfam05483 361 LEELLRTEQQRLEkNEDQLKIITMELQKKSSEL-----EEMTKFKNNKEV-ELEELKKILAEDEKLldeKKQFEKIAEEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 706 QDLEccnnQKL--LLEYEKYQ----ELQLKSQRMQEE-YEKQLRD-NDETKSQALE--ELTEFYEAKLQEKTGLLEEAQe 775
Cdd:pfam05483 435 KGKE----QELifLLQAREKEihdlEIQLTAIKTSEEhYLKEVEDlKTELEKEKLKniELTAHCDKLLLENKELTQEAS- 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 776 DVRQQLREFEETKKQIEEDEDREIQDIKTkyerklRDEKESNLRlkGETGIMRKKFSSLQKEIEertndIELLKSEQ--M 853
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIEN------LEEKEMNLR--DELESVREEFIQKGDEVK-----CKLDKSEEnaR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 854 KLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNqelekfkfvldykiKELKKQIEPRENEIKVMKEQIQEME 933
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN--------------KALKKKGSAENKQLNAYEIKVNKLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 934 AELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDL--EALVRRFKTDLHnCVAYIQEPGLLKEKIRGLFEKYVQ 1011
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadEAVKLQKEIDKR-CQHKIAEMVALMEKHKHQYDKIIE 721
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929692 1012 RADmvEIAGLNSDLQQEYARQREHLERNLATLKKKVI---KEGELHRTDYVRI---MQENVSLIKE 1071
Cdd:pfam05483 722 ERD--SELGLYKNKEQEQSSAKAALEIELSNIKAELLslkKQLEIEKEEKEKLkmeAKENTAILKD 785
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
722-985 |
3.99e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 722 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTGLLEEAQEdvrqqLREFEETKKQieededrEIQD 801
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 802 IKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGL----------KR 871
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLedqnsklskeRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 872 EIQER-------------------------DETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMK 926
Cdd:pfam01576 156 LLEERiseftsnlaeeeekakslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929692 927 EQIQEMEAELE----RFH----------KQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDL 985
Cdd:pfam01576 236 AQLAKKEEELQaalaRLEeetaqknnalKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
791-1150 |
4.46e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 791 IEEDEDRE--------IQDIKTKYERKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIELLKSEQMKLQGIIRS 861
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 862 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEaELERFHK 941
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 942 QNTQLElnitELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEpglLKEKIRGLFEKYvqrADMVEIAGL 1021
Cdd:PRK03918 294 EYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE---LKKKLKELEKRL---EELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1022 NSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKTRs 1101
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG- 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568929692 1102 qevpesviskdvvgststmRLNEQEETGRIIEMQRLEIRRLRDQIQEQE 1150
Cdd:PRK03918 443 -------------------RELTEEHRKELLEEYTAELKRIEKELKEIE 472
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
612-1091 |
4.61e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 612 AEEVLvtkTDMEEKAQIMLELKTRVEELKMENEYQLRLKDmNYTEKIKELTDkfiqEMESLKTKNQVLKTEKEKQDIShR 691
Cdd:PRK02224 239 ADEVL---EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRE----RLEELEEERDDLLAEAGLDDAD-A 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 692 ERLEELVDKQTRELQDLEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTEfyEAKLQEKTglLE 771
Cdd:PRK02224 310 EAVEARREELEDRDEELR-----------DRLEECRVAAQAHNEEAESLREDADDLEERA-EELRE--EAAELESE--LE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 772 EAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYER--KLRDEKESNL-RLKGETGIMRKKFSSLQK------------ 836
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGNaeDFLEELREERdELREREAELEATLRTARErveeaealleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 837 ----------------EIEERTNDIELLKSEQMKLQGIIRSLEKDIqglkreiqERDETIQDKEKRIYDLKKKNQELEKf 900
Cdd:PRK02224 453 kcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEE- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 901 kfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQemRKEQQKERdLEALvRR 980
Cdd:PRK02224 524 ------LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKER-IESL-ER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 981 FKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVE-----IAGLNSDLQQ---EYARQ-REHLERNLATLKKKvIKEG 1051
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrerKRELEAEFDEariEEAREdKERAEEYLEQVEEK-LDEL 672
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 568929692 1052 ELHRTDYV-RI-MQENVslIKEINELRRELKLTRSQIYDLES 1091
Cdd:PRK02224 673 REERDDLQaEIgAVENE--LEELEELRERREALENRVEALEA 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-1079 |
4.90e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 603 IKREREVGFAEEVLVTKTDMEEKAQIMLELKtRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTE 682
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 683 KEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 762
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 763 LQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 842
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 843 NDIELLKSEQMKlqgiirslekdiQGLKREIQERDETIQDKEKRIYDlkkkNQELekfkfvldykIKELKKQIEPRENEI 922
Cdd:PTZ00121 1771 EEIRKEKEAVIE------------EELDEEDEKRRMEVDKKIKDIFD----NFAN----------IIEGGKEGNLVINDS 1824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 923 KVMkeqiqEMEAELERFHKQNTQLElNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNcvayIQEPGLLKEKI 1002
Cdd:PTZ00121 1825 KEM-----EDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE----IEEADEIEKID 1894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1003 RGLFEKYVQRADMveiAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELH------RTDYVRIMQENVSLIKEINELR 1076
Cdd:PTZ00121 1895 KDDIEREIPNNNM---AGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDmcindfSSKFCDYMKDNISSGNCSDEER 1971
|
...
gi 568929692 1077 REL 1079
Cdd:PTZ00121 1972 KEL 1974
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
627-1104 |
5.20e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 627 QIMLELKTRVEELKMENE--YQLRLKDMNYTEKIKELTDKFIQEMESLKT-KNQVLKTEKEKQD------ISHRERLEEL 697
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKClKEDMLEDSNTQIEqlrkmmLSHEGVLQEI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 698 --------------------------------VDKQTRELQ--------------------DLECCNNQKLLLEYEKYQE 725
Cdd:pfam15921 190 rsilvdfeeasgkkiyehdsmstmhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 726 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQEKTG 768
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEELEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 769 LLEEAQEDV---RQQLREFEETKKQIEEDEDREIQDIKtKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 845
Cdd:pfam15921 350 QLVLANSELteaRTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 846 EllkseqmKLQGIIRSLEKDIQGlkrEIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKEL---KKQIEPRENEI 922
Cdd:pfam15921 429 Q-------RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 923 KVMKEQIQEMEAELERFHKQNTQLELNITELLQKLratdQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQepgLLKEKI 1002
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1003 RGLFEKYVQR-----ADMVEIAGLNSDLQ------QEYARQREHLERNLATLKKKViKEGELHRTDYVRIMQENVSLIKE 1071
Cdd:pfam15921 572 ENMTQLVGQHgrtagAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEARV-SDLELEKVKLVNAGSERLRAVKD 650
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 568929692 1072 I----NELRRELKLTRSQIYDLESALKVSK---KTRSQEV 1104
Cdd:pfam15921 651 IkqerDQLLNEVKTSRNELNSLSEDYEVLKrnfRNKSEEM 690
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
727-979 |
6.93e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 727 QLKSQrMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTGLLEEAQEDVRQQLREFEETKKQIE--EDEDREIQDIKT 804
Cdd:PRK02224 191 QLKAQ-IEEKEEKDLHERLNGLESELAELDEEIE-RYEEQREQARETRDEADEVLEEHEERREELEtlEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 805 KYERKlRDEkesnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKE 884
Cdd:PRK02224 269 ETERE-REE------LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 885 K-------RIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEaelERFHKQNTQLElNITELLQKL 957
Cdd:PRK02224 342 EeaeslreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR---ERFGDAPVDLG-NAEDFLEEL 417
|
250 260
....*....|....*....|..
gi 568929692 958 RATDQEMRkeqQKERDLEALVR 979
Cdd:PRK02224 418 REERDELR---EREAELEATLR 436
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
657-1099 |
2.16e-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: 61.96 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 657 KIKELTDKFIQEMESLKTKNQVLK------TEKEKQDISHRERLEELvDKQTRELQDLECCNNQKL--LLEYEKYQELQL 728
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKnldknlNKDEEKINNSNNKIKIL-EQQIKDLNDKLKKNKDKInkLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 729 KSQRMQ--------EEYEKQLRDNDETKSQALEELTefyeaKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDED---R 797
Cdd:TIGR04523 113 KNDKEQknklevelNKLEKQKKENKKNIDKFLTEIK-----KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniqK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 798 EIQDIKTKYERKLRdeKESNLRLKGE-TGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQER 876
Cdd:TIGR04523 188 NIDKIKNKLLKLEL--LLSNLKKKIQkNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 877 DETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEprENEIKVMKEQIQEMEAELERFHKQNTQLELNITEL--- 953
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLneq 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 954 LQKLRATDQEMRKE-QQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIrglfekyvqradmveiaglnSDLQQEYARQ 1032
Cdd:TIGR04523 344 ISQLKKELTNSESEnSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI--------------------NDLESKIQNQ 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929692 1033 REhlernLATLKKKVIKEGElhrtdyvrimQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKT 1099
Cdd:TIGR04523 404 EK-----LNQQKDEQIKKLQ----------QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
828-985 |
3.05e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyK 907
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-------E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 908 IKELKKQIEP---------RENEIKV-----------------------MKEQIQEMEAELERFHKQNTQLELNITELLQ 955
Cdd:COG4942 99 LEAQKEELAEllralyrlgRQPPLALllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190
....*....|....*....|....*....|
gi 568929692 956 KLRATDQEMRKEQQKERDLEALVRRFKTDL 985
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
623-1093 |
3.20e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 623 EEKAQIMLELKTRVEElKMENEYQLRLKDMNytEKIKELTDKfIQEMESLKTKNQVLKTEKEKQDISHRERLEelvdkqt 702
Cdd:PRK02224 183 SDQRGSLDQLKAQIEE-KEEKDLHERLNGLE--SELAELDEE-IERYEEQREQARETRDEADEVLEEHEERRE------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 703 rELQDLECcnnqklllEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfyeakLQEKTGLLEEAQEDVRQQLR 782
Cdd:PRK02224 252 -ELETLEA--------EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 783 EFEETKKQIEEDEDREIQDIKTKYERKLRdEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSL 862
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 863 EK----------DIQGLKREIQE-RDETIQDKEKRIYDLKKKNQELEKFKFVLDY-KIKELKKQIE--PRENEIKVMKEQ 928
Cdd:PRK02224 397 RErfgdapvdlgNAEDFLEELREeRDELREREAELEATLRTARERVEEAEALLEAgKCPECGQPVEgsPHVETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 929 IQEMEAELERFHKQNTQLELNItELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKI------ 1002
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELeaeaee 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1003 -RGLFEKYVQRADMV--EIAGLNSDLqQEYARQREHLERNLATLKKKVIKEGELHRtdyvriMQENVSLIKEINELRRE- 1078
Cdd:PRK02224 556 kREAAAEAEEEAEEAreEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIER------LREKREALAELNDERREr 628
|
490
....*....|....*
gi 568929692 1079 LKLTRSQIYDLESAL 1093
Cdd:PRK02224 629 LAEKRERKRELEAEF 643
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
724-964 |
3.64e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 724 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 803
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 804 TKYERKLRdekesNLRLKGETGIMRKKFSSlqkeieertNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDK 883
Cdd:COG4942 104 EELAELLR-----ALYRLGRQPPLALLLSP---------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 884 EKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQE 963
Cdd:COG4942 170 EAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
.
gi 568929692 964 M 964
Cdd:COG4942 243 T 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1098 |
4.46e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 859 IRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELER 938
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 939 FHKQNTQLELNITELLQKL-RATDQEMRKEQQKERDLEALVRRFKTdlhncVAYIQEpgLLKEKIRGLfekyvqRADMVE 1017
Cdd:COG4942 95 LRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQY-----LKYLAP--ARREQAEEL------RADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1018 IAGLNSDLQQEYARQREhLERNLATLKKKVIKEGELHRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSK 1097
Cdd:COG4942 162 LAALRAELEAERAELEA-LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
.
gi 568929692 1098 K 1098
Cdd:COG4942 241 E 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1092 |
4.91e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 864 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERfhkqn 943
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK-------QLAALERRIAALARRIRALEQELAALEAELAE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 944 tqLELNITELLQKLratdqemrkEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGL-FEKYVQRADMVEIAGLN 1022
Cdd:COG4942 88 --LEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1023 SDlQQEYARQREHLERNLATLkKKVIKEGELHRTDYVRIMQENVSLIKeinELRRELKLTRSQIYDLESA 1092
Cdd:COG4942 157 AD-LAELAALRAELEAERAEL-EALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQE 221
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
613-977 |
5.49e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.52 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 613 EEVLVTKTDMEEKAQIMLELKTRVEElkmeNEYQLRLKDMNYTeKIKELTDKFIQEMESLKTKNQVLKT-----EKEKQD 687
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE----KERAIEATNAEIT-KLRSRVDLKLQELQHLKNEGDHLRNvqtecEALKLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 688 ISHRERLEELVDKQTRELQDLECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAklqE 765
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL---E 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 766 KTGLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERT 842
Cdd:pfam15921 634 KVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 843 NDIELLKSEQ-------MKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQI 915
Cdd:pfam15921 713 NTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 916 EPRENEIKVMKEQIQEMEAELERFHKQNTQLElnitELLQklRATDQEMRKEQQKERDLEAL 977
Cdd:pfam15921 793 EVLRSQERRLKEKVANMEVALDKASLQFAECQ----DIIQ--RQEQESVRLKLQHTLDVKEL 848
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
547-1151 |
6.33e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 547 RAMKYpLSLQKEYNEYQAHAgpvmkmLLTFDDQFLLTvgedgclftWKVFDKDGRGIKREREVgFAEEVLVTKTDMEEKA 626
Cdd:COG1196 211 KAERY-RELKEELKELEAEL------LLLKLRELEAE---------LEELEAELEELEAELEE-LEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 627 QIMLELKTRVEELKmENEYQLRLKDMNYTEKIKELTDKfIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQ 706
Cdd:COG1196 274 LELEELELELEEAQ-AEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 707 DLEccnnqkllleyekyqelqlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEktgllEEAQEDVRQQLREFEE 786
Cdd:COG1196 352 ELE-------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----LRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 787 TKKQIEEDEDREIQDIKTKYERKLRDEKESnlrlkgetgimrkkfSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDI 866
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEE---------------EEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 867 QGLKREIQERDETIQDKEKRIYDLKKKNQELEKFkfvlDYKIKELKKQIEPRE------NEIKVMKEQIQEMEAEL---- 936
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGF----LEGVKAALLLAGLRGlagavaVLIGVEAAYEAALEAALaaal 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 937 -ERFHKQNTQLELNITELLQKL--RATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYiqepgllkEKIRGLFEKYVQRA 1013
Cdd:COG1196 549 qNIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRARAALAAALARGAIGAAVDLVAS--------DLREADARYYVLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1014 DMVEIAGLNSDLQQEYARQREHLERNLATLKKkvIKEGELHRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESAL 1093
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLE--GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 1094 KVSKKTRSQEvpesviskdvvgsTSTMRLNEQEETGRIIEMQRLEIRRLRDQIQEQEQ 1151
Cdd:COG1196 699 LLAEEEEERE-------------LAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
631-994 |
6.34e-09 |
|
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: 59.97 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 631 ELKTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQD--L 708
Cdd:COG5185 150 EASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKeiI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 709 ECCNNQKLLLEYEKYQELqlkSQRMQEEYEKQLRDNDETKsqaleeltefyEAKLQEKTGLLEEAQEDVRQQLREFEETK 788
Cdd:COG5185 230 NIEEALKGFQDPESELED---LAQTSDKLEKLVEQNTDLR-----------LEKLGENAESSKRLNENANNLIKQFENTK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 789 KQIEEDEDREIQDIKTKYERKLRDEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIELLKSEQMKLQG 857
Cdd:COG5185 296 EKIAEYTKSIDIKKATESLEEQLAAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVELSKS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 858 I--IRSLEKDIQGLKREIQERDETIQDKEKRIydlkkkNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAE 935
Cdd:COG5185 376 SeeLDSFKDTIESTKESLDEIPQNQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929692 936 LER-FHKQNTQLELNITELLQKLRATDQEMRKEQQKER-DLEALVRRFKTDLHNCVAYIQE 994
Cdd:COG5185 450 LNKvMREADEESQSRLEEAYDEINRSVRSKKEDLNEELtQIESRVSTLKATLEKLRAKLER 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
828-1080 |
6.63e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKReIQERDETIQD---KEKRIYDLKKKNQELEKFkfvl 904
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDvasAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 905 DYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQ-------KERDLEAL 977
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleerfAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 978 VRRFKTDLHNCV-AYIQEPGLLKEKIRGLFEKYVQRADMvEIAGLNSDLQ--QEYAR-----QREHLERNLATLKKKVIK 1049
Cdd:COG4913 764 ERELRENLEERIdALRARLNRAEEELERAMRAFNREWPA-ETADLDADLEslPEYLAlldrlEEDGLPEYEERFKELLNE 842
|
250 260 270
....*....|....*....|....*....|..
gi 568929692 1050 EGELHRTDYVRIMQENVSLIKE-INELRRELK 1080
Cdd:COG4913 843 NSIEFVADLLSKLRRAIREIKErIDPLNDSLK 874
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
605-937 |
1.14e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 605 REREVGFAE-EVLVTKTDMEEKAQIMLELKTRVEELKMENEYQLRLKDMNYTEKiKELTDkfiqemeslKTKNQVLKTEK 683
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN-KELTQ---------EASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 684 EKQDISHRERLEELVDKQTRELQDLEccNNQKLLLEY------EKYQELQLKSQRMQE-----EYE-------------- 738
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKE--MNLRDELESvreefiQKGDEVKCKLDKSEEnarsiEYEvlkkekqmkilenk 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 739 -KQLRDNDETKSQALEELTEfyEAKLQEKTGLLEEAQEDVrqqlREFEETKKQIE-EDEDREIQDIKTKYERKLRDEKES 816
Cdd:pfam05483 596 cNNLKKQIENKNKNIEELHQ--ENKALKKKGSAENKQLNA----YEIKVNKLELElASAKQKFEEIIDNYQKEIEDKKIS 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 817 NLRLKGE---TGIMRKKFSSLQKEIEERTndiellkseQMKLQGIIRSLEKDIQGLKREIQERDEtiqdkEKRIYdlKKK 893
Cdd:pfam05483 670 EEKLLEEvekAKAIADEAVKLQKEIDKRC---------QHKIAEMVALMEKHKHQYDKIIEERDS-----ELGLY--KNK 733
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568929692 894 NQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELE 937
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
604-949 |
1.48e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 604 KREREVgfAEEVLVTKTDMEEKAQIMLELKTRVEELK------------MENEYQLRLKDmNYTEKIKELtDKFIQEMES 671
Cdd:PRK03918 398 KAKEEI--EEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLE-EYTAELKRI-EKELKEIEE 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 672 LKTKNQVLKTEKEKQDISHRE--RLEELVDkQTRELQD-LECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDndetk 748
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESEliKLKELAE-QLKELEEkLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE----- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 749 sqaLEELTEFyEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYER--KLRDEKESNLRLKGETGI 826
Cdd:PRK03918 548 ---LEKLEEL-KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 827 MRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRslEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfVLDy 906
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKK---TLE- 697
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568929692 907 KIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELN 949
Cdd:PRK03918 698 KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
619-973 |
1.58e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 619 KTDMEEKAQIMLELKTRVEElkmeNEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQvLKTEKEKQDishrERLEELV 698
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEIND----KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ-LEEKTKLQD----ENLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 699 DKQ---TRELQDLECCNNQKLLLEYEKYQELQLKSQ---RMQEEYEKQLRDNDETKSQALEELTEFyeaklQEKTGLLEE 772
Cdd:pfam05483 289 EKKdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKticQLTEEKEAQMEELNKAKAAHSFVVTEF-----EATTCSLEE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 773 AQEDVRQQLREFEETKKQIEededREIQDIKTKYER--KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTndiELLKS 850
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIIT----MELQKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA---EELKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 851 EQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKK-------KNQELEKFKFVLDYKIKELKKQIEPRENEIK 923
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTelekeklKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568929692 924 VMKEQIQEMEAELERFHKQNTQLELNITELLQKLratdQEMRKEQQKERD 973
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL----ESVREEFIQKGD 562
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
645-1149 |
1.74e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 645 YQLRLKDMNY--TEKIKELTDKFIQEMESLKtKNQVLKTEKEKQDISHRERLEELVDKQTRELQDLECCNnqkllleyek 722
Cdd:pfam05483 61 YQEGLKDSDFenSEGLSRLYSKLYKEAEKIK-KWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN---------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 723 yQELQLKSQRMQEEYEKQLRDNDETKSqaLEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEET-KKQIEEDEDREIQD 801
Cdd:pfam05483 130 -EKVSLKLEEEIQENKDLIKENNATRH--LCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNiEKMILAFEELRVQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 802 IKTKYER--KLRDEKESNLRLKGEtgimrkkfssLQKEIEERTNDIELL------KSEQMK-LQGIIRSLEKDIQGLKRE 872
Cdd:pfam05483 207 ENARLEMhfKLKEDHEKIQHLEEE----------YKKEINDKEKQVSLLliqiteKENKMKdLTFLLEESRDKANQLEEK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 873 IQERDETIQDKEKRIYDLKKknqELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITE 952
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLTK---ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 953 LLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKirglfeKYVQRADMVEIAGLNSDLQQEyARQ 1032
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN------KEVELEELKKILAEDEKLLDE-KKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1033 REHLERNLATLKKKVI-----KEGELH--RTDYVRIMQENVSLIKEINELRREL---KLTRSQIYDLESALKVSKKTRSQ 1102
Cdd:pfam05483 427 FEKIAEELKGKEQELIfllqaREKEIHdlEIQLTAIKTSEEHYLKEVEDLKTELekeKLKNIELTAHCDKLLLENKELTQ 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568929692 1103 EVPESVI-----SKDVVGSTST-MRLNEQEETGRIIEMQ-RLEIRRLRDQIQEQ 1149
Cdd:pfam05483 507 EASDMTLelkkhQEDIINCKKQeERMLKQIENLEEKEMNlRDELESVREEFIQK 560
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
775-1150 |
2.46e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 775 EDVRQQLRE-FEETKKQIEEDEDREIQDIKTKYERKLRD------EKESNLRLKGETgimRKKFSSLQKEIEERTNDIEL 847
Cdd:PRK02224 179 ERVLSDQRGsLDQLKAQIEEKEEKDLHERLNGLESELAEldeeieRYEEQREQARET---RDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 848 LKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKnQELEkfkfvlDYKIKELKKQIEPRENEIKVMKE 927
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLD------DADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 928 QIQEMEAELERFHKQNTQLELNITELlqklratDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEpglLKEKIRGLFE 1007
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEE---LEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1008 KY----VQRAdmvEIAGLNSDLQQEYARQREHLERNLATLK--KKVIKEGElhrtdyvRIMQE--------------NVS 1067
Cdd:PRK02224 399 RFgdapVDLG---NAEDFLEELREERDELREREAELEATLRtaRERVEEAE-------ALLEAgkcpecgqpvegspHVE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1068 LIKE----INELRRELKLTRSQIYDLESALKVSKKTRSQEvpESVISKDVVGSTSTMRLNEQEETgriIEMQRLEIRRLR 1143
Cdd:PRK02224 469 TIEEdrerVEELEAELEDLEEEVEEVEERLERAEDLVEAE--DRIERLEERREDLEELIAERRET---IEEKRERAEELR 543
|
....*..
gi 568929692 1144 DQIQEQE 1150
Cdd:PRK02224 544 ERAAELE 550
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
640-1042 |
2.60e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.52 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 640 KMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQDLEccNNQKLL-- 717
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE--EQETLLgt 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 718 -LEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEF-YEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEeDE 795
Cdd:TIGR00606 777 iMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ-DQ 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 796 DREIQDIKTKYErKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQgiiRSLEKDIQGLKREIQE 875
Cdd:TIGR00606 856 QEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE---TFLEKDQQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 876 RDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELK-KQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITEll 954
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT-- 1009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 955 QKLRatdQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKirglfEKYVQRADMVEIAGLNSDL----QQEYA 1030
Cdd:TIGR00606 1010 QKIQ---ERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMK-----QEHQKLEENIDLIKRNHVLalgrQKGYE 1081
|
410
....*....|..
gi 568929692 1031 RQREHLERNLAT 1042
Cdd:TIGR00606 1082 KEIKHFKKELRE 1093
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
725-976 |
2.90e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.84 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 725 ELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIKT 804
Cdd:COG1340 12 ELEEKIEELREEIE-ELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 805 KYE--RKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTndieLLKSEQMKLQGIIRSLEKDIQGLKREIQERDEtIQD 882
Cdd:COG1340 90 LREelDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV----LSPEEEKELVEKIKELEKELEKAKKALEKNEK-LKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 883 KEKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQ 962
Cdd:COG1340 165 LRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250
....*....|....
gi 568929692 963 EMRKEQQKERDLEA 976
Cdd:COG1340 238 ELRELRKELKKLRK 251
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
717-970 |
3.05e-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: 56.74 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 717 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTGLLEEAQEdVRQQLREF-- 784
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 785 -----------EETKKQIE-------------EDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 840
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 841 RTNDIELLKSEQMKLQGIIRSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELEKFKFVLDYKIKELKKQIEPREN 920
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568929692 921 EIKVMKEQIQEMEAEL-ERFHKQNTQLElnitELLQKLRATDQEMRKEQQK 970
Cdd:pfam15905 283 KCKLLESEKEELLREYeEKEQTLNAELE----ELKEKLTLEEQEHQKLQQK 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
744-918 |
6.53e-08 |
|
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: 54.93 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 744 NDETKSQALEELTEfYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYERKLRDEKESNLRLKGE 823
Cdd:COG1579 1 AMPEDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 824 TGIMR-----KKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRiydLKKKNQELE 898
Cdd:COG1579 79 EEQLGnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELE 155
|
170 180
....*....|....*....|
gi 568929692 899 KFKFVLDYKIKELKKQIEPR 918
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
664-1104 |
7.71e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 664 KFIQEM--ESLKTKNQVLKTEKEKQDISHRERLEELvDKQTRELQDleccnnqklllEYEKYQELQLKSQRMQEEYE--K 739
Cdd:COG4717 41 AFIRAMllERLEKEADELFKPQGRKPELNLKELKEL-EEELKEAEE-----------KEEEYAELQEELEELEEELEelE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 740 QLRDNDETKSQALEELTEFY---------EAKLQEKTGLLEEAQE------DVRQQLREFEETKKQIEEDEDREIQDIKT 804
Cdd:COG4717 109 AELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEErleelrELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 805 KYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQ-------------------------GII 859
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallglgGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 860 RSLEKDIQGL-------------------KREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEpREN 920
Cdd:COG4717 269 LSLILTIAGVlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 921 EIKVMKEQIQEMEAELERfhkqnTQLELNITELLQKLRATDQEM-RKEQQKERDLEALVRRFKTdlhncvayiqepglLK 999
Cdd:COG4717 348 ELQELLREAEELEEELQL-----EELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEE--------------LE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1000 EKIRGLFEKYVQRADMVEIAGLNSDLQQ------EYARQREHLERNLATLKKKvIKEGElHRTDYVRIMQENVSLIKEIN 1073
Cdd:COG4717 409 EQLEELLGELEELLEALDEEELEEELEEleeeleELEEELEELREELAELEAE-LEQLE-EDGELAELLQELEELKAELR 486
|
490 500 510
....*....|....*....|....*....|.
gi 568929692 1074 ELRRELKLTRSQIYDLESALKVSKKTRSQEV 1104
Cdd:COG4717 487 ELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
604-1101 |
7.98e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 604 KREREVGFAEEVL--VTKTDMEEKAQIMLELKTRVEELKME--------NEYQLRLKDMNYTE-KIKELTDKFIQEMESL 672
Cdd:TIGR02169 262 ELEKRLEEIEQLLeeLNKKIKDLGEEEQLRVKEKIGELEAEiaslersiAEKERELEDAEERLaKLEAEIDKLLAEIEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 673 KTKNQVLKTEKEKQDISHRERLEELVDKQtRELQDLECcNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAL 752
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLR-AELEEVDK-EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 753 EELTEFY------EAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEeDEDREIQDIKTKY---ERKLR------DEKESN 817
Cdd:TIGR02169 420 EELADLNaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLS-KYEQELYDLKEEYdrvEKELSklqrelAEAEAQ 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 818 LRLKGETGIMRKKFSSLQKE--------------IEER------------------TND------IELLKSEQM------ 853
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKAsiqgvhgtvaqlgsVGERyataievaagnrlnnvvvEDDavakeaIELLKRRKAgratfl 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 854 -------------------------------------------------------KLQGIIR--SLEKDI---------- 866
Cdd:TIGR02169 579 plnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarRLMGKYRmvTLEGELfeksgamtgg 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 867 -----------QGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIkvmkeqiQEMEAE 935
Cdd:TIGR02169 659 sraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-------EQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 936 LERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVA-----YIQEPGLLKEKIRGLFEKYV 1010
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1011 QRADMVEIAGLNSDLQQEYARQ-REHLERNLATLKKKvIKEgelhrtdyvrIMQENVSLIKEINELRRELKLTRSQIYDL 1089
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQ-IKS----------IEKEIENLNGKKEELEEELEELEAALRDL 880
|
650
....*....|..
gi 568929692 1090 ESALKVSKKTRS 1101
Cdd:TIGR02169 881 ESRLGDLKKERD 892
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
749-980 |
8.71e-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: 55.93 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 749 SQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIktkyERKLRDekesnlrLKGETGIMR 828
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAAL----ARRIRA-------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 829 KKFSSLQKEIEERTNDIELLKSEqmkLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKI 908
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 909 KELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRR 980
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
627-1150 |
1.15e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 627 QIMLELKTRVEELKMENEYQLRLKDMNYTEKI------KELTDKFIqEMESLKTKNQVLKTEKEKQdishRERLEELVDK 700
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSItidhlrRELDDRNM-EVQRLEALLKAMKSECQGQ----MERQMAAIQG 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 701 QTRELQDLeccnnQKLLLEYEKYQEL------QLKSQRMQ-EEYEKQLRD---NDETKSQALE----ELTEF---YEAKL 763
Cdd:pfam15921 456 KNESLEKV-----SSLTAQLESTKEMlrkvveELTAKKMTlESSERTVSDltaSLQEKERAIEatnaEITKLrsrVDLKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 764 QEKTGLLEEaQEDVRQQLREFEETKKQIEEdEDREIQDIKTKYE------------------RKLRDEKESN---LRLKg 822
Cdd:pfam15921 531 QELQHLKNE-GDHLRNVQTECEALKLQMAE-KDKVIEILRQQIEnmtqlvgqhgrtagamqvEKAQLEKEINdrrLELQ- 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 823 ETGIMRKKFSSLQKEIEERTNDIELLK-------SEQMKLQGIIR------------------SLEKDIQGLKREIQERD 877
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKqerdqllnevktsrnelnSLSEDYEVLKRNFRNKS 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 878 ETIQDKEKRI-YDLKKKNQELEKFKFVLD-------YKIK---ELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQL 946
Cdd:pfam15921 688 EEMETTTNKLkMQLKSAQSELEQTRNTLKsmegsdgHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFL 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 947 ELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLlkekirglfeKYVQRADMVEiaglnsdlQ 1026
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL----------QFAECQDIIQ--------R 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1027 QEYARQREHLERNL-------------ATLKKKVIKEGELHRT-DYVRIMQENVSLIKeiNELRRELKLTRSQIYDLESA 1092
Cdd:pfam15921 830 QEQESVRLKLQHTLdvkelqgpgytsnSSMKPRLLQPASFTRThSNVPSSQSTASFLS--HHSRKTNALKEDPTRDLKQL 907
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 1093 LkvskktrsQEVpesvisKDVVGSTSTMRLNEQEETGRIIEMQRLEiRRLRDQIQEQE 1150
Cdd:pfam15921 908 L--------QEL------RSVINEEPTVQLSKAEDKGRAPSLGALD-DRVRDCIIESS 950
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
601-901 |
1.29e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 601 RGIKREREVGFAEEVlvTKTDMEEKAQIMLELktrvEELKMENEYQLrlkdmnytEKIKELTDKfiQEMESLKTKNQVLK 680
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQEERK--RELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 681 TEKekqdISHRERLE-ELVDKQTRELQDLECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFY 759
Cdd:pfam17380 374 ISR----MRELERLQmERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 760 EAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKfSSLQKEIE 839
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR-KLLEKEME 523
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 840 ERTNDIelLKSEQMKLQGIIRSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELEKFK 901
Cdd:pfam17380 524 ERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
770-913 |
1.42e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 55.63 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 770 LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIELLK 849
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---RLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929692 850 SEQmklqgiIRSLEKDiqglkREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyKIKELKK 913
Cdd:COG2433 455 SEE------RREIRKD-----REISRLDREIERLERELEEERERIEELKR-------KLERLKE 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
741-983 |
1.53e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 741 LRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQedvrQQLREFEETKKQIEededreiqdiktkyerklrdekesnlrL 820
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVD---------------------------L 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 821 KGETGIMRKKFSSLQKEIEErtndielLKSEQMKLQGIIRSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQELE 898
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 899 KfKFVLDY-KIKELKKQIEPRENEIKVMKEQI-QEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEA 976
Cdd:COG3206 284 A-RYTPNHpDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
....*..
gi 568929692 977 LVRRFKT 983
Cdd:COG3206 363 ARELYES 369
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
621-921 |
1.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 621 DMEEKAQIMLELKTRVEELKMENE-YQLRLKDMNytEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVD 699
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIEnVKSELKELE--ARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 700 KQTRELQDLEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQ--ALEELTEFYEAKLQEKTGLLEEAQEDV 777
Cdd:TIGR02169 809 RIEARLREIE-----------QKLNRLTLEKEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELEEELEELEAAL 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 778 RQQLREFEETKKQIEEDED--REIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQmKL 855
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAqlRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DV 956
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 856 QGIIRSLEKDIQGLK----REIQERDETiqdkEKRIYDLKKKNQELEKFKfvldykiKELKKQIEPRENE 921
Cdd:TIGR02169 957 QAELQRVEEEIRALEpvnmLAIQEYEEV----LKRLDELKEKRAKLEEER-------KAILERIEEYEKK 1015
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
620-1151 |
1.79e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 620 TDMEEKAQIMLELKTRVEELKM----ENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDIS------ 689
Cdd:TIGR00618 216 TYHERKQVLEKELKHLREALQQtqqsHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaapl 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 690 --HRERLEELVDKQTRELQDLECCNNqKLLLEYEKYQELQLKSQRMQEEY--EKQLRDNDETKSQALEELTEFYEAKLQE 765
Cdd:TIGR00618 296 aaHIKAVTQIEQQAQRIHTELQSKMR-SRAKLLMKRAAHVKQQSSIEEQRrlLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 766 KTGLLE-EAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKlRDEKESNLRLKGETGIMRKKFSSLQKEIEERTND 844
Cdd:TIGR00618 375 HTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 845 IELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKF--------------------VL 904
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdidnpgpltrrmqRG 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 905 DYKIKELKKQIEPRE-------NEIKVMKEQIQEMEAELERFhkqnTQLELNITELLQKLRATDQEMRKEQQKERDLEal 977
Cdd:TIGR00618 534 EQTYAQLETSEEDVYhqltserKQRASLKEQMQEIQQSFSIL----TQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE-- 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 978 vrrfktdlhncvayIQEPGLLKEKIRGLFEKyvqrADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTD 1057
Cdd:TIGR00618 608 --------------DMLACEQHALLRKLQPE----QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1058 yvrimQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKTRSQEVPESVISKDV-----VGSTSTMRLNEQEETGR-- 1130
Cdd:TIGR00618 670 -----LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFneienASSSLGSDLAAREDALNqs 744
|
570 580
....*....|....*....|.
gi 568929692 1131 IIEMQRLEIRRLRDQIQEQEQ 1151
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFN 765
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
619-1014 |
1.90e-07 |
|
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: 55.60 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 619 KTDMEEKAQIMLELKTRVEELKMENEyqlrlKDMNYTEKIKEltdkfiqemeSLKTKNQ---VLKTEKEkqdiSHRERLE 695
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS-----DCKQHIEVLKE----------SLTAKEQraaILQTEVD----ALRLRLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 696 E---LVDKQTRELQDLeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFY 759
Cdd:pfam10174 356 EkesFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERV 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 760 EAkLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyERKLRDEKESnlrLKGETGIMRKKFSSLQKEIE 839
Cdd:pfam10174 425 KS-LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELT 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 840 ERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIydlkKKNQELEkfkfvLDYKIK-ELKKQIEPR 918
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL----KKAHNAE-----EAVRTNpEINDRIRLL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 919 ENEIKVMKEQIQEMEAELERfhkqntqlelniteLLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQE-PGL 997
Cdd:pfam10174 564 EQEVARYKEESGKAQAEVER--------------LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHgQQE 629
|
410
....*....|....*..
gi 568929692 998 LKEKIRGLFEKYVQRAD 1014
Cdd:pfam10174 630 MKKKGAQLLEEARRRED 646
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
385-597 |
3.24e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 54.15 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 385 PLHSASITGLDTCIRKPLIATCSLDRSVRIWNYESN-TLELYKEYQEEAYTVSLHPSGHYIVVGFADKlrlmnlliddir 463
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADG------------ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 464 pfkeysvrgckecsfsngghlfaavngnVIHIFTTTSLENINILKGHTGKIlreipafdviyTSITISHSGRMIFVGTSV 543
Cdd:COG2319 143 ----------------------------TVRLWDLATGKLLRTLTGHSGAV-----------TSVAFSPDGKLLASGSDD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568929692 544 GTIRAmkYPLSLQKEYNEYQAHAGPVMKMLLTFDDQFLLTVGEDGclfTWKVFD 597
Cdd:COG2319 184 GTVRL--WDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADG---TVRLWD 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
604-1086 |
4.63e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 604 KREREVGFAEEVLVTKTDMEEKAQIMLELKTRVEELKMENEyQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEK 683
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 684 EKQD------ISHRERLEELVDKQTRELQDLEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTE 757
Cdd:COG1196 365 EALLeaeaelAEAEEELEELAEELLEALRAAA--ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 758 FYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKE 837
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 838 IE--------ERTNDIELLKSEQMKLQGIIRSLEKD----IQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLD 905
Cdd:COG1196 523 AGavavligvEAAYEAALEAALAAALQNIVVEDDEVaaaaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 906 YKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRfktdl 985
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA----- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 986 hncvayIQEPGLLKEKIRGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQEN 1065
Cdd:COG1196 678 ------EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500
....*....|....*....|....*
gi 568929692 1066 VSLIKE----INELRRELKLTRSQI 1086
Cdd:COG1196 752 ALEELPeppdLEELERELERLEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1152 |
5.40e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 606 EREVGFAEEVLVTKTDMEEKAQIMLELKTRVEELKMENEYQlRLKDMNYTEKIKELTDKFIQEM----------ESLKTK 675
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 676 NQVLKTEKEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 750
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 751 ALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYERKlrdEKESNLRLKGETGim 827
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELEkfkfvldyK 907
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEKK--------K 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 908 IKELKKQIEprenEIKVMKEQIQEMEAELERFHKQNTQLElnitellQKLRATDQEMRKEQQKERDLEALVRRFKTDLHN 987
Cdd:PTZ00121 1393 ADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAE-------EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 988 CVAYIQEPGLLKEKIRGLFEKyvQRADMVEIAGLNSDLQQEYARQREHLERNLATLKK--KVIKEGELHRTDYVRIMQE- 1064
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEa 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1065 -NVSLIKEINELRRELKLTRSqiydlESALKVSKKTRSQEVPESVISK-------DVVGSTSTMRLNEQEETGRIIEMQR 1136
Cdd:PTZ00121 1540 kKAEEKKKADELKKAEELKKA-----EEKKKAEEAKKAEEDKNMALRKaeeakkaEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
570
....*....|....*..
gi 568929692 1137 LEIRRLR-DQIQEQEQV 1152
Cdd:PTZ00121 1615 AEEAKIKaEELKKAEEE 1631
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
828-983 |
6.11e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTnDIELLKSEQMK---LQGIIRSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELEK 899
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 900 FKFVLDYKIKELKKQIEPRENEIKVMKeqiQEMEAELERfHKQNTQLElNITELLQKlratdqEMRKEQQKERDLEALVR 979
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEAR---SEERREIRK-DREISRLD-REIERLER------ELEEERERIEELKRKLE 496
|
....
gi 568929692 980 RFKT 983
Cdd:COG2433 497 RLKE 500
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
653-1057 |
6.12e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.93 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 653 NYTEKIKELTDKFIQEMESLKTKNQVLKT----EKEKQDISHRERLEEL-VDKQTRELqdLECCNNqkllLEYEKYQELQ 727
Cdd:COG5022 758 RYLRRRYLQALKRIKKIQVIQHGFRLRRLvdyeLKWRLFIKLQPLLSLLgSRKEYRSY--LACIIK----LQKTIKREKK 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 728 LKSqrmqeeyekqlRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEE--DEDREIQDIKTK 805
Cdd:COG5022 832 LRE-----------TEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkIDVKSISSLKLV 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 806 YER------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDET 879
Cdd:COG5022 901 NLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDL 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 880 IQDKEKRIYDLKKKNQELEKFKfvldykiKELkkqiepreNEIKVMKEQIQEMEAELERFHKQNTQLElNITELLQKLRA 959
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFK-------KEL--------AELSKQYGALQESTKQLKELPVEVAELQ-SASKIISSEST 1040
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 960 TDQEMRKEQQKERDLEALVRRFKTDLHNcVAYIQEPGLLKEKirglfEKYVQRADMVEIAGLNSDLQQEYARQREHLERN 1039
Cdd:COG5022 1041 ELSILKPLQKLKGLLLLENNQLQARYKA-LKLRRENSLLDDK-----QLYQLESTENLLKTINVKDLEVTNRNLVKPANV 1114
|
410
....*....|....*...
gi 568929692 1040 LATLKKKVIKEGELHRTD 1057
Cdd:COG5022 1115 LQFIVAQMIKLNLLQEIS 1132
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
835-938 |
6.92e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 835 QKEIEERTNDIEL-LKSEQMKLQgiiRSLEKDIQGLKREIQERDETIQDKEKRiydLKKKNQELEKFKFVLDYKIKELKK 913
Cdd:PRK12704 48 KKEAEAIKKEALLeAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEEN---LDRKLELLEKREEELEKKEKELEQ 121
|
90 100
....*....|....*....|....*
gi 568929692 914 QIEPRENEIKVMKEQIQEMEAELER 938
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQLQELER 146
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
658-987 |
9.60e-07 |
|
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: 52.93 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 658 IKELTDK--FIQEMESLKTKNQVLK-TEKEKQDIshRERLEELVDKQTR---ELQDLEccnnqkllleyEKYQELQ--LK 729
Cdd:pfam06160 72 AEELNDKyrFKKAKKALDEIEELLDdIEEDIKQI--LEELDELLESEEKnreEVEELK-----------DKYRELRktLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 730 SQRMQ-----EEYEKQLrDNDETKSQALEELTE---FYEAK------------LQEKT----GLLEEAQEDVRQQLREFE 785
Cdd:pfam06160 139 ANRFSygpaiDELEKQL-AEIEEEFSQFEELTEsgdYLEARevlekleeetdaLEELMedipPLYEELKTELPDQLEELK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 786 ETKKQIEEDE--------DREIQDIKTKYERKLrdEKESNLRLKGetgiMRKKFSSLQKEIEERTNDIEL-LKSEQ--MK 854
Cdd:pfam06160 218 EGYREMEEEGyalehlnvDKEIQQLEEQLEENL--ALLENLELDE----AEEALEEIEERIDQLYDLLEKeVDAKKyvEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 855 LQGIIRSLEKDIQGLKREIQERDETIQDKekriYDLkkKNQELEKFKfVLDYKIKELKKQIEPRENEIKVMKEQIQEMEA 934
Cdd:pfam06160 292 NLPEIEDYLEHAEEQNKELKEELERVQQS----YTL--NENELERVR-GLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568929692 935 ELERFHKQNTQLELNITELLQKLratdQEMRKEQQKERDleaLVRRFKTDLHN 987
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESL----QSLRKDELEARE---KLDEFKLELRE 410
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
904-1103 |
9.63e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 904 LDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQN--TQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRF 981
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 982 KTDL---HNCVAYIQEPGLLKEKIRGLFEKYVQRADMV---------------EIAGLNSDLQQEYARQREHLERNLATL 1043
Cdd:COG3206 246 RAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialraQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 1044 KKkviKEGELHRT--DYVRIMQENVSLIKEINELRRELKLTRSQiydLESALKVSKKTRSQE 1103
Cdd:COG3206 326 QA---REASLQAQlaQLEARLAELPELEAELRRLEREVEVAREL---YESLLQRLEEARLAE 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
839-1151 |
1.00e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 839 EERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPR 918
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 919 ENEIKVMKEQIQEMEAELERF-------HKQNTQLELNITELLQKLRATDQEMR---------KEQQKERDLEAL----- 977
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMkerakkaGAQRKEEEAERKQLQAKLQQTEEELRslskefqelRNSLAQRDTQVLqlqdt 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 978 VRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEiaGLNSDLqQEYARQREH---------LERNLATLK---- 1044
Cdd:pfam07888 215 ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVE--GLGEEL-SSMAAQRDRtqaelhqarLQAAQLTLQlada 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1045 KKVIKEGELHRTDYVRIMQENVSLIKEinelrRELKLTRsQIYDLESALKVSKKTRSQEVPESVISKD---VVGSTSTMR 1121
Cdd:pfam07888 292 SLALREGRARWAQERETLQQSAEADKD-----RIEKLSA-ELQRLEERLQEERMEREKLEVELGREKDcnrVQLSESRRE 365
|
330 340 350
....*....|....*....|....*....|....
gi 568929692 1122 LNEQEETGRII----EMQRLEIRRLRDQIQEQEQ 1151
Cdd:pfam07888 366 LQELKASLRVAqkekEQLQAEKQELLEYIRQLEQ 399
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
723-1141 |
1.29e-06 |
|
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: 52.92 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 723 YQELQLKSQRMQEEYEKQLRDndetKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFE--ETKKQIEEDEDREIQ 800
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAE----LNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEalEDQHGAFLDADIETA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 801 DIKTKYERKLRDEKES-NLRLKGETGIMRK---KFSSLQKEIEERTN-DIELLKSEQMKL-QGIIRSL---EKDIQGLKR 871
Cdd:pfam12128 343 AADQEQLPSWQSELENlEERLKALTGKHQDvtaKYNRRRSKIKEQNNrDIAGIKDKLAKIrEARDRQLavaEDDLQALES 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 872 EIQERDET----IQDKEKRIydlkkkNQELEKFKFVLDYKI--KELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQ 945
Cdd:pfam12128 423 ELREQLEAgkleFNEEEYRL------KSRLGELKLRLNQATatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 946 LELNITELLQKLRatDQEMRKEQQKERdLEALVRRFKTDLHNCVAYIQ-EPGLLKEKIRGL-------------FEKYVQ 1011
Cdd:pfam12128 497 ARKRRDQASEALR--QASRRLEERQSA-LDELELQLFPQAGTLLHFLRkEAPDWEQSIGKVispellhrtdldpEVWDGS 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1012 RADMVEIAGLNSDLQQ----EYARQREHLERNLATLKKKVIKEGELHRtdyvRIMQENVSLIKEINELRRELKLTRS--- 1084
Cdd:pfam12128 574 VGGELNLYGVKLDLKRidvpEWAASEEELRERLDKAEEALQSAREKQA----AAEEQLVQANGELEKASREETFARTalk 649
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 1085 -------QIYDLESALKVSK----KTRSQEVPESVIS----KDVVGSTSTMRLNEQEETGRIIEMQRLEIRR 1141
Cdd:pfam12128 650 narldlrRLFDEKQSEKDKKnkalAERKDSANERLNSleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
747-1086 |
1.29e-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: 53.13 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 747 TKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEdEDREIQDIKTKYERK------LRDEKESNLRL 820
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK-VNRDIQRLKNDIEEQetllgtIMPEEESAKVC 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 821 KGETGIMRKkfssLQKEIEERTNDIELLKSeqmKLQGIirSLEKDIQGLKREIQERDET--------------IQDKEKR 886
Cdd:TIGR00606 788 LTDVTIMER----FQMELKDVERKIAQQAA---KLQGS--DLDRTVQQVNQEKQEKQHEldtvvskielnrklIQDQQEQ 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 887 IYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRK 966
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 967 EQQKERDLealvrrfKTDLHNCVAYIQEpglLKEKIRGLFEKYVQRADmVEIAGLNSDLqQEYARQREHLERNLATLKKK 1046
Cdd:TIGR00606 939 AQDKVNDI-------KEKVKNIHGYMKD---IENKIQDGKDDYLKQKE-TELNTVNAQL-EECEKHQEKINEDMRLMRQD 1006
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568929692 1047 VIKEGELHrtdyvRIMQENVSLIK---EINELRRELKLTRSQI 1086
Cdd:TIGR00606 1007 IDTQKIQE-----RWLQDNLTLRKrenELKEVEEELKQHLKEM 1044
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
668-961 |
3.21e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 668 EMESLKTKNQVLKTEKEKqdisHRERLEELVdKQTRELQdleccnnQKLLLEYEKYQELQLKSQRMQEEYE---KQLRDN 744
Cdd:COG1340 9 SLEELEEKIEELREEIEE----LKEKRDELN-EELKELA-------EKRDELNAQVKELREEAQELREKRDelnEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 745 DETKSQALEELTEFYEaKLQEKTGLLEEAQEDVRqqlrEFEETKKQIEEDEDR-EIQDIKTKYERKLRDEKESnlrlkge 823
Cdd:COG1340 77 KEERDELNEKLNELRE-ELDELRKELAELNKAGG----SIDKLRKEIERLEWRqQTEVLSPEEEKELVEKIKE------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 824 tgiMRKKFSSLQKEIEERtNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfv 903
Cdd:COG1340 145 ---LEKELEKAKKALEKN-EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK---- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 904 ldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATD 961
Cdd:COG1340 217 ---EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
646-1009 |
3.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 646 QLRLKDMNYTEKIKELtDKFIQEMESLKTKNQVLKTEKEK--QDISHRERLEELVDKQtRELQDLECCNnQKLLLEYEKY 723
Cdd:COG4717 82 EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKleKLLQLLPLYQELEALE-AELAELPERL-EELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 724 QELQLKSQRMQEEYEK-------QLRDNDETKSQALEELTEFYEAklqektglLEEAQEDVRQQLREFEETKKQIEEDED 796
Cdd:COG4717 159 RELEEELEELEAELAElqeeleeLLEQLSLATEEELQDLAEELEE--------LQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 797 R-EIQDIKTKYERKLRDEK--------------------ESNLRLKG-----------ETGIMRKKFSSLQKEIEERTND 844
Cdd:COG4717 231 QlENELEAAALEERLKEARlllliaaallallglggsllSLILTIAGvlflvlgllalLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 845 IELLKSEQMKLQGI--------------IRSLEKDIQGLKREIQERDEtiQDKEKRIYDLKKKNQELEKFKFVLD----Y 906
Cdd:COG4717 311 PALEELEEEELEELlaalglppdlspeeLLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAGVEDeeelR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 907 KIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNT--QLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTD 984
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410 420
....*....|....*....|....*
gi 568929692 985 lHNCVAYIQEPGLLKEKIRGLFEKY 1009
Cdd:COG4717 469 -GELAELLQELEELKAELRELAEEW 492
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
734-971 |
3.56e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 734 QEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYERKLRDE 813
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE-AEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 814 KESNlrlkGETGIMRKKFSSlqKEIEERTNDIELLKSEQMKLQGIIRSLEKDiqglKREIQERDETIQDKEKriyDLKKK 893
Cdd:COG3883 96 YRSG----GSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKAD----KAELEAKKAELEAKLA---ELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 894 NQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKE 971
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
762-1098 |
3.82e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 762 KLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsnlrlkgetgiMRKKFSSLQKEIEER 841
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ-----------AREELEQLEEELEQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 842 TNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENE 921
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 922 IKVMKEQIQEMEAELERFhkQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEK 1001
Cdd:COG4372 152 LKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1002 IRGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQENVSLIKEINELRRELKL 1081
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330
....*....|....*..
gi 568929692 1082 TRSQIYDLESALKVSKK 1098
Cdd:COG4372 310 IGALEDALLAALLELAK 326
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
667-899 |
7.88e-06 |
|
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: 49.18 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 667 QEMESLKTKNQVLKTEKEK------QDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQ 740
Cdd:pfam09728 39 KDLKKLKKKQDQLQKEKDQlqselsKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 741 LRDNDETKSQALEELTEFYE--AKLQEKTGLLEE------AQEDVRQQLRE------FEETKKQIEEDEDREIQDIKTKY 806
Cdd:pfam09728 119 MEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaTEEEEKKAQEKEVAKARELKAQV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 807 ERKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETI------ 880
Cdd:pfam09728 199 QTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALlemaee 274
|
250 260
....*....|....*....|
gi 568929692 881 -QDKEKRIYDLKKKNQELEK 899
Cdd:pfam09728 275 rQKLKEELEKLQKKLEKLEN 294
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
614-985 |
8.41e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 614 EVLVTKTDMEEKAQIMLELKTRVEELKMENEYQLRLKDMNYtEKIKELTDkFIQEMESLKTKNQVLKTEkekqdisHRER 693
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNL-ELESEIIE-LKKSLSSDLIENLEFKTE-------LIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 694 LEELVDKQTRELQdleccnnqkLLLEYEKYQELqlksQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEA 773
Cdd:COG5022 933 LKKLLNNIDLEEG---------PSIEYVKLPEL----NKLHEV-ESKLKETSEEYEDLLKKSTILVREGNKANSELKNFK 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 774 QE--DVRQQLREFEETKKQIEEdEDREIQDIKTKYeRKLRDEKESNLRLKGETGIMR---KKFSSLQKEIEERTNDIE-- 846
Cdd:COG5022 999 KElaELSKQYGALQESTKQLKE-LPVEVAELQSAS-KIISSESTELSILKPLQKLKGlllLENNQLQARYKALKLRREns 1076
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 847 LLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN----QELEKFKFVLDYKIKELKKQIEPRENEI 922
Cdd:COG5022 1077 LLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKlnllQEISKFLSQLVNTLEPVFQKLSVLQLEL 1156
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929692 923 KVMKEQIQ-EMEAELERFHKQNTQLELNITELLQKLRATDQEMrkeQQKERDLEALVRRFKTDL 985
Cdd:COG5022 1157 DGLFWEANlEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEV---NDLKNELIALFSKIFSGW 1217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
755-1085 |
8.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 755 LTEFYEAKLQEKtgLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYE--RKLRDEKESnlrlkgetgiMRKKFS 832
Cdd:COG4717 39 LLAFIRAMLLER--LEKEADELFKPQGRKPELNLKELKELE-EELKEAEEKEEeyAELQEELEE----------LEEELE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 833 SLQKEIEERTNDIELLK---------SEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfV 903
Cdd:COG4717 106 ELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE---L 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 904 LDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKE--RDLEALVRRF 981
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllLIAAALLALL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 982 KTDLHNCVAYIQEPGLLKEKIrGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLE-RNLATLKKKVIKEGELHRT---D 1057
Cdd:COG4717 263 GLGGSLLSLILTIAGVLFLVL-GLLALLFLLLAREKASLGKEAEELQALPALEELEeEELEELLAALGLPPDLSPEellE 341
|
330 340
....*....|....*....|....*...
gi 568929692 1058 YVRIMQENVSLIKEINELRRELKLTRSQ 1085
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELE 369
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
744-941 |
9.38e-06 |
|
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: 48.91 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 744 NDETKSQALEELTEFYEAKLQEKTGLLEEAQEdVRQQLREFEetkKQIEEDEDrEIQDIKTKYERKLRDEKESnlrlkge 823
Cdd:cd22656 108 DDEELEEAKKTIKALLDDLLKEAKKYQDKAAK-VVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 824 tgIMRKKFSSLQKEIEErtndiellkseqmKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelekfkfv 903
Cdd:cd22656 176 --IARKEIKDLQKELEK-------------LNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 568929692 904 LDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHK 941
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
635-1117 |
9.38e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 635 RVEELKMENEYQLRLKDMNYTEKIKELTDKfiqEMESLKTKNQVLKTEKEKQDIShrERLEELVDKQT---RELQDlecc 711
Cdd:COG5022 919 LIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKETS--EEYEDLLKKSTilvREGNK---- 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 712 NNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQEKTGLLEEAQEDVRQQLR 782
Cdd:COG5022 990 ANSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQKLKGLLLLENNQLQARYK 1067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 783 EFEETKKQIEEDEDREIQDIKTKYERK---LRDEKESNLRLKGETGIMR------KKFSSLQKEIEERTNDIELLKSEQM 853
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQEISKFLSQLVNTLEPVFQ 1147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 854 KLQGiirsLEKDIQGLKREIQERDETIQDKEKRIYdlkkknQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEmE 933
Cdd:COG5022 1148 KLSV----LQLELDGLFWEANLEALPSPPPFAALS------EKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFS-G 1216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 934 AELERFHKQNTQLELNITELLQKLRAT-DQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQR 1012
Cdd:COG5022 1217 WPRGDKLKKLISEGWVPTEYSTSLKGFnNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVG 1296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1013 ADMVEIAGLNSdLQQEYARQrehLERNlATLKKKVIKEGELHRTDYVRIMQENVSLIKE-----INELRRELKLTRSQIY 1087
Cdd:COG5022 1297 LFNALRTKASS-LRWKSATE---VNYN-SEELDDWCREFEISDVDEELEELIQAVKVLQllkddLNKLDELLDACYSLNP 1371
|
490 500 510
....*....|....*....|....*....|.
gi 568929692 1088 DLESALKVSKKTRSQEVP-ESVISKDVVGST 1117
Cdd:COG5022 1372 AEIQNLKSRYDPADKENNlPKEILKKIEALL 1402
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
613-974 |
9.94e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 613 EEVLVTKTDMEEKAQIMLELKTRV-----------EELKMENEYqlrLKDMNYTEKIKELTDKfIQEMESLKTKNQVLKT 681
Cdd:PRK04778 205 EELAALEQIMEEIPELLKELQTELpdqlqelkagyRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 682 EKEKQDIShrERLEELVDKQTRElqdleccnnqkllleYEKYQELQLKSQRMQEEYEKQLRDNDETKSQaLEELTEFYEa 761
Cdd:PRK04778 281 EEKNEEIQ--ERIDQLYDILERE---------------VKARKYVEKNSDTLPDFLEHAKEQNKELKEE-IDRVKQSYT- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 762 klqektgLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyerklrdekesnlrlkgetgimrkkFSSLQKEIEER 841
Cdd:PRK04778 342 -------LNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 842 TNDIELLKSEQMKLQGIIRSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELEKFKFVLDYKIKELK 912
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 913 KQIEPRENEIKVMKEQIQEMEAELERFHKQNTQL--ELNITE-LLQ---KLRATDQEMRKEQQKERDL 974
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEELveNATLTEqLIQyanRYRSDNEEVAEALNEAERL 529
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
614-1150 |
1.09e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 614 EVLVTKTDMEEKAQIMLELKTRVEelKMENEYQLRLKdmnytekiKEltDKFIQEMESLKTKNQVLKTEKEKQDISHRER 693
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 694 LEEL---VDKQTRELQDL------ECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 762
Cdd:pfam01576 231 IAELraqLAKKEEELQAAlarleeETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 763 LQEKTGLLEEAQEDVRQQLREFEETKKQIEED---EDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIE 839
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 840 ERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRiydLKKKNQELEKFKFVL---DYKIKELKKQIE 916
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK---LSKLQSELESVSSLLneaEGKNIKLSKDVS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 917 PRENEIKVMKEQIQE--------------MEAE---LERFHKQNTQLELNITELLQKLRATDQEMRKEQQKE----RDLE 975
Cdd:pfam01576 465 SLESQLQDTQELLQEetrqklnlstrlrqLEDErnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDagtlEALE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 976 ALVRRFKTDLHNCVAYIQEPGLLKEKIrglfEKYVQRadmveiaglnsdLQQEY---ARQREHLERNLATLKKKVIKEGE 1052
Cdd:pfam01576 545 EGKKRLQRELEALTQQLEEKAAAYDKL----EKTKNR------------LQQELddlLVDLDHQRQLVSNLEKKQKKFDQ 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1053 L---HRTDYVRIMQENVSLIKEINE-------LRRELKLTRSQIYDLESALKVSKKtrsqEVPESVISKDVVGSTstmrL 1122
Cdd:pfam01576 609 MlaeEKAISARYAEERDRAEAEAREketralsLARALEEALEAKEELERTNKQLRA----EMEDLVSSKDDVGKN----V 680
|
570 580 590
....*....|....*....|....*....|..
gi 568929692 1123 NEQEETGRIIEMQRLEIR----RLRDQIQEQE 1150
Cdd:pfam01576 681 HELERSKRALEQQVEEMKtqleELEDELQATE 712
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
672-985 |
2.45e-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: 48.63 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 672 LKTKNQVLKTEKEKQdiSHRERLEELVDKQTRELQDLECCNNQklLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQA 751
Cdd:pfam01576 485 LNLSTRLRQLEDERN--SLQEQLEEEEEAKRNVERQLSTLQAQ--LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 752 LEELTEFYEaKLQEKTGLLEEAQEDV-------RQQLREFEETKKQIEEDEDREiQDIKTKYERKlRDEKESNLRLKgET 824
Cdd:pfam01576 561 LEEKAAAYD-KLEKTKNRLQQELDDLlvdldhqRQLVSNLEKKQKKFDQMLAEE-KAISARYAEE-RDRAEAEAREK-ET 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 825 gimrkKFSSLQKEIEErtndiellkseqmkLQGIIRSLEKDIQGLKREIqerDETIQDKEkriyDLKKKNQELEKFKFVL 904
Cdd:pfam01576 637 -----RALSLARALEE--------------ALEAKEELERTNKQLRAEM---EDLVSSKD----DVGKNVHELERSKRAL 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 905 DYKIKELKKQIEPRENEIKVMKE-------QIQEMEAELER-FHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEA 976
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQATEDaklrlevNMQALKAQFERdLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA 770
|
....*....
gi 568929692 977 LVRRFKTDL 985
Cdd:pfam01576 771 AKKKLELDL 779
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
425-593 |
2.56e-05 |
|
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: 47.33 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 425 YKEYQEEAYTVSLHPSGHYIVVGFADK-LRLMNLliDDIRPFKEY-----SVRGCKECSFSNGghLFAAVNGNVIHIFTT 498
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDL--ETGELLRTLkghtgPVRDVAASADGTY--LASGSSDKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 499 TSLENINILKGHTGKIlreipafdviyTSITISHSGRMIFVGTSVGTIR----AMKYPLSlqkeynEYQAHAGPVMKMLL 574
Cdd:cd00200 81 ETGECVRTLTGHTSYV-----------SSVAFSPDGRILSSSSRDKTIKvwdvETGKCLT------TLRGHTDWVNSVAF 143
|
170
....*....|....*....
gi 568929692 575 TFDDQFLLTVGEDGCLFTW 593
Cdd:cd00200 144 SPDGTFVASSSQDGTIKLW 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
613-899 |
2.65e-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: 48.43 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 613 EEVLVTKTDMEEKAQIMLELKTRVEELKME---NEYQLRLKDMNYTEKIKELTDKFIQEMESLktknqvLKTEKEKQDIS 689
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqDLQDVRLHLQQCSQELALKLTALHALQLTL------TQERVREHALS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 690 HRERLEELVDKQTRELQDLEccnNQKLLLEYEKYQELQLKSQ-RMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTG 768
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQ---SEKEQLTYWKEMLAQCQTLlRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 769 LLEEAQEDVRQQLREFEETKKQIEEDEDREIQdIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE----RTND 844
Cdd:TIGR00618 744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdediLNLQ 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568929692 845 IELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEK 899
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
905-1107 |
2.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 905 DYKIKELKKQIEPRENEIKVMKEQIQEMEAELErfhkqntQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTD 984
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 985 LHNCVAYIQEPGLLKEKIRGL-----FEKYVQRADMVE-IAGLNSDLQQEYARQREHLERNLATLKKKvIKEGELHRTDY 1058
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgsesFSDFLDRLSALSkIADADADLLEELKADKAELEAKKAELEAK-LAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568929692 1059 VRIMQENVSLIKE----INELRRELKLTRSQIYDLESALKVSKKTRSQEVPES 1107
Cdd:COG3883 167 EAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
609-817 |
3.19e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 609 VGFAEEVLVTKTDMEEKAQIMLEL-KTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEmesLKTKNQVLKtEKEKQD 687
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKE---LRERRNELQ-KLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 688 ISHrerlEELVDKQTRELQDLEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDNDETKSQaLEELTEFYEAKLQEKT 767
Cdd:PRK12704 92 LQK----EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQELEKKEEE-LEELIEEQLQELERIS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568929692 768 GLleeAQEDVRQQLreFEETKKQIEEDEDREIQDIKTKYerKLRDEKESN 817
Cdd:PRK12704 149 GL---TAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
667-971 |
3.37e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.21 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 667 QEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQDleccnnqkllleyeKYQELQLKSQRMQEEYEKQLR---- 742
Cdd:pfam09731 106 KEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATA--------------VAKEAKDDAIQAVKAHTDSLKeasd 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 743 ---DNDETKSQALEELTEFYEAKLQEKTGLLEEAQED-VRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKesnl 818
Cdd:pfam09731 172 taeISREKATDSALQKAEALAEKLKEVINLAKQSEEEaAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQ---- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 819 rLKGETGIMRKKFsslQKEIEERTNDI-----ELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 893
Cdd:pfam09731 248 -YKELVASERIVF---QQELVSIFPDIipvlkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 894 NQE------LEKFKFVLDYKIKELKKQIEPRENEI-KVMKEqiqEMEAELERFHKQNTQlelnitELLQKLRATDQEMRK 966
Cdd:pfam09731 324 ELDklaeelSARLEEVRAADEAQLRLEFEREREEIrESYEE---KLRTELERQAEAHEE------HLKDVLVEQEIELQR 394
|
....*
gi 568929692 967 EQQKE 971
Cdd:pfam09731 395 EFLQD 399
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
572-967 |
3.92e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 572 MLLTFDDQFLLTVGEDGCLFTWKVFDKDGRGIKREREvgfaEEVLVTKTDMEEKAQIMLELKTRVEELKmENEYQLRLKD 651
Cdd:pfam07888 22 MLLVVPRAELLQNRLEECLQERAELLQAQEAANRQRE----KEKERYKRDREQWERQRRELESRVAELK-EELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 652 MNYTEKIKELTDKfiqeMESLKTKNQVLKTEKEkqdiSHRERLEELVDkqtrelqDLECCNNQKLLLEYE----KYQELQ 727
Cdd:pfam07888 97 EELEEKYKELSAS----SEELSEEKDALLAQRA----AHEARIRELEE-------DIKTLTQRVLERETElermKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 728 LKSQRMQEEYEkqlRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE 807
Cdd:pfam07888 162 AGAQRKEEEAE---RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 808 -RKLRDEKESNLR----LKGETGIMRKKFSSLQKEIEE-RTNDIEL-LKSEQMKL-------------QGIIRSLEKDiq 867
Cdd:pfam07888 239 lRSLQERLNASERkvegLGEELSSMAAQRDRTQAELHQaRLQAAQLtLQLADASLalregrarwaqerETLQQSAEAD-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 868 glKREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldykikELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLE 947
Cdd:pfam07888 317 --KDRIEKLSAELQRLEERLQEERMEREKLEV----------ELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQ 384
|
410 420
....*....|....*....|
gi 568929692 948 LNITELLQKLRATDQEMRKE 967
Cdd:pfam07888 385 AEKQELLEYIRQLEQRLETV 404
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
655-980 |
4.12e-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: 48.04 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 655 TEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHR--ERLEELVDKQTRELQDLECCNnqkllleyekyQELQLKSQR 732
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNitVRLQDLTEKLSEAEDMLACEQ-----------HALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 733 MQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRD 812
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 813 EKESNLRLKGEtgimRKKFSSLQKEIEERTNdieLLKSEQMKLQGIIRSLEKDIQGLKRE----IQERDETIQDKEKRIY 888
Cdd:TIGR00618 699 LAQCQTLLREL----ETHIEEYDREFNEIEN---ASSSLGSDLAAREDALNQSLKELMHQartvLKARTEAHFNNNEEVT 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 889 DLKKKNQELEKFKFVLDYKIKELkkqiEPRENEIKVMKEQIQE--------MEAELERFHKQNTQLELNITELLQKLRAT 960
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNRLR----EEDTHLLKTLEAEIGQeipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
330 340
....*....|....*....|
gi 568929692 961 DQEMRKEQQKERDLEALVRR 980
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQE 867
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
637-873 |
4.14e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 637 EELKMENEYQLRLKDMN--YTEKIKELTDKFIQEMESLKT-----KNQVLKTEKEKQDIShrERLEELVDKQTRELQDLE 709
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNgeNIARKQNKYDELVEEAKTIKAeieelTDELLNLVMDIEDPS--AALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 710 CCnnQKLLLEYEKYQELQLKSQRMQEEYEKqLRDNDETKSQALEELTefyeaKLQEKTGLLEEAQEDVRQQLREFEETKK 789
Cdd:PHA02562 273 QF--QKVIKMYEKGGVCPTCTQQISEGPDR-ITKIKDKLKELQHSLE-----KLDTAIDELEEIMDEFNEQSKKLLELKN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 790 QIEEdEDREIQdiktKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLqGIIRSLEKDiQGL 869
Cdd:PHA02562 345 KIST-NKQSLI----TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR-GIVTDLLKD-SGI 417
|
....
gi 568929692 870 KREI 873
Cdd:PHA02562 418 KASI 421
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
619-1090 |
6.14e-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: 47.27 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 619 KTDMEEKAQImleLKTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELV 698
Cdd:TIGR00618 388 KTTLTQKLQS---LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 699 DKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEE---YEKQLRDNDETKSQALEE--LTEFYEAKLQEkTGLLEEA 773
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcpLCGSCIHPNPARQDIDNPgpLTRRMQRGEQT-YAQLETS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 774 QEDVRQQLREFEETKKQIEEDEDREIQDIkTKYERKLRDEKESNLRLKGETGIMRKKfssLQKEIEERTNDIELLKSEQM 853
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSF-SILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEAEDMLACEQHALLR 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 854 KLQGII---------RSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDY--KIKELKKQIEPRENEI 922
Cdd:TIGR00618 620 KLQPEQdlqdvrlhlQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAlqKMQSEKEQLTYWKEML 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 923 KVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATD---QEMRKEQQKERD--LEALVRRFKTDLHNCVAYIQEPGL 997
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREdalNQSLKELMHQARtvLKARTEAHFNNNEEVTAALQTGAE 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 998 LKEKIRGLFEKYVQRADMV-EIAGLNSDLQQE--------------YARQREHLERNLATLKKKV--IKEGELHRTDYVR 1060
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDThLLKTLEAEIGQEipsdedilnlqcetLVQEEEQFLSRLEEKSATLgeITHQLLKYEECSK 859
|
490 500 510
....*....|....*....|....*....|
gi 568929692 1061 IMQENVSLIKEINELRRELKLTRSQIYDLE 1090
Cdd:TIGR00618 860 QLAQLTQEQAKIIQLSDKLNGINQIKIQFD 889
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
618-949 |
6.55e-05 |
|
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: 47.36 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 618 TKTDMEEKAQIMLELKTRVEELKMENEYQLRLKDMNYTEKIKEltdKFIQEMESLKTKNQVLKTEKEkqdishRERLEEL 697
Cdd:pfam13166 122 LDKEKEKLEADFLDECWKKIKRKKNSALSEALNGFKYEANFKS---RLLREIEKDNFNAGVLLSDED------RKAALAT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 698 VDKQTR-ELQDLECcnNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKL-----------QE 765
Cdd:pfam13166 193 VFSDNKpEIAPLTF--NVIDFDALEKAEILIQKVIGKSSAIEELIKNPD--LADWVEQGLELHKAHLdtcpfcgqplpAE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 766 KTGLLEEA-QEDVRQQLREFEETKKQIEEDEDREIQDIKT--KYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER- 841
Cdd:pfam13166 269 RKAALEAHfDDEFTEFQNRLQKLIEKVESAISSLLAQLPAvsDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKr 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 842 ------------TNDIELLKSEQMKLQGIIR-------SLEKD------------IQGLKREIQERDETIQDKEKRIYDL 890
Cdd:pfam13166 349 kdpfksieldsvDAKIESINDLVASINELIAkhneitdNFEEEknkakkklrlhlVEEFKSEIDEYKDKYAGLEKAINSL 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 568929692 891 KKKNQELEKFKFVLDYKIKELkkqieprENEIKVMKEQIQEMEAELERFHKQNTQLELN 949
Cdd:pfam13166 429 EKEIKNLEAEIKKLREEIKEL-------EAQLRDHKPGADEINKLLKAFGFGELELSFN 480
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
828-976 |
6.57e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 828 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELEKFKFVL--- 904
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 905 ---DY-------------------KIKELKKQIEPRENEIKVMKEQIQEMEAELErfhKQNTQLELNITELLQKLRATDQ 962
Cdd:COG3883 113 sfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELE---AAKAELEAQQAEQEALLAQLSA 189
|
170
....*....|....
gi 568929692 963 EMRKEQQKERDLEA 976
Cdd:COG3883 190 EEAAAEAQLAELEA 203
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
691-1151 |
6.92e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.05 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 691 RERLEELVDKQTRELQDLeccnNQKLLLEYEKYQELQLKSQRMQEE-YEKQLRDNDETKSQALEELTEFY-EAKLQEKTg 768
Cdd:pfam07111 131 RKNLEEGSQRELEEIQRL----HQEQLSSLTQAHEEALSSLTSKAEgLEKSLNSLETKRAGEAKQLAEAQkEAELLRKQ- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 769 lLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKlrdekesnlrlkgetgimrKKFSSLQKEIEERTN---DI 845
Cdd:pfam07111 206 -LSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQ-------------------ELLDTMQHLQEDRADlqaTV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 846 ELLkseQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDL-------------KKKNQELEKFKFV--LDYKIKE 910
Cdd:pfam07111 266 ELL---QVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLlnrwrekvfalmvQLKAQDLEHRDSVkqLRGQVAE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 911 LKKQIEPRENEIKVMKEQIQEMEAEL--ERFHKQNTQLELNitellqklRATDQEMRKEQQ---KERDLEALVRRFKTD- 984
Cdd:pfam07111 343 LQEQVTSQSQEQAILQRALQDKAAEVevERMSAKGLQMELS--------RAQEARRRQQQQtasAEEQLKFVVNAMSSTq 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 985 --LHNCVAYIQE-----PGLLK---------EKIRGLFEKYVQRADM--------VEIAGLNSDLQQEYARQREHLERNL 1040
Cdd:pfam07111 415 iwLETTMTRVEQavariPSLSNrlsyavrkvHTIKGLMARKVALAQLrqescpppPPAPPVDADLSLELEQLREERNRLD 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1041 ATLKKKV-IKEGELHRTDYvRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKTRSQEVPESviskdvvGSTST 1119
Cdd:pfam07111 495 AELQLSAhLIQQEVGRARE-QGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEA-------ASLRQ 566
|
490 500 510
....*....|....*....|....*....|...
gi 568929692 1120 MRLNEQEETGRIIEMQRLEIR-RLRDQIQEQEQ 1151
Cdd:pfam07111 567 ELTQQQEIYGQALQEKVAEVEtRLREQLSDTKR 599
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
784-1050 |
7.64e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 784 FEETKKQIEE---DEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIELLKSEQMKLQG 857
Cdd:PTZ00440 423 LKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMKSFYdliISEKDSMDSKEKKESSDSNYQEKVDE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 858 IIRSLE--------------------KDIQGLKREIQERDETIQDKEKRIYDLKK--------KNQELEKFKFVLDY--K 907
Cdd:PTZ00440 503 LLQIINsikeknnivnnnfkniedyyITIEGLKNEIEGLIELIKYYLQSIETLIKdeklkrsmKNDIKNKIKYIEENvdH 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 908 IKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRatdqemrkeqqkERDLEALVRRFKTDLHN 987
Cdd:PTZ00440 583 IKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFY------------KGDLQELLDELSHFLDD 650
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929692 988 CVAYIQEpGLLKEKIRGLFEKYVQRADmvEIAGLNSDLQQEYARQREHLERNLATLKKKVIKE 1050
Cdd:PTZ00440 651 HKYLYHE-AKSKEDLQTLLNTSKNEYE--KLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKK 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-886 |
8.40e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 657 KIKELTDKFIQEMESLKTKNQVLKTEKEKqdishRERLEELVDKQTRELQDLECCNNQKLLLEY-------EKYQELQLK 729
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQ-----IELLEPIRELAERYAAARERLAELEYLRAAlrlwfaqRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 730 SQRMQEEYEK---QLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkY 806
Cdd:COG4913 297 LEELRAELARleaELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERL----ERELEERERRRAR--------L 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 807 ERKLRDekesnLRLKGETGimRKKFSSLQKEIEERTNDielLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKR 886
Cdd:COG4913 365 EALLAA-----LGLPLPAS--AEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
750-894 |
8.40e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 750 QALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDED--------REIQDIK---TKYERKLRDEKESNL 818
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnKEYEALQkeiESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929692 819 RLKGETGIMRKKFSSLQKEIEERTNDIELLKSEqmkLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN 894
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPPELLALYERIRKR 186
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
627-916 |
9.03e-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: 46.71 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 627 QIMLELKTRVEELkmENEYQLrlkdmnyTEKIKEltdkfiqemeSLKTKNQVLKTEKEKqDISHRERLEE----LVDKQT 702
Cdd:pfam01576 692 QQVEEMKTQLEEL--EDELQA-------TEDAKL----------RLEVNMQALKAQFER-DLQARDEQGEekrrQLVKQV 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 703 RELQ-DLECCNNQK-LLLEYEKYQELQLK--------SQRMQEEYEKQL-----------RDNDETKSQALEELTEFYEA 761
Cdd:pfam01576 752 RELEaELEDERKQRaQAVAAKKKLELDLKeleaqidaANKGREEAVKQLkklqaqmkdlqRELEEARASRDEILAQSKES 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 762 --KLQEKTGLLEEAQEDvrqqLREFEETKKQIEEDEDREIQDIKTKYERK--LRDEKEsnlRLKGetgimrkKFSSLQKE 837
Cdd:pfam01576 832 ekKLKNLEAELLQLQED----LAASERARRQAQQERDELADEIASGASGKsaLQDEKR---RLEA-------RIAQLEEE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 838 IEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELE-----KFKF---VLDYKIK 909
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEgtvksKFKSsiaALEAKIA 977
|
....*..
gi 568929692 910 ELKKQIE 916
Cdd:pfam01576 978 QLEEQLE 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
755-1152 |
1.00e-04 |
|
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: 46.55 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 755 LTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYERKLRDEKESNLRLKGEtgimRKKFSSL 834
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-INNSNNKIKILEQQIKDLNDKLKKN----KDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 835 QKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQ 914
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 915 IEPRENEIKVMKEQI-----------------QEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEAL 977
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 978 VRRFKTDLHNcvaYIQEPGLLKEKIRGLfEKYVQRADMvEIAGLNSDLQQEYARQrehLERNLATLKKKVIKegelhrtd 1057
Cdd:TIGR04523 262 QNKIKKQLSE---KQKELEQNNKKIKEL-EKQLNQLKS-EISDLNNQKEQDWNKE---LKSELKNQEKKLEE-------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1058 yvrIMQENVSLIKEINELRRELKLTRSQIYDLESalKVSKKTRSQEVPESVISKdvvgststmRLNEQEETGRIIEMQRL 1137
Cdd:TIGR04523 326 ---IQNQISQNNKIISQLNEQISQLKKELTNSES--ENSEKQRELEEKQNEIEK---------LKKENQSYKQEIKNLES 391
|
410
....*....|....*
gi 568929692 1138 EIRRLRDQIQEQEQV 1152
Cdd:TIGR04523 392 QINDLESKIQNQEKL 406
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
745-1151 |
1.24e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.16 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 745 DETKSQALEELTEFYEAKLQEktglleeaqedVRQQLREFEETKKQieeDEDREIQDIKTKYERKLRDEKEsnlrlKGET 824
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSE-----------IQKSLDKRKHTQNV---ALNKKLSDIKTEYLYELNVLKE-----KSEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 825 GIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDK----EKRIYDLKKKNQELEKF 900
Cdd:NF033838 114 ELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKtlelEIAESDVEVKKAELELV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 901 KFVL-----DYKIKELKKQIEPRENEIKVMKE-QIQEMEAELERFHKQNTQLELNITELlqkLRATDQEMRKEQQKERDL 974
Cdd:NF033838 194 KEEAkeprdEEKIKQAKAKVESKKAEATRLEKiKTDREKAEEEAKRRADAKLKEAVEKN---VATSEQDKPKRRAKRGVL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 975 EALVRRFK--TDLHNCVAYIQE-----PGLLKEKIRGLFEKYVQRAdmveiaglnsdlQQEYARQREHLERNLATLKKKV 1047
Cdd:NF033838 271 GEPATPDKkeNDAKSSDSSVGEetlpsPSLKPEKKVAEAEKKVEEA------------KKKAKDQKEEDRRNYPTNTYKT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1048 IkEGELHRTDyVRIMQENVSLIKEI-NELRRELKLTRSQIyDLESalKVSKKTRSQEVpesviskdvvgstSTMRLNEQE 1126
Cdd:NF033838 339 L-ELEIAESD-VKVKEAELELVKEEaKEPRNEEKIKQAKA-KVES--KKAEATRLEKI-------------KTDRKKAEE 400
|
410 420
....*....|....*....|....*
gi 568929692 1127 ETGRIIEmqrlEIRRLRDQIQEQEQ 1151
Cdd:NF033838 401 EAKRKAA----EEDKVKEKPAEQPQ 421
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
673-1080 |
1.27e-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: 46.00 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 673 KTKNQVLKTEKEKQDISHRERLEEL--VDKQTRELQDLEccnnqKLLLEYEKYQELQLKSqrmQEEYEKQLRDndetksq 750
Cdd:pfam06160 7 KIYKEIDELEERKNELMNLPVQEELskVKKLNLTGETQE-----KFEEWRKKWDDIVTKS---LPDIEELLFE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 751 aLEELTE---FYEAK--LQEKTGLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYeRKLRDEKESNlrlkgetg 825
Cdd:pfam06160 72 -AEELNDkyrFKKAKkaLDEIEELLDDIEEDIKQILEELDELLES-EEKNREEVEELKDKY-RELRKTLLAN-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 826 imRKKFSSLQKEIEERTNDIELLKSEQMKL---------QGIIRSLEKDIQGLKR---EIQERDETIQDK-EKRIYDLKK 892
Cdd:pfam06160 141 --RFSYGPAIDELEKQLAEIEEEFSQFEELtesgdyleaREVLEKLEEETDALEElmeDIPPLYEELKTElPDQLEELKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 893 KNQELEKFKFVLDYkikelkKQIEPrenEIKVMKEQIQEMEAELERFHKQNTQLELN-ITELLQKLRATdqeMRKEQQKE 971
Cdd:pfam06160 219 GYREMEEEGYALEH------LNVDK---EIQQLEEQLEENLALLENLELDEAEEALEeIEERIDQLYDL---LEKEVDAK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 972 RDLEALVRRFKTDLHNCVAYIQEpglLKEKIRGLFEKYVQRADMVEIaglnsdlQQEYARQREHLERNLATLKKKvIKEG 1051
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKE---LKEELERVQQSYTLNENELER-------VRGLEKQLEELEKRYDEIVER-LEEK 355
|
410 420
....*....|....*....|....*....
gi 568929692 1052 ELHRTDYVRIMQENVSLIKEINELRRELK 1080
Cdd:pfam06160 356 EVAYSELQEELEEILEQLEEIEEEQEEFK 384
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
837-1102 |
1.36e-04 |
|
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: 46.37 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 837 EIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIY----DLKKKNQELEKFKFVLDYKIKELK 912
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRtlddQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 913 KQIEPRENEIKV-MKEQIQEMEAELERFHKQNTQLElnitELLQKLRATDQEMRKEQQKERDLEALVrrfKTDLHNCVAY 991
Cdd:pfam12128 322 SELEALEDQHGAfLDADIETAAADQEQLPSWQSELE----NLEERLKALTGKHQDVTAKYNRRRSKI---KEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 992 IQEPgllKEKIRGlfEKYVQRADMveiaglNSDLQQEYARQREHLERNLATLK--KKVIKE--GELH-RTDYVRIMQENV 1066
Cdd:pfam12128 395 IKDK---LAKIRE--ARDRQLAVA------EDDLQALESELREQLEAGKLEFNeeEYRLKSrlGELKlRLNQATATPELL 463
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568929692 1067 SLIK----EINELRRELKLTRSQIYDLESALKVSKKTRSQ 1102
Cdd:pfam12128 464 LQLEnfdeRIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
655-1049 |
1.66e-04 |
|
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: 45.98 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 655 TEKIKELTDKFIQEMESLKTKNQvlktEKEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKyQELQLKSQRMQ 734
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQA----AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK-QSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 735 EEY-----------EKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIK 803
Cdd:pfam12128 674 AERkdsanerlnslEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 804 TKYERKLRdekesnlrlkgETGIMRKKFSSLQKEIEERTNDIELlkseqmklqgiIRSLEKDIQGLKREIQERdeTIQDK 883
Cdd:pfam12128 754 TWYKRDLA-----------SLGVDPDVIAKLKREIRTLERKIER-----------IAVRRQEVLRYFDWYQET--WLQRR 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 884 EKRIYDLKKKNQELEKFKFVLDYKIKELKKQIepreneikvmkeqiqemeAELERFHKQNTQLELNITELLQKLRAtdqE 963
Cdd:pfam12128 810 PRLATQLSNIERAISELQQQLARLIADTKLRR------------------AKLEMERKASEKQQVRLSENLRGLRC---E 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 964 MRKeqQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEIAGLNSDLQQEYARQREhlerNLATL 1043
Cdd:pfam12128 869 MSK--LATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLRE----EDHYQ 942
|
....*.
gi 568929692 1044 KKKVIK 1049
Cdd:pfam12128 943 NDKGIR 948
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
656-970 |
1.84e-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: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 656 EKIKELTDKFIQEMESLKTKNQVLKTEKEKQdishrerlEELVDKQTRELQDLECcnNQKLLLEYE-KYQELQLKSQRMQ 734
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA--------CEIRDQITSKEAQLES--SREIVKSYEnELDPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 735 EEYEKQLRDNDETKS-QALEELTEFYEAKLQEKtglLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDE 813
Cdd:TIGR00606 259 HNLSKIMKLDNEIKAlKSRKKQMEKDNSELELK---MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 814 KESNLR---LKGETGIMRKKFSSLQKEIEERTNDIELLKSeQMKLQGIIRSLEKDIQ-----GLKREIQERD-----ETI 880
Cdd:TIGR00606 336 RLLNQEkteLLVEQGRLQLQADRHQEHIRARDSLIQSLAT-RLELDGFERGPFSERQiknfhTLVIERQEDEaktaaQLC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 881 QDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRAT 960
Cdd:TIGR00606 415 ADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS 494
|
330
....*....|
gi 568929692 961 DQEMRKEQQK 970
Cdd:TIGR00606 495 LTETLKKEVK 504
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
614-1127 |
1.97e-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: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 614 EVLVTKTDMEEKAQIMLELKTRVEELKMENEYQLRLKDMNYTEKIKELTDKFI------QEMESlKTKNQVLKTEKEKQD 687
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHtlvierQEDEA-KTAAQLCADLQSKER 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 688 IShRERLEELVDKQTRELQDLEccnNQKLLLEYEKYQELQLKSQRMQ-EEYEKQLRDNDETKSQALEELTEFYEAKLQE- 765
Cdd:TIGR00606 423 LK-QEQADEIRDEKKGLGRTIE---LKKEILEKKQEELKFVIKELQQlEGSSDRILELDQELRKAERELSKAEKNSLTEt 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 766 ---KTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQ------DIKTKYERKLRDEKESNLRLKGETGIMRKKfSSLQK 836
Cdd:TIGR00606 499 lkkEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLED 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 837 EIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYD----------LKKKNQELEKFKFVL-- 904
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgsqdeesdLERLKEEIEKSSKQRam 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 905 ----------------------------DYKIK-ELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQL--------- 946
Cdd:TIGR00606 658 lagatavysqfitqltdenqsccpvcqrVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrqs 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 947 -----ELNITELLQKLRATDQEMRKEQ----QKERDLEALVRRFKT--DLHNCVAYIQEPGLLKEKIRGLFEKYVQRADM 1015
Cdd:TIGR00606 738 iidlkEKEIPELRNKLQKVNRDIQRLKndieEQETLLGTIMPEEESakVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1016 VEI------------------------AGLNSDLQQEYARQREHLERNLATLKKKVIKEGE-LHRTDyvRIMQENVSLIK 1070
Cdd:TIGR00606 818 SDLdrtvqqvnqekqekqheldtvvskIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTnLQRRQ--QFEEQLVELST 895
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 568929692 1071 EINELRRELKLTRSQIYDLESAlkvsKKTRSQEVPESVISKDVVGSTSTMRLNEQEE 1127
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETF----LEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
770-984 |
2.01e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 770 LEEAQEDVRQQLRE-----FEETKKQIEEDEDREIQDIKTKYER---KLRDEKESNLRLKGETGIMRKK----------- 830
Cdd:PRK05771 14 LKSYKDEVLEALHElgvvhIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdvee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 831 -FSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEK------DIQ-------------GLKREIQERDETI---------- 880
Cdd:PRK05771 94 eLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyis 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 881 QDKEKRIY-------DLKKKNQELEKF---KFVLDYK--IKELKKQIEPRENEIkvmKEQIQEMEAELERFHKQNTQLEL 948
Cdd:PRK05771 174 TDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEELL 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 568929692 949 NITELLqklratdqemrkEQQKERdLEALVRRFKTD 984
Cdd:PRK05771 251 ALYEYL------------EIELER-AEALSKFLKTD 273
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
691-985 |
2.18e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 691 RERLEELVDKQTRELQDLEccnNQKLLLEYEKYQELQLKSQRmQEEYEKQLRDNDETKSQALEELTE------------- 757
Cdd:PRK04778 24 RKRNYKRIDELEERKQELE---NLPVNDELEKVKKLNLTGQS-EEKFEEWRQKWDEIVTNSLPDIEEqlfeaeelndkfr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 758 FYEAK--LQEKTGLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYeRKLRDEKESNlrlkgetgimRKKFSSLQ 835
Cdd:PRK04778 100 FRKAKheINEIESLLDLIEEDIEQILEELQELLES-EEKNREEVEQLKDLY-RELRKSLLAN----------RFSFGPAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 836 KEIEERTNDIE--LLKSEQMKLQG-------IIRSLEKDIQGLKR---EIQERDETIQDK-------------------- 883
Cdd:PRK04778 168 DELEKQLENLEeeFSQFVELTESGdyveareILDQLEEELAALEQimeEIPELLKELQTElpdqlqelkagyrelveegy 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 884 -------EKRIYDLKKKNQELEKFKFVLD-----YKIKELKKQI----EPRENEI---KVMKEQIQEMEAELERFHKQNT 944
Cdd:PRK04778 248 hldhldiEKEIQDLKEQIDENLALLEELDldeaeEKNEEIQERIdqlyDILEREVkarKYVEKNSDTLPDFLEHAKEQNK 327
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568929692 945 QLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDL 985
Cdd:PRK04778 328 ELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEIT 368
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
810-954 |
3.58e-04 |
|
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: 44.20 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 810 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGI------IRSLEKDIQGLKREIQERDETIQDK 883
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 884 EKRIYDLKKKNQEL-EKFKFVL------------------------DYKIKELKKQIEPRENEIKVMKEQIQEMEAELER 938
Cdd:pfam17060 174 DRELTELTSTISKLkDKYDFLSrefefykqhhehggnnsiktatkhEFIISELKRKLQEQNRLIRILQEQIQFDPGALHD 253
|
170
....*....|....*.
gi 568929692 939 FHKQNTQLELNITELL 954
Cdd:pfam17060 254 NGPKNLVLNGAIAAVL 269
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
777-973 |
3.70e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 777 VRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQ 856
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 857 GIIRSLEKDI-------------QGLKREiQERDETIQDK----EKRIYDLKKKNQELEKFKFVLD---YKIKELKKQIE 916
Cdd:PHA02562 269 SKIEQFQKVIkmyekggvcptctQQISEG-PDRITKIKDKlkelQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKIS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568929692 917 PRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEmRKEQQKERD 973
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT-KSELVKEKY 403
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
729-1002 |
3.78e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 729 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 803
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 804 TKYERKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQD 882
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 883 KEKRIYD----LKKKNQELEkfkfvldykikELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLeLNITELLQKLR 958
Cdd:PRK01156 620 SIREIENeannLNNKYNEIQ-----------ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRI-NDIEDNLKKSR 687
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568929692 959 ATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKI 1002
Cdd:PRK01156 688 KALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
763-1152 |
3.85e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 763 LQEKTGLLEEAQEDVRQQLREFEETKKQIEEDE------DREIQDIKTKYERKLRDEKESNLRLKGETGI---------- 826
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEkshsitLKEIERLSIEYNNAMDDYNNLKSALNELSSLedmknryese 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 827 MRKKFSSLQ---------KEIEERTNDIELLKS--------EQMKLQGIIRSLEKDIQGLKREIQERDETIQ-------- 881
Cdd:PRK01156 258 IKTAESDLSmeleknnyyKELEERHMKIINDPVyknrnyinDYFKYKNDIENKKQILSNIDAEINKYHAIIKklsvlqkd 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 882 -----DKEKRIYDLKKKNQELEKFKfvLDY-----KIKELKKQIEPRENEIKVMKEQI-----------QEMEAELERFH 940
Cdd:PRK01156 338 yndyiKKKSRYDDLNNQILELEGYE--MDYnsylkSIESLKKKIEEYSKNIERMSAFIseilkiqeidpDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 941 KQNTQLELNITELLQKLRATDQemrKEQQKERDLEALVRRFK-----TDL------HNCVAYIQEPGLLKEKIR------ 1003
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALRE---NLDELSRNMEMLNGQSVcpvcgTTLgeeksnHIINHYNEKKSRLEEKIReieiev 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1004 -GLFEKYVQRADMVE-IAG------LNSDLQQEYAR-QREHLERNLATLKKKVIKEGEL--------------HRTDYVR 1060
Cdd:PRK01156 493 kDIDEKIVDLKKRKEyLESeeinksINEYNKIESARaDLEDIKIKINELKDKHDKYEEIknrykslkledldsKRTSWLN 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1061 IMQEnVSLIkEINELRRELKLTRSQIYDLESALK---VSKKTRSQEVPESVISKDVVGSTSTMRLNEQEETGRIIEMQRL 1137
Cdd:PRK01156 573 ALAV-ISLI-DIETNRSRSNEIKKQLNDLESRLQeieIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRG 650
|
490
....*....|....*
gi 568929692 1138 EIRRLRDQIQEQEQV 1152
Cdd:PRK01156 651 KIDNYKKQIAEIDSI 665
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
676-1093 |
4.25e-04 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 44.57 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 676 NQVLKTEKEKQDIsHRERLE--ELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRD---------- 743
Cdd:PTZ00332 134 NAIAKMEKVEEEL-RRSQLDatQLAQVPTATLKNIEDIMNVTQIQNALASTDDQIKTQLAQLEKTNEIQNvamhdgemqv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 744 ---NDETKSQALEELTEFyeakLQEKTGLLEEAqEDVRQQLREFEETKKQIEEdEDREIQDIKtkyeRKLRDEKESNLrl 820
Cdd:PTZ00332 213 aeeQMWTKVQLQERLIEL----VADKFRLIGKC-EEENKSFSKIHEVQKQANQ-ETSQMKDAK----RRLKQRCETDL-- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 821 kgetgimrkkfsslqKEIEERTNDIELLKSEQMKLQGIIRslEKDiqglKREIQERDETIQDKEKRIYDLKKKNQELEKF 900
Cdd:PTZ00332 281 ---------------KHIHDAIQKADLEDAEAMKRYATNK--EKS----ERFIRENEDRQEEAWNKIQDLERQLQRLGTE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 901 KFvldykiKELKKQIEP--RENEIKVMKEQIQEMEAE---LERFHKQNTQLELNITELLQKLRA------------TDQE 963
Cdd:PTZ00332 340 RF------EEVKRRIEEndREEKRRVEYQQFLEVAGQhkkLLELTVYNCDLALRCTGLVEELVSegcaavkarhdkTNQD 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 964 M---RKEQQKERdLEALVRRFKTdlHNCVAYIQEPgLLKEKIRGLFEKYVQRADMVEI----AGLNSDLQQEYARQREHL 1036
Cdd:PTZ00332 414 LaalRLQVHKEH-LEYFRMLYLT--LGSLIYKKEK-RLEEIDRNIRTTHIQLEFCVETfdpnAKKHADMKKELYKLRQGV 489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568929692 1037 ERNLATLKKKVIKEGELHRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESAL 1093
Cdd:PTZ00332 490 EEELAMLKEKQAQALEMFKESEEALDAAGIEFVHPVDENNEEVLTRRSKMVEYRSHL 546
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
679-926 |
5.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 679 LKTEKEKQDISH----RERLEELVDKQTRELQDL-ECCNNQKLLLEYEKYQELQ--LKSQRMQEEYEKQLRDNDETKSQA 751
Cdd:PRK01156 462 LGEEKSNHIINHynekKSRLEEKIREIEIEVKDIdEKIVDLKKRKEYLESEEINksINEYNKIESARADLEDIKIKINEL 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 752 LEELTEFYEAKLQEKTGLLEEAQE---------------DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYERKL 810
Cdd:PRK01156 542 KDKHDKYEEIKNRYKSLKLEDLDSkrtswlnalavisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 811 R--DEKESNLRLKgetgimRKKFSSLQKEIEERTNDIELLKSEQMKLQGIirslEKDIQGLKREIQERDETIQDKEKRIY 888
Cdd:PRK01156 622 ReiENEANNLNNK------YNEIQENKILIEKLRGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALD 691
|
250 260 270
....*....|....*....|....*....|....*...
gi 568929692 889 DLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMK 926
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
753-891 |
5.34e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.23 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 753 EELTEFYeAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---RKLRDEKESNLRLKGEtgimrk 829
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 830 kfssLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLK 891
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
889-1151 |
5.78e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 889 DLKKKNQ-ELEKfkfvLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNI---TELLQKLRATDQEM 964
Cdd:pfam05667 328 ELQQQREeELEE----LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYkvkKKTLDLLPDAEENI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 965 RKEQQK----ERDLEALVRRFKTdlHNcVAYIQEPGLLKEKIRGLFEKYVQRADmvEIAGLNSDLQQ--EYARQREHLER 1038
Cdd:pfam05667 404 AKLQALvdasAQRLVELAGQWEK--HR-VPLIEEYRALKEAKSNKEDESQRKLE--EIKELREKIKEvaEEAKQKEELYK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1039 NLATLKKKVIKEGelHRTDYVRIMQENVSLIK----EINELRRELKLTRSQIYDLESALKvskktRSQEVPESVISKDVV 1114
Cdd:pfam05667 479 QLVAEYERLPKDV--SRSAYTRRILEIVKNIKkqkeEITKILSDTKSLQKEINSLTGKLD-----RTFTVTDELVFKDAK 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568929692 1115 GSTS---------TMRLN-EQ-----EETGRIIEmqrlEIRRLRDQIQEQEQ 1151
Cdd:pfam05667 552 KDESvrkaykylaALHENcEQliqtvEETGTIMR----EIRDLEEQIETESG 599
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
387-416 |
5.95e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 5.95e-04
10 20 30
....*....|....*....|....*....|
gi 568929692 387 HSASITGLDTCIRKPLIATCSLDRSVRIWN 416
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
837-1046 |
6.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 837 EIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKriydlkkknqelekfkfvldyKIKELKKQIE 916
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---------------------EIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 917 PRENEIKVMKEQIQEMEAELERFHKQNTQLEL-----NITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAY 991
Cdd:COG3883 76 EAEAEIEERREELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568929692 992 IQEPGLLKEKIRGLfEKYVQRAdMVEIAGLNSDLQQEYARQREHLERNLATLKKK 1046
Cdd:COG3883 156 LAELEALKAELEAA-KAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
614-977 |
6.74e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 614 EVLVTKTDMEEKAQIMLELKTRVEELKMENE----YQLRLKDMNytEKIKELTDKF-IQEMESLKTKN------QVLKTE 682
Cdd:pfam05557 126 ELQSTNSELEELQERLDLLKAKASEAEQLRQnlekQQSSLAEAE--QRIKELEFEIqSQEQDSEIVKNskselaRIPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 683 KEKQDI-SHRERLEELvdKQTRELQDLECCNNQKLLLEYEKYQE----LQLKSQRMQEEYE--KQLRDNDETKSQALEEL 755
Cdd:pfam05557 204 KELERLrEHNKHLNEN--IENKLLLKEEVEDLKRKLEREEKYREeaatLELEKEKLEQELQswVKLAQDTGLNLRSPEDL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 756 TEFYEAKLQEKTGLLEEaQEDVRQQLREFEETKKQIEEDED---REIQDIKTKYERK---LRDEKESNLRLKGETGIMRK 829
Cdd:pfam05557 282 SRRIEQLQQREIVLKEE-NSSLTSSARQLEKARRELEQELAqylKKIEDLNKKLKRHkalVRRLQRRVLLLTKERDGYRA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 830 KFSSLQKEIEERTNDIELLKS----EQM--KLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFV 903
Cdd:pfam05557 361 ILESYDKELTMSNYSPQLLERieeaEDMtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929692 904 LDYKikELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTqLELNITELLQkLRATDQEMRKEQQKErDLEAL 977
Cdd:pfam05557 441 EEVD--SLRRKLETLELERQRLREQKNELEMELERRCLQGD-YDPKKTKVLH-LSMNPAAEAYQQRKN-QLEKL 509
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
749-1035 |
6.95e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.53 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 749 SQALEEL------TEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERkLRDEKESNLRLKG 822
Cdd:pfam04108 20 RSLLEELvvllakIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDK-LRNTPVEPALPPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 823 ETG-------IMRKKFSSLQKEIEErtnDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDEtIQDKEKRIYDLKKKNQ 895
Cdd:pfam04108 99 EEKqktlldfIDEDSVEILRDALKE---LIDELQAAQESLDSDLKRFDDDLRDLQKELESLSS-PSESISLIPTLLKELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 896 ELEK------FKFVLDY-KIKELKKQIEPRENE---------------IKVMKEQIQEMEAELERFHKQNTQLELNITEL 953
Cdd:pfam04108 175 SLEEemasllESLTNHYdQCVTAVKLTEGGRAEmlevlendarelddvVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 954 ---LQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYV-----QRADMVEIAGLNSDL 1025
Cdd:pfam04108 255 lsaLQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSLLleverRREWAEKMKKILRKL 334
|
330
....*....|
gi 568929692 1026 QQEYARQREH 1035
Cdd:pfam04108 335 AEELDRLQEE 344
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
676-980 |
8.09e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 676 NQVLKTEKEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQ----ELQLKSQRMQEEYEKQLRDNDETKSQA 751
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 752 LEELTEFYEAKLQEKTGLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKF 831
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 832 SSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKnqelekfkfvldyKIKEL 911
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR-------------LAEEA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929692 912 KKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQ----LELNITELLQKLRATDQEMRKEQQKERDLEALVRR 980
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEhrreLEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
384-416 |
9.59e-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: 9.59e-04
10 20 30
....*....|....*....|....*....|...
gi 568929692 384 YPLHSASITGLDTCIRKPLIATCSLDRSVRIWN 416
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
636-937 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 636 VEELKMENEYQLRLKDMN-YTEKIKELTDKFIQEMESLKTknqVLKTEKE-KQDISHRERLEELVDKQTRELQDLECcNN 713
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDeCIKKIKELKNHILSEESNIDT---YFKNADEnNENVLLLFKNIEMADNKSQHILKIKK-DN 1476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 714 QKLLLEYE--KYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKtglLEEAQEDVRQQLREF 784
Cdd:TIGR01612 1477 ATNDHDFNinELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEI 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 785 EETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKE--------IEERTNDIeLLKSEQMKLQ 856
Cdd:TIGR01612 1554 KDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFEnkflkisdIKKKINDC-LKETESIEKK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 857 giIRSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKK----NQELEKFKFVLDYKIKELKKQIEPRENEI-K 923
Cdd:TIGR01612 1633 --ISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKEldelDSEIEKIEIDVDQHKKNYEIGIIEKIKEIaI 1710
|
330
....*....|....
gi 568929692 924 VMKEQIQEMEAELE 937
Cdd:TIGR01612 1711 ANKEEIESIKELIE 1724
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
848-971 |
1.35e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 848 LKSEQMKLQGIIRSLEKDIQGLKREI--QERDETIQDKEKRIYDLKKKNQELEKfkfvldykikeLKKQIEPRENEIKVM 925
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQK-----------LEKRLLQKEENLDRK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568929692 926 KEQIQEMEAELERFHKQNTQLELNITELLQKLratdQEMRKEQQKE 971
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEEL----EELIEEQLQE 143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
622-980 |
1.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 622 MEEKAQIMLELKTRVEELKMENEYQLRLKdmnytEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQ 701
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELE-----EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 702 TRELQDLECCNNQkllLEYEKYQELQLKSQRMQEEYEKQLRDND------------ETKSQALEELTEFYEAKLQEKTGL 769
Cdd:COG4717 209 AELEEELEEAQEE---LEELEEELEQLENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 770 L------EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKkfssLQKEIEERTN 843
Cdd:COG4717 286 LallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE----LLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 844 DIELLKSEQMKLQGIIRSLEKDIQGLkREIQERDETIQDKEKRIYDLKKK-NQELEKFKFVLDY--------KIKELKKQ 914
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEEL-RAALEQAEEYQELKEELEELEEQlEELLGELEELLEAldeeeleeELEELEEE 440
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929692 915 IEPRENEIKVMKEQIQEMEAELERFHKQNTqlelnITELLQKlratdQEMRKEQQKERDLEALVRR 980
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGE-----LAELLQE-----LEELKAELRELAEEWAALK 496
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-189 |
1.44e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 42.59 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 26 DEQIIIFPSGNHCVK-YNID-QKWQKFIAGSdkSQGMLALAISPNRRYLAiseTVQEKPAVTIYELSSipcrkRKVLNNF 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 104 DFQVQKFTSMAFSPDSKYLLTQTSppDSNLVYWLWEKQKVMAIIKADSqnNPIYQVSISSqDNSQVcITGS--GVFKLLR 181
Cdd:COG2319 285 TGHSGGVNSVAFSPDGKLLASGSD--DGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSP-DGKTL-ASGSddGTVRLWD 358
|
....*...
gi 568929692 182 FAEGTLKQ 189
Cdd:COG2319 359 LATGELLR 366
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
629-1129 |
1.47e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.01 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 629 MLELKTR----VEELKMENEyqlrlKDMNYTEKIkeltDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELvdkqtre 704
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKETLAKQHKEAMAVF------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 705 lqdleccnnqkllleyekYQELQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEA------KLQEKtglLEEAQEDV 777
Cdd:pfam15818 66 ------------------KKQLQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKAlqvskySLQKK---VSEMEQKL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 778 RQQLREFEETKKQIEEDEdreiqdiktKYERKLrdekesnlrlKGETGIMRKKFSSLQKEIEERtndIELLKseqmKLQG 857
Cdd:pfam15818 123 QLHLLAKEDHHKQLNEIE---------KYYATI----------TGQFGLVKENHGKLEQNVQEA---IQLNK----RLSA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 858 IIRSLEKDIQGLKREiqerdetiqdkekriydLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQeMEAEL- 936
Cdd:pfam15818 177 LNKKQESEICSLKKE-----------------LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLN-MELELn 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 937 ERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEAlvrrfktdlhncvayiqEPGLLKEKIRGLfekyvQRadmv 1016
Cdd:pfam15818 239 KKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEA-----------------ELKALKENNQTL-----ER---- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1017 eiaglNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLEsalKVS 1096
Cdd:pfam15818 293 -----DNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQK---KFE 364
|
490 500 510
....*....|....*....|....*....|....*...
gi 568929692 1097 KKTRSQEVPE-----SVISKDVVGSTSTMRLNEQEETG 1129
Cdd:pfam15818 365 EDKKFQNVPEvnnenSEMSTEKSENLIIQKYNSEQEIR 402
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
826-1090 |
1.47e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 42.52 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 826 IMRKKFSSLQKEIEERTNDI-------ELLKSEQMKLQGiirslekDIQGLKREIQERDETIQDK-----EKRIYDLKkk 893
Cdd:COG4477 21 IMRKKHYKEIDRLEERKLEImnrpvldELSKVKKLNLSG-------QTEEKFEEWRQKWDEIVTKqlpeiEELLFDAE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 894 nQELEKFKFvldykiKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRatdqEMRKEQQKERD 973
Cdd:COG4477 92 -EAADKFRF------KKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYR----ELRKTLLAHRH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 974 --------LEALVRRFKTDLHNCVAYIQEpG----------LLKEKIRGLFEKyvqradMVEIAGLNSDLQQEYARQREH 1035
Cdd:COG4477 161 sfgpaaeeLEKQLEELEPEFEEFEELTES-GdyleareileQLEEELNALEEL------MEEIPPLLKELQTELPDQLEE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568929692 1036 LERNLATLKKKvikegelhrtDYVRimqENVSLIKEINELRRELKLTRSQIYDLE 1090
Cdd:COG4477 234 LKSGYREMKEQ----------GYVL---EHLNIEKEIEQLEEQLKEALELLEELD 275
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
503-606 |
1.59e-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: 41.94 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 503 NINILKGHTGKIlreipafdviyTSITISHSGRMIFVGTSVGTIRamKYPLSLQKEYNEYQAHAGPVMKMLLTFDDQFLL 582
Cdd:cd00200 1 LRRTLKGHTGGV-----------TCVAFSPDGKLLATGSGDGTIK--VWDLETGELLRTLKGHTGPVRDVAASADGTYLA 67
|
90 100
....*....|....*....|....
gi 568929692 583 TVGEDGCLftwKVFDKDGRGIKRE 606
Cdd:cd00200 68 SGSSDKTI---RLWDLETGECVRT 88
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
914-1151 |
1.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 914 QIEPRENEIKVmkEQIQEMEAELERFhkqNTQLEL-----NITELLQKLRATDQEMRKEQQKERDLEALVRRFK------ 982
Cdd:COG3206 60 LVEPQSSDVLL--SGLSSLSASDSPL---ETQIEIlksrpVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTvepvkg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 983 TDLHNcVAYI-QEPGLLKEKIRGLFEKYVQRadmveiaglNSDLQQEYARQ-REHLERNLATLKKKVIK-EGELH----R 1055
Cdd:COG3206 135 SNVIE-ISYTsPDPELAAAVANALAEAYLEQ---------NLELRREEARKaLEFLEEQLPELRKELEEaEAALEefrqK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1056 TDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESALK-VSKKTRSQEVPESVISKDVVGSTSTMRLNEQEetGRIIEM 1134
Cdd:COG3206 205 NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELE--AELAEL 282
|
250 260
....*....|....*....|...
gi 568929692 1135 QRL------EIRRLRDQIQEQEQ 1151
Cdd:COG3206 283 SARytpnhpDVIALRAQIAALRA 305
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
690-984 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 690 HRERLEELVDKQTRELQDLEccNNQKLLLEYEKYQELQLKSQRMQEEY---EKQLRDNDETKS--QALEELTEFYEAKLQ 764
Cdd:COG4913 625 ELAEAEERLEALEAELDALQ--ERREALQRLAEYSWDEIDVASAEREIaelEAELERLDASSDdlAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 765 EKTGLLEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSS----LQKEI 838
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRleAAEDLARLELRALLEERFAAALGDAVERELRENLEEridaLRARL 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 839 EERTNDIELLKSE-----QMKLQGIIRSLEK--DIQGLKREIQERDetIQDKEKRIYDLKKKNQElekfkfvldYKIKEL 911
Cdd:COG4913 783 NRAEEELERAMRAfnrewPAETADLDADLESlpEYLALLDRLEEDG--LPEYEERFKELLNENSI---------EFVADL 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 912 KKQIeprENEIKVMKEQIQEMEAELE----------RFHKQNTQLElNITELLQKLR-----ATDQEMRKEQQKERDLEA 976
Cdd:COG4913 852 LSKL---RRAIREIKERIDPLNDSLKripfgpgrylRLEARPRPDP-EVREFRQELRavtsgASLFDEELSEARFAALKR 927
|
....*...
gi 568929692 977 LVRRFKTD 984
Cdd:COG4913 928 LIERLRSE 935
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
771-976 |
1.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 771 EEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYERklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIELLKS 850
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA----ELDALQAELEE------------------LNEEYNELQAELEALQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 851 EQMKLQGIIRSLEKDIQGLKREIQERD-------------------------ETIQDKEKRIYD-LKKKNQELEKFKFVL 904
Cdd:COG3883 73 EIAEAEAEIEERREELGERARALYRSGgsvsyldvllgsesfsdfldrlsalSKIADADADLLEeLKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 905 DYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEA 976
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
625-1104 |
1.89e-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: 42.52 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 625 KAQIMLELKTRVEELKMENEYQLRLKDMNYTEKIKELtdkfiQEMES-LKTKNQVLKTEKEKQDISHRERLEEL------ 697
Cdd:pfam12128 381 RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDL-----QALESeLREQLEAGKLEFNEEEYRLKSRLGELklrlnq 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 698 VDKQTRELQDLEccNNQKLLleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFyEAKLQEKTGLLEEAQEDV 777
Cdd:pfam12128 456 ATATPELLLQLE--NFDERI---ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQA-SRRLEERQSALDELELQL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 778 RQQ---LREFEETKKQIEEDE--------------------DREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSL 834
Cdd:pfam12128 530 FPQagtLLHFLRKEAPDWEQSigkvispellhrtdldpevwDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKA 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 835 QKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQdkekRIYDLK-----KKNQELEKFKFVLDYKIK 909
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR----RLFDEKqsekdKKNKALAERKDSANERLN 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 910 ELKKQIEPRENEIKVMKEQIQEMEAELeRFHKQNTQLELnITELLQKLRATDQEMRK------------EQQKERDLEAL 977
Cdd:pfam12128 686 SLEAQLKQLDKKHQAWLEEQKEQKREA-RTEKQAYWQVV-EGALDAQLALLKAAIAArrsgakaelkalETWYKRDLASL 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 978 ------VRRFKTDLHNCVAYIQEPGLLKEKIRGLF----EKYVQRAD-----MVEIAGLNSDLQQEYARQ-------REH 1035
Cdd:pfam12128 764 gvdpdvIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqETWLQRRPrlatqLSNIERAISELQQQLARLiadtklrRAK 843
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 1036 LERNLATLKKKVIKEGELHRTdyVRIMQENVSLIKE---INELRRELKLTRSQIYDLESALKVSKKTRSQEV 1104
Cdd:pfam12128 844 LEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEdanSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYV 913
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
792-1105 |
2.01e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 792 EEDEDREIQDIKTKYERKLRDEKESNLRlKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMK-LQGIIRSLEKDIQGLK 870
Cdd:PLN02939 70 DENGQLENTSLRTVMELPQKSTSSDDDH-NRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEdLVGMIQNAEKNILLLN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 871 reiQERDETIQDKEKRIYDLKKKNQELEkfkfVLDYKIKELKKQIE-----------PRENEIKVMKEQIQEMEA----- 934
Cdd:PLN02939 149 ---QARLQALEDLEKILTEKEALQGKIN----ILEMRLSETDARIKlaaqekihveiLEEQLEKLRNELLIRGATeglcv 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 935 -----ELERFHKQNTQLELNITELLQKL---RATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLK-----EK 1001
Cdd:PLN02939 222 hslskELDVLKEENMLLKDDIQFLKAELievAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQydcwwEK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1002 IRGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLErnlATLKKKVIKEGELHRTDyvrIMQENVSLIKEINELRRELKL 1081
Cdd:PLN02939 302 VENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE---ASLKEANVSKFSSYKVE---LLQQKLKLLEERLQASDHEIH 375
|
330 340 350
....*....|....*....|....*....|..
gi 568929692 1082 TRSQIY--------DLESALKVSKKTRSQEVP 1105
Cdd:PLN02939 376 SYIQLYqesikefqDTLSKLKEESKKRSLEHP 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
755-1040 |
2.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 755 LTEFYEAKLQEKTGLLEEAqEDVRQQLREFEETKKQIEEDEDR-----EIQDIKTKYERKLRDekesnlrlKGETGIMRK 829
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAA-DALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARER--------LAELEYLRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 830 KFSSLQKEIEertndIELLKSEqmklqgiIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKnqelekfkfvldykIK 909
Cdd:COG4913 280 ALRLWFAQRR-----LELLEAE-------LEELRAELARLEAELERLEARLDALREELDELEAQ--------------IR 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 910 ELK-KQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDlhnc 988
Cdd:COG4913 334 GNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---- 409
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568929692 989 vayiqepglLKEKIRGLFEKYVQRADmvEIAGL---NSDLQQEYARQREHLERNL 1040
Cdd:COG4913 410 ---------AEAALRDLRRELRELEA--EIASLerrKSNIPARLLALRDALAEAL 453
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
342-461 |
2.17e-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: 41.83 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 342 CLCFSPSEETLIASTNKNQLYSI---TMSLTEISKGEAahfeyllyplhSASITGLDTCIRKPLIATCSLDRSVRIWNYE 418
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKGKC-----------GGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568929692 419 SNTLeLYKEYqeeaytvslhpsghyivvgfaDKLRLMNLLIDD 461
Cdd:cd22857 297 TRQL-LSKVY---------------------LKQRLTAVVFDS 317
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
656-985 |
2.18e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 656 EKIKELTDKF---IQEMESLKTKNQVLKTE-KEKQDISHRE--RLEELVDKQTRELQDleccnnqkllleyekyQELQLK 729
Cdd:pfam00038 4 EQLQELNDRLasyIDKVRFLEQQNKLLETKiSELRQKKGAEpsRLYSLYEKEIEDLRR----------------QLDTLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 730 SQRMQEEYEkqlRDNdetksqaLEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEET-------KKQIEEDEDrEIQDI 802
Cdd:pfam00038 68 VERARLQLE---LDN-------LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEAtlarvdlEAKIESLKE-ELAFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 803 KTKYERKLRDekesnlrlkgetgimrkkfssLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGL-KREIQERDETIQ 881
Cdd:pfam00038 137 KKNHEEEVRE---------------------LQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIaAKNREEAEEWYQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 882 DKEKRIYDLKKKNQElekfkfvldykikelkkQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLratD 961
Cdd:pfam00038 196 SKLEELQQAAARNGD-----------------ALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERY---E 255
|
330 340
....*....|....*....|....
gi 568929692 962 QEMRKEQQKERDLEALVRRFKTDL 985
Cdd:pfam00038 256 LQLADYQELISELEAELQETRQEM 279
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
635-1003 |
2.18e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 635 RVEELKMENEYQLRLKDmNYTEKIKELTDKfIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRElQDLECCNNQ 714
Cdd:TIGR01612 1230 KIDEEKKKSEHMIKAME-AYIEDLDEIKEK-SPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD-ENISDIREK 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 715 KLLLEYEKYQELQLKSqrMQEEYEKQLRDNDETKS---QALEELTEFYEA-----------KLQEKTGLLEEAQEDVRQQ 780
Cdd:TIGR01612 1307 SLKIIEDFSEESDIND--IKKELQKNLLDAQKHNSdinLYLNEIANIYNIlklnkikkiidEVKEYTKEIEENNKNIKDE 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 781 LREFEETKKQIEEDEDreIQDIKTKYERKLRDekesnlrlkgetgimrkkfsslqKEIEERTNDIELLKSEqmklqgiIR 860
Cdd:TIGR01612 1385 LDKSEKLIKKIKDDIN--LEECKSKIESTLDD-----------------------KDIDECIKKIKELKNH-------IL 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 861 SLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFK-----FVLDYKIKELKKQIEprenEIKVMKEQIQEMEAE 935
Cdd:TIGR01612 1433 SEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFNINELKEHID----KSKGCKDEADKNAKA 1508
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 936 LERFHKQNTQLELNITELLQKLRATDQEMRKEQQKeRDLEALVRRFKtDLHNcvAYIQEPGLLKEKIR 1003
Cdd:TIGR01612 1509 IEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIK-DAHK--KFILEAEKSEQKIK 1572
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
880-1003 |
2.29e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 880 IQDKEKRIYDLKK------------KNQELEKFKFVLDykikELKKQIEPRENEIKVMKEQIQEMEA----ELERFHKQN 943
Cdd:pfam09787 20 LQSKEKLIASLKEgsgvegldsstaLTLELEELRQERD----LLREEIQKLRGQIQQLRTELQELEAqqqeEAESSREQL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 944 TQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCvayIQEPGLLKEKIR 1003
Cdd:pfam09787 96 QELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR---IKDREAEIEKLR 152
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
667-897 |
2.31e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.15 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 667 QEMESLKTKNQVLKTEKEKqdishrerleelvDKQTreLQDLEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDE 746
Cdd:pfam09726 444 QENDLLQTKLHNAVSAKQK-------------DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 747 TKSQALEELTEFYEAKLQEKTglLEEAQEDVRQQLREFE-ETKK-----QIEEDEDREIqDIKTKyerKLRDEKESnlrl 820
Cdd:pfam09726 492 KKRKKEEEATAARAVALAAAS--RGECTESLKQRKRELEsEIKKlthdiKLKEEQIREL-EIKVQ---ELRKYKES---- 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568929692 821 KGETGIMRKKFSSLQKEIEERTNDielLKSE-QMKLqgiirSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 897
Cdd:pfam09726 562 EKDTEVLMSALSAMQDKNQHLENS---LSAEtRIKL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
858-986 |
2.35e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 858 IIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEikvmKEQIQEMEAELE 937
Cdd:pfam13851 20 ITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568929692 938 RFHKQNTQLELNITELLQKLratdqemrkeQQKERDLEALVRRFKTDLH 986
Cdd:pfam13851 96 VLEKELKDLKWEHEVLEQRF----------EKVERERDELYDKFEAAIQ 134
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
502-1066 |
2.50e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 502 ENINILKGHTGKILREIPAFDVIYTSITISHSGRMIFVGTSVGTIRAMKYPLSLQKEYNEYQAHAGPVMKMLLTFDDQFL 581
Cdd:TIGR01612 292 EHAAITHEHIDAELNDIKKHPMINDKELRPHGKRLIKILESEGEQGHIINKLIFLEKEFEDTIHKSDIYKDECLSNHLFM 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 582 LT-VGEDGCLFTWKVFDKDGRGIKREREVGF--AEEVLVTKTDMEEKAQIMLELKTRVEELKMENeyqlrlKDMNYTEKI 658
Cdd:TIGR01612 372 EDyLKDDKISPYYYEFLEEIKKIAKQRAIFFynAKKLKHLEILYKHQEDILNNFHKTIERLIFEK------PDPNNNNIF 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 659 KELTDKFIQEMEslKTKNQVLKT---EKEKQDISHRErLEELVDKQTRelQDleccNNQKLLLEYEKyqELQLKSQRMqE 735
Cdd:TIGR01612 446 KDDFDEFNKPIP--KSKLKALEKrffEIFEEEWGSYD-IKKDIDENSK--QD----NTVKLILMRMK--DFKDIIDFM-E 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 736 EYEkqlRDNDETKSQALEELTEFYEAKL-QEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIqdiktKYERKLRDEK 814
Cdd:TIGR01612 514 LYK---PDEVPSKNIIGFDIDQNIKAKLyKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSI-----HLEKEIKDLF 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 815 ESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKsEQMKLQGIIRSLEKDIQGLKR--------EIQERDE---TIQDK 883
Cdd:TIGR01612 586 DKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIK-KAIDLKKIIENNNAYIDELAKispyqvpeHLKNKDKiysTIKSE 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 884 EKRIY--DLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNitellqKLRATD 961
Cdd:TIGR01612 665 LSKIYedDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKN------ELLDII 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 962 QEMRKEQQKE--RDLEALVRRFK-------TDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEIAglNSDLQQEYARQ 1032
Cdd:TIGR01612 739 VEIKKHIHGEinKDLNKILEDFKnkekelsNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIK--DEDAKQNYDKS 816
|
570 580 590
....*....|....*....|....*....|....*
gi 568929692 1033 REHlernlatLKKKVIKEGELHRT-DYVRIMQENV 1066
Cdd:TIGR01612 817 KEY-------IKTISIKEDEIFKIiNEMKFMKDDF 844
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
712-812 |
2.80e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 712 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQI 791
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 568929692 792 EEDEDREIQDIKTKYERKLRD 812
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
835-1147 |
2.82e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 835 QKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQglkrEIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQ 914
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEIS----NIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 915 IEPRENEIKVMKEQIQEMEAELERFHKQNTQlelnitellqkLRATDQEMRKEQQKERDLEALVRRFKtDLHNCVAYIQe 994
Cdd:PRK01156 227 YNNAMDDYNNLKSALNELSSLEDMKNRYESE-----------IKTAESDLSMELEKNNYYKELEERHM-KIINDPVYKN- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 995 pgllKEKIRGLFEKYVQRADMVEI-AGLNSDLQQEYARQREhlernLATLKKkvikegelHRTDYVRIMQENVSLIKEIN 1073
Cdd:PRK01156 294 ----RNYINDYFKYKNDIENKKQIlSNIDAEINKYHAIIKK-----LSVLQK--------DYNDYIKKKSRYDDLNNQIL 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929692 1074 ELRRELKLTRSQIYDLESalkVSKKTRSQEvpesvISKDVVGSTSTMRLNEQEETGRIIEMQRLEIRRLRDQIQ 1147
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIES---LKKKIEEYS-----KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
692-939 |
3.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 692 ERLEELVDKqtreLQDLEccnnQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEktglLE 771
Cdd:PRK00409 516 EKLNELIAS----LEELE----RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE----AK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 772 EAQEDVRQQLREFEetKKQIEEDEDREIQDIKTKYERKLrDEKESNLRLKGETgimrkkfsslQKEIEErtND-IELLKS 850
Cdd:PRK00409 584 KEADEIIKELRQLQ--KGGYASVKAHELIEARKRLNKAN-EKKEKKKKKQKEK----------QEELKV--GDeVKYLSL 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 851 EQMklqGIIRSLEKDiqglkREIQERDETIQDKEKrIYDLKK-KNQELEKFKfvldyKIKELKKQIEPRENEIKVMKEQI 929
Cdd:PRK00409 649 GQK---GEVLSIPDD-----KEAIVQAGIMKMKVP-LSDLEKiQKPKKKKKK-----KPKTVKPKPRTVSLELDLRGMRY 714
|
250
....*....|
gi 568929692 930 QEMEAELERF 939
Cdd:PRK00409 715 EEALERLDKY 724
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
728-902 |
3.41e-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: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 728 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTGLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 804
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 805 kyERKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIqdKE 884
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 568929692 885 KRIYDLKKKNQELEKFKF 902
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
667-1103 |
3.96e-03 |
|
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: 41.21 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 667 QEMESLKTKNQVLKTEKEK--QDISHRERLEELVDKQTRELQDLEccnNQKLLLEYEKYQ------ELQLKSQRMQEEY- 737
Cdd:pfam05622 21 QQVSLLQEEKNSLQQENKKlqERLDQLESGDDSGTPGGKKYLLLQ---KQLEQLQEENFRletardDYRIKCEELEKEVl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 738 EKQLRDNDETK----SQAL-EELTEFYEAklQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTK--YERKL 810
Cdd:pfam05622 98 ELQHRNEELTSlaeeAQALkDEMDILRES--SDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTlqLEEEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 811 RdeKESNLRLKGETgiMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQglkREIQERDEtiqdkekriydL 890
Cdd:pfam05622 176 K--KANALRGQLET--YKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKE---RLIIERDT-----------L 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 891 KKKNQELEKFKFVLDYKIKE---LKKQIEPRENEIKVM-----KEQIQEMEAELERFH-KQNTQLELNITELLQKLRATD 961
Cdd:pfam05622 238 RETNEELRCAQLQQAELSQAdalLSPSSDPGDNLAAEImpaeiREKLIRLQHENKMLRlGQEGSYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 962 Q-------EMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVE-----IAGLNSDLQQEY 1029
Cdd:pfam05622 318 RrkneletQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQkkkeqIEELEPKQDSNL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1030 ARQREHLERNLaTLKKKVIKEGELHRTDYVRIMQE---------NVSLIKEINELRRELKLTRSQIYDLESALKVSKKTR 1100
Cdd:pfam05622 398 AQKIDELQEAL-RKKDEDMKAMEERYKKYVEKAKSviktldpkqNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQR 476
|
...
gi 568929692 1101 SQE 1103
Cdd:pfam05622 477 EQE 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
907-1152 |
4.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 907 KIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLH 986
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 987 ncvayiQEPGLLKEKIRGLFEkyvqradMVEIAGLNSDLQQEYARQrehLERNLATLKkkvikegelhrtdyvRIMQENV 1066
Cdd:COG4942 101 ------AQKEELAELLRALYR-------LGRQPPLALLLSPEDFLD---AVRRLQYLK---------------YLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1067 SLIKEINELRRELKLTRSQIydlesalkvskktrsqevpesviskdvvgststmrLNEQEETGRIIEMQRLEIRRLRDQI 1146
Cdd:COG4942 150 EQAEELRADLAELAALRAEL-----------------------------------EAERAELEALLAELEEERAALEALK 194
|
....*.
gi 568929692 1147 QEQEQV 1152
Cdd:COG4942 195 AERQKL 200
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
657-783 |
5.09e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 657 KIKELTDKFIQEMES-----LKTKNQVLKTEKEKQdishrerleelVDKQTRELQDLEccnnQKLLLEYEKYQELQLKSQ 731
Cdd:cd16269 167 KAEEVLQEFLQSKEAeaeaiLQADQALTEKEKEIE-----------AERAKAEAAEQE----RKLLEEQQRELEQKLEDQ 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568929692 732 -RMQEEYEKQLRDN-DETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLRE 783
Cdd:cd16269 232 eRSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE 285
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
724-804 |
5.44e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.19 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 724 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 803
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 568929692 804 T 804
Cdd:cd06503 117 K 117
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
879-1047 |
6.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 879 TIQDKEKRIYDLkkknQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITElLQKLR 958
Cdd:COG1579 1 AMPEDLRALLDL----QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-VEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 959 ATDQEMRKEQQKERDLEALVRRfktdlhncVAYIQ-EPGLLKEKIRGLFEKY-VQRADMVEIAGLNSDLQQEYARQREHL 1036
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKE--------IESLKrRISDLEDEILELMERIeELEEELAELEAELAELEAELEEKKAEL 147
|
170
....*....|.
gi 568929692 1037 ERNLATLKKKV 1047
Cdd:COG1579 148 DEELAELEAEL 158
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
909-976 |
7.40e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 7.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929692 909 KELKKQIEPRENEIKVMKEQIQEMEAELErfhKQNTQLELNITELLQKLRATDQEMRKEQQK-ERDLEA 976
Cdd:pfam03938 22 AQLEKKFKKRQAELEAKQKELQKLYEELQ---KDGALLEEEREEKEQELQKKEQELQQLQQKaQQELQK 87
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
862-1052 |
7.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 862 LEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKiKELKKQIEPRENEIKVMKEQIQEMEAELERfhk 941
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKLEKRLLQKEENLDR--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 942 qntqlelnitellqKLRATDQEMRKEQQKERDLEALVRRFKTdlhncvayiqepglLKEKIRGLFEKYVQRadMVEIAGl 1021
Cdd:PRK12704 101 --------------KLELLEKREEELEKKEKELEQKQQELEK--------------KEEELEELIEEQLQE--LERISG- 149
|
170 180 190
....*....|....*....|....*....|...
gi 568929692 1022 nsdLQQEYARQR--EHLERNLATLKKKVIKEGE 1052
Cdd:PRK12704 150 ---LTAEEAKEIllEKVEEEARHEAAVLIKEIE 179
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
832-937 |
8.54e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 832 SSLQKEIEERTNDIELLKSEQMKLQGiirslEKDIQGLKREIQERDEtIQDKEKRIYDLKKKNQElEKfkfVLDYKIKEL 911
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEKEALKK-----EQDEASFERLAELRDE-LAELEEELEALKARWEA-EK---ELIEEIQEL 476
|
90 100
....*....|....*....|....*.
gi 568929692 912 KKQIEPRENEIKVMKEQIQEMEAELE 937
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELA 502
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
869-1102 |
8.59e-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: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 869 LKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEA---ELERFHKQNTQ 945
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 946 ----LELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQradmvEIAGL 1021
Cdd:pfam07888 116 ekdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE-----ELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1022 NSDLQQ------EYARQREHLERNLATLKKKVikeGELHRTDyvrimQENVSLIKEINELRRELKLTRSQIYDLESALK- 1094
Cdd:pfam07888 191 SKEFQElrnslaQRDTQVLQLQDTITTLTQKL---TTAHRKE-----AENEALLEELRSLQERLNASERKVEGLGEELSs 262
|
....*....
gi 568929692 1095 -VSKKTRSQ 1102
Cdd:pfam07888 263 mAAQRDRTQ 271
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
834-957 |
8.78e-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: 39.62 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 834 LQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQElekfkfvldyKIKELKK 913
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKE----------KLKKLLQ 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568929692 914 QIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKL 957
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
621-789 |
8.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 621 DMEEKAQIMLELKTRVEELKMEneyQLRLKdmnytEKIKELTDKFIQemeslktKNQVLKTEKekqdiSHRERLEELVDK 700
Cdd:PRK04863 979 MLAKNSDLNEKLRQRLEQAEQE---RTRAR-----EQLRQAQAQLAQ-------YNQVLASLK-----SSYDAKRQMLQE 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 701 QTRELQDLEccnnqkllLEYEKYQELQLKSQRmqEEYEKQLRDNDETKSQALEELTeFYEAKLQEKTGLLEEAQEDVRQQ 780
Cdd:PRK04863 1039 LKQELQDLG--------VPADSGAEERARARR--DELHARLSANRSRRNQLEKQLT-FCEAEMDNLTKKLRKLERDYHEM 1107
|
....*....
gi 568929692 781 LREFEETKK 789
Cdd:PRK04863 1108 REQVVNAKA 1116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
605-882 |
9.36e-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: 40.43 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 605 REREVGFAEEVLVTKTDMEEKAQIML-ELKTRVEELKME-NEYQLRLKDMNYT----EKIKELTDKFIQEMESLKTK--N 676
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELaEAEAEIEELEAQiEQLKEELKALREAldelRAELTLLNEEAANLRERLESleR 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 677 QVLKTEKEKQDISHR-ERLEELVDKQTRELQDLeccnnQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEEL 755
Cdd:TIGR02168 832 RIAATERRLEDLEEQiEELSEDIESLAAEIEEL-----EELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 756 tefyEAKLQEKTGLLEEAQEdvrqQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQ 835
Cdd:TIGR02168 907 ----ESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929692 836 KEI--------------EERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQER-DETIQD 882
Cdd:TIGR02168 979 NKIkelgpvnlaaieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-1080 |
9.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 859 IRSLEKDIQGLKReIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDyKIKELKKQIEPRENEIKV--MKEQIQEMEAEL 936
Cdd:COG4913 227 ADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLA-ELEYLRAALRLWFAQRRLelLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 937 ERFHKQNTQLELNITELLQKLRATDQEMR-----KEQQKERDLEALVRRfktdlhncvayiqepgllKEKIRGLFEKYVQ 1011
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERE------------------LEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929692 1012 RADMVEIAGLNSdlQQEYARQREHLERNLATLKKkvikEGELHRTDYVRIMQENVSLIKEINELRRELK 1080
Cdd:COG4913 367 LLAALGLPLPAS--AEEFAALRAEAAALLEALEE----ELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
855-1150 |
9.43e-03 |
|
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: 40.44 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 855 LQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRE--------------- 919
Cdd:TIGR02169 140 LQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrerekaeryqallke 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 920 ----------NEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDL-EALVRRFKTDLH-- 986
Cdd:TIGR02169 220 kreyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGel 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 987 -----NCVAYIQEPGLLKEKIRGLFEKYVQRADMV--EIAGLNSDLqQEYARQREHLERNLATLKK-------KVIKEGE 1052
Cdd:TIGR02169 300 eaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELEREI-EEERKRRDKLTEEYAELKEeledlraELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929692 1053 LHRTDYVRIMQENV---SLIKEINELRRE-------LKLTRSQIYDLESALKvSKKTRSQEVPESVISKDVVGSTSTMRL 1122
Cdd:TIGR02169 379 EFAETRDELKDYREkleKLKREINELKREldrlqeeLQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340
....*....|....*....|....*...
gi 568929692 1123 neqEETGRIIEMQRLEIRRLRDQIQEQE 1150
Cdd:TIGR02169 458 ---EQLAADLSKYEQELYDLKEEYDRVE 482
|
|
|