|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
919-1025 |
9.09e-52 |
|
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: 180.87 E-value: 9.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 919 IQIMVQFRRGLQLQPLDKFIQSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDLLLKEATKHGSAQYL 998
Cdd:cd03277 107 IELLVKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYF 186
|
90 100
....*....|....*....|....*..
gi 281366582 999 FVTPKLLRDLNYNEHLCVSIVHNSKTV 1025
Cdd:cd03277 187 LITPKLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
14-160 |
7.55e-47 |
|
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: 167.00 E-value: 7.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 14 GRIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRVYGR 93
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366582 94 tpnttetfrriinsnglstfsvndkdtskknflaavsSFNIQVSNLCQFLPQDRVQDFSKMNPQELL 160
Cdd:cd03277 81 -------------------------------------PGNIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-425 |
8.06e-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: 85.89 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 22 KDFVSYSEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNK-------TSATIIVRVYGRT 94
Cdd:TIGR02169 11 KSFGKKKVIPFSKG--FTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKngqsgneAYVTVTFKNDDGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 95 PNTTETF---RRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQvSNLCQFLPQDRVQDFSKMNPQE--LLLNTMSSVCD 169
Cdd:TIGR02169 89 FPDELEVvrrLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVErrKIIDEIAGVAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 170 EDlinsfNSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAKKLWVETQAGEAKAAEM 249
Cdd:TIGR02169 168 FD-----RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 250 KTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEK-AAIDGKMDSLKQGIYQKKYELEQNIK 328
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 329 KSRRTATECDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAME-----------QYSRRRQLEqKLNDEM 397
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaetrdeLKDYREKLE-KLKREI 401
|
410 420
....*....|....*....|....*...
gi 281366582 398 IPEITAYKLKIERLRNVKMQkIDEIRAK 425
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEE-LADLNAA 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-1001 |
2.90e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.34 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 193 REKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQK-LQVYSAKKLWVETQAGEAKA--AEMKTQVKNAKTQSDKLKNQHDK 269
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKeLYALANEISRLEQQKQILRErlANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 270 LLQS-------QEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQ 342
Cdd:TIGR02168 335 LAEElaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 343 LVENKIYELETLNKSR-PLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEM---IPEITAYKLKIERLRN-VKMQ 417
Cdd:TIGR02168 415 RRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELeeaEQALDAAERELAQLQArLDSL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 418 KIDEIRAKNPNLVVAMNWLAQNKqrykLNVYDPMILEL-TVQNhEDAKFLENVVAQRdLFAFACEDKGDMSDLINELcVK 496
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLKNQSG----LSGILGVLSELiSVDE-GYEAAIEAALGGR-LQAVVVENLNAAKKAIAFL-KQ 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 497 QKLGVNVIYCAPSDRLVYSPKTPIDDLRSF-GFRSYLVDLVTGPI---PLINKLCASYSIhnipigteaVGNYTSSIPKA 572
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTEIQGNDREILKNIeGFLGVAKDLVKFDPklrKALSYLLGGVLV---------VDDLDNALELA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 573 IRVYFGG----------SKKFVVT-ASRYRSDTIL---------------TESSIRAKNQLITVDSQQLALVMKQCSEAV 626
Cdd:TIGR02168 639 KKLRPGYrivtldgdlvRPGGVITgGSAKTNSSILerrreieeleekieeLEEKIAELEKALAELRKELEELEEELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 627 KESDSIKNAITQTDNEFERLQAVA--------------KDEQEKRRKLDQKIAHFNSLKTEIETLQKKLEALRN--SDSL 690
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVeqleeriaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlKEEL 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 691 DCLETNFcNSLHKDLKKIFDADAELCSCLKAIdrliiEKNMAQTKVSIYMLqhETQIEALKESEEQSKAATRDFQQLLQC 770
Cdd:TIGR02168 799 KALREAL-DELRAELTLLNEEAANLRERLESL-----ERRIAATERRLEDL--EEQIEELSEDIESLAAEIEELEELIEE 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 771 LENQISDVNKRKSAIQGLCH----------GEIPTSSKfpfkkEFRELENiDLPELREAIHDFQARLECMK--------- 831
Cdd:TIGR02168 871 LESELEALLNERASLEEALAllrseleelsEELRELES-----KRSELRR-ELEELREKLAQLELRLEGLEvridnlqer 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 832 -----SVNSEAI--------SSYQGLQNEVKQLEEGIQE--SVNQAkSIE---------SGMSNLYDKWEPKLNSLVETI 887
Cdd:TIGR02168 945 lseeySLTLEEAealenkieDDEEEARRRLKRLENKIKElgPVNLA-AIEeyeelkeryDFLTAQKEDLTEAKETLEEAI 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 888 S-----TKfSEFMESIEYV--------------GEVVLSKTDKYDFDSYGIQIMVQFrRGLQLQPLDKFiqSGGERAVsI 948
Cdd:TIGR02168 1024 EeidreAR-ERFKDTFDQVnenfqrvfpklfggGEAELRLTDPEDLLEAGIEIFAQP-PGKKNQNLSLL--SGGEKAL-T 1098
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 281366582 949 AIySL--SLQHVTHVPFRCVDEINQGMDATN-ERhiFDLLLKEATKHgsAQYLFVT 1001
Cdd:TIGR02168 1099 AL-ALlfAIFKVKPAPFCILDEVDAPLDDANvER--FANLLKEFSKN--TQFIVIT 1149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
22-1001 |
1.79e-15 |
|
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: 81.56 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 22 KDFVSYSE---ITFHPKHylNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRV-------- 90
Cdd:pfam02463 8 EGFKSYAKtviLPFSPGF--TAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVeitfdned 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 91 -YGRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMNPQE-LLLNTMSSVC 168
Cdd:pfam02463 86 hELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERrLEIEEEAAGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 169 DEDLINSFNSLKQMRT---------------EQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAK 233
Cdd:pfam02463 166 RLKRKKKEALKKLIEEtenlaeliidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 234 ------KLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDG 307
Cdd:pfam02463 246 lrdeqeEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 308 KMDSLKQGI------------------------------YQKKYELEQNIKKSRRTATE--------------------- 336
Cdd:pfam02463 326 AEKELKKEKeeieelekelkeleikreaeeeeeeeleklQEKLEQLEEELLAKKKLESErlssaaklkeeelelkseeek 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 337 -CDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVK 415
Cdd:pfam02463 406 eAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 416 MQKIDEIRAKNPNLVvamnwlAQNKQRYKLNVYDPMILELTVQNH---EDAKFLENVVAQRDLFAFACEDKGDMSDLINE 492
Cdd:pfam02463 486 LELLLSRQKLEERSQ------KESKARSGLKVLLALIKDGVGGRIisaHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 493 LCVKQKLGVNViycaPSDRLVYSPKTPIDDLRSFGFRSYLVDLVTGPIPLINKLCASYSIHNIPIG----------TEAV 562
Cdd:pfam02463 560 VEERQKLVRAL----TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvvegilkdTELT 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 563 GNYTSSIPKAIRVYFGGS-----------------KKFVVTASRYRSDTILTES----------SIRAKNQLITVDSQQL 615
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSleeglaeksevkaslseLTKELLEIQELQEKAESELakeeilrrqlEIKKKEQREKEELKKL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 616 ALVMKQCSEAVKESDSIKNAITQTDNEFERLQAVAKDE--QEKRRKLDQKIAHFNS---------LKTEIETLQKKLEAL 684
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLkekelaeerEKTEKLKVEEEKEEK 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 685 RNSDSLDCLETNFCNSLHKDLKKIFDADAELCSC--LKAIDRLIIEKNMAQTKV-----SIYMLQHETQIEALKESEEQS 757
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikEEELEELALELKEEQKLEklaeeELERLEEEITKEELLQELLLK 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 758 KAATRDF--------------------QQLLQCLENQISDVNKRKSAIQGLCH-----GEIPTSSKFPFKKEFRELENID 812
Cdd:pfam02463 876 EEELEEQklkdeleskeekekeekkelEEESQKLNLLEEKENEIEERIKEEAEillkyEEEPEELLLEEADEKEKEENNK 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 813 LPELREAIHDFQARLECMKsVNSEAISSYQGLQNEVKQLEEGIQESVNQAKSIESGMSNLYDKWEPKLNSLVETISTKFS 892
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGK-VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 893 EFMESIEYVGEVVLSKTDKYDFDSYGIQIMVQFrRGLQLQPLDKFiqSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQG 972
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARP-PGKGVKNLDLL--SGGEKTLVALALIFAIQKYKPAPFYLLDEIDAA 1111
|
1130 1140
....*....|....*....|....*....
gi 281366582 973 MDATNeRHIFDLLLKEATKHgsAQYLFVT 1001
Cdd:pfam02463 1112 LDDQN-VSRVANLLKELSKN--AQFIVIS 1137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
24-862 |
5.26e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 24 FVSYSEITFHPKHYLnvLTGPNGSGKSTIVSAIILGLGGEPILL-----------DRSasVADYI---QSNKTSATIIVR 89
Cdd:COG4913 14 FDGVHTIDFDGRGTL--LTGDNGSGKSTLLDAIQTLLVPAKRPRfnkaandagksDRT--LLSYVrgkYGSERDEAGTRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 90 VYGRTPNTT----ETFRriiNSNGLSTFSV----------NDKDTSKKNFLAAVSSFNIQ----------VSNLCQFLPQ 145
Cdd:COG4913 90 VYLRPGDTWsaiaATFA---NDGSGQTVTLaqvfwlkgdaSSLGDVKRFFVIADGPLDLEdfeefahgfdIRALKARLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 146 DRVQDFSK----------------MNPQELLLNTMSS-------------VCDE--------DLINSFNSLKQMRTEqan 188
Cdd:COG4913 167 QGVEFFDSfsaylarlrrrlgigsEKALRLLHKTQSFkpigdlddfvreyMLEEpdtfeaadALVEHFDDLERAHEA--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 189 vhanrekeksdLVKKQKRLEHLQMTVSQYKEREEVKQKLQvysakklwvetqagEAKAAEMKTQVKNAKTQSDKLKNQHD 268
Cdd:COG4913 244 -----------LEDAREQIELLEPIRELAERYAAARERLA--------------ELEYLRAALRLWFAQRRLELLEAELE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 269 KLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDG-KMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENK 347
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 348 IYELETLnksrpliVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEmipeITAYKLKIERLRNvkmqkideiRAKN- 426
Cdd:COG4913 379 AEEFAAL-------RAEAAALLEALEEELEALEEALAEAEAALRDLRRE----LRELEAEIASLER---------RKSNi 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 427 -PNLVVAMNWLAQNkqrykLNVY--DPMIL-EL-TVQNHEDA------KFLEN-----VVAQRDLFAFAcedkgdmsDLI 490
Cdd:COG4913 439 pARLLALRDALAEA-----LGLDeaELPFVgELiEVRPEEERwrgaieRVLGGfaltlLVPPEHYAAAL--------RWV 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 491 NELcvkqKLGVNVIY--CAPSDRLVYSPKTPIDDL------RSFGFRSYLVDLVTGPIPLInkLCASysihnipigTEAV 562
Cdd:COG4913 506 NRL----HLRGRLVYerVRTGLPDPERPRLDPDSLagkldfKPHPFRAWLEAELGRRFDYV--CVDS---------PEEL 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 563 GNYTSSIPKAIRVYFGGS---KKfvvTASRYRSDTILTESSIRAKNQLITvDSQQLALVMKQCSEAVKESDSIKNAITQT 639
Cdd:COG4913 571 RRHPRAITRAGQVKGNGTrheKD---DRRRIRSRYVLGFDNRAKLAALEA-ELAELEEELAEAEERLEALEAELDALQER 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 640 DNEFERLQAVAKDE------QEKRRKLDQKIAHFNSLKTEIETLQKKLEALRNSDsldcletnfcNSLHKDLKKIFDADA 713
Cdd:COG4913 647 REALQRLAEYSWDEidvasaEREIAELEAELERLDASSDDLAALEEQLEELEAEL----------EELEEELDELKGEIG 716
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 714 ELCSCLKAIDRLIIE-KNMAQTKVSIYMLQHETQIEALKESEEQSKAAtrdfQQLLQCLENQISDVNKRKSAIQG----- 787
Cdd:COG4913 717 RLEKELEQAEEELDElQDRLEAAEDLARLELRALLEERFAAALGDAVE----RELRENLEERIDALRARLNRAEEelera 792
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 788 ---------LCHGEIPTSSKFP--FKKEFRELENIDLPELREAIhdFQARLECMKSvNSEAISSYqgLQNEVKQLEEGIQ 856
Cdd:COG4913 793 mrafnrewpAETADLDADLESLpeYLALLDRLEEDGLPEYEERF--KELLNENSIE-FVADLLSK--LRRAIREIKERID 867
|
....*.
gi 281366582 857 EsVNQA 862
Cdd:COG4913 868 P-LNDS 872
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
19-206 |
7.23e-11 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 62.51 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 19 VYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSAS-----VADYIQSNKTSATIIVRVY-- 91
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGggfvkGDIRIGLEGKGKAYVEITFen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 92 --GRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSF---NIQVSNLCQFLPQDRVQDFSKMNPQELLlntmss 166
Cdd:pfam13476 81 ndGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELlksDKIILPLLVFLGQEREEEFERKEKKERL------ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 281366582 167 vcdEDLINSFNSLKQMRtEQANVHANREKEKSDLVKKQKR 206
Cdd:pfam13476 155 ---EELEKALEEKEDEK-KLLEKLLQLKEKKKELEELKEE 190
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-396 |
3.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 177 NSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMtvsqyKEREEVKQKLQVYSAKKLWVET-QAGEAKAAEMKTQVKN 255
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQA-----EEYELLAELARLEQDIARLEERrRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 256 AKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTAT 335
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366582 336 ECDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDE 396
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
15-94 |
7.19e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.86 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSY---SEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRVY 91
Cdd:COG0419 1 KLLRLRLENFRSYrdtETIDFDDG--LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHG 78
|
...
gi 281366582 92 GRT 94
Cdd:COG0419 79 GKR 81
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
15-429 |
8.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSY--SEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVrvyg 92
Cdd:PRK03918 2 KIEELKIKNFRSHksSVVEFDDG--INLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 93 rtpnttetfrriinsnglsTFSVNDKD-TSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFS-KMNPQELLLN-------- 162
Cdd:PRK03918 76 -------------------KFEKNGRKyRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVeRLIPYHVFLNaiyirqge 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 163 ---------TMSSVCD-----EDLINSFNSLKQMRTEQANvhanREKEKSDLVKKQKRLEHLQMTvsQYKEREEVKQKLQ 228
Cdd:PRK03918 137 idailesdeSREKVVRqilglDDYENAYKNLGEVIKEIKR----RIERLEKFIKRTENIEELIKE--KEKELEEVLREIN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 229 VYSAKKlwVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIE---KEKESLRKALLEKTRLLENAVAEKAAI 305
Cdd:PRK03918 211 EISSEL--PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKVKELKEL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 306 DGKMDS------LKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENKIYELETLNKSRPLIVSELERAKEScAAARGKA 379
Cdd:PRK03918 289 KEKAEEyiklseFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 281366582 380 MEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVKMQKIDEIRAKNPNL 429
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
15-90 |
4.89e-06 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 49.77 E-value: 4.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366582 15 RIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAI-ILGLGGEPilldRSASVADYIQSNKTSATIIVRV 90
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIyLLAPGRSH----RTARDKELIRFGAEAAVIHGRV 74
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
22-90 |
1.51e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 45.42 E-value: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366582 22 KDFVSYSEIT--FHPKhyLNVLTGPNGSGKSTIVSAI-ILGLGGEpillDRSASVADYIQSNKTSATIIVRV 90
Cdd:TIGR00611 9 TDFRNYDAVDleLSPG--VNVIVGPNGQGKTNLLEAIyYLALGRS----HRTSRDKPLIRFGAEAFVIEGRV 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
919-1025 |
9.09e-52 |
|
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: 180.87 E-value: 9.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 919 IQIMVQFRRGLQLQPLDKFIQSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDLLLKEATKHGSAQYL 998
Cdd:cd03277 107 IELLVKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYF 186
|
90 100
....*....|....*....|....*..
gi 281366582 999 FVTPKLLRDLNYNEHLCVSIVHNSKTV 1025
Cdd:cd03277 187 LITPKLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
14-160 |
7.55e-47 |
|
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: 167.00 E-value: 7.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 14 GRIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRVYGR 93
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366582 94 tpnttetfrriinsnglstfsvndkdtskknflaavsSFNIQVSNLCQFLPQDRVQDFSKMNPQELL 160
Cdd:cd03277 81 -------------------------------------PGNIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
919-1024 |
1.75e-17 |
|
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: 81.20 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 919 IQIMVQFRRGLQLQPLDKFIQSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDLLLKEATKhgSAQYL 998
Cdd:cd03239 75 VEITFDKSYFLVLQGKVEQILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH--TSQFI 152
|
90 100
....*....|....*....|....*.
gi 281366582 999 FVTPKLLRDLNYNEHLCVSIVHNSKT 1024
Cdd:cd03239 153 VITLKKEMFENADKLIGVLFVHGVST 178
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-425 |
8.06e-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: 85.89 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 22 KDFVSYSEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNK-------TSATIIVRVYGRT 94
Cdd:TIGR02169 11 KSFGKKKVIPFSKG--FTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKngqsgneAYVTVTFKNDDGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 95 PNTTETF---RRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQvSNLCQFLPQDRVQDFSKMNPQE--LLLNTMSSVCD 169
Cdd:TIGR02169 89 FPDELEVvrrLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVErrKIIDEIAGVAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 170 EDlinsfNSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAKKLWVETQAGEAKAAEM 249
Cdd:TIGR02169 168 FD-----RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 250 KTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEK-AAIDGKMDSLKQGIYQKKYELEQNIK 328
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 329 KSRRTATECDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAME-----------QYSRRRQLEqKLNDEM 397
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaetrdeLKDYREKLE-KLKREI 401
|
410 420
....*....|....*....|....*...
gi 281366582 398 IPEITAYKLKIERLRNVKMQkIDEIRAK 425
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEE-LADLNAA 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-1001 |
2.90e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.34 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 193 REKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQK-LQVYSAKKLWVETQAGEAKA--AEMKTQVKNAKTQSDKLKNQHDK 269
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKeLYALANEISRLEQQKQILRErlANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 270 LLQS-------QEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQ 342
Cdd:TIGR02168 335 LAEElaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 343 LVENKIYELETLNKSR-PLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEM---IPEITAYKLKIERLRN-VKMQ 417
Cdd:TIGR02168 415 RRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELeeaEQALDAAERELAQLQArLDSL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 418 KIDEIRAKNPNLVVAMNWLAQNKqrykLNVYDPMILEL-TVQNhEDAKFLENVVAQRdLFAFACEDKGDMSDLINELcVK 496
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLKNQSG----LSGILGVLSELiSVDE-GYEAAIEAALGGR-LQAVVVENLNAAKKAIAFL-KQ 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 497 QKLGVNVIYCAPSDRLVYSPKTPIDDLRSF-GFRSYLVDLVTGPI---PLINKLCASYSIhnipigteaVGNYTSSIPKA 572
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTEIQGNDREILKNIeGFLGVAKDLVKFDPklrKALSYLLGGVLV---------VDDLDNALELA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 573 IRVYFGG----------SKKFVVT-ASRYRSDTIL---------------TESSIRAKNQLITVDSQQLALVMKQCSEAV 626
Cdd:TIGR02168 639 KKLRPGYrivtldgdlvRPGGVITgGSAKTNSSILerrreieeleekieeLEEKIAELEKALAELRKELEELEEELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 627 KESDSIKNAITQTDNEFERLQAVA--------------KDEQEKRRKLDQKIAHFNSLKTEIETLQKKLEALRN--SDSL 690
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVeqleeriaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlKEEL 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 691 DCLETNFcNSLHKDLKKIFDADAELCSCLKAIdrliiEKNMAQTKVSIYMLqhETQIEALKESEEQSKAATRDFQQLLQC 770
Cdd:TIGR02168 799 KALREAL-DELRAELTLLNEEAANLRERLESL-----ERRIAATERRLEDL--EEQIEELSEDIESLAAEIEELEELIEE 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 771 LENQISDVNKRKSAIQGLCH----------GEIPTSSKfpfkkEFRELENiDLPELREAIHDFQARLECMK--------- 831
Cdd:TIGR02168 871 LESELEALLNERASLEEALAllrseleelsEELRELES-----KRSELRR-ELEELREKLAQLELRLEGLEvridnlqer 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 832 -----SVNSEAI--------SSYQGLQNEVKQLEEGIQE--SVNQAkSIE---------SGMSNLYDKWEPKLNSLVETI 887
Cdd:TIGR02168 945 lseeySLTLEEAealenkieDDEEEARRRLKRLENKIKElgPVNLA-AIEeyeelkeryDFLTAQKEDLTEAKETLEEAI 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 888 S-----TKfSEFMESIEYV--------------GEVVLSKTDKYDFDSYGIQIMVQFrRGLQLQPLDKFiqSGGERAVsI 948
Cdd:TIGR02168 1024 EeidreAR-ERFKDTFDQVnenfqrvfpklfggGEAELRLTDPEDLLEAGIEIFAQP-PGKKNQNLSLL--SGGEKAL-T 1098
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 281366582 949 AIySL--SLQHVTHVPFRCVDEINQGMDATN-ERhiFDLLLKEATKHgsAQYLFVT 1001
Cdd:TIGR02168 1099 AL-ALlfAIFKVKPAPFCILDEVDAPLDDANvER--FANLLKEFSKN--TQFIVIT 1149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
22-1001 |
1.79e-15 |
|
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: 81.56 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 22 KDFVSYSE---ITFHPKHylNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRV-------- 90
Cdd:pfam02463 8 EGFKSYAKtviLPFSPGF--TAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVeitfdned 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 91 -YGRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMNPQE-LLLNTMSSVC 168
Cdd:pfam02463 86 hELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERrLEIEEEAAGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 169 DEDLINSFNSLKQMRT---------------EQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAK 233
Cdd:pfam02463 166 RLKRKKKEALKKLIEEtenlaeliidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 234 ------KLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDG 307
Cdd:pfam02463 246 lrdeqeEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 308 KMDSLKQGI------------------------------YQKKYELEQNIKKSRRTATE--------------------- 336
Cdd:pfam02463 326 AEKELKKEKeeieelekelkeleikreaeeeeeeeleklQEKLEQLEEELLAKKKLESErlssaaklkeeelelkseeek 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 337 -CDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVK 415
Cdd:pfam02463 406 eAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 416 MQKIDEIRAKNPNLVvamnwlAQNKQRYKLNVYDPMILELTVQNH---EDAKFLENVVAQRDLFAFACEDKGDMSDLINE 492
Cdd:pfam02463 486 LELLLSRQKLEERSQ------KESKARSGLKVLLALIKDGVGGRIisaHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 493 LCVKQKLGVNViycaPSDRLVYSPKTPIDDLRSFGFRSYLVDLVTGPIPLINKLCASYSIHNIPIG----------TEAV 562
Cdd:pfam02463 560 VEERQKLVRAL----TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvvegilkdTELT 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 563 GNYTSSIPKAIRVYFGGS-----------------KKFVVTASRYRSDTILTES----------SIRAKNQLITVDSQQL 615
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSleeglaeksevkaslseLTKELLEIQELQEKAESELakeeilrrqlEIKKKEQREKEELKKL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 616 ALVMKQCSEAVKESDSIKNAITQTDNEFERLQAVAKDE--QEKRRKLDQKIAHFNS---------LKTEIETLQKKLEAL 684
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLkekelaeerEKTEKLKVEEEKEEK 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 685 RNSDSLDCLETNFCNSLHKDLKKIFDADAELCSC--LKAIDRLIIEKNMAQTKV-----SIYMLQHETQIEALKESEEQS 757
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikEEELEELALELKEEQKLEklaeeELERLEEEITKEELLQELLLK 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 758 KAATRDF--------------------QQLLQCLENQISDVNKRKSAIQGLCH-----GEIPTSSKFPFKKEFRELENID 812
Cdd:pfam02463 876 EEELEEQklkdeleskeekekeekkelEEESQKLNLLEEKENEIEERIKEEAEillkyEEEPEELLLEEADEKEKEENNK 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 813 LPELREAIHDFQARLECMKsVNSEAISSYQGLQNEVKQLEEGIQESVNQAKSIESGMSNLYDKWEPKLNSLVETISTKFS 892
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGK-VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 893 EFMESIEYVGEVVLSKTDKYDFDSYGIQIMVQFrRGLQLQPLDKFiqSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQG 972
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARP-PGKGVKNLDLL--SGGEKTLVALALIFAIQKYKPAPFYLLDEIDAA 1111
|
1130 1140
....*....|....*....|....*....
gi 281366582 973 MDATNeRHIFDLLLKEATKHgsAQYLFVT 1001
Cdd:pfam02463 1112 LDDQN-VSRVANLLKELSKN--AQFIVIS 1137
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
16-89 |
1.17e-12 |
|
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: 68.01 E-value: 1.17e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281366582 16 IHSVYCKDFVSYS--EITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVR 89
Cdd:cd03276 1 IESITLKNFMCHRhlQIEFGPR--VNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVT 74
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
940-1002 |
2.84e-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: 63.77 E-value: 2.84e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366582 940 SGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDLLLKEATKHGSAQYLFVTP 1002
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
24-862 |
5.26e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 24 FVSYSEITFHPKHYLnvLTGPNGSGKSTIVSAIILGLGGEPILL-----------DRSasVADYI---QSNKTSATIIVR 89
Cdd:COG4913 14 FDGVHTIDFDGRGTL--LTGDNGSGKSTLLDAIQTLLVPAKRPRfnkaandagksDRT--LLSYVrgkYGSERDEAGTRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 90 VYGRTPNTT----ETFRriiNSNGLSTFSV----------NDKDTSKKNFLAAVSSFNIQ----------VSNLCQFLPQ 145
Cdd:COG4913 90 VYLRPGDTWsaiaATFA---NDGSGQTVTLaqvfwlkgdaSSLGDVKRFFVIADGPLDLEdfeefahgfdIRALKARLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 146 DRVQDFSK----------------MNPQELLLNTMSS-------------VCDE--------DLINSFNSLKQMRTEqan 188
Cdd:COG4913 167 QGVEFFDSfsaylarlrrrlgigsEKALRLLHKTQSFkpigdlddfvreyMLEEpdtfeaadALVEHFDDLERAHEA--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 189 vhanrekeksdLVKKQKRLEHLQMTVSQYKEREEVKQKLQvysakklwvetqagEAKAAEMKTQVKNAKTQSDKLKNQHD 268
Cdd:COG4913 244 -----------LEDAREQIELLEPIRELAERYAAARERLA--------------ELEYLRAALRLWFAQRRLELLEAELE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 269 KLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDG-KMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENK 347
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 348 IYELETLnksrpliVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEmipeITAYKLKIERLRNvkmqkideiRAKN- 426
Cdd:COG4913 379 AEEFAAL-------RAEAAALLEALEEELEALEEALAEAEAALRDLRRE----LRELEAEIASLER---------RKSNi 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 427 -PNLVVAMNWLAQNkqrykLNVY--DPMIL-EL-TVQNHEDA------KFLEN-----VVAQRDLFAFAcedkgdmsDLI 490
Cdd:COG4913 439 pARLLALRDALAEA-----LGLDeaELPFVgELiEVRPEEERwrgaieRVLGGfaltlLVPPEHYAAAL--------RWV 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 491 NELcvkqKLGVNVIY--CAPSDRLVYSPKTPIDDL------RSFGFRSYLVDLVTGPIPLInkLCASysihnipigTEAV 562
Cdd:COG4913 506 NRL----HLRGRLVYerVRTGLPDPERPRLDPDSLagkldfKPHPFRAWLEAELGRRFDYV--CVDS---------PEEL 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 563 GNYTSSIPKAIRVYFGGS---KKfvvTASRYRSDTILTESSIRAKNQLITvDSQQLALVMKQCSEAVKESDSIKNAITQT 639
Cdd:COG4913 571 RRHPRAITRAGQVKGNGTrheKD---DRRRIRSRYVLGFDNRAKLAALEA-ELAELEEELAEAEERLEALEAELDALQER 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 640 DNEFERLQAVAKDE------QEKRRKLDQKIAHFNSLKTEIETLQKKLEALRNSDsldcletnfcNSLHKDLKKIFDADA 713
Cdd:COG4913 647 REALQRLAEYSWDEidvasaEREIAELEAELERLDASSDDLAALEEQLEELEAEL----------EELEEELDELKGEIG 716
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 714 ELCSCLKAIDRLIIE-KNMAQTKVSIYMLQHETQIEALKESEEQSKAAtrdfQQLLQCLENQISDVNKRKSAIQG----- 787
Cdd:COG4913 717 RLEKELEQAEEELDElQDRLEAAEDLARLELRALLEERFAAALGDAVE----RELRENLEERIDALRARLNRAEEelera 792
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 788 ---------LCHGEIPTSSKFP--FKKEFRELENIDLPELREAIhdFQARLECMKSvNSEAISSYqgLQNEVKQLEEGIQ 856
Cdd:COG4913 793 mrafnrewpAETADLDADLESLpeYLALLDRLEEDGLPEYEERF--KELLNENSIE-FVADLLSK--LRRAIREIKERID 867
|
....*.
gi 281366582 857 EsVNQA 862
Cdd:COG4913 868 P-LNDS 872
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
19-206 |
7.23e-11 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 62.51 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 19 VYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSAS-----VADYIQSNKTSATIIVRVY-- 91
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGggfvkGDIRIGLEGKGKAYVEITFen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 92 --GRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSF---NIQVSNLCQFLPQDRVQDFSKMNPQELLlntmss 166
Cdd:pfam13476 81 ndGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELlksDKIILPLLVFLGQEREEEFERKEKKERL------ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 281366582 167 vcdEDLINSFNSLKQMRtEQANVHANREKEKSDLVKKQKR 206
Cdd:pfam13476 155 ---EELEKALEEKEDEK-KLLEKLLQLKEKKKELEELKEE 190
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-914 |
1.34e-09 |
|
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: 62.29 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSY---SEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGG------EPILLDRSASVADYIQSNKT--- 82
Cdd:TIGR00618 2 KPLRLTLKNFGSYkgtHTIDFTALGPIFLICGKTGAGKTTLLDAITYALYGklprrsEVIRSLNSLYAAPSEAAFAElef 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 83 -------SATIIVRVYGRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMN 155
Cdd:TIGR00618 82 slgtkiyRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 156 PQE---LLLNTMSSvcdeDLINSFNSLKQMRTEQANVHANREKEKSDLVK------KQKRLEHLQMTVSQYKEREEVKQK 226
Cdd:TIGR00618 162 SKEkkeLLMNLFPL----DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTlctpcmPDTYHERKQVLEKELKHLREALQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 227 LQVYSAK-----KLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQ------------EQIEKEKESLRKALL 289
Cdd:TIGR00618 238 TQQSHAYltqkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplaahikavTQIEQQAQRIHTELQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 290 EKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLvENKIYELETLNKSRPLIVSELERAK 369
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS-CQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 370 ESCA------AARGKAMEQYSRRRQLEQKLNdEMIPEITAYKLKIERLRNVKMQKIDEIRAKNPNLVVAmnwlaqnKQRY 443
Cdd:TIGR00618 397 SLCKeldilqREQATIDTRTSAFRDLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES-------AQSL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 444 KLNVYDPMILELTVQNHEDAKFLENVVAQRdLFAFACEDKGDMSDLINELCVKQKLGVNviyCAPSDRLVYSPKTPIDDL 523
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPL---TRRMQRGEQTYAQLETSE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 524 RSfgfrsylvdlVTGPIPLINKLCASYS------IHNIPIGTEAVGNYTSSIPKaIRVYFGGSKKFVVTASRYRsDTILT 597
Cdd:TIGR00618 545 ED----------VYHQLTSERKQRASLKeqmqeiQQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAE-DMLAC 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 598 ESSIRAKNQLITVDSQQLALVMKQCSEAVKESDSIKNAITQTDNEFERLQAVAKDEQEKRRKLDQKIAHFNSLKTEIETL 677
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQL 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 678 QKKLEALRNSDSLdcletnfCNSLHKDLKKIFDADAELCSCLKA-IDRLIIEKNMAQTKVSIYMLQHETQIEALKESEEQ 756
Cdd:TIGR00618 693 TYWKEMLAQCQTL-------LRELETHIEEYDREFNEIENASSSlGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 757 SKAATRDFQQLLQCLENQISDVNKRKSAIQGLCHgeiptsSKFPFKKEFRELENIDLPELREAIHDFQARLECMKSVNSE 836
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH------LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE 839
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366582 837 AISSYQGLQNEVKQLEEGIQEsVNQAKSIESGMSNLYDKWEPKLNSLVETISTKFSEFMESIEYVGEVVLSKTDKYDF 914
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQ-LAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
16-86 |
5.47e-09 |
|
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: 56.55 E-value: 5.47e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366582 16 IHSVYCKDFVSYSEITFHP-KHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVAD---YIQSNKTSATI 86
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGgSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLaggGVKAGINSASV 75
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-396 |
3.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 177 NSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMtvsqyKEREEVKQKLQVYSAKKLWVET-QAGEAKAAEMKTQVKN 255
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQA-----EEYELLAELARLEQDIARLEERrRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 256 AKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTAT 335
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366582 336 ECDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDE 396
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
939-1004 |
7.13e-08 |
|
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: 53.13 E-value: 7.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281366582 939 QSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDlLLKEATKHGsAQYLFVTPKL 1004
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAE-AILEHLVKG-AQVIVITHLP 141
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
15-94 |
7.19e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.86 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSY---SEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRVY 91
Cdd:COG0419 1 KLLRLRLENFRSYrdtETIDFDDG--LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHG 78
|
...
gi 281366582 92 GRT 94
Cdd:COG0419 79 GKR 81
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-90 |
8.15e-08 |
|
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: 52.75 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 11 QLAGRIHSVYCKDfvsySEITFHPKHyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRV 90
Cdd:cd03227 1 KIVLGRFPSYFVP----NDVTFGEGS-LTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFTR 75
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
15-429 |
8.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSY--SEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVrvyg 92
Cdd:PRK03918 2 KIEELKIKNFRSHksSVVEFDDG--INLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 93 rtpnttetfrriinsnglsTFSVNDKD-TSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFS-KMNPQELLLN-------- 162
Cdd:PRK03918 76 -------------------KFEKNGRKyRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVeRLIPYHVFLNaiyirqge 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 163 ---------TMSSVCD-----EDLINSFNSLKQMRTEQANvhanREKEKSDLVKKQKRLEHLQMTvsQYKEREEVKQKLQ 228
Cdd:PRK03918 137 idailesdeSREKVVRqilglDDYENAYKNLGEVIKEIKR----RIERLEKFIKRTENIEELIKE--KEKELEEVLREIN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 229 VYSAKKlwVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIE---KEKESLRKALLEKTRLLENAVAEKAAI 305
Cdd:PRK03918 211 EISSEL--PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKVKELKEL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 306 DGKMDS------LKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENKIYELETLNKSRPLIVSELERAKEScAAARGKA 379
Cdd:PRK03918 289 KEKAEEyiklseFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 281366582 380 MEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVKMQKIDEIRAKNPNL 429
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-425 |
1.46e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 170 EDLINSFNSLKQMRTEQANVHANREKEKSDLVKKQKRLEhlQMTVSQYKEREEVKQKLQVYSAK--KLWVETQAGEAKAA 247
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERleEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 248 EMKTQVKNAKTQSDKLKNQHDKLlqsqeqiEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNI 327
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDEL-------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 328 KKSRRTATECDNLNQlvenkiyELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLnDEMIPEITAYKLK 407
Cdd:TIGR02168 859 AEIEELEELIEELES-------ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-EELREKLAQLELR 930
|
250
....*....|....*...
gi 281366582 408 IERLRNVKMQKIDEIRAK 425
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEE 948
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
15-137 |
2.80e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.08 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSYS--EITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNK-TSATIIVRVY 91
Cdd:COG3950 2 RIKSLTIENFRGFEdlEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEfGDSAKLILYY 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 281366582 92 GrtpntteTFRRIinSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVS 137
Cdd:COG3950 82 G-------TSRLL--LDGPLKKLERLKEEYFSRLDGYDSLLDEDSN 118
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
179-426 |
4.26e-07 |
|
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: 53.96 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANREKEKSDL----VKKQKRLEHLQMTVSQYK---EREEVKQKLQVYSAKKLWVETQAGEAKAAEMKT 251
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLeiqlTAIKTSEEHYLKEVEDLKtelEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 252 QVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALlEKTRllENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSR 331
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL-ESVR--EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 332 RTATECDNLNQLVENK---IYELETLNKS--------------RPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLN 394
Cdd:pfam05483 591 ILENKCNNLKKQIENKnknIEELHQENKAlkkkgsaenkqlnaYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE 670
|
250 260 270
....*....|....*....|....*....|..
gi 281366582 395 DEMIPEITAYKLKIERLrnVKMQKIDEIRAKN 426
Cdd:pfam05483 671 EKLLEEVEKAKAIADEA--VKLQKEIDKRCQH 700
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
43-136 |
4.29e-07 |
|
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: 52.19 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 43 GPNGSGKSTIVSAIILGLGGEPILLdRSASVADYI----QSNKTSATIIVR-VYGRTPNTTETFRRIINSNGlSTFSVND 117
Cdd:cd03275 29 GPNGSGKSNLMDAISFVLGEKSSHL-RSKNLKDLIyrarVGKPDSNSAYVTaVYEDDDGEEKTFRRIITGGS-SSYRING 106
|
90
....*....|....*....
gi 281366582 118 KDTSKKNFLAAVSSFNIQV 136
Cdd:cd03275 107 KVVSLKEYNEELEKINILV 125
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
15-146 |
4.58e-07 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 53.23 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAI-ILGLGGEPilldRSASVADYIQSNKTSATIIVRVygR 93
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIyLLATGRSF----RTARDAELIRFGADGFRVRAEV--E 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 281366582 94 TPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVssFNIQVsnlcqFLPQD 146
Cdd:COG1195 75 RDGREVRLGLGLSRGGKKRVRINGKPVRRLSDLAGL--LPVVL-----FSPED 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-396 |
2.49e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 205 KRLEHLQmtvsqyKERE------EVKQKLQVYSAkKLWVetqageAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIE 278
Cdd:COG1196 200 RQLEPLE------RQAEkaeryrELKEELKELEA-ELLL------LKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 279 KEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENKIYELETLNKSR 358
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190
....*....|....*....|....*....|....*...
gi 281366582 359 PLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDE 396
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
15-90 |
4.89e-06 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 49.77 E-value: 4.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366582 15 RIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAI-ILGLGGEPilldRSASVADYIQSNKTSATIIVRV 90
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIyLLAPGRSH----RTARDKELIRFGAEAAVIHGRV 74
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
179-423 |
5.26e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANReKEKSDLVKKQKRLE-HLQMTVSQY----KEREE-VKQ--KLQVySAKKLWVETQAGEAKAAEMK 250
Cdd:pfam01576 748 VKQVRELEAELEDER-KQRAQAVAAKKKLElDLKELEAQIdaanKGREEaVKQlkKLQA-QMKDLQRELEEARASRDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 251 TQvknAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLE---NAVAEKAAIDGKMDSLKQGIYQKKYELEQ-- 325
Cdd:pfam01576 826 AQ---SKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEeq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 326 -NIK----KSRRTATECDNLN----------QLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEqySRRRQLE 390
Cdd:pfam01576 903 sNTEllndRLRKSTLQVEQLTtelaaerstsQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALE--AKIAQLE 980
|
250 260 270
....*....|....*....|....*....|....*.
gi 281366582 391 QKLNDEMIPEITAYKL---KIERLRNVKMQKIDEIR 423
Cdd:pfam01576 981 EQLEQESRERQAANKLvrrTEKKLKEVLLQVEDERR 1016
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
16-90 |
5.75e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 49.22 E-value: 5.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366582 16 IHSVYCKDFVSYSEIT--FHPKHylNVLTGPNGSGKSTIVSAI-ILGLGGEpillDRSASVADYIQSNKTSATIIVRV 90
Cdd:cd03242 1 LKSLELRNFRNYAELEleFEPGV--TVLVGENAQGKTNLLEAIsLLATGKS----HRTSRDKELIRWGAEEAKISAVL 72
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
16-446 |
1.34e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 16 IHSVYCKDFVSY--SEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEpillDRSASVADYIQSNKTSAT-------- 85
Cdd:PRK01156 3 IKRIRLKNFLSHddSEIEFDTG--INIITGKNGAGKSSIVDAIRFALFTD----KRTEKIEDMIKKGKNNLEvelefrig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 86 ----IIVRVYGRTPNTTETFRRIINSNGLSTFSVNDKDT---------SKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFS 152
Cdd:PRK01156 77 ghvyQIRRSIERRGKGSRREAYIKKDGSIIAEGFDDTTKyieknilgiSKDVFLNSIFVGQGEMDSLISGDPAQRKKILD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 153 KMnpqeLLLNTMSSVCD--EDLINSFnslkqmrteQANVhANREKEKSDLVKKQKRLEHLQMTVSQykerEEVKQKLQVY 230
Cdd:PRK01156 157 EI----LEINSLERNYDklKDVIDML---------RAEI-SNIDYLEEKLKSSNLELENIKKQIAD----DEKSHSITLK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 231 SAKKLWVETQAGEAKAAEMKTQVKNAKTQSDKLK--NQHDKLLQSQEQIEKEKESLRKALLEKTRLLEN--AVAEKAAID 306
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNryESEIKTAESDLSMELEKNNYYKELEERHMKIINdpVYKNRNYIN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 307 ------GKMDSLKQGIYQKKYEL---EQNIKKSRRTATECDNLNQL------VENKIYELETLNKSRPLIVSELERAKes 371
Cdd:PRK01156 299 dyfkykNDIENKKQILSNIDAEInkyHAIIKKLSVLQKDYNDYIKKksryddLNNQILELEGYEMDYNSYLKSIESLK-- 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366582 372 caaargKAMEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVKMQKIDEIRAKNPNLVVAMNWLAQNKQRYKLN 446
Cdd:PRK01156 377 ------KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-423 |
1.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 183 RTEQANVHANREKEKSDLVKKQkrlehlqmtVSQYKEREEVKQKLQVYSAKKLwvETQAGEAKAAEMKTQVKNAKTQSDK 262
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKK---------AEEAKKAAEAAKAEAEAAADEA--EAAEEKAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 263 LKNQH----DKLLQSQEQIEKEKESLRKALLEKTRLLEnaVAEKAAIDGKMDSLKQGIYQKKYELEqnIKKSRRTATECD 338
Cdd:PTZ00121 1385 KKAEEkkkaDEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 339 NLNQLVENKIYELETLNKSRPliVSELERAKESCAAARGKAMEqySRRRQLEQKLNDEMipEITAYKLKIERLRNV-KMQ 417
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEA--KKAEEAKKADEAKKAeEAK 1534
|
....*.
gi 281366582 418 KIDEIR 423
Cdd:PTZ00121 1535 KADEAK 1540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-395 |
1.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 170 EDLINSFNSLKQMRTEQANvHANREKEKSDLVKKQKRlEHLQMTVSQYKEREEVKQklqvysAKKLWVETQAGEAKAAEM 249
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEE-EKKKVEQLKKKEAEEKKK------AEELKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 250 KTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKAllEKTRLLENAVAEKAAIDGKMDSL-KQGIYQKKYELEQNIK 328
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA--EELKKKEAEEKKKAEELKKAEEEnKIKAEEAKKEAEEDKK 1744
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 329 KS---RRTATECDNLNQLVENKIYELETLNKSRPLIVSElerakescaaarGKAMEQYSRRRQLEQKLND 395
Cdd:PTZ00121 1745 KAeeaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE------------ELDEEDEKRRMEVDKKIKD 1802
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
15-334 |
2.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILglggepILLDRSASVADYIqsnktsatiiVRVYGRT 94
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRA------MLLERLEKEADEL----------FKPQGRK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 95 PnttetfrrIINSNGLSTFSVNDKDTSKKNflaavssfniqvsnlcqflpqdrvqdfskmnpqelllntmssvcdEDLIN 174
Cdd:COG4717 66 P--------ELNLKELKELEEELKEAEEKE---------------------------------------------EEYAE 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 175 SFNSLKQMRTEQANVhanrEKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAKklWVETQAGEAKAAEMKTQVK 254
Cdd:COG4717 93 LQEELEELEEELEEL----EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER--LEELEERLEELRELEEELE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 255 NAKTQSDKLKNQHDKLLQSQ--------EQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGiyQKKYELEQN 326
Cdd:COG4717 167 ELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE--LEAAALEER 244
|
....*...
gi 281366582 327 IKKSRRTA 334
Cdd:COG4717 245 LKEARLLL 252
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
29-138 |
3.23e-05 |
|
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: 46.81 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 29 EITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGepilldrSASvADYIQSNKTSAtIIVRVYGRTPNTTETF------- 101
Cdd:cd03241 16 ELDFEEG--LTVLTGETGAGKSILLDALSLLLGG-------RAS-ADLIRSGAEKA-VVEGVFDISDEEEAKAlllelgi 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 281366582 102 --------RRIINSNGLSTFSVNDKDTSKKnFLAAVSS--FNIQVSN 138
Cdd:cd03241 85 eddddliiRREISRKGRSRYFINGQSVTLK-LLRELGSllVDIHGQH 130
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
22-105 |
4.11e-05 |
|
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: 45.72 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 22 KDFVSY---SEITFHPKHYLN--VLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATI---------- 86
Cdd:cd03279 9 KNFGPFreeQVIDFTGLDNNGlfLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVsftfqlggkk 88
|
90 100
....*....|....*....|.
gi 281366582 87 --IVRVYGRtpnTTETFRRII 105
Cdd:cd03279 89 yrVERSRGL---DYDQFTRIV 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-425 |
4.66e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 194 EKEKSDLVKKQKRLEHLQMTVSQY----KEREEVKQKLQvysakKLWVETQAGEAKAAEMKTQVKNAKTQSDKLKnqhdK 269
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYiklsEFYEEYLDELR-----EIEKRLSRLEEEINGIEERIKELEEKEERLE----E 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 270 LLQSQEQIEKEKESLRkallEKTRLLENAVAEKAaidgKMDSLKQ--GIYQKKyELEQNIKKSRRTATECDNLNQLVENK 347
Cdd:PRK03918 343 LKKKLKELEKRLEELE----ERHELYEEAKAKKE----ELERLKKrlTGLTPE-KLEKELEELEKAKEEIEEEISKITAR 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366582 348 IYELETLNKSRPLIVSELERAKESCAAArgkameqysrRRQLEQKLNDEMIPEitaYKLKIERLRNvKMQKIDEIRAK 425
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCPVC----------GRELTEEHRKELLEE---YTAELKRIEK-ELKEIEEKERK 477
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-104 |
5.11e-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: 45.29 E-value: 5.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366582 28 SEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLGGE-PILLDRSASVADYIQSNKTSATIIVRVYGRTPNTTETFRRI 104
Cdd:cd03240 16 SEIEFFSP--LTLIVGQNGAGKTTIIEALKYALTGElPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRSL 91
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
15-138 |
8.63e-05 |
|
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: 46.15 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEpilLDRSASVAD-YIQSNKTSATIIVRVYgr 93
Cdd:COG3593 2 KLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS---SSRKFDEEDfYLGDDPDLPEIEIELT-- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 281366582 94 tpnTTETFRRIINSNGlstfsvndKDTSKKNFLAAVSSFNIQVSN 138
Cdd:COG3593 77 ---FGSLLSRLLRLLL--------KEEDKEELEEALEELNEELKE 110
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
15-428 |
8.96e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 46.65 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSV-YCKDFVSYSEITFhpKHYLNVLTGPNGSGKSTIvSAIILGLGGEPILLDRSASVAdyIQSNKTSATIIVRVYGR 93
Cdd:COG4694 4 KIKKLkNVGAFKDFGWLAF--FKKLNLIYGENGSGKSTL-SRILRSLELGDTSSEVIAEFE--IEAGGSAPNPSVRVFNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 94 -------------------TPNTTETFRRIINSNGlstfSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKM 154
Cdd:COG4694 79 dfveenlrsgeeikgiftlGEENIELEEEIEELEK----EIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 155 NPQEL-------LLNTMSSVCDEDLINSFNSLKQMRTEQANVHANREkEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKL 227
Cdd:COG4694 155 FASSGrnyrkanLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPIT-PLPDLKALLSEAETLLEKSAVSSAIEELAALI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 228 QvYSAKKLWVEtqAGEAKAAEMKTQV---------KNAKTQ-----SDKLKNQHDKLLQSQEQIEKEKESLRKalLEKTR 293
Cdd:COG4694 234 Q-NPGNSDWVE--QGLAYHKEEEDDTcpfcqqelaAERIEAleayfDDEYEKLLAALKDLLEELESAINALSA--LLLEI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 294 LLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTAT-ECDNLNQLVENKIYELETLNKSRPLIVSELERAKESC 372
Cdd:COG4694 309 LRTLLPSAKEDLKAALEALNALLETLLAALEEKIANPSTSIDlDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366582 373 AAA-----RGKAMEQYSRRRQLEQKLNDEmIPEITAYKLKIERLRNvkmqKIDEIRAKNPN 428
Cdd:COG4694 389 RKKleaheLAELKEDLSRYKAEVEELIEE-LKTIKALKKALEDLKT----EISELEAELSS 444
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
614-786 |
9.75e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 614 QLALVMKQCSEAVKESDSIKNAITQTDNEFERLQAVAKDEQEKRRKLDQKIAhfnSLKTEIETLQKKLEAL--------- 684
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERreelgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 685 ---RNSDSLDCLE--------TNFCNSLHKdLKKIFDADAELcscLKAIDRLIIEKNMAQTKVSIYMLQHETQIEALKES 753
Cdd:COG3883 94 alyRSGGSVSYLDvllgsesfSDFLDRLSA-LSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|...
gi 281366582 754 EEQSKAATRDFQQLLQCLENQISDVNKRKSAIQ 786
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
15-330 |
1.00e-04 |
|
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: 46.05 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGL-GGEPILLDRSASVADYIQSNKTSATIIVRVYGR 93
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLnNKEKFFEDDFLVLYLKDVIKIDKEDLNIFENIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 94 TPNTTE---TFRRIINSNgLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMNPQELLLNtmSSVCDE 170
Cdd:pfam13175 82 FSIDIEidvEFLLILFGY-LEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYI--YNNYYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 171 DLINSFNSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLqmTVSQYKEREEVKQKLQVYSAKKLWVETQAGEAKAAEMK 250
Cdd:pfam13175 159 DEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKL--INELEKSINYHENVLENLQIKKLLISADRNASDEDSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 251 TQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENavaekaAIDGKMDSLKQGIYQKKYELEQNIKKS 330
Cdd:pfam13175 237 INSLLGALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKN------ILFKKIDKLKDFGYPPFLNPEIEIKKD 310
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
15-56 |
1.15e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.69 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 281366582 15 RIHSVYCKDFVSYSEITFHPkHYLNVLTGPNGSGKSTIVSAI 56
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPL-GPLTVLIGANGSGKSNLLDAL 41
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
253-425 |
1.27e-04 |
|
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: 45.88 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 253 VKNAKTQSDKlkNQHDKLLQ-SQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGkmdslKQGIY--QKKYELEQNIKK 329
Cdd:pfam17380 278 VQHQKAVSER--QQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR-----QAAIYaeQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 330 SRRTATECDNLNQLVE--------NKIYELETLNKSRPlivSELERAKESCAAARGKAMEQYSRRRQLEQKLNdemipEI 401
Cdd:pfam17380 351 ERIRQEERKRELERIRqeeiameiSRMRELERLQMERQ---QKNERVRQELEAARKVKILEEERQRKIQQQKV-----EM 422
|
170 180
....*....|....*....|....
gi 281366582 402 TAYKLKIERLRNVKMQKIDEIRAK 425
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERAR 446
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
22-90 |
1.51e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 45.42 E-value: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366582 22 KDFVSYSEIT--FHPKhyLNVLTGPNGSGKSTIVSAI-ILGLGGEpillDRSASVADYIQSNKTSATIIVRV 90
Cdd:TIGR00611 9 TDFRNYDAVDleLSPG--VNVIVGPNGQGKTNLLEAIyYLALGRS----HRTSRDKPLIRFGAEAFVIEGRV 74
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
180-356 |
1.92e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 180 KQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEReevkqklqVYSAKKLWVETQAGEAKAAEMKTQVKNAKTQ 259
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEK--------LVSTEKEKIEEKSETEKLLEYITELSCVSEQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 260 SDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEkaaIDGKMDSLKQgiyQKKYELEQNIKKSRRTATECDN 339
Cdd:pfam15905 238 VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD---LNEKCKLLES---EKEELLREYEEKEQTLNAELEE 311
|
170
....*....|....*..
gi 281366582 340 LNQLVENKIYELETLNK 356
Cdd:pfam15905 312 LKEKLTLEEQEHQKLQQ 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
179-366 |
3.22e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEreEVKQKlqvysakklwvetqagEAKAAEMKTQVKNAKT 258
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK--EIKRL----------------ELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 259 QSDKLKNQHD-KLLQSQ-EQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRtate 336
Cdd:COG1579 81 QLGNVRNNKEyEALQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA---- 156
|
170 180 190
....*....|....*....|....*....|
gi 281366582 337 cdnlnqlvenkiyELETLNKSRPLIVSELE 366
Cdd:COG1579 157 -------------ELEELEAEREELAAKIP 173
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-421 |
3.47e-04 |
|
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: 44.67 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 178 SLKQMRTEQANVHANREKEKsdLVKKQKRLEHLQmtvsqyKEREEVKQKLQVYSAKKLWVETQAGEAKAAEMK------- 250
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKER--LEELEEDLSSLE------QEIENVKSELKELEARIEELEEDLHKLEEALNDlearlsh 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 251 TQVKNAKTQSDKLKNQHDKLLQSQEQIEKE--KESLRKALLEKTR---------LLENAVAEKAAID---GKMDSLKQGI 316
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKlnRLTLEKEYLEKEIqelqeqridLKEQIKSIEKEIEnlnGKKEELEEEL 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 317 YQKKYELEQNIKKSRRTATECDNL-NQL--VENKIYELETLNKSRPLIVSELErAKESCAAARGKAMEQySRRRQLEQKL 393
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELeAQLreLERKIEELEAQIEKKRKRLSELK-AKLEALEEELSEIED-PKGEDEEIPE 948
|
250 260 270
....*....|....*....|....*....|..
gi 281366582 394 NDEMIPEITAYKLKIER----LRNVKMQKIDE 421
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEeiraLEPVNMLAIQE 980
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
243-429 |
5.16e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 243 EAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQiEKEKESLRkallEKTRLLENAVAEKAAI--------------DGK 308
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLE----ERREDLEELIAERRETieekreraeelrerAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 309 MDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENKIYELETLNKSRPLIV---SELERAKESCAA-------ARGK 378
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAdaeDEIERLREKREAlaelndeRRER 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 281366582 379 AMEQYSRRRQLEQKLNDEMIPEITAYKLKIER-LRNVKmQKIDEIRAKNPNL 429
Cdd:PRK02224 629 LAEKRERKRELEAEFDEARIEEAREDKERAEEyLEQVE-EKLDELREERDDL 679
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
15-155 |
7.35e-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: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 15 RIHSVYCKDFVSYSEIT----FHPKhyLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYI----QSNKTSATI 86
Cdd:cd03273 2 HIKEIILDGFKSYATRTvisgFDPQ--FNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIykrgQAGITKASV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366582 87 IVRVYGRTPNTTE---------TFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMN 155
Cdd:cd03273 80 TIVFDNSDKSQSPigfenypeiTVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMG 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
623-864 |
9.37e-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: 42.83 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 623 SEAVKESDSIKNAITQTDNEFERLQAVAKDEQEKRRKLDQKIAhfnSLKTEIETLQKKLEALRnsDSLDCLETNFcNSLH 702
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQELAALE--AELAELEKEI-AELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 703 KDLKKIFDADAELcscLKAIDR---------LIIEKNMAQTKVSIYMLQH-----ETQIEALKESEEQSKAATRDFQQLL 768
Cdd:COG4942 97 AELEAQKEELAEL---LRALYRlgrqpplalLLSPEDFLDAVRRLQYLKYlaparREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 769 QCLENQISDVNKRKSAIQGLchgeiptsskfpfKKEFRELenidLPELREAIHDFQARLEcmksvnsEAISSYQGLQNEV 848
Cdd:COG4942 174 AELEALLAELEEERAALEAL-------------KAERQKL----LARLEKELAELAAELA-------ELQQEAEELEALI 229
|
250
....*....|....*.
gi 281366582 849 KQLEEGIQESVNQAKS 864
Cdd:COG4942 230 ARLEAEAAAAAERTPA 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
194-423 |
1.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 194 EKEKSDLVKKqkRLEHLQMTVSQYKEREEVKQKLQvySAKKLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQS 273
Cdd:PTZ00121 1481 EAKKADEAKK--KAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 274 QEQIEKEK--ESLRKALLEKTRLLENA----VAEKAAIDGKMDSLKQGIYQKKYELE---------QNIKKSRRTATECD 338
Cdd:PTZ00121 1557 LKKAEEKKkaEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKkaeeakikaEELKKAEEEKKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 339 NLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEqySRRRQLEQKLNDEMIPEITAYKLKIERLRNV---K 415
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEAKKAEELKKKeaeE 1714
|
....*...
gi 281366582 416 MQKIDEIR 423
Cdd:PTZ00121 1715 KKKAEELK 1722
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
16-119 |
1.08e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.26 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 16 IHSVYCKDF--VSYSEITFHPkhyLNVLTGPNGSGKSTIVSAIILGLGGEPILL--DRSASVADYiqsnKTSATIIVRVY 91
Cdd:COG4938 1 IKSISIKNFgpFKEAELELKP---LTLLIGPNGSGKSTLIQALLLLLQSNFIYLpaERSGPARLY----PSLVRELSDLG 73
|
90 100
....*....|....*....|....*...
gi 281366582 92 GRTPNTTETFRRIINSNGLSTFSVNDKD 119
Cdd:COG4938 74 SRGEYTADFLAELENLEILDDKSKELLE 101
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
207-425 |
1.15e-03 |
|
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: 42.79 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 207 LEHLQMTVSQYKEREEVKQKLqvysakkLWVETQAGEAKAAEMKTQVKNAKTQSDKLKN---QHDKLLQSQEQIEKEKES 283
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKI-------ITMELQKKSSELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 284 LRKALLEKTRLLENAVAEKAAIDGKMDSLK-------QGIYQKKYELEQNIKKSRRTATECDNLnqLVENKIYELETLNk 356
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKtseehylKEVEDLKTELEKEKLKNIELTAHCDKL--LLENKELTQEASD- 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366582 357 srplIVSELERAKE---SCAAARGKAMEQYSRRRQLEQKLNDEMipeitayklkiERLRNVKMQKIDEIRAK 425
Cdd:pfam05483 511 ----MTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDEL-----------ESVREEFIQKGDEVKCK 567
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
22-61 |
1.37e-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: 40.91 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281366582 22 KDFVSYSEITFHPKhyLNVLTGPNGSGKSTIVSAIILGLG 61
Cdd:cd03278 10 KSFADKTTIPFPPG--LTAIVGPNGSGKSNIIDAIRWVLG 47
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-424 |
1.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 183 RTEQANVHANREKEKSDLVKK---QKRLEHLQMTVSQYKEREEVKQKLQvySAKKlwvetQAGEA-KAAEMKTQVKNAKT 258
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKaeeAKKADEAKKKAEEAKKADEAKKKAE--EAKK-----KADEAkKAAEAKKKADEAKK 1517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 259 QSDKLKNQHDKLLQSQEQIE--KEKESLRKA-LLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTAT 335
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADeaKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 336 EcdnlnqlvenKIYELETLNKSRPLIVSELERAKescAAARGKAMEQYSRRRQLEQKLNDEmipeitayKLKIERLRnvK 415
Cdd:PTZ00121 1598 M----------KLYEEEKKMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEE--------KKKAEELK--K 1654
|
....*....
gi 281366582 416 MQKIDEIRA 424
Cdd:PTZ00121 1655 AEEENKIKA 1663
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
194-394 |
1.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 194 EKEKSDLVKKQKRLEHLQMtvsqyKEREEVKQKLQVYSAK-KLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQ 272
Cdd:COG4717 52 EKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKeEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 273 SQEQIEkEKESLRKALLEKTRLLENAVAEKAAIDG---KMDSLKQGIYQKKYELEQniKKSRRTATECDNLNQLVEnkiy 349
Cdd:COG4717 127 LLPLYQ-ELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEE--LLEQLSLATEEELQDLAE---- 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 281366582 350 ELETLNKSRPLIVSELERAKESCAAARgKAMEQYSRRRQLEQKLN 394
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELE-EELEQLENELEAAALEE 243
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
30-57 |
1.81e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 1.81e-03
10 20
....*....|....*....|....*....
gi 281366582 30 ITFHPK-HYLnvLTGPNGSGKSTIVSAII 57
Cdd:pfam13555 17 IPIDPRgNTL--LTGPSGSGKSTLLDAIQ 43
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
179-309 |
3.16e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANREKEKSdlvKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAKKLwvetqagEAKAAEMKTQVKNAKT 258
Cdd:TIGR02794 91 QKELEQRAAAEKAAKQAEQA---AKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA-------KEEAAKQAEEEAKAKA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 281366582 259 QSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKM 309
Cdd:TIGR02794 161 AAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAA 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
179-370 |
3.67e-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: 41.16 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYK-EREEVKQKLQVYSAKKLWVETQAGEAKAAEMKTQVKNAK 257
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 258 TQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKaaiDGKMDSLKQGIYQKKyELEQNIKKSrrtatec 337
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN---QSYKQEIKNLESQIN-DLESKIQNQ------- 403
|
170 180 190
....*....|....*....|....*....|...
gi 281366582 338 DNLNQLVENKIyelETLNKSRPLIVSELERAKE 370
Cdd:TIGR04523 404 EKLNQQKDEQI---KKLQQEKELLEKEIERLKE 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-425 |
4.05e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 231 SAKKLWVETQAGEAKAAEMKTQVknaktqsDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMD 310
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERL-------EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 311 SLKQGIYQKKYELEQnikksrrtatecdnLNQLVENKIYELETLNKSrpliVSELERAKESCAAARGKameqysrrrqLE 390
Cdd:TIGR02169 734 KLKERLEELEEDLSS--------------LEQEIENVKSELKELEAR----IEELEEDLHKLEEALND----------LE 785
|
170 180 190
....*....|....*....|....*....|....*
gi 281366582 391 QKLNDEMIPEITAYKLKIERLRNVKMQKIDEIRAK 425
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
198-397 |
4.30e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 198 SDLVKKQKRLEHLQMTVSQYKErEEVKQKLQVYSAKKLWVETQAGEAKAAEMKT---QVKNAKTQSDKLKNQHDKLLQSQ 274
Cdd:pfam10174 510 SSGLKKDSKLKSLEIAVEQKKE-ECSKLENQLKKAHNAEEAVRTNPEINDRIRLleqEVARYKEESGKAQAEVERLLGIL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 275 EQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLVEnkiyELETL 354
Cdd:pfam10174 589 REVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEE----LMGAL 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 281366582 355 NKSRplivSELERAK------ESCAAARGKAME--QYSRRRQLEQKLndEM 397
Cdd:pfam10174 665 EKTR----QELDATKarlsstQQSLAEKDGHLTnlRAERRKQLEEIL--EM 709
|
|
| COG4185 |
COG4185 |
Predicted ABC-type ATPase or kinase [General function prediction only]; |
34-77 |
7.13e-03 |
|
Predicted ABC-type ATPase or kinase [General function prediction only];
Pssm-ID: 443339 Cd Length: 197 Bit Score: 39.10 E-value: 7.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 281366582 34 PKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDrsasvADYI 77
Cdd:COG4185 2 AMPRLYIIAGPNGAGKSTFARTILPEELGGLEFVN-----ADLI 40
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
186-370 |
8.12e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 186 QANVhANREKEKSDLVK-------------KQKRLEHLQMTVSQYKEREEVKQKLQVYSAKKLWVETQAGE-------AK 245
Cdd:pfam15905 121 SASV-ASLEKQLLELTRvnellkakfsedgTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQknlehskGK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 246 AAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAvaekAAIDGKMDSLKQGIYQKKYELEQ 325
Cdd:pfam15905 200 VAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELL----KEKNDEIESLKQSLEEKEQELSK 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 281366582 326 NIKKsrrTATECDNLNQLVENKIYELETLNKSRpliVSELERAKE 370
Cdd:pfam15905 276 QIKD---LNEKCKLLESEKEELLREYEEKEQTL---NAELEELKE 314
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
179-348 |
8.68e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKER----------EEVKQKLQVYSAKKLW-VETQAGEAKAA 247
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRlqqirnllkgGKVGGKALRPSQRVLLqAEQALLNAQND 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 248 EMKTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLL-ENAVAEKAAIDGKMDSLKQGIYQKkyELEQN 326
Cdd:PRK11281 210 LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLsEKTVQEAQSQDEAARIQANPLVAQ--ELEIN 287
|
170 180
....*....|....*....|..
gi 281366582 327 IKKSRRTATECDNLNQLVENKI 348
Cdd:PRK11281 288 LQLSQRLLKATEKLNTLTQQNL 309
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
179-479 |
9.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 179 LKQMRTEQANVHANREKEKSDLVKKQKRLEhlqmtvsqyKEREEVKQKLQVYSAKklwvetqagEAKAAEMKTQVKNAKT 258
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELE---------ELNEQLQAAQAELAQA---------QEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 259 QSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGI-YQKKYELEQNIKKSRRTATEC 337
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqALSEAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366582 338 DNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVKMQ 417
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366582 418 KIDEIRAKNPNLVVAmnwlAQNKQRYKLNVYDPMILELTVQNHEDAKFLENVVAQRDLFAFA 479
Cdd:COG4372 276 EELEIAALELEALEE----AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| |
