|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
950-1052 |
2.00e-62 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 211.30 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 950 VQFRRNTRMHELTPHHQSGGERSVTTMLYLMSLQELNRCPFRVVDEINQGMDPVNERRVFDIVVRAACGVNTSQYFFITP 1029
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 302129641 1030 KLLQNLQYAEQMTILCVHNGPQM 1052
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
40-185 |
2.30e-56 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 193.97 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 40 GAIVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYVKRGCQRGSVEIELYRT 119
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302129641 120 RGNlivtreiqvennqstwmlnkkhasqkaveeavrelhIQVGNLCQFLPQEKVGEFAKMSNSELL 185
Cdd:cd03277 81 PGN------------------------------------IQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
966-1048 |
7.41e-29 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 113.94 E-value: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 966 QSGGERSVTTMLYLMSLQELNRCPFRVVDEINQGMDPVNERRVFDIVVRAACgvNTSQYFFITPKLLQNLQYAEQMTILC 1045
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
...
gi 302129641 1046 VHN 1048
Cdd:cd03239 173 VHG 175
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
42-136 |
1.02e-23 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 99.30 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPGP-KLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKV---GLYVKRGCQRGSVEIELY 117
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITFD 80
|
90
....*....|....*....
gi 302129641 118 rtRGNLIVTREiQVENNQS 136
Cdd:cd03239 81 --KSYFLVLQG-KVEQILS 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-1028 |
4.95e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 96.66 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 203 ELKTFRTKERDLENVCKEKGNFLEKARQRNERNKLDVERyymkkrhldriqmLEKKKpwveyETARKELEGVKKERDEMK 282
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAE-------------LEEKL-----EELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 283 RKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEAdrQKRI 362
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 363 GHTQLMIRDLQKELqnmgtiedvtpqiEAINAELRNIQEERARLESESLDLRRdkdeitgEFARLQNRLRSLDDMMkike 442
Cdd:TIGR02168 443 EELEEELEELQEEL-------------ERLEEALEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQ---- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 443 eklrSRFRDTYTALEWLRKNRDRYEGVVhEPMMLVINVrDARHAKYIETHISVNdLRAFVFQRQDDNDKFMNEMRDTQRL 522
Cdd:TIGR02168 499 ----ENLEGFSEGVKALLKNQSGLSGIL-GVLSELISV-DEGYEAAIEAALGGR-LQAVVVENLNAAKKAIAFLKQNELG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 523 RVNSIIAPTESCSKRPPSRPIETLKPYGFISYLREMFDAPEE---VMSYLCHQYR-VNDVPIGTEKTK------------ 586
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkALSYLLGGVLvVDDLDNALELAKklrpgyrivtld 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 587 -------GMI--------------ESVIKDL------------------------------QLRTIYTAEERYNVKKSAY 615
Cdd:TIGR02168 652 gdlvrpgGVItggsaktnssilerRREIEELeekieeleekiaelekalaelrkeleeleeELEQLRKELEELSRQISAL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 616 SNNVVSSNSALRPPQFLTTTIDVE-------------ERRQLEEQLRAAERQKQSIDQRMAAIREQQANLDRRDNELRAN 682
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKElteleaeieeleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 683 ----KKKLSDLKSKKRQLEQKISTKQDSLRQMEQNEINLVAIEEEANAKIAAVNNKKVTIMGEYLSHLQSKARLNmekvy 758
Cdd:TIGR02168 812 ltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE----- 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 759 laLQSAGLSAEKTKLETDVRESSAELKRAEVDYTKLDKIKTNLLMTCKTLMKRASEICNMTPGETAVPEELHAAFSLLPE 838
Cdd:TIGR02168 887 --EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 839 T-LDEIDAMLNEERTRAECFTGLSDAVVDEYNRREQEIKNLEKELDDKTNELTTYRRNIAEAKERWLNPLKKLVELINVR 917
Cdd:TIGR02168 965 DdEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 918 FSDFFQSMQCAGEVDLHSENEEEYDKYGIRIQVQF--RRNTRMHELtphhqSGGERSVTTMLYLMSLQELNRCPFRVVDE 995
Cdd:TIGR02168 1045 FQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPpgKKNQNLSLL-----SGGEKALTALALLFAIFKVKPAPFCILDE 1119
|
890 900 910
....*....|....*....|....*....|...
gi 302129641 996 INQGMDPVNERRVFDIVVRAAcgvNTSQYFFIT 1028
Cdd:TIGR02168 1120 VDAPLDDANVERFANLLKEFS---KNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-1012 |
6.29e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFP-GPKLNMIVGANGTGKSSIVCAI--CLGLAGKTSVlgRGDKVGLYV---KRGCQRGSVEIE 115
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPfSKGFTVISGPNGSGKSNIGDAIlfALGLSSSKAM--RAERLSDLIsngKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 116 LY------RTRGNLIVTREIQV--ENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLcQFLPQEKVGEFAKMSNSELLEA 187
Cdd:TIGR02169 80 VTfknddgKFPDELEVVRRLKVtdDGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 188 TEKSVGPPEMYE----FHCELKTFRTKERDLENVCKEKGNFLEkaRQRNERNKLdvERY---------YMKKRHLDRIQM 254
Cdd:TIGR02169 159 IDEIAGVAEFDRkkekALEELEEVEENIERLDLIIDEKRQQLE--RLRREREKA--ERYqallkekreYEGYELLKEKEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 255 LEKKKPWVEYE--TARKELEGVKKERDE----MKRKLRFLKEA-----------QEPLLRKIRSVESELQPIEQQMKEMT 317
Cdd:TIGR02169 235 LERQKEAIERQlaSLEEELEKLTEEISElekrLEEIEQLLEELnkkikdlgeeeQLRVKEKIGELEAEIASLERSIAEKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 318 NRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMGT---------------I 382
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdelkdyrekL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 383 EDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRS-------------RF 449
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskyeqelyDL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 450 RDTYTALE---------------WLRKNRDRYEGVVHEPMMLVINVR------------DARHAKYIETHISvNDLRAFV 502
Cdd:TIGR02169 475 KEEYDRVEkelsklqrelaeaeaQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAG-NRLNNVV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 503 FQRQDDNDKFMNEMRDTQRLR-----VNSIiaptescskRPPSRPIETLKPYGFISYLREMFDAPEE---VMSY------ 568
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKAGRatflpLNKM---------RDERRDLSILSEDGVIGFAVDLVEFDPKyepAFKYvfgdtl 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 569 ----------LCHQYRV----------NDVPIGTEKTKGMIESVIKDLQLRTIYTAEERYNVKKSAYS---------NNV 619
Cdd:TIGR02169 625 vvedieaarrLMGKYRMvtlegelfekSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrrieNRL 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 620 VSSNSALRPPQFLTTTIDVE------ERRQLEEQLRAAERQKQSIDQRMAAIREQQANLDRR--DNELRANKKKLSDLKS 691
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARieELEEDLHKLEEALNDL 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 692 KKRQLEQKISTKQDSLRQMEQNEINLVAIEEEANAKIaavnnKKVTIMGEYLShlQSKARLNMEKVYLALQSAGLSAEKT 771
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIE 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 772 KLETDVRESSAELKRAEVDYTKLDKIKTNLLMTCKTLMKRASEI-CNMTPGETAVPE------ELHAAFSLLPETLDEID 844
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELeRKIEELEAQIEKkrkrlsELKAKLEALEEELSEIE 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 845 AMLNEERTRAECFTGLSDaVVDEYNRREQEIKNLE-----------------KELDDKTNELTTYRRNIAEAKERwLNPL 907
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEpvnmlaiqeyeevlkrlDELKEKRAKLEEERKAILERIEE-YEKK 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 908 KKLV-----ELINVRFSDFFQSMQcAGEVDLHSENEEEYDKYGIRIQVQFRRNT--RMHELtphhqSGGERSVTTMLYLM 980
Cdd:TIGR02169 1016 KREVfmeafEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPvqRLEAM-----SGGEKSLTALSFIF 1089
|
1130 1140 1150
....*....|....*....|....*....|..
gi 302129641 981 SLQELNRCPFRVVDEINQGMDPVNERRVFDIV 1012
Cdd:TIGR02169 1090 AIQRYKPSPFYAFDEVDMFLDGVNVERVAKLI 1121
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
964-1049 |
5.41e-18 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 82.41 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 964 HHQSGGERSVTTMLYLMSLQELNRCPFRVVDEINQGMDPVNERRVFDIVVRAAcgVNTSQYFFITPKLLQNLQYAEQMTI 1043
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHL--VKGAQVIVITHLPELAELADKLIHI 153
|
....*.
gi 302129641 1044 LCVHNG 1049
Cdd:cd03227 154 KKVITG 159
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
42-1008 |
1.49e-16 |
|
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: 85.41 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFP-GPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYV----KRGCQRGSVEI-- 114
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPfSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEItf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 115 -----ELYRTRGNLIVTREIqVENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLcQFLPQEKVGEFAKMSNSELLEATE 189
Cdd:pfam02463 82 dnedhELPIDKEEVSIRRRV-YRGGDSEYYINGKNVTKKEVAELLESQGISPEAY-NFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 190 KSVGPPEMYEFHCE--LKTFRTKERDLEN---VCKEKGNFL-----EKARQRNERNKLDVERYYMK-------KRHLDRI 252
Cdd:pfam02463 160 EEAAGSRLKRKKKEalKKLIEETENLAELiidLEELKLQELklkeqAKKALEYYQLKEKLELEEEYllyldylKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 253 QMLEKKKPWVEYETA---------RKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQpIEQQMKEMTNRIKEA 323
Cdd:pfam02463 240 DLLQELLRDEQEEIEsskqeiekeEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL-KLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 324 TQKCKQKHDQLELKNKEV------------------DDIKQDMSLKQTEEADRQKRIGHTQL----MIRDLQKELQNMGT 381
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEieelekelkeleikreaeEEEEEELEKLQEKLEQLEEELLAKKKleseRLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 382 IEDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSL-DDMMKIKEEKLRSRFRDTYTALEWLR 460
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEeLEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 461 K---------NRDRYEGVVHEPMMLVINVRDARHAKYIETHISVNDLRAFVFQRQ-------DDNDKFMNEMRDTQRLRV 524
Cdd:pfam02463 479 LvklqeqlelLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlgvavenYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 525 NSIIAPTESCSKRPPSRPIETLKPYGFISYLREMFDAPEEV-------------MSYLCHQYRVN---DVPIGTEKTKGM 588
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIdpilnlaqldkatLEADEDDKRAKvveGILKDTELTKLK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 589 IESVIKDLQLRTIYTAEER--------YNVKKSAYSNNVVSSNSALRPPQFLTTTIDVEERRQLEEQLRAAERQKQSIDQ 660
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGlaeksevkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 661 R----------------------------------------------MAAIREQQANLDRRDNELRANKKKLSDLKSKKR 694
Cdd:pfam02463 719 AeelladrvqeaqdkineelkllkqkideeeeeeeksrlkkeekeeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 695 QLEQKISTKQDSLRQMEQNEINLVAIEEEANAKIAAVNNKKVTIMGEYLSHLQSKARLNM---------------EKVYL 759
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERleeeitkeellqellLKEEE 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 760 ALQSAGLSAEKTKLETDVRESSAELKRAEVDYTKLDKIKTNLLMTCKTLMKRASEIcnmtpgetAVPEELHAAFSLLPET 839
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE--------EEPEELLLEEADEKEK 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 840 LDEIDAMLNEERTRAECFTGLSDAV----VDEYNRREQEIKNLEKELDDKTNELTTYRRNIAEAKERWLNPLKKLVELIN 915
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVnlmaIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 916 VRFSDFFQSMQCAGEVDLHSENEEEYDKYGIRIQVQFR--RNTRMHELtphhqSGGERSVTTMLYLMSLQELNRCPFRVV 993
Cdd:pfam02463 1031 KGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPgkGVKNLDLL-----SGGEKTLVALALIFAIQKYKPAPFYLL 1105
|
1130
....*....|....*
gi 302129641 994 DEINQGMDPVNERRV 1008
Cdd:pfam02463 1106 DEIDAALDDQNVSRV 1120
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
42-116 |
1.61e-14 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 73.40 E-value: 1.61e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYVKRGCQRGSVEIEL 116
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTL 75
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
44-123 |
2.15e-13 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 68.93 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 44 RITMHNFLTYDHSEV--FPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDkvglYVKRGCQRGSVEIELYRTRG 121
Cdd:cd03227 1 KIVLGRFPSYFVPNDvtFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS----GVKAGCIVAAVSAELIFTRL 76
|
..
gi 302129641 122 NL 123
Cdd:cd03227 77 QL 78
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
45-190 |
4.93e-13 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 68.68 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 45 ITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYV------KRGCQRGSVEIELYR 118
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302129641 119 TRG----NLIVTREIQVENNQSTWMLNKKHASQKAVEEAVRELHIQVG---NLCQFLPQEKVGEFAKMSNSELLEATEK 190
Cdd:pfam13476 81 NDGrytyAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKiilPLLVFLGQEREEEFERKEKKERLEELEK 159
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
967-1044 |
1.50e-11 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 64.54 E-value: 1.50e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302129641 967 SGGERSVTTMLYLMSLQELNRCPFRVVDEINQGMDPVNERRVFDIVVRAACGVNTSQYFFITPKLLQNLQYAEQMTIL 1044
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
42-127 |
8.32e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 62.72 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFP-GPKLNMIVGANGTGKSSIVCAICLGLAGKTSvlGRGDKVGLYVKRGCQRGSVEIELYRTR 120
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDfDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
....*..
gi 302129641 121 GNLIVTR 127
Cdd:COG0419 80 KRYRIER 86
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
42-434 |
1.43e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 65.69 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTsvlgRGDKVGLYVKRGCQRGSVEIELYRTRG 121
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 122 NLIVTREIQ-----------VENNQSTWMLNKKHASqKAVEEAVRELHIQV------------GNLCQFLPQEKVGEFAK 178
Cdd:PRK01156 79 VYQIRRSIErrgkgsrreayIKKDGSIIAEGFDDTT-KYIEKNILGISKDVflnsifvgqgemDSLISGDPAQRKKILDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 179 MSNSELLEATEKSVGP------PEMYEFHCELKTFRTKERDLENVCKE------KGNFLEKARQR---------NERNKL 237
Cdd:PRK01156 158 ILEINSLERNYDKLKDvidmlrAEISNIDYLEEKLKSSNLELENIKKQiaddekSHSITLKEIERlsieynnamDDYNNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 238 DVE------------RYYMKKRHLD-RIQMLEKKK---PWVEYETARKELEGVKKERDEMKRKLRFLKEAqEPLLRKIRS 301
Cdd:PRK01156 238 KSAlnelssledmknRYESEIKTAEsDLSMELEKNnyyKELEERHMKIINDPVYKNRNYINDYFKYKNDI-ENKKQILSN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 302 VESELQPIEQQMKEMTNRIKEatqkckqkHDQLELKNKEVDDIKQDMSLKQTEEADRQ---KRIGHTQLMIRDLQKELQN 378
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKD--------YNDYIKKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIER 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 302129641 379 MGTIEDVTPQIEAINAELrniqeerarLESESLDLRRDKDEITGEFARLQNRLRSL 434
Cdd:PRK01156 389 MSAFISEILKIQEIDPDA---------IKKELNEINVKLQDISSKVSSLNQRIRAL 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-996 |
2.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 226 EKARQ----RNERNKLDVERYYMKKRHLD--------RIQMLEKKKpwveyETARKELEGVKKERDEMKRKLRFLKEAQE 293
Cdd:COG1196 210 EKAERyrelKEELKELEAELLLLKLRELEaeleeleaELEELEAEL-----EELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 294 PLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQ 373
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 374 KELQNMGTiedvtpQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTY 453
Cdd:COG1196 365 EALLEAEA------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 454 TALEWLRKNRDRYEGVVHEPMMLVINVRDARhAKYIETHISVNDLRAFVfQRQDDNDKFMNEMRDTQRLRVNSIIAPTES 533
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELL-EEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 534 CSKRPPSRPIETLkpygfISYLREMFDAPEEVMSYLCHQYRVNDvpigTEKTKGMIESVIKDLQLRtiytaeerynvkKS 613
Cdd:COG1196 517 AGLRGLAGAVAVL-----IGVEAAYEAALEAALAAALQNIVVED----DEVAAAAIEYLKAAKAGR------------AT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 614 AYSNNVVSSNSALRPPQFLTTtiDVEERRQLEEQLRAAERQKQSIDQRMAAIREQQANLDRRDNELRANKKKLSDLKSKK 693
Cdd:COG1196 576 FLPLDKIRARAALAAALARGA--IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 694 RQLEQKISTKQDSLRQMEQNEINLVAIEEEANAKIAAvnnkkvtimgEYLSHLQSKARLNMEKVYLALQSAGLSAEktKL 773
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE----------EELELEEALLAEEEEERELAEAEEERLEE--EL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 774 ETDVRESSAELKRAEVDYTKLDkiktnllmtcktlmkraseicnmtpgETAVPEELHAAFSLLPETLDEIDAMLNE-ERT 852
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLE--------------------------EEELLEEEALEELPEPPDLEELERELERlERE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 853 RAEcftgLSD---AVVDEYNRREQEIKNLEKELDDKTNELTTYRRNIA----EAKERwlnpLKKLVELINVRFSDFFQSM 925
Cdd:COG1196 776 IEA----LGPvnlLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEeidrETRER----FLETFDAVNENFQELFPRL 847
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302129641 926 QCAGEVDLHSENEEEYDKYGIRIQVQFR--RNTRMHELtphhqSGGERSVTTMLYLMSLQELNRCPFRVVDEI 996
Cdd:COG1196 848 FGGGEAELLLTDPDDPLETGIEIMAQPPgkKLQRLSLL-----SGGEKALTALALLFAIFRLNPSPFCVLDEV 915
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
265-470 |
1.39e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 265 ETARKELEGVKKERDEMKRKLRFLKeaqepllRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDI 344
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALK-------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 345 KQDMSLKQTEEADR----QKRIGHTQLMI-------RDLQKELQNMGTIedvtpqIEAINAELRNIQEERARLESESLDL 413
Cdd:COG4942 96 RAELEAQKEELAELlralYRLGRQPPLALllspedfLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 414 RRDKDEITGEFARLQNRLRSLDDMMKIKEE---KLRSRFRDTYTALEWLRKNRDRYEGVV 470
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKllaRLEKELAELAAELAELQQEAEELEALI 229
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-449 |
4.98e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYVKRGCQRGSVEIELYRTRG 121
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 122 NLIVTREIQVENNQSTWMLNKK--HASQKAVEEAVREL----------HIQVGNLCQFLPQEKVGE--FAKMSNSELLEA 187
Cdd:PRK03918 83 KYRIVRSFNRGESYLKYLDGSEvlEEGDSSVREWVERLipyhvflnaiYIRQGEIDAILESDESREkvVRQILGLDDYEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 188 TEKSVGPPemyefhceLKTFRTKERDLENVCKEKGNFLEKARQRNERnkldveryymKKRHLDRIQMLEKKKPWVeyeta 267
Cdd:PRK03918 163 AYKNLGEV--------IKEIKRRIERLEKFIKRTENIEELIKEKEKE----------LEEVLREINEISSELPEL----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 268 RKELEGVKKERDEMKRklrfLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEAtqkcKQKHDQLELKNKEVDDIKQD 347
Cdd:PRK03918 220 REELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL----KKEIEELEEKVKELKELKEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 348 MSLKQTEEADRQKrighTQLMIRDLQKELqnmgtiEDVTPQIEAINAELRNIQEERARLEseslDLRRDKDEITGEFARL 427
Cdd:PRK03918 292 AEEYIKLSEFYEE----YLDELREIEKRL------SRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL 357
|
410 420
....*....|....*....|....
gi 302129641 428 QNRLRSLDDMMKIKE--EKLRSRF 449
Cdd:PRK03918 358 EERHELYEEAKAKKEelERLKKRL 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
298-445 |
1.20e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 298 KIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHtqlMIRDLQKELQ 377
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 378 NMGTIE---------DVTPQIEAIN-------AELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIK 441
Cdd:COG3883 101 SVSYLDvllgsesfsDFLDRLSALSkiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
....
gi 302129641 442 EEKL 445
Cdd:COG3883 181 EALL 184
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-430 |
1.90e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 261 WVEYETARKELEgvkkERDEMKRKLR--FLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQL-ELK 337
Cdd:COG4913 261 AERYAAARERLA----ELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 338 NKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLqkELQNMGTIED-------VTPQIEAINAELRNIQEERARLESES 410
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRARLEALLAAL--GLPLPASAEEfaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|
gi 302129641 411 LDLRRDKDEITGEFARLQNR 430
Cdd:COG4913 415 RDLRRELRELEAEIASLERR 434
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
42-914 |
3.76e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTY-DHSEVF--PGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGD--KVGLYVKRGCQRG-----S 111
Cdd:TIGR00618 3 PLRLTLKNFGSYkGTHTIDftALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIrsLNSLYAAPSEAAFaelefS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 112 VEIELYRTRGNLIVTREIQVENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLCQ----------FLPQEKVGEFAKMSN 181
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKldyktftrvvLLPQGEFAQFLKAKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 182 SELLEATEkSVGPPEMYEfhcelkTFRTKERDLENVCKEKGNFLEKarqRNERNKLDVERyyMKKRHLDRIQMLEKKKpw 261
Cdd:TIGR00618 163 KEKKELLM-NLFPLDQYT------QLALMEFAKKKSLHGKAELLTL---RSQLLTLCTPC--MPDTYHERKQVLEKEL-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 262 veyetarKELEGVKKERDEMKRKLRFLKEAQEPLLRKirsvESELQPIEQQMKEMTNRIKEatqkckqkhdqLELKNKEV 341
Cdd:TIGR00618 229 -------KHLREALQQTQQSHAYLTQKREAQEEQLKK----QQLLKQLRARIEELRAQEAV-----------LEETQERI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 342 DDIKQDMSL----KQTEEADRQKRIGHTQLMIR--DLQKELQNMGTIEDVTPQIEAINAELRNI--QEERARLESESLDL 413
Cdd:TIGR00618 287 NRARKAAPLaahiKAVTQIEQQAQRIHTELQSKmrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATS 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 414 RRD----KDEITGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYTALEWLRKNRDRYEGVVH-----EPMMLVINVRDAR 484
Cdd:TIGR00618 367 IREiscqQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHakkqqELQQRYAELCAAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 485 HAKYIETHISVNDLRAFVFQRQDDnDKFMNEMRDTQRLRVNSIIAPTESCSKRPPSRPIETLKPYGFISYLREMFDAPEE 564
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 565 VMSYLCH-QYRVNDVPIGTEKTKGMIESVIKDLQLRTIYTAEERYNVKKSAYSNNVVSS--NSALRPPQFLTTTID--VE 639
Cdd:TIGR00618 526 LTRRMQRgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdiPNLQNITVRLQDLTEklSE 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 640 ERRQLEEQLRAAERQKQsIDQRMAAIREQQANLDRRDNELRANKKKLSDLKSKKRQLEQKISTKQDSLRQMEQNEINLVA 719
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQ-PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 720 IEEEAN--AKIAAVNNKKVTIMGEYLSHLQSKARLnMEKVYLALQSAG------LSAEKTKLETDVRESSAELKRAEVDY 791
Cdd:TIGR00618 685 MQSEKEqlTYWKEMLAQCQTLLRELETHIEEYDRE-FNEIENASSSLGsdlaarEDALNQSLKELMHQARTVLKARTEAH 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 792 TKLDKIKTNLLMTCKTLMKRASEICNMTpgetavpEELHAAFSLLPETLDEIdamlneeRTRAECFTGLSDAVVDEYNRR 871
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFN-------RLREEDTHLLKTLEAEI-------GQEIPSDEDILNLQCETLVQE 829
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 302129641 872 EQEIKNLEKELDDKTNELTTYRRNIAEAKERWLNPLKKLVELI 914
Cdd:TIGR00618 830 EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKII 872
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-756 |
1.03e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 171 EKVGEFAKMSNSELLEATEKSVGPPEMYEFHCELKTFRTKE-RDLENVCK-EKGNFLEKARQRNERNKLDveryYMKKRH 248
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEaRKADELKKaEEKKKADEAKKAEEKKKAD----EAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 249 LDRIQMLEKKKpwvEYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCK 328
Cdd:PTZ00121 1312 EEAKKADEAKK---KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 329 QKHDQLELKNKEVDDIKQDMSLKQTEE----ADRQKRIGHTQLMIRDLQKELQNMGTIEDVTPQIEainaELRNIQEERA 404
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAakkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----EAKKAEEAKK 1464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 405 RLESESldlRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYTALEwLRKNRDRyegvvhepmmlvinvRDAR 484
Cdd:PTZ00121 1465 KAEEAK---KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEA---------------KKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 485 HAKYIETHISVNDLRAFVFQRQDDNDKFMNEMRDTQRLRvNSIIAPTESCSKRPPSRPIETLKPYGFISYLREMFDAPEE 564
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 565 VMSYLCHQYRVNDVPIGTEKTKGMIESVIKDLQLRTIYTAEERY--NVKKSAYSNNVVSSNSALRPPQFLTTTIDV---- 638
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkae 1684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 639 EERRQLEEQLRAAERQKQSIDQrmaaIREQQANLDRRDNELRANKKKLSDLKSKKRQLEQKISTKQDSLRQMEQNEINLV 718
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
570 580 590
....*....|....*....|....*....|....*...
gi 302129641 719 AIEEEANAKIAAVNNKKVTIMGEYLSHLQSKARLNMEK 756
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-465 |
1.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 253 QMLEKKKPWVEYETAR---KELEGVKKERDEMKRKLRFLKEAQEpLLRKIRSVESELQPIEQQMKemTNRIKEATQKckq 329
Cdd:COG4913 216 YMLEEPDTFEAADALVehfDDLERAHEALEDAREQIELLEPIRE-LAERYAAARERLAELEYLRA--ALRLWFAQRR--- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 330 khdqLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMGT--IEDVTPQIEAINAELRNIQEERARLE 407
Cdd:COG4913 290 ----LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 408 S--ESLDLRRDKDEitGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYTALEWLRKNRDR 465
Cdd:COG4913 366 AllAALGLPLPASA--EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
295-473 |
2.16e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 295 LLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRightqlmIRDLQK 374
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 375 ELQNMGTIEDvtpqIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYT 454
Cdd:COG1579 81 QLGNVRNNKE----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*....
gi 302129641 455 ALEWLRKNRDRYEGVVHEP 473
Cdd:COG1579 157 ELEELEAEREELAAKIPPE 175
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-436 |
2.69e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 182 SELLEATEKSVGPPEMYEFHCELKTFRTKERDLENVCKEKGNFLEKARQRNERNKLDVERYYMKKRHLDRIQMlekkkpw 261
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEA------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 262 vEYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESEL-------QPIEQQMKEMTNRIKEATQKCKQKHDQL 334
Cdd:PRK02224 259 -EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 335 ELKNKEVDDIKQDMSLKQTEEADRQKRIGhtqlmirDLQKELQNMGT--------IEDVTPQIEAINAELRNIQEERARL 406
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAA-------ELESELEEAREavedrreeIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270
....*....|....*....|....*....|
gi 302129641 407 ESESLDLRRDKDEITGEFARLQNRLRSLDD 436
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARE 440
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
203-443 |
2.88e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 203 ELKTFRTKERDLENVCKEkgnfLEKARQRNERNKLDVERYYMKKRHLDRIQMLEKKKPWVEYETARKELEGVKKERDEMK 282
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 283 RKlrflkeaqeplLRKIRSVESELQPIEQQMKEMTNRIKEATQKCK------QKHDQLELKNK---EVDDIKQDmsLKQT 353
Cdd:PRK03918 405 EE-----------ISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELLEEytaELKRIEKE--LKEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 354 EEADRQKRIGHTQL-MIRDLQKELQNMGTIEDvtpQIEAINAELRNIQEERARLESESLD-LRRDKDEITGEFARLQNRL 431
Cdd:PRK03918 472 EEKERKLRKELRELeKVLKKESELIKLKELAE---QLKELEEKLKKYNLEELEKKAEEYEkLKEKLIKLKGEIKSLKKEL 548
|
250
....*....|..
gi 302129641 432 RSLDDMMKIKEE 443
Cdd:PRK03918 549 EKLEELKKKLAE 560
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
42-117 |
8.09e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 48.84 E-value: 8.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302129641 42 IVRITMHNFLTYDHSEV-FP-GPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYVKRGCQRGSVEIELY 117
Cdd:COG3950 3 IKSLTIENFRGFEDLEIdFDnPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLILY 80
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
235-801 |
1.61e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 235 NKLDVERYYMKKRHLDRIQMLEKkkpwvEYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMK 314
Cdd:pfam15921 327 SQLRSELREAKRMYEDKIEELEK-----QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 315 EMTNRikeatqkckqkhdqlELKNK-EVDDIKQDMSlkqteeaDRQKRIGHTQLMIRDLQKELQnmGTIEDVTPQIEAIN 393
Cdd:pfam15921 402 RLWDR---------------DTGNSiTIDHLRRELD-------DRNMEVQRLEALLKAMKSECQ--GQMERQMAAIQGKN 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 394 AELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRSrFRDTYTALEWLRKNRDryegvvhep 473
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA-IEATNAEITKLRSRVD--------- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 474 mmlvINVRDARHAKYIETHISvndlrafvfQRQDDNDKFMNEMRDTQRLrvnsiiaptescskrppsrpietlkpygfIS 553
Cdd:pfam15921 528 ----LKLQELQHLKNEGDHLR---------NVQTECEALKLQMAEKDKV-----------------------------IE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 554 YLREMFdapeEVMSYLCHQYRVNDVPIGTEKTKgmIESVIKDLQLRTiytaeERYNVKKSaysnnvvSSNSALRPPQFLT 633
Cdd:pfam15921 566 ILRQQI----ENMTQLVGQHGRTAGAMQVEKAQ--LEKEINDRRLEL-----QEFKILKD-------KKDAKIRELEARV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 634 TTIDVEERRQL---EEQLRAAERQKQSIDQRMAAIREQQANLDRRDNE---LRAN-KKKLSDLKSKKRQLEQKISTKQDS 706
Cdd:pfam15921 628 SDLELEKVKLVnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDyevLKRNfRNKSEEMETTTNKLKMQLKSAQSE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 707 LRQMeQNEINLVAIEEEANAKIAAVNNKKVTIMGEYLSHLQSKARL--------NMEKVYLALQSAGLSAEKTKLETDVR 778
Cdd:pfam15921 708 LEQT-RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFleeamtnaNKEKHFLKEEKNKLSQELSTVATEKN 786
|
570 580
....*....|....*....|...
gi 302129641 779 ESSAELKRAEVDYTKLDKIKTNL 801
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANM 809
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
264-468 |
1.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 264 YETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCkqkhDQLELKNKEVDD 343
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL----EKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 344 IKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNM-GTIEDVTPQIEAINaELRNIQEERARLESESLDLRRDKDEITG 422
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 302129641 423 EFARLQNRLRSLDDMMKIKEEKlRSRFRDTYTALEWLRKNRDRYEG 468
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKRLEELEE 359
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
42-140 |
2.94e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.06 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLT-YDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGLYVKR-GCQRGSVEIELYRT 119
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIReGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|....*....
gi 302129641 120 RGN-LIVTREIQVENN-------QSTWML 140
Cdd:cd03240 81 NGKkYTITRSLAILENvifchqgESNWPL 109
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
210-461 |
4.39e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 210 KERDLENVCKEKGNfLEKARQRNERNKLDVERYymkkRHLDRIQMLEKKKPwveyETARKELEGVKKERDEMKRKLRFLK 289
Cdd:pfam17380 346 RERELERIRQEERK-RELERIRQEEIAMEISRM----RELERLQMERQQKN----ERVRQELEAARKVKILEEERQRKIQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 290 EaQEPLLRKIRSVESELQPIEQQM--KEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQL 367
Cdd:pfam17380 417 Q-QKVEMEQIRAEQEEARQREVRRleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 368 MI-RDLQKELQNMGTIEDVTPQIEAINAELRN-IQEERARLESEslDLRRDKDEItgefarlQNRLRSLDDMMKIKEEkl 445
Cdd:pfam17380 496 ILeKELEERKQAMIEEERKRKLLEKEMEERQKaIYEEERRREAE--EERRKQQEM-------EERRRIQEQMRKATEE-- 564
|
250
....*....|....*.
gi 302129641 446 RSRFRDTYTALEWLRK 461
Cdd:pfam17380 565 RSRLEAMEREREMMRQ 580
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
954-1028 |
5.51e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 45.15 E-value: 5.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302129641 954 RNTRMHELtphhqSGGERSVTTMLYLMSLQELNRCPFRVVDEINQGMDPVNERRVFDIVVRAAcgvNTSQYFFIT 1028
Cdd:cd03278 107 KVQRLSLL-----SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS---KETQFIVIT 173
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
251-414 |
9.23e-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: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 251 RIQMLEKKKpwveyETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATqkckqK 330
Cdd:COG1579 18 ELDRLEHRL-----KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 331 HDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMgtIEDVTPQIEAINAELRNIQEERARLESES 410
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 302129641 411 LDLR 414
Cdd:COG1579 166 EELA 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-459 |
9.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 297 RKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEAdrqkrightqlmIRDLQKEL 376
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE------------IAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 377 QnmgtiedvtpQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYTAL 456
Cdd:COG4913 678 E----------RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
...
gi 302129641 457 EWL 459
Cdd:COG4913 748 RAL 750
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
41-161 |
1.09e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 45.53 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 41 AIVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGK---TSVLGRgdkvglYVKRGCQRGSVEIELY 117
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRsfrTARDAE------LIRFGADGFRVRAEVE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 302129641 118 RTRGNLIVtrEIQVENNQST-WMLNKKhaSQKAVEEAVRELHIQV 161
Cdd:COG1195 75 RDGREVRL--GLGLSRGGKKrVRINGK--PVRRLSDLAGLLPVVL 115
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
241-378 |
1.27e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 241 RYYMKKRHLDRIQMLEKKkpwveyetARKELEGVKKERDEMKRKLrfLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRI 320
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEEE--------AKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 302129641 321 KEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIghtQLMIRDLQKELQN 378
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL---EELIEEQLQELER 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-455 |
1.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 226 EKARQRNERNKLDVEryymKKRHLDRIQMLEKKKpwveyETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESE 305
Cdd:COG4942 21 AAAEAEAELEQLQQE----IAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 306 L----QPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDD-IKQDMSLKQTEEADRQ--KRIGHTQLMIRDLQKELQN 378
Cdd:COG4942 92 IaelrAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDaVRRLQYLKYLAPARREqaEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302129641 379 MgtIEDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYTA 455
Cdd:COG4942 172 E--RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
42-137 |
1.57e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.18 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTY-----------DHSEVFpgpklnMIVGANGTGKSSIVCAICLGLAGKTSvlGRGDKVGLYVKRGCQRG 110
Cdd:cd03279 3 PLKLELKNFGPFreeqvidftglDNNGLF------LICGPTGAGKSTILDAITYALYGKTP--RYGRQENLRSVFAPGED 74
|
90 100
....*....|....*....|....*....
gi 302129641 111 SVEIELYRTRGNLI--VTREIQVENNQST 137
Cdd:cd03279 75 TAEVSFTFQLGGKKyrVERSRGLDYDQFT 103
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
243-435 |
1.60e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 243 YMKKRHLDRIQMLEKKKPWVE--YETARKELEGVKKERDEMKRK--LRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTN 318
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEeqLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 319 RIKEATQKCKQKHDQLE--LKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNM---------GTIEDVTP 387
Cdd:COG3206 241 RLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALraqlqqeaqRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 302129641 388 QIEAINAELRNIQEERARLESES----------LDLRRDKDEITGEFARLQNRLRSLD 435
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLaelpeleaelRRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-902 |
1.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 225 LEKARQRneRNKL-----DVERYymkKRHLDRIQMLEKKKPWVEYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKI 299
Cdd:COG4913 244 LEDAREQ--IELLepireLAERY---AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 300 RSVESELQPIEQQMKEM-TNRIKEATQKCKQKHDQLELKNKEVDDIKQ-----DMSLKQTEE--ADRQKRIGHTQLMIRD 371
Cdd:COG4913 319 DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEAllaalGLPLPASAEefAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 372 LQKELQNmgtiedvtpQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLddmMKIKEEKL------ 445
Cdd:COG4913 399 ELEALEE---------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA---LGLDEAELpfvgel 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 446 ---RSRFRDTYTALE-WLRKNRDRyegvvhepmMLVinvrDARHAKYIETHISVNDLRAFVfqrqddndkfmnemrDTQR 521
Cdd:COG4913 467 ievRPEEERWRGAIErVLGGFALT---------LLV----PPEHYAAALRWVNRLHLRGRL---------------VYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 522 LRVNSIIAPTESCSKRPPSRPIETlKPYGFISYLREMFdapEEVMSYLChqyrVNDVpigtEKTKGMIESVIKDLQLRTI 601
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLDF-KPHPFRAWLEAEL---GRRFDYVC----VDSP----EELRRHPRAITRAGQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 602 YTAEERyNVKKSAYSNNVVSSNSAlrppqfltttidvEERRQLEEQLRAAERQKQSIDQRMAAIREQQANLDRRDNELRA 681
Cdd:COG4913 587 GTRHEK-DDRRRIRSRYVLGFDNR-------------AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 682 nKKKLSDLKSKKRQLEQKISTKQDSLRQMEQNEINLVAIEEEAnakiaavnnkkvtimgeylshlqskARLNMEKVYLAL 761
Cdd:COG4913 653 -LAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQL-------------------------EELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 762 QSAGLSAEKTKLETDVRESSAELKRAEVDYTKLDKIKTNLLMTCktLMKRASEIcnmtpGETAVPEELHAAFSllpETLD 841
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAA-----LGDAVERELRENLE---ERID 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 842 EIDAMLNEERTRAE-----------CFTGLSDAVVDEYN---------------RREQEIKNLEKEL--DDKTNELTTYR 893
Cdd:COG4913 777 ALRARLNRAEEELEramrafnrewpAETADLDADLESLPeylalldrleedglpEYEERFKELLNENsiEFVADLLSKLR 856
|
....*....
gi 302129641 894 RNIAEAKER 902
Cdd:COG4913 857 RAIREIKER 865
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
42-161 |
1.91e-04 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 44.49 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTY-DHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLgRGDKVGLYVKRGCQRG------SVEI 114
Cdd:cd03275 1 LKRLELENFKSYkGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHL-RSKNLKDLIYRARVGKpdsnsaYVTA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 302129641 115 ElYRTRGNLIVTREIQVENNQSTWMLNKKHASQKAVEEAVRELHIQV 161
Cdd:cd03275 80 V-YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILV 125
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
203-445 |
2.29e-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: 45.40 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 203 ELKTFRTKERDLENVCKEKGNFLEKARQRNERNKLDVERYYMKKRHLDR-IQMLEK---------KKPWVEYETARKELE 272
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESkIQNQEKlnqqkdeqiKKLQQEKELLEKEIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 273 GVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQ 352
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 353 TEEADRQKRIGHTQLMIRDLQKElqnmgtiedvtpqIEAINAELRNIQEERARLESE--SLDLRRDKDEITGEFARLQNR 430
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESE-------------KKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQT 576
|
250
....*....|....*
gi 302129641 431 LRSLDDMMKIKEEKL 445
Cdd:TIGR04523 577 QKSLKKKQEEKQELI 591
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-436 |
2.55e-04 |
|
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: 45.11 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 225 LEKARQRNERN--KLDVERYYMKKRHLD-RIQMLEKKkpwveyeTARKELEGVK--KERDEMKRKLRFLKEAQEPLLRKI 299
Cdd:pfam15921 590 VEKAQLEKEINdrRLELQEFKILKDKKDaKIRELEAR-------VSDLELEKVKlvNAGSERLRAVKDIKQERDQLLNEV 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 300 RSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQL--ELKNKEVDDIKQDMSLKQTEEADrqkriGHTQLMIRDLQKELQ 377
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmQLKSAQSELEQTRNTLKSMEGSD-----GHAMKVAMGMQKQIT 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302129641 378 -NMGTIEDVTPQIEAINAELRN-------IQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDD 436
Cdd:pfam15921 738 aKRGQIDALQSKIQFLEEAMTNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
587-901 |
3.61e-04 |
|
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: 44.66 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 587 GMIESVI--KDLQLRTIYtaEE-----RYNVKKSAYSNNVVSSNSALRPPQFLTTtidvEERRQ---LEEQLRAAER--- 653
Cdd:TIGR02168 144 GKISEIIeaKPEERRAIF--EEaagisKYKERRKETERKLERTRENLDRLEDILN----ELERQlksLERQAEKAERyke 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 654 ---QKQSIDQRMAAIR--EQQANLDRRDNELRANKKKLSDLKSKKRQLEQKISTKQDSLRQMEQNEINLVAIEEEANAKI 728
Cdd:TIGR02168 218 lkaELRELELALLVLRleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 729 AAVNNKKVtimgeylSHLQSKARLNMEKVYLALQSAGLSAEKTKLETDVRESSAELKRAEVDYTKLDKIKTNLLMTCKTL 808
Cdd:TIGR02168 298 SRLEQQKQ-------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 809 MKRASEIcnmtpgeTAVPEELHAAFSLLPETLDEIDAMLNEERTRAEcftglsdAVVDEYNRREQEIKNLEKELDDktNE 888
Cdd:TIGR02168 371 ESRLEEL-------EEQLETLRSKVAQLELQIASLNNEIERLEARLE-------RLEDRRERLQQEIEELLKKLEE--AE 434
|
330
....*....|...
gi 302129641 889 LTTYRRNIAEAKE 901
Cdd:TIGR02168 435 LKELQAELEELEE 447
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
42-193 |
3.97e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 43.40 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTY-DHSEVFP-GPKLNMIVGANGTGKSSIVCAICLGLAGKTSVLGRGDKVGL-YVKRGCQRGS--VEIEL 116
Cdd:cd03272 1 IKQVIIQGFKSYkDQTVIEPfSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALlHEGSGPSVMSayVEIIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 117 YRTRGNLI-----VTREIQVENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLCQFLPQEKVGEFAKMSNSELLEATEKS 191
Cdd:cd03272 81 DNSDNRFPidkeeVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEMQQLS 160
|
..
gi 302129641 192 VG 193
Cdd:cd03272 161 GG 162
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
203-443 |
4.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 203 ELKTFRTKERDLENVCKEKGNFLEKARqRNERNKLDVERYYMKKRHLDRIQMLEKKKPWVEYETAR-------------- 268
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKekliklkgeikslk 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 269 ---KELEGVKKERDEMKRKLRFLKEAQEPLLRKIRS--------VESELQPIEQQMKEMtNRIKEATQKCKQKHDQLELK 337
Cdd:PRK03918 546 kelEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEY-LELKDAEKELEREEKELKKL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 338 NKEVDDIKQDMSLKQTEeadrqkrightqlmIRDLQKELQNMGTIEDVTpQIEAINAELRNIQEERARLESESLDLRRDK 417
Cdd:PRK03918 625 EEELDKAFEELAETEKR--------------LEELRKELEELEKKYSEE-EYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260
....*....|....*....|....*.
gi 302129641 418 DEITGEFARLQNRlrsLDDMMKIKEE 443
Cdd:PRK03918 690 EEIKKTLEKLKEE---LEEREKAKKE 712
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
42-168 |
5.80e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 42.67 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPG--PKLNMIVGANGTGKSSIVCAIC--LGLAGKTSVlgRGDKV-GLYVKRGcQRG----SV 112
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGfdPQFNAITGLNGSGKSNILDAICfvLGITNLSTV--RASNLqDLIYKRG-QAGitkaSV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302129641 113 EIEL-----------YRTRGNLIVTREIqVENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLcQFL 168
Cdd:cd03273 80 TIVFdnsdksqspigFENYPEITVTRQI-VLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNP-HFL 144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
639-815 |
6.28e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 639 EERRQLEEQLRAAERQKQSIDQRMAAIREQQANLDRRDNELRANKKKLSDLKSKKRQLEQKIST--------KQDSLRQM 710
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 711 EQNEINLVAIEEEANAKIAAVNNKKVTIMgeylshlQSKARLNMEKVYLALQSAGLSAEKTKLETDVRESSAELKRAEVD 790
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELA-------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180
....*....|....*....|....*
gi 302129641 791 YTKLDKIKTNLLMTCKTLMKRASEI 815
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARL 232
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
42-84 |
6.35e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 6.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICL 84
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRL 45
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
265-449 |
7.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 265 ETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDI 344
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 345 KQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMgtiedvTPQIEAINAELRNIQEERARLESEslDLRRDKDEITGEF 424
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAER------EEELKELEEQLESLQEELAALEQE--LQALSEAEAEQAL 185
|
170 180
....*....|....*....|....*
gi 302129641 425 ARLQNRLRSLDDMMKIKEEKLRSRF 449
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIE 210
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
41-130 |
7.81e-04 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 42.84 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 41 AIVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLgLAgktsvLGRGDKVGLY---VKRGCQRGSVEIELY 117
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-----PGRSHRTARDkelIRFGAEAAVIHGRVE 75
|
90
....*....|...
gi 302129641 118 RTRGNLIVTREIQ 130
Cdd:PRK00064 76 KGGRELPLGLEID 88
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-409 |
7.96e-04 |
|
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: 43.56 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 124 IVTREIQVENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLCQFLPQEKVGEFAKMSNSEL---LEATEKsvgppEMYEF 200
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELiflLQAREK-----EIHDL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 201 HCELKTFRTKERDLENVCKEKGNFLEKARQRN------------ERNKLDVERYYMK---KRHLDRI--------QMLEK 257
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNieltahcdklllENKELTQEASDMTlelKKHQEDIinckkqeeRMLKQ 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 258 KKPWVEYETA-RKELEGVKKE----RDEMKRKLRFLKEaqepllrKIRSVESELQPIEQQMKEMTNrikeatqKCKQKHD 332
Cdd:pfam05483 536 IENLEEKEMNlRDELESVREEfiqkGDEVKCKLDKSEE-------NARSIEYEVLKKEKQMKILEN-------KCNNLKK 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 333 QLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKEL----QNMGTIEDvTPQIEainAELRNIQEERARLES 408
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELasakQKFEEIID-NYQKE---IEDKKISEEKLLEEV 677
|
.
gi 302129641 409 E 409
Cdd:pfam05483 678 E 678
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
44-98 |
1.04e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 302129641 44 RITMHNFLTYDHSEVFP-GPKLNMIVGANGTGKSSIVCAI--CLGLAGKTSVlgRGDK 98
Cdd:cd03278 3 KLELKGFKSFADKTTIPfPPGLTAIVGPNGSGKSNIIDAIrwVLGEQSAKSL--RGEK 58
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
255-443 |
1.14e-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: 42.31 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 255 LEKKKPWveYETARKELEGVKKErdemkrklrflkeaqepLLRKIRSVESELQPIEQQMkemtNRIKEATQKCKQKHDQL 334
Cdd:smart00787 128 LEAKKMW--YEWRMKLLEGLKEG-----------------LDENLEGLKEDYKLLMKEL----ELLNSIKPKLRDRKDAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 335 ELKNKEVDDIKQDMSLKQTEEADRQKRightqlmirDLQKELQnmgtiedvtpQIEAINAELRNIQEERARLESESLDLR 414
Cdd:smart00787 185 EEELRQLKQLEDELEDCDPTELDRAKE---------KLKKLLQ----------EIMIKVKKLEELEEELQELESKIEDLT 245
|
170 180 190
....*....|....*....|....*....|....
gi 302129641 415 RDKDEITGEFA-----RLQNRLRSLDDMMKIKEE 443
Cdd:smart00787 246 NKKSELNTEIAeaekkLEQCRGFTFKEIEKLKEQ 279
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
271-431 |
1.18e-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: 42.57 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 271 LEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSL 350
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 351 KQT----EEADRQKRIGHTQLMIRDL-QKELQNMGTIEDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFA 425
Cdd:pfam07888 116 EKDallaQRAAHEARIRELEEDIKTLtQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
....*.
gi 302129641 426 RLQNRL 431
Cdd:pfam07888 196 ELRNSL 201
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-712 |
1.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 263 EYETARKELEGVKKERDEMKRKLRFLKEAQE--PLLRKIRSVESELQPIEQQMKEMTNRIKEAtqkcKQKHDQLELKNKE 340
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 341 VDDIKQDMslkqteeadrqkrighTQLMIRDLQKELQnmgtiedvtpQIEAINAELRNIQEERARLESESLDLRRDKDEI 420
Cdd:COG4717 172 LAELQEEL----------------EELLEQLSLATEE----------ELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 421 TGEFARLQNRLRSLDDMMKIKEEKLRSRFRDTYTALEwlrknrdryeGVVHEPMMLVINVrdarhAKYIETHISVNDLRA 500
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALL----------GLGGSLLSLILTI-----AGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 501 FVFQRQddNDKFMNEMRDTQRLRVNSIIAPTESCSKRPPSRPIETLKPYGFISYLREMFDAPEEVMSYLCHQYRVNDVPI 580
Cdd:COG4717 291 LLLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 581 GTEKTKGMIESVIKDL-QLRTIYTAEERYNVKKSAYSNNVVSSNSALRPPQFLTTTIDVEErrqLEEQLRAAERQKQSID 659
Cdd:COG4717 369 EQEIAALLAEAGVEDEeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEELE 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 302129641 660 QRMAAIREQQANLDRRDNELRANkkklsdlkSKKRQLEQKISTKQDSLRQMEQ 712
Cdd:COG4717 446 EELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAE 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-375 |
1.63e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 203 ELKTFRTKERDLENVCKEKGNFLEKARQRNERNKLDVERYYMKKRHLDriQMLEKKKPWVEYETARKELEGVKKERDEMK 282
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 283 RKLRFLKEAQEpllrKIRSVESELQPIEQQMKEMTNRIKEAT----QKCKQKHDQLElknKEVDDIKQDMSLKQTEEADR 358
Cdd:COG4717 153 ERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQ---QRLAELEEELEEAQEELEEL 225
|
170
....*....|....*..
gi 302129641 359 QKRIGHTQLMIRDLQKE 375
Cdd:COG4717 226 EEELEQLENELEAAALE 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-467 |
1.68e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 287 FLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQ 366
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 367 LMIRDLQKELQNMGT-IEDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKE-EK 444
Cdd:COG4372 108 EEAEELQEELEELQKeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAlDE 187
|
170 180
....*....|....*....|...
gi 302129641 445 LRSRFRDTYTALEWLRKNRDRYE 467
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIE 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-910 |
1.84e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 243 YMKKRHLDRIqmLEkkkpwvEYETARKELEGVKKERDEMKRKLRFLkeaqepLLRKIRSVESELQPIEQQMKEMTNRIKE 322
Cdd:pfam15921 70 YPGKEHIERV--LE------EYSHQVKDLQRRLNESNELHEKQKFY------LRQSVIDLQTKLQEMQMERDAMADIRRR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 323 ATQKCKQKHDQLElknKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMGTIedvTPQIEAINAELRNIQEE 402
Cdd:pfam15921 136 ESQSQEDLRNQLQ---NTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSI---LVDFEEASGKKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 403 RARLESESLDLRRDK--DEITGEFARLQNRLRSLDDMMkikeEKLRSRFRDTYTALewLRKNRDRYEGVVHEPMMLVINV 480
Cdd:pfam15921 210 MSTMHFRSLGSAISKilRELDTEISYLKGRIFPVEDQL----EALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 481 RDARHAKYIETHISVNDLRAFVFQRQDDNDKFMNEMRDTQrlrvnSIIAPTESC---SKRPPSRPIETLKPYGFISYlRE 557
Cdd:pfam15921 284 TEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE-----STVSQLRSElreAKRMYEDKIEELEKQLVLAN-SE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 558 MFDAPEEVMSYLCHQYRVNDvpigtektkgMIESVIKDLQLRTIYTAEERYNVKK--SAYSNNVVSSNSALRppQFLTTT 635
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDD----------QLQKLLADLHKREKELSLEKEQNKRlwDRDTGNSITIDHLRR--ELDDRN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 636 IDVEerrQLEEQLRAAERQKQ-SIDQRMAAIREQQANLDRrdneLRANKKKLSDLKSKKRQLEQKISTKQDSLRQMEQNE 714
Cdd:pfam15921 426 MEVQ---RLEALLKAMKSECQgQMERQMAAIQGKNESLEK----VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 715 INLVAIEEEANAKIAAVNNKKVTIM----------------GEYLSHLQSKA---RLNM---EKVYLALQ---------- 762
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRsrvdlklqelqhlkneGDHLRNVQTECealKLQMaekDKVIEILRqqienmtqlv 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 763 ------SAGLSAEKTKLETDVRESSAELKRAEVDYTKLDKIKTNLLMTCKTLMKRASEICNmtpgetAVPEELHAafslL 836
Cdd:pfam15921 579 gqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN------AGSERLRA----V 648
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302129641 837 PETLDEIDAMLNEERTRAECFTGLSDavvdEYNRREQEIKNLEKELDDKTNELTTYRRNIAEAKERWLNPLKKL 910
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSE----DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
317-406 |
2.03e-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: 41.67 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 317 TNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNM-GTIEDVTPQIEAINAE 395
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELRAE 98
|
90
....*....|.
gi 302129641 396 LRNIQEERARL 406
Cdd:COG4942 99 LEAQKEELAEL 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-434 |
2.68e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 269 KELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDM 348
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 349 SLKQTEEADRQKRIGHTQLMIRDLQKELQNMGTiedvtpQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQ 428
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK------ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
....*.
gi 302129641 429 NRLRSL 434
Cdd:TIGR04523 194 NKLLKL 199
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
225-472 |
2.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 225 LEKARQRNERNKLDVERYYMKKRHL-----DRIQMLEKKKPWV---EYETARKELEGVKKERDEMKRKLRFLKEAQEPLL 296
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSldqlkAQIEEKEEKDLHErlnGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 297 RKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKEL 376
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 377 QNM-GTIEDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFA-------RLQNRLRSLDDMMkikeEKLRSR 448
Cdd:PRK02224 324 EELrDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEeareaveDRREEIEELEEEI----EELRER 399
|
250 260 270
....*....|....*....|....*....|.
gi 302129641 449 FRDTYTAL-------EWLRKNRDRYEGVVHE 472
Cdd:PRK02224 400 FGDAPVDLgnaedflEELREERDELREREAE 430
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
42-326 |
3.49e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 41.05 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTS---VLGRGDKVGLYVKrgcqrgsVEIELYR 118
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKffeDDFLVLYLKDVIK-------IDKEDLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 119 TRGNLIVTREIQV--------ENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLCQFLPQEKVGEFAKMSNSELLEATEK 190
Cdd:pfam13175 76 IFENISFSIDIEIdvefllilFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 191 svgpPEMYEFHCELKTFRTKERDLENVCKEKGNFLEKARQRNERNKLDVERYYMKKRHldrIQMLEKKKPWVEYETARKE 270
Cdd:pfam13175 156 ----YYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYH---ENVLENLQIKKLLISADRN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 302129641 271 legVKKERDEMKRKL--RFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQK 326
Cdd:pfam13175 229 ---ASDEDSEKINSLlgALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKN 283
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
242-434 |
3.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 242 YYMKKRHLDRIQMLEKKKPWVEYETARKELEGVKKER--------DEMKRKLRFLKEAQEpLLRKIRSVESELQ--PIEQ 311
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLELLDRIEELQE-LLREAEELEEELQleELEQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 312 QMKEMTNR-----IKEATQKCKQKHDQLELKNkEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRdlqkelqnmgtIEDVT 386
Cdd:COG4717 371 EIAALLAEagvedEEELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEEELEEE-----------LEELE 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 302129641 387 PQIEAINAELRNIQEERARLESESLDLRRDK--DEITGEFARLQNRLRSL 434
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELREL 488
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
214-431 |
4.06e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 214 LENVCKEKGNFLEKARQRNERNKLDVERYYMKKRHLDRI------QMLEKKKPWVEYETARKELEGVKKE----RDEMKR 283
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelesRVAELKEELRQSREKHEELEEKYKElsasSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 284 KLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQleLKNKEVDDIKQDMSLKQTEEADRQ---- 359
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQ--RKEEEAERKQLQAKLQQTEEELRSlske 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 360 ---------KRIGHTQLMIRDLQKELQNMGTIEDVTPQIEAINAELRNIQEERARLESESLDLRRDKDEITGEFARLQNR 430
Cdd:pfam07888 194 fqelrnslaQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAE 273
|
.
gi 302129641 431 L 431
Cdd:pfam07888 274 L 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-312 |
4.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTsvlgRGDKVGLYVKRGCQRGSVEIELYRTRG 121
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL----EKEADELFKPQGRKPELNLKELKELEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 122 NLIVTREIQVENNQSTWMLNKKHASQKAVEEAVRELHIQVGNLCQFLPQEKVGEFAKMSNSELLEATEKsvgppemyefh 201
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 202 ceLKTFRTKERDLENVCKEkgnfLEKARQRNERnkldveryymKKRHLDRIQMLEKKKPWVEYETARKELEGVKKERDEM 281
Cdd:COG4717 148 --LEELEERLEELRELEEE----LEELEAELAE----------LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
250 260 270
....*....|....*....|....*....|.
gi 302129641 282 KRKLRFLKEAQEPLLRKIRSVESELQPIEQQ 312
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
196-466 |
4.42e-03 |
|
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: 41.19 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 196 EMYEFHCELKTFRTKERDLENVCKEKGNFLEKARQRNERNKLDVERYYM-----KKRHLDRIQ-----------MLEKKK 259
Cdd:TIGR00606 263 KIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQrtvreKERELVDCQreleklnkerrLLNQEK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 260 PWVEYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKI-RSVESELQ---PIEQQMKEMTNRIKEATQKCKQKHDQLE 335
Cdd:TIGR00606 343 TELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFeRGPFSERQiknFHTLVIERQEDEAKTAAQLCADLQSKER 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 336 LKNKEVDDIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMgtiEDVTPQIEAINAELRNIQEERARLESESLDLRR 415
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQL---EGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 302129641 416 DKDEIT--GEFARLQNRLRSLDDMMKIKEEKLRSR------FRDTYTALEWLRKNRDRY 466
Cdd:TIGR00606 500 KKEVKSlqNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQIRKIKSRH 558
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
42-91 |
4.44e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 40.26 E-value: 4.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 302129641 42 IVRITMHNFLTYDHSEVFPGPKLNMIVGANGTGKSSIVCAICLGLAGKTS 91
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRAS 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
252-445 |
4.66e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 252 IQMLEKKKPWVEYETARKeLEGVKKERDEMKRKLRFLKEAQEPLLRKIRsvesELQPIEQQMKEMTNRIKEATQKCKQKH 331
Cdd:COG4717 48 LERLEKEADELFKPQGRK-PELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 332 DQLELKN--KEVDDIKQDMS------------LKQTEEADRQKRIGHTQLMIRDLQKELQNMGTIEDVTPQIEAINAELR 397
Cdd:COG4717 123 KLLQLLPlyQELEALEAELAelperleeleerLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 302129641 398 NIQEERARLESESLDLRRDKDEITGEFARLQNRLRSLDDMMKIKEEKL 445
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
263-499 |
4.84e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 263 EYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVD 342
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 343 DIKQDMSLKQTEEADRQKrighTQLMIRDLQKELQNmgtiEDVTPQIEainaelRNIQEERARLESEsLDLRRDKDEITG 422
Cdd:COG1340 96 ELRKELAELNKAGGSIDK----LRKEIERLEWRQQT----EVLSPEEE------KELVEKIKELEKE-LEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 423 EFARLQNRLRSLDDMM-----KIKE-----EKLRSRFRDTYTALEWLRKNRDRYegvvHEPMMLVINVRDARHAKYIETH 492
Cdd:COG1340 161 KLKELRAELKELRKEAeeihkKIKElaeeaQELHEEMIELYKEADELRKEADEL----HKEIVEAQEKADELHEEIIELQ 236
|
....*..
gi 302129641 493 ISVNDLR 499
Cdd:COG1340 237 KELRELR 243
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
225-418 |
6.18e-03 |
|
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: 40.51 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 225 LEKARQRNERNKLDVEryYMKKRHLdrIQMlekkkpwvEYETARKELEGVKKERDEMKRKL-RFLKEAQEPLLRKIRSVE 303
Cdd:pfam07111 481 LELEQLREERNRLDAE--LQLSAHL--IQQ--------EVGRAREQGEAERQQLSEVAQQLeQELQRAQESLASVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 304 SELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVDD-IKQDMSlkqteeaDRQKRIGHTQlmiRDLQKELQNMGTI 382
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETrLREQLS-------DTKRRLNEAR---REQAKAVVSLRQI 618
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 302129641 383 EDVTPQIEAINAELRNIQEERARLESESL-----DLRRDKD 418
Cdd:pfam07111 619 QHRATQEKERNQELRRLQDEARKEEGQRLarrvqELERDKN 659
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
641-902 |
6.21e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 641 RRQLEEQLRAAERQKQsidqrmAAIR--EQQANLDRRDNELRANKKKLSDLKSkkRQLEQKISTKQDSLRQMEQNEINLV 718
Cdd:COG1196 195 LGELERQLEPLERQAE------KAERyrELKEELKELEAELLLLKLRELEAEL--EELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 719 AIEEEANAKIAAVNNKKVTIMGEYLSHLQSKARLNMEKVYLALQSAGLSAEKTKLETDVRESSAELKRAEVDYTKLDKIK 798
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 799 TNLLMTCKTLMKRASEIcnmtpgETAVPEELHAAFSLLPETLDEIDAMLNEERTRAECftglsdavVDEYNRREQEIKNL 878
Cdd:COG1196 347 EEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEAL 412
|
250 260
....*....|....*....|....
gi 302129641 879 EKELDDKTNELTTYRRNIAEAKER 902
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEE 436
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-447 |
9.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 263 EYETARKELEGVKKERDEMKRKLRFLKEAQEPLLRKIRSVESELQPIEQQMKEMTNRIKEATQKCKQKHDQLELKNKEVD 342
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302129641 343 DIKQDMSLKQTEEADRQKRIGHTQLMIRDLQKELQNMgtiedvtpQIEAINAELRNIQEERARLESESLDLRRDKDEITG 422
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQAL--------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
170 180
....*....|....*....|....*
gi 302129641 423 EFARLQNRLRSLDDMMKIKEEKLRS 447
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKLGLALS 236
|
|
| |
