|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
898-1000 |
3.00e-67 |
|
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: 224.40 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 898 VKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITP 977
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 2217376290 978 KLLQNLPYSEKMTVLFVYNGPHM 1000
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
51-196 |
9.99e-58 |
|
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: 197.82 E-value: 9.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 51 GSIVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRA 130
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376290 131 SGnlvitreidvaknqsfwfinkksttqkiveekvaalNIQVGNLCQFLPQDKVGEFAKLSKIELL 196
Cdd:cd03277 81 PG------------------------------------NIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
914-996 |
3.11e-28 |
|
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: 112.02 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 914 QSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACkeNTSQYFFITPKLLQNLPYSEKMTVLF 993
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
...
gi 2217376290 994 VYN 996
Cdd:cd03239 173 VHG 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-976 |
1.76e-19 |
|
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: 94.74 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYER-----KRHLDLIEMLEAKRPwvEYENVRQEYEEVKLV 288
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkEELESLEAELEELEA--ELEELESRLEELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 289 RDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDR-QRRIGNTRKMIEDLQNELKTTE 367
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 368 NcenlqpqidaitnDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDhivrfdnlmnqkedkLRQRFRDTYDAVLWLR 447
Cdd:TIGR02168 461 E-------------ALEELREELEEAEQALDAAERELAQLQARLDSLER---------------LQENLEGFSEGVKALL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 448 NNRDKFKQ---RVCEPI-------------------MLTVRD-------------NKKLRVNAVIAPKSSYADKAPSRSL 492
Cdd:TIGR02168 513 KNQSGLSGilgVLSELIsvdegyeaaieaalggrlqAVVVENlnaakkaiaflkqNELGRVTFLPLDSIKGTEIQGNDRE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 493 NELKQYGFFSYLRELFDAPD---PVMSYLCCQYHIhevpvgtektrerIERVIQETRLKQIYTAEEKYVVKT-------- 561
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPklrKALSYLLGGVLV-------------VDDLDNALELAKKLRPGYRIVTLDgdlvrpgg 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 562 --SFYSNKVISS-----------------------NTSLKVAQFLTVTVDLEQRRH-LEEQLKEIHRKLQAVDSGLIALR 615
Cdd:TIGR02168 660 viTGGSAKTNSSilerrreieeleekieeleekiaELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLARLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 616 ETSKHLEHkdnELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEE--------------------------- 668
Cdd:TIGR02168 740 AEVEQLEE---RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkeelkalrealdelraeltlln 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 669 -------------EERKASTK---------IKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDY 726
Cdd:TIGR02168 817 eeaanlrerleslERRIAATErrledleeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 727 MAASSQLRLTEQHFIELdenrQRLLQKCKELMKRARQVCNlGAEQ-------TLPQEYQTVFQDLPNTLDEIDALLTEER 799
Cdd:TIGR02168 897 EELSEELRELESKRSEL----RRELEELREKLAQLELRLE-GLEVridnlqeRLSEEYSLTLEEAEALENKIEDDEEEAR 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 800 SRASCFTG-------LNPTIVQEYtkreeeieqltEELKGKKVELDQYREN-----------ISQVKERWLNPLKELVEK 861
Cdd:TIGR02168 972 RRLKRLENkikelgpVNLAAIEEY-----------EELKERYDFLTAQKEDlteaketleeaIEEIDREARERFKDTFDQ 1040
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 862 INEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKF--RSSTQLHELtphhqSGGERSVSTMLYLMALQELNRCPFR 939
Cdd:TIGR02168 1041 VNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPpgKKNQNLSLL-----SGGEKALTALALLFAIFKVKPAPFC 1115
|
890 900 910
....*....|....*....|....*....|....*....
gi 2217376290 940 VVDEINQGMDPINERRVFEMVvntacKE--NTSQYFFIT 976
Cdd:TIGR02168 1116 ILDEVDAPLDDANVERFANLL-----KEfsKNTQFIVIT 1149
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
53-127 |
3.31e-18 |
|
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: 83.51 E-value: 3.31e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376290 53 IVRISMENFLTYDICEVSPGP-HLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKV---GFFVKRGCSRGMVEIEL 127
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITF 79
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
912-1000 |
1.28e-17 |
|
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: 81.25 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 912 HHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKenTSQYFFITPKLLQNLPYSEKMTV 991
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
|
....*....
gi 2217376290 992 LFVYNGPHM 1000
Cdd:cd03227 154 KKVITGVYK 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-975 |
1.93e-17 |
|
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: 88.20 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTYDICEVSP-GPHLNMIVGANGTGKSSIVCAI--CLGLAGKPAFmgRADKVGFFV---KRGCSRGMVEIE 126
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPfSKGFTVISGPNGSGKSNIGDAIlfALGLSSSKAM--RAERLSDLIsngKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 127 LF------RASGNLVITREIDVAKN--QSFWFINKKSTTQKIVEEKVAALNIQVGNLcQFLPQDKVGEFAKLSKIELLEA 198
Cdd:TIGR02169 80 VTfknddgKFPDELEVVRRLKVTDDgkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 199 TEKSIGPPE----MHKYHCELKNLREKEKQLETSCKEKTEYLQKM-VQRN--ERYK--QDVERFYERKRHLDLIEMLEAK 269
Cdd:TIGR02169 159 IDEIAGVAEfdrkKEKALEELEEVEENIERLDLIIDEKRQQLERLrREREkaERYQalLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 270 RPWVEYE----------------NVRQEYEEVKLVRDRVKEEVRKLKEG-QIPVTCRIEEMENERHNLEARIKEKIEELQ 332
Cdd:TIGR02169 239 KEAIERQlasleeeleklteeisELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 333 QA--LIVKQNEELDRQR----------------------RIGNTRKMIEDLQNEL---------------KTTENCENLQ 373
Cdd:TIGR02169 319 DAeeRLAKLEAEIDKLLaeieelereieeerkrrdklteEYAELKEELEDLRAELeevdkefaetrdelkDYREKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 374 PQIDAITNDLRRIQDEKALCEGEIID----------------------------KRRERETLEKEKKSVDDHIVRFDNLM 425
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADlnaaiagieakineleeekedkaleikkQEWKLEQLAADLSKYEQELYDLKEEY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 426 NQKEDKLRQ----------RFRDTYDAVLWLRNNRDKFKQRVcEPIMLTVRDNKKL--------------RVNAVIAPKS 481
Cdd:TIGR02169 479 DRVEKELSKlqrelaeaeaQARASEERVRGGRAVEEVLKASI-QGVHGTVAQLGSVgeryataievaagnRLNNVVVEDD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 482 SYADKA----------------------PSRSLNELKQYGFFSYLRELFDAPD---PVMSY----------------LCC 520
Cdd:TIGR02169 558 AVAKEAiellkrrkagratflplnkmrdERRDLSILSEDGVIGFAVDLVEFDPkyePAFKYvfgdtlvvedieaarrLMG 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 521 QYH-------IHE---VPVGTEKTRERIERVIQETRLKQIYTAEEKYVVKTSFYS---------NKVISSNTSLKVAQFL 581
Cdd:TIGR02169 638 KYRmvtlegeLFEksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrrieNRLDELSQELSDASRK 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 582 TVTVDLE------QRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLE------------------------------HKD 625
Cdd:TIGR02169 718 IGEIEKEieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEarieeleedlhkleealndlearlshsripEIQ 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 626 NELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEE-----EERKAS--TKIKEINVQKAKLVTELTNLIKIC 698
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqridlKEQIKSieKEIENLNGKKEELEEELEELEAAL 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 699 TSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELMKRARQvcnlgaeqtlPQEYQ 778
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE----------DEEIP 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 779 TVFQDLPNTLDEIDALltEERSRAscFTGLNPTIVQEYtkreEEIEQLTEELKGKKVELDQYRENISQVKERwLNPLK-- 856
Cdd:TIGR02169 948 EEELSLEDVQAELQRV--EEEIRA--LEPVNMLAIQEY----EEVLKRLDELKEKRAKLEEERKAILERIEE-YEKKKre 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 857 ---ELVEKINEKFSNFFSSMQcAGEVDLHTENEEDYDKYGIRIRVKFRSST--QLHELtphhqSGGERSVSTMLYLMALQ 931
Cdd:TIGR02169 1019 vfmEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPvqRLEAM-----SGGEKSLTALSFIFAIQ 1092
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....
gi 2217376290 932 ELNRCPFRVVDEINQGMDPINERRVFEMVvntacKENTSQYFFI 975
Cdd:TIGR02169 1093 RYKPSPFYAFDEVDMFLDGVNVERVAKLI-----REKAGEAQFI 1131
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
56-238 |
2.06e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 72.91 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 56 ISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV------KRGCSRGMVEIELFR 129
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 130 ASG--------NLVITREIDVAKNQSFWFINKKSTTQKIVEEKVAALNIQVgNLCQFLPQDKVGEFAKLSKIELLEATEK 201
Cdd:pfam13476 81 NDGrytyaierSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217376290 202 SIgppemhKYHCELKNLREKEKQLETSCKEKTEYLQK 238
Cdd:pfam13476 160 AL------EEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
915-992 |
1.64e-13 |
|
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: 70.32 E-value: 1.64e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376290 915 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVL 992
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
53-127 |
2.98e-13 |
|
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: 69.55 E-value: 2.98e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376290 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIEL 127
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTL 75
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-763 |
1.11e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLETScKEKTEYLQKMVQRNERYKQDVERfyerkrhldlIEMLEAKRPWVEYENVRQEYEEVKLVRDRVK 293
Cdd:COG4913 233 HFDDLERAHEALEDA-REQIELLEPIRELAERYAAARER----------LAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 294 EEVRKLKEGQIPVTCRIEEMENERHNLEARIKE----KIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTT--- 366
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaee 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 367 --ENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKE-------KKSVDDHIVRFDNLMNQ----KEDKLR 433
Cdd:COG4913 382 faALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrKSNIPARLLALRDALAEalglDEAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 434 -------------------------QRFR-----DTYDAVL-WLRNNrdKFKQRVcepIMLTVRDNKKlRVNAVIAPKSS 482
Cdd:COG4913 462 fvgelievrpeeerwrgaiervlggFALTllvppEHYAAALrWVNRL--HLRGRL---VYERVRTGLP-DPERPRLDPDS 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 483 YADKApsrslnELKQYGFFSYLRELFDAPdpvMSYLCCQyhihevpvgTEKTRERIERVIQETRL-KQIYTAEEKyvvKT 561
Cdd:COG4913 536 LAGKL------DFKPHPFRAWLEAELGRR---FDYVCVD---------SPEELRRHPRAITRAGQvKGNGTRHEK---DD 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 562 SFY--SNKVISSNTSLKVAQFLTVTVDLEQRRH-LEEQLKEIHRKLQAVDSGLIALRETSKHLEHkDNELRQKKKELLER 638
Cdd:COG4913 595 RRRirSRYVLGFDNRAKLAALEAELAELEEELAeAEERLEALEAELDALQERREALQRLAEYSWD-EIDVASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 639 KTKKRQLEQKiSSKLGSLKLMEQDtcnLEEEERKASTKIKEINVQKAKLVTELTNLikictslhiqkVDLILQNTTVISE 718
Cdd:COG4913 674 EAELERLDAS-SDDLAALEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQA-----------EEELDELQDRLEA 738
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2217376290 719 KNKLESDYMAASSQLRL----TEQHFIELDENRQRLLQKCKELMKRARQ 763
Cdd:COG4913 739 AEDLARLELRALLEERFaaalGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-976 |
1.58e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 151 INKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKVGEFAKLSKIELLEATEKSIGPPEMHKYHCELKNLREKEKQLETSCK 230
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 231 EKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENV-RQEYEEVKLVRDRVKEEVRKLKEGQipvtcR 309
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEeSIELKQGKLTEEKEELEKQELKLLK-----D 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 310 IEEMENERHNLEAR--IKEKIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTEncenlqpqIDAITNDLRRIQ 387
Cdd:pfam02463 464 ELELKKSEDLLKETqlVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR--------IISAHGRLGDLG 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 388 DEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYDAVLWLR---NNRDKFKQRVCEPIMLT 464
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKATLEA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 465 VRDNKKLRVNAVIAPKSSYADKAPSRSLNELKQYGFFSYLRELFDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQE 544
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 545 TRLKQIYTAEEKYvvKTSFYSNKVISSNTSLKVAQFLtVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHK 624
Cdd:pfam02463 696 RRQLEIKKKEQRE--KEELKKLKLEAEELLADRVQEA-QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 625 DNELR------QKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELT-----N 693
Cdd:pfam02463 773 EKELAeerektEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQkleklA 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 694 LIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELMKRARQVCNLGAEQTL 773
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 774 PQEYQTVFQDLP---------NTLDEIDALLTEERSRASCFTGLNPTIVQEYTKREEEIEQLTEELKGKKVELDQYRENI 844
Cdd:pfam02463 933 YEEEPEELLLEEadekekeenNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAII 1012
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 845 SQVKERWLNPLKELVEKINEKFSNFFSsMQCAGEVDLHTENEEDYDKYGIRIRVKFRSSTQLHELTphhQSGGERSVSTM 924
Cdd:pfam02463 1013 EETCQRLKEFLELFVSINKGWNKVFFY-LELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDL---LSGGEKTLVAL 1088
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 2217376290 925 LYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 976
Cdd:pfam02463 1089 ALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS---KNAQFIVIS 1137
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
53-138 |
2.43e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 61.18 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTY-DICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAfmGRADKVGFFVKRGCSRGMVEIELFRAS 131
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
....*..
gi 2217376290 132 GNLVITR 138
Cdd:COG0419 80 KRYRIER 86
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
55-127 |
1.71e-09 |
|
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: 57.75 E-value: 1.71e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376290 55 RISMENFLTYDICE-VSPG-PHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRadkvGFFVKRGCSRGMVEIEL 127
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR----RSGVKAGCIVAAVSAEL 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
53-865 |
7.24e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRASG 132
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 133 NLVITREIDvaKNQSFWFINKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKV--GEFAKLskIELLEATEKSIGP-PEMH 209
Cdd:PRK03918 83 KYRIVRSFN--RGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLNAIYIrqGEIDAI--LESDESREKVVRQiLGLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 210 KYHCELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPwVEYENVRQEYEEVklvr 289
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKEL---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 290 DRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKE---KIEELQQalIVKQNEEL----DRQRRIGNTRKMIEDLQNE 362
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEElkkEIEELEE--KVKELKELkekaEEYIKLSEFYEEYLDELRE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 363 LKTTEncENLQPQIDAItndlrriqdEKALCEGEiiDKRRERETLEKEKKSVDDHIVRFdnlmnqkedklrQRFRDTYDA 442
Cdd:PRK03918 312 IEKRL--SRLEEEINGI---------EERIKELE--EKEERLEELKKKLKELEKRLEEL------------EERHELYEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 443 VLWLRNNRDKFKQRV-CEPIMLTVRDNKKLR---------VNAVIAPKSSYADKAPSR--SLNELKQYGffsylrelfda 510
Cdd:PRK03918 367 AKAKKEELERLKKRLtGLTPEKLEKELEELEkakeeieeeISKITARIGELKKEIKELkkAIEELKKAK----------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 511 pdpvmsylccqyhiHEVPV-GTEKTRERIERVIQEtrlkqiYTAEEKYVVKTsfysnkvissntsLKVAQfltvtvdlEQ 589
Cdd:PRK03918 436 --------------GKCPVcGRELTEEHRKELLEE------YTAELKRIEKE-------------LKEIE--------EK 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 590 RRHLEEQLKEIhRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERKTKK-RQLEQKISSKLGSLKLMEQDTCNLEE 668
Cdd:PRK03918 475 ERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 669 EERkastKIKEINVQKAKLVTELTNLIKICTSLHIQKVDlilqntTVISEKNKLESDYmaassqlrlteQHFIELDENRQ 748
Cdd:PRK03918 554 LKK----KLAELEKKLDELEEELAELLKELEELGFESVE------ELEERLKELEPFY-----------NEYLELKDAEK 612
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 749 RLLQKCKELMKRARQVCNLGAEQtlpQEYQTVFQDLPNTLDEIDALLTEErsrascftglnptivqEYTKREEEIEQLTE 828
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEEL---AETEKRLEELRKELEELEKKYSEE----------------EYEELREEYLELSR 673
|
810 820 830
....*....|....*....|....*....|....*..
gi 2217376290 829 ELKGKKVELDQYRENISQVKeRWLNPLKELVEKINEK 865
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIK-KTLEKLKEELEEREKA 709
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
53-431 |
3.10e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.06 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTYDICEVSP-GPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV----KRGCSRGMVEI-- 125
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPfSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEItf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 126 -----ELFRASGNLVITREIdVAKNQSFWFINKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKVgEFAKLSKIELLEATE 200
Cdd:pfam02463 82 dnedhELPIDKEEVSIRRRV-YRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKI-EIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 201 KSIGPPEmhkyhcELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQ 280
Cdd:pfam02463 160 EEAAGSR------LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 281 EYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNlEARIKEKIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQ 360
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376290 361 NELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDK 431
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-398 |
1.59e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLE---TSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDliEMLEAKRPWVEYENVRQEYEEVKLVRD 290
Cdd:COG4717 72 ELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 291 RVKEEVRKLKEGQIpvtcRIEEMENERHNLEARIKEKIEELQQAlivKQNEELDRQRRIGNTRKMIEDLQNELKTTEN-C 369
Cdd:COG4717 150 ELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEeL 222
|
170 180
....*....|....*....|....*....
gi 2217376290 370 ENLQPQIDAITNDLRRIQDEKALCEGEII 398
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLL 251
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
53-163 |
2.48e-07 |
|
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: 53.36 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLglagkpAFMGRADKVgfFVKRGCSRGMVEIE------ 126
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSL------LLGGRASAD--LIRSGAEKAVVEGVfdisde 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217376290 127 ----------LFRASGNLVITREIDvAKNQSFWFINKKSTTQKIVEE 163
Cdd:cd03241 73 eeakalllelGIEDDDDLIIRREIS-RKGRSRYFINGQSVTLKLLRE 118
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
53-435 |
3.32e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPafmgRADKVGFFVKRGCSRGMVEIELFRASG 132
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 133 NLVITREID-----------VAKNQSFWFINKKSTTqKIVEEKVAALNIQVGNLCQFLPQDKV-----GEFAKLSKI--E 194
Cdd:PRK01156 79 VYQIRRSIErrgkgsrreayIKKDGSIIAEGFDDTT-KYIEKNILGISKDVFLNSIFVGQGEMdslisGDPAQRKKIldE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 195 LLEATEKSIGPPEMHK----YHCELKNLREKEKQLETSCKEkTEYLQKMVQRNERYKQDVERfyerkrhldliemlEAKR 270
Cdd:PRK01156 158 ILEINSLERNYDKLKDvidmLRAEISNIDYLEEKLKSSNLE-LENIKKQIADDEKSHSITLK--------------EIER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 271 PWVEYENVRQEYEEVK--LVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDR--- 345
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKsaLNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDyfk 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 346 -QRRIGNTRKMIEDLQNELKttencenlqpQIDAITNDLRRIQDEKAlcegEIIDKRRERETLEKEKKSVDDHIVRFDNL 424
Cdd:PRK01156 303 yKNDIENKKQILSNIDAEIN----------KYHAIIKKLSVLQKDYN----DYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
410
....*....|.
gi 2217376290 425 MNQKEDKLRQR 435
Cdd:PRK01156 369 LKSIESLKKKI 379
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
53-151 |
4.52e-06 |
|
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: 48.76 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLT-YDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAG-KPAFMGRADKVGFFVKRGCSRGMVEIELFRA 130
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGeLPPNSKGGAHDPKLIREGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|....*....
gi 2217376290 131 SGN-LVITREIDVAKN-------QSFWFI 151
Cdd:cd03240 81 NGKkYTITRSLAILENvifchqgESNWPL 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-944 |
4.88e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 218 LREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRhlDLIEMLEAKRPWVE-YENVRQEYEEVKLVRDRVKEEV 296
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA--ELARLEQDIARLEErRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 297 RKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTENCENlqpQI 376
Cdd:COG1196 333 EELEE-------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA---QL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 377 DAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYDAVLWLRNNRDKFKQR 456
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 457 vcepimLTVRDNKKLRVNAVIAPKSSYAdkapsrslnelkqyGFFSYLRELFDAPDPVMSYLCCQYHIHEVPVGTEKTRE 536
Cdd:COG1196 483 ------LEELAEAAARLLLLLEAEADYE--------------GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 537 RIERVIQETRLKQIYTAEE--KYVVKT-----SFYSNKVISSNTSLKVAQ--------FLTVTVDLEQRRHLEEQLKEIH 601
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAaiEYLKAAkagraTFLPLDKIRARAALAAALargaigaaVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 602 RKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEqdtcnlEEEERKASTKIKEIN 681
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL------EELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 682 VQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELmKRA 761
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL-ERE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 762 RQ----VcNLGAEQtlpqEYQTVFQDLpNTLDEIDALLTEERSRascftgLNpTIVQEYTKReeeieqlteelkgkkvel 837
Cdd:COG1196 776 IEalgpV-NLLAIE----EYEELEERY-DFLSEQREDLEEARET------LE-EAIEEIDRE------------------ 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 838 dqyrenisqVKERwlnpLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRV-----KFRSSTQLheltph 912
Cdd:COG1196 825 ---------TRER----FLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLETGIEIMAqppgkKLQRLSLL------ 885
|
730 740 750
....*....|....*....|....*....|..
gi 2217376290 913 hqSGGERSVSTMLYLMALQELNRCPFRVVDEI 944
Cdd:COG1196 886 --SGGEKALTALALLFAIFRLNPSPFCVLDEV 915
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-711 |
1.45e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 244 ERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEME--------- 314
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 315 NERHNLEARIKEKIEELQQALIvKQNEELDRQRRIGNTRKMIEDLQNELKTTENCENLQ--PQIDAITNDLRRIQDEKAL 392
Cdd:COG4717 132 QELEALEAELAELPERLEELEE-RLEELRELEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 393 CEGEIIDKRRERETLEKEKKSVDDHIVRFDnlMNQKEDKLRQRFRDTYDAVLWLRNNRDKFKQRVCEPIMLTVR-----D 467
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllaL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 468 NKKLRVNAVIAPKSSYADKAPSRSLNELKQYGFFSYLREL----FDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQ 543
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 544 ETRLKQIytaeekyvvktsFYSNKVISsntslkVAQFLTVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEH 623
Cdd:COG4717 369 EQEIAAL------------LAEAGVED------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 624 KDnELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTC--NLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSL 701
Cdd:COG4717 431 EE-ELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
490
....*....|
gi 2217376290 702 HIQKVDLILQ 711
Cdd:COG4717 510 REERLPPVLE 519
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
76-416 |
1.72e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 76 NMIVGANGTGKSSIVCAICLGLAGKPaFmgRADKVGFFV----KRGCsrgMVEIELFRASGNLVITR-------EIDV-- 142
Cdd:PHA02562 30 TLITGKNGAGKSTMLEALTFALFGKP-F--RDIKKGQLInsinKKDL---LVELWFEYGEKEYYIKRgikpnvfEIYCng 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 143 --------AKNQSFWF-----INKKSTTQ---------------------KIVEEkvaALNIQVgnlcqflpqdkVGEFA 188
Cdd:PHA02562 104 klldesasSKDFQKYFeqmlgMNYKSFKQivvlgtagyvpfmqlsaparrKLVED---LLDISV-----------LSEMD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 189 KLSKIELLEATEKsIGPPEMHKYHCE--LKNLREKEKQLETSCKEKTEYLQKMVQRN----ERYKQDVERFYErkrhldl 262
Cdd:PHA02562 170 KLNKDKIRELNQQ-IQTLDMKIDHIQqqIKTYNKNIEEQRKKNGENIARKQNKYDELveeaKTIKAEIEELTD------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 263 iEMLEAKRPWVEYEN----VRQEYEEVKLVRDRVKEEVRKLKEGQIPVTC---------RIEEMENERHNLEARIkEKIE 329
Cdd:PHA02562 242 -ELLNLVMDIEDPSAalnkLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCtqqisegpdRITKIKDKLKELQHSL-EKLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 330 ELQQALIVKQNEELDRQRRIgntrkmiEDLQNELkttencENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEK 409
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKKL-------LELKNKI------STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
....*..
gi 2217376290 410 EKKSVDD 416
Cdd:PHA02562 387 ELDKIVK 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
214-435 |
7.97e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHL-DLIEMLEAKRpwveyENVRQEYEEVKLVRDRV 292
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeERLEELEEEL-----AELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 293 KEEVRKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQAlivkQNEELDRQRRIGNTRKMIEDLQNELkttencENL 372
Cdd:COG1196 343 EEELEEAEE-------ELEEAEAELAEAEEALLEAEAELAEA----EEELEELAEELLEALRAAAELAAQL------EEL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376290 373 QPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQR 435
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
274-798 |
1.23e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERH----NLEARIKEKIEELQQALIV---------KQN 340
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHerkqVLEKELKHLREALQQTQQShayltqkreAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 341 EELDRQRRIGNTRKMIEDLQNELKTTencENLQPQIDAITNDLRRIQDEKALCEgeiIDKRRER--ETLEKEKKSVDDHI 418
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVL---EETQERINRARKAAPLAAHIKAVTQ---IEQQAQRihTELQSKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 419 VRFDNLMNQKEDKLRQR------------FRDTYDAVLWLRNNRDKFKQRVcEPImltvrdnKKLRVNAVIAPKSSYADK 486
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRrllqtlhsqeihIRDAHEVATSIREISCQQHTLT-QHI-------HTLQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 487 APSRSLNELKQYGFFSYLRELFDAPDPVMSYLCCQYHIHEVPV----GTEKTRERIERVIQETRLKQIYTAEEKYVVKTS 562
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 563 FYSNKVISSNT-SLKVAQFLTvtvdlEQRRHLEEQLKEIHRKLQAVD-------------SGLIALRETSKHLEHKDNEL 628
Cdd:TIGR00618 480 QIHLQETRKKAvVLARLLELQ-----EEPCPLCGSCIHPNPARQDIDnpgpltrrmqrgeQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 629 RQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELtnLIKICTSLHIQKVDL 708
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL--LRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 709 ILQNttvISEKNKLESDYMAAsSQLRLTEQhfielDENRQRLLQKCKELMKRARqvcNLGAEQTLPQEYQTVFQDLPnTL 788
Cdd:TIGR00618 633 HLQQ---CSQELALKLTALHA-LQLTLTQE-----RVREHALSIRVLPKELLAS---RQLALQKMQSEKEQLTYWKE-ML 699
|
570
....*....|
gi 2217376290 789 DEIDALLTEE 798
Cdd:TIGR00618 700 AQCQTLLREL 709
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-459 |
1.97e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLETSCKEKTEYLqkmvqrnERYKQDVERFYERKRHLDliEMLEakrpwvEYENVRQEYEEVKlvrdrvk 293
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEAD--EVLE------EHEERREELETLE------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 294 EEVRKLKEgqipvtcRIEEMENERHNLEARI---KEKIEELQQALivkqNEELDRQRRIGNTRKMIEDLQNEL-----KT 365
Cdd:PRK02224 258 AEIEDLRE-------TIAETEREREELAEEVrdlRERLEELEEER----DDLLAEAGLDDADAEAVEARREELedrdeEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 366 TENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKE----KKSVDDHIVRFDNLMNQKEDkLRQRFRDT-- 439
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEleeaREAVEDRREEIEELEEEIEE-LRERFGDApv 405
|
250 260
....*....|....*....|....*
gi 2217376290 440 -----YDAVLWLRNNRDKFKQRVCE 459
Cdd:PRK02224 406 dlgnaEDFLEELREERDELREREAE 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
588-801 |
2.02e-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: 45.43 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 588 EQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERK----TKKRQLEQKISSKLGSLKLMEQDT 663
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 664 CNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIEL 743
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376290 744 DENRQRLLQKCKELMKRA------RQVCNLGAEQTLPQEYQTVFQDLPNTLDEIDALLTEERSR 801
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLeeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-435 |
2.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 218 LREKEKQLETsckekteyLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPW------------------VEYENVR 279
Cdd:COG1196 195 LGELERQLEP--------LERQAEKAERYRELKEELKELEAELLLLKLRELEAELeeleaeleeleaeleeleAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 280 QEYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIK---EKIEELQQALIVKQNEELDRQRRIGNTRKMI 356
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 357 EDLQNELKTTENC-ENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQR 435
Cdd:COG1196 347 EEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
915-976 |
2.47e-04 |
|
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: 43.22 E-value: 2.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217376290 915 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 976
Cdd:cd03278 115 SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS---KETQFIVIT 173
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-368 |
2.72e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKrhldliEMLEAKRpwveyENVRQEYEEVKLVR-DRV 292
Cdd:PRK02224 583 ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR------ERLAEKR-----ERKRELEAEFDEARiEEA 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 293 KEEVRKLKEGQIPVTCRIEEMENERHNLEARI---KEKIEELqqalivkqnEEL-DRQRRIGNTRKMIEDLQNELKTTEN 368
Cdd:PRK02224 652 REDKERAEEYLEQVEEKLDELREERDDLQAEIgavENELEEL---------EELrERREALENRVEALEALYDEAEELES 722
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
230-390 |
3.76e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 230 KEKTEYLQKMVQRNERYKQDVERfyERKRHLD-----LIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQI 304
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQ--ENKRLTEplqkaQEEVEELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 305 PVTCRIEEMENERHNLEARIKEKIEELQQAlIVKQNEELdrQRRIGNTRKMIEDLQNELKTTENCENLQP-QIDAITNDL 383
Cdd:pfam13851 110 VLEQRFEKVERERDELYDKFEAAIQDVQQK-TGLKNLLL--EKKLQALGETLEKKEAQLNEVLAAANLDPdALQAVTEKL 186
|
....*..
gi 2217376290 384 RRIQDEK 390
Cdd:pfam13851 187 EDVLESK 193
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
261-398 |
3.85e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 261 DLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEgqipvtcRIEEMENERHNLEARIKEK---IEELQQAL-- 335
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKderIERLERELse 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 336 --------------IVKQNEELDR-QRRIGNTRKMIEDLQNELKTTENCENLQ--------PQIDAITND-LRRIQDEKA 391
Cdd:COG2433 453 arseerreirkdreISRLDREIERlERELEEERERIEELKRKLERLKELWKLEhsgelvpvKVVEKFTKEaIRRLEEEYG 532
|
....*..
gi 2217376290 392 LCEGEII 398
Cdd:COG2433 533 LKEGDVV 539
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
194-734 |
4.68e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 194 ELLEATEKSIGPPEMHKYHCELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERkrhLDLIEMLEAkrpwv 273
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER---REELETLEA----- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEgqipvtcRIEEMENERHnlEARIKEKIEELQQALIVKQNEELDR-----QRR 348
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRE-------RLEELEEERD--DLLAEAGLDDADAEAVEARREELEDrdeelRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 349 IGNTRKMIEDLQNELKT-TENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKE----KKSVDDHIVRFDN 423
Cdd:PRK02224 330 LEECRVAAQAHNEEAESlREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 424 LMNQKE------DKLRQRFRDTYDAVLWLRNNRDKFKQRVCE-------------PIMLTVrDNKKLRVNAVIAPKSSYA 484
Cdd:PRK02224 410 AEDFLEelreerDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsPHVETI-EEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 485 DKAPSRS--LNELKQygffsyLRELFDAPDPVMSYL-CCQYHIHEVPVGTEKTRERIERvIQETRLKQIYTAEEKYVVKT 561
Cdd:PRK02224 489 EEVEEVEerLERAED------LVEAEDRIERLEERReDLEELIAERRETIEEKRERAEE-LRERAAELEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 562 SFYSNkviSSNTSLKVAQFLTVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERktk 641
Cdd:PRK02224 562 EAEEE---AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER--- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 642 KRQLEQKISSKlgSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTE---LTNLIKICTSLHIQKVDliLQNT----- 713
Cdd:PRK02224 636 KRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREA--LENRveale 711
|
570 580
....*....|....*....|.
gi 2217376290 714 TVISEKNKLESDYMAASSQLR 734
Cdd:PRK02224 712 ALYDEAEELESMYGDLRAELR 732
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
53-95 |
4.88e-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: 4.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217376290 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICL 95
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRL 45
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
53-117 |
6.46e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 6.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376290 53 IVRISMENFLTYDICEV--SPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRG 117
Cdd:COG3950 3 IKSLTIENFRGFEDLEIdfDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNG 69
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
588-803 |
8.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 588 EQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLE 667
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 668 EEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENR 747
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376290 748 QRLLQKCKELMKRARQvcnlgaEQTLPQEYQTVFQDLpntLDEIDALLTEERSRAS 803
Cdd:COG1196 382 EELAEELLEALRAAAE------LAAQLEELEEAEEAL---LERLERLEEELEELEE 428
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
52-145 |
1.15e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 42.45 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 52 SIVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLgLAgkpafMGRadkvGF-------FVKRGCSRGMVE 124
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-----PGR----SHrtardkeLIRFGAEAAVIH 71
|
90 100
....*....|....*....|.
gi 2217376290 125 IELFRASGNLVITREIDVAKN 145
Cdd:PRK00064 72 GRVEKGGRELPLGLEIDKKGG 92
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-420 |
1.22e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 326 EKIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTENcenlqpQIDAITNDLRRIQDEKALCEGEIIDKRRERE 405
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER------RIAALARRIRALEQELAALEAELAELEKEIA 93
|
90
....*....|....*
gi 2217376290 406 TLEKEKKSVDDHIVR 420
Cdd:COG4942 94 ELRAELEAQKEELAE 108
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
222-367 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 222 EKQLETSCKEKTEYLQKMVQRN-------ERYKQDVERFYERKRHL--DLIEMLEAKRPWVE-YENVRQEYEEVKLVRDR 291
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANrqrekekERYKRDREQWERQRRELesRVAELKEELRQSREkHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 292 VKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKIEELQQaliVKqneelDRQRRIGNTRKMIE----DLQNELKTTE 367
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER---MK-----ERAKKAGAQRKEEEaerkQLQAKLQQTE 184
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
580-802 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 580 FLTVTVDLEQRRHLEEQLKEIHRKLQAvdsglialretskhLEHKDNELRQKKKELLErktKKRQLEQKISSKLGSLKLM 659
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAE--------------LEKELAALKKEEKALLK---QLAALERRIAALARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 660 EQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLeSDYMAASSQLRLTE-- 737
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQae 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376290 738 ---QHFIELDENRQRLLQKCKELMK-RARQVCNLGAEQTLPQEYQTVFQDLPNTLDEIDALLTEERSRA 802
Cdd:COG4942 154 elrADLAELAALRAELEAERAELEAlLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
53-93 |
2.33e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2217376290 53 IVRISMENFLTYDICEVSPGPhLNMIVGANGTGKSSIVCAI 93
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDAL 41
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-403 |
2.65e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKR--------PWVEYENVRQEYEEV 285
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelerldaSSDDLAALEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 286 KLVRDRVKEEVRKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQALIVKQNEELdrqrrigntrkmiEDLQNELKT 365
Cdd:COG4913 698 EAELEELEEELDELKG-------EIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-------------ALLEERFAA 757
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217376290 366 TENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRE 403
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
53-99 |
3.26e-03 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 40.92 E-value: 3.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217376290 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAG 99
Cdd:PRK14079 3 LLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTG 49
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
53-203 |
3.81e-03 |
|
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: 40.32 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTY-DICEVSP-GPHLNMIVGANGTGKSSIVCAICLGLAGkpAFMG-RADKVGFFVKRGCSR----GMVEI 125
Cdd:cd03272 1 IKQVIIQGFKSYkDQTVIEPfSPKHNVVVGRNGSGKSNFFAAIRFVLSD--EYTHlREEQRQALLHEGSGPsvmsAYVEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 126 eLFRASGN--------LVITREIDVAKNQsfWFINKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKVGEFAKLS-----K 192
Cdd:cd03272 79 -IFDNSDNrfpidkeeVRLRRTIGLKKDE--YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKqdeqqE 155
|
170
....*....|.
gi 2217376290 193 IELLEATEKSI 203
Cdd:cd03272 156 MQQLSGGQKSL 166
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
211-652 |
4.06e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 211 YHCELKNLREKEKQLETSCKEKTEYLQKM---VQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYEN--VRQEYEEV 285
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEAEQRIkelEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNkhLNENIENK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 286 KLVRDRVKEEVRKLKegqipvtcRIEEMENERHNLEARiKEKIE-ELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELK 364
Cdd:pfam05557 224 LLLKEEVEDLKRKLE--------REEKYREEAATLELE-KEKLEqELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 365 TTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVrfdnLMNQKEDKLRQRFrDTYDAVL 444
Cdd:pfam05557 295 LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVL----LLTKERDGYRAIL-ESYDKEL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 445 WLRNNRDKFKQRVCEPIMLT-----VRDNKKLRVNAVIAPKSSYADKAPS--RSLNELKQYgffsylRELFDAPDPVMSY 517
Cdd:pfam05557 370 TMSNYSPQLLERIEEAEDMTqkmqaHNEEMEAQLSVAEEELGGYKQQAQTleRELQALRQQ------ESLADPSYSKEEV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 518 LCCQYHIHEVPVGTEKTRERI---ERVIQETRLKQIYTAEEKYVVKtsfysnkvISSNTSLKVAQflTVTVDLEQRRHLE 594
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKnelEMELERRCLQGDYDPKKTKVLH--------LSMNPAAEAYQ--QRKNQLEKLQAEI 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376290 595 EQLKEIHRKLQAVDSGLIALRETSKHLEHKdnELRQKKKELLERKTKKRQLEQKISSK 652
Cdd:pfam05557 514 ERLKRLLKKLEDDLEQVLRLPETTSTMNFK--EVLDLRKELESAELKNQRLKEVFQAK 569
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
588-861 |
5.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 588 EQRRHLEEQLKEIHRKLQAVDSgliALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLE 667
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLRE---ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 668 EEERKASTKIKEINvqkaklvTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDEnr 747
Cdd:COG4372 108 EEAEELQEELEELQ-------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 748 QRLLQKCKELMKRARQVCNLGAEQTLPQEYQTVFQDLPNTLDEIDALLTEERSRASCFTGLNPTIVQEYTKREEEIEQLT 827
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270
....*....|....*....|....*....|....
gi 2217376290 828 EELKGKKVELDQYRENISQVKERWLNPLKELVEK 861
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
875-997 |
5.27e-03 |
|
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, like 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: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.77 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 875 CAGEVDLHTENEEDYDKYGIRIRVKFRSstQLheltphhqSGGERSVSTMLYLMALQelnrCPFRVVDEINQGMDPINER 954
Cdd:cd00267 52 TSGEILIDGKDIAKLPLEELRRRIGYVP--QL--------SGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRE 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2217376290 955 RVFEMVVNTACKENTsqYFFITPKLLQNLPYSEKmtVLFVYNG 997
Cdd:cd00267 118 RLLELLRELAEEGRT--VIIVTHDPELAELAADR--VIVLKDG 156
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
53-190 |
5.90e-03 |
|
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: 39.17 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 53 IVRISMENFLTY------DICEVSPGPhLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIE 126
Cdd:cd03279 3 PLKLELKNFGPFreeqviDFTGLDNNG-LFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFT 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376290 127 lFRASGNLV-ITREIDVAKNQsfwFINkksttqkiveekvaalniqvgnlCQFLPQdkvGEFAKL 190
Cdd:cd03279 82 -FQLGGKKYrVERSRGLDYDQ---FTR-----------------------IVLLPQ---GEFDRF 116
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
588-687 |
6.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 588 EQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSL----------K 657
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakeI 158
|
90 100 110
....*....|....*....|....*....|.
gi 2217376290 658 LMEQdtcnLEEE-ERKASTKIKEInVQKAKL 687
Cdd:PRK12704 159 LLEK----VEEEaRHEAAVLIKEI-EEEAKE 184
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
290-457 |
6.99e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 290 DRVKEEVRKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDrqrrIGNTRKMIEDLQNELKTTENc 369
Cdd:COG1579 20 DRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 370 enlQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYDAVLWLRNN 449
Cdd:COG1579 88 ---NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*...
gi 2217376290 450 RDKFKQRV 457
Cdd:COG1579 165 REELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
190-429 |
7.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 190 LSKIELLEATEKSIGPPEMHKYHCELKNLREKEKQLETScKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEak 269
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE-- 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 270 rpwvEYENVRQEYEEVKLVRDRVK-EEVRKLKEGqipvtcriEEMENERHNLEARIKEKIEEL--------QQALIVKQN 340
Cdd:PTZ00121 1657 ----EENKIKAAEEAKKAEEDKKKaEEAKKAEED--------EKKAAEALKKEAEEAKKAEELkkkeaeekKKAEELKKA 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376290 341 EELDRQRRIGNTRKMIEDLQN--ELKTTENCEN-LQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDdh 417
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKaeEAKKDEEEKKkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD-- 1802
|
250
....*....|..
gi 2217376290 418 ivRFDNLMNQKE 429
Cdd:PTZ00121 1803 --IFDNFANIIE 1812
|
|
| |
