|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
956-1072 |
4.85e-66 |
|
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: 221.70 E-value: 4.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 956 EKPKDYAEW-KIEIMVKFRDNAPLKKLDSHTQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVE 1034
Cdd:cd03277 96 DRVGEFAKLsPIELLVKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVE 175
|
90 100 110
....*....|....*....|....*....|....*...
gi 6324539 1035 NACAENTSQYFLITPKLLTGLHYHEKMRIHCVMAGSWI 1072
Cdd:cd03277 176 TACKEGTSQYFLITPKLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
40-198 |
4.54e-54 |
|
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: 187.80 E-value: 4.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 40 GSIIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEITLKNS 119
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324539 120 PNvtdieyidardetikitriitrskrrsdylindyqvsesvvktlvaqlNIQLDNLCQFLSQERVEEFARLKSVKLLV 198
Cdd:cd03277 81 PG------------------------------------------------NIQVDNLCQFLPQDRVGEFAKLSPIELLV 111
|
|
| Smc5_CC_C |
cd22879 |
C-terminal coiled-coil domain of Saccharomyces cerevisiae structural maintenance of ... |
739-811 |
1.48e-25 |
|
C-terminal coiled-coil domain of Saccharomyces cerevisiae structural maintenance of chromosomes protein 5 (Smc5) and similar proteins; Smc5 acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. It functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Smc5 is a component of the Smc5-Smc6 complex which plays a critical role in chromosome stability maintenance, DNA replication, homologous recombination, and double-stranded DNA damage repair. Smc5 contains N- and C-terminal coiled-coil (CC) domains, which wrap together to form an intertwined coiled-coil structure. The model corresponds to the C-terminal CC domain of Smc5.
Pssm-ID: 467855 [Multi-domain] Cd Length: 73 Bit Score: 100.77 E-value: 1.48e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324539 739 DVSQKIKDIDDQIQQLLLKQRHLLSKMASSMKSLKNCQKELISTQILQFEAQNMDVSMNDVIGFFNEREADLK 811
Cdd:cd22879 1 DVSQKIKDCEAQIASLLKKQTKLLREMVEFMKKLQDCQKELLEADIAYFEARNLERSMNEVIGFFNEKEEELR 73
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-1048 |
8.55e-23 |
|
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: 105.54 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY-TLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSK-----IEIT 115
Cdd:TIGR02169 2 IERIELENFKSFgKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSgneayVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 116 LKNSPNVTDIEYidardeTIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNIQLD--------NLCQFLS---QER 184
Cdd:TIGR02169 82 FKNDDGKFPDEL------EVVRRLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEgynvvlqgDVTDFISmspVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 185 ---------VEEFAR--------LKSVKLLVETIRSIDASLLDVLD-----------------ELRELQGNE-------- 222
Cdd:TIGR02169 156 rkiideiagVAEFDRkkekaleeLEEVEENIERLDLIIDEKRQQLErlrrerekaeryqallkEKREYEGYEllkekeal 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 223 -----------QSLQKDLDFKKAKIVHLRQESDKLRKSVESLRDFQNKKGEIE----------LHSQLLPYV-------- 273
Cdd:TIGR02169 236 erqkeaierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkekigeLEAEIASLErsiaeker 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 274 KVKDHKEKLNIYKEEYERAKANLRAILKD-----------KKPFANTKKTLE---NQVEELTEKCSLKTDEFLKAKEKIN 339
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREieeerkrrdklTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYREKLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 340 EIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILaqthlpeksvfEDIDIKRKEIINKEGEIRDLI 419
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-----------EDKALEIKKQEWKLEQLAADL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 420 SEIDAKANAINHEMRSIQRQAESKTKSLTTTDKigilnqdqDLKEVRDAVLMVREHPEMKDKILEPPIMTVSAINAQFAA 499
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEA--------QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 500 YLAQC-VDYNTSKALTVVDSDSYKLFANPILDKFKVN------LRELSSADTTPPVPAETvrdlGFEGYLSDFITGDKR- 571
Cdd:TIGR02169 537 YATAIeVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGratflpLNKMRDERRDLSILSED----GVIGFAVDLVEFDPKy 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 572 ---VMKMLCQTSKIHTIPVSRRELTPAQIKKL----------IT---PRPNGKILFKRIIHGN--RLVDIKQSAYGSKQV 633
Cdd:TIGR02169 613 epaFKYVFGDTLVVEDIEAARRLMGKYRMVTLegelfeksgaMTggsRAPRGGILFSRSEPAElqRLRERLEGLKRELSS 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 634 FPTDV-SIKQTNFYQGSIMSNEQK--IRIENEIINLKNEYN-------DRKSTLDALSNQKSGYRHELSELASKNDDINR 703
Cdd:TIGR02169 693 LQSELrRIENRLDELSQELSDASRkiGEIEKEIEQLEQEEEklkerleELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 704 EAHQ----LNEIRKKYTMrkSTIETLREKLDQLKREaRKDVSQKIKDIDDQIQQLLLKQRHLLSKMassmkslKNCQKEL 779
Cdd:TIGR02169 773 DLHKleeaLNDLEARLSH--SRIPEIQAELSKLEEE-VSRIEARLREIEQKLNRLTLEKEYLEKEI-------QELQEQR 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 780 IstqilqfEAQNMDVSMNDVIGFFNEREADLKSQYEDKKKFVKEM--------RDTPEFQSWMREIRSYDQDTKEKLNKv 851
Cdd:TIGR02169 843 I-------DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlgdlkKERDELEAQLRELERKIEELEAQIEK- 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 852 AEKYEEEGNFNLSFVQDVLDKLESEIAMVNHDESAVTILDQVTAELRELEHTV----------PQQSKDLETIKAKLKED 921
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIralepvnmlaIQEYEEVLKRLDELKEK 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 922 HAVLEPKLDDIV------------------SKISARFARLFNNV-GSAGAVRLEKPKDYAEWKIEIMVKFRDNaPLKKLD 982
Cdd:TIGR02169 995 RAKLEEERKAILerieeyekkkrevfmeafEAINENFNEIFAELsGGTGELILENPDDPFAGGLELSAKPKGK-PVQRLE 1073
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324539 983 ShtQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVENAcaeNTSQYFLIT 1048
Cdd:TIGR02169 1074 A--MSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKA---GEAQFIVVS 1134
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
42-1028 |
4.15e-19 |
|
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: 93.50 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY-TLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFI--KNGQDVSK--IEITL 116
Cdd:pfam02463 2 LKRIEIEGFKSYaKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsKSGAFVNSaeVEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 117 KNSPNVTDIEyidarDETIKITRIITRSKrRSDYLINDYQVSESVVKTLVAQLNIQLDNLcQFLSQERVEEFARLKSVKL 196
Cdd:pfam02463 82 DNEDHELPID-----KEEVSIRRRVYRGG-DSEYYINGKNVTKKEVAELLESQGISPEAY-NFLVQGGKIEIIAMMKPER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 197 LVETIRSIDASLLDV-----LDELRELQGNEQSLQ-KDLDFKKAKIVHLRQESDKLRKSVESLRDFqnKKGEIELHSQLL 270
Cdd:pfam02463 155 RLEIEEEAAGSRLKRkkkeaLKKLIEETENLAELIiDLEELKLQELKLKEQAKKALEYYQLKEKLE--LEEEYLLYLDYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 271 PYVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKT-LENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIR 349
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 350 DEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAQTHLPEKSVFEDID---------------------IKRKEI 408
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQekleqleeellakkkleserlSSAAKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 409 INKEGEIRDL----ISEIDAKANAINHEMRSIQRQAESKTKSLT--TTDKIGILNQDQDLKEVRDAVLMVREHPEMKDKI 482
Cdd:pfam02463 393 KEEELELKSEeekeAQLLLELARQLEDLLKEEKKEELEILEEEEesIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 483 LEPPIMTVS---------AINAQFAAYLAQCVDYNTSKALTVVDSDSYKLFAN----------PILDKFKV-NLRELSSA 542
Cdd:pfam02463 473 LLKETQLVKlqeqlelllSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIsahgrlgdlgVAVENYKVaISTAVIVE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 543 DTTPPVPAETVRDLGFEGYLSDFITGDKRVMKMLCQTSKIHTIPVSRRELTPAQIKKLITPRPNGKILFKRIIHGNRLVD 622
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 623 IKQSAYGSKQVFPTDVSIKQTNFYQGSIMS----------------NEQKIRIENEIINLKNEYNDRKSTLDALSNQKSG 686
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSevkaslseltkelleiQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 687 YRHELSELASKNDDINREAHQLNEIRKKYTMRKSTIETLREKLDQLKREARKD----VSQKIKDIDDQIQQLLLK----Q 758
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEkselSLKEKELAEEREKTEKLKveeeK 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 759 RHLLSKMASSMKSLKNCQK----------------ELISTQILQFEAQNMDVSMNDVIGFFNEREADLKSQYEDK----- 817
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKeeaelleeeqllieqeEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEllqel 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 818 --------------KKFVKEMRDTPEFQSWMREIRSYD---QDTKEKLNKVAEKYEEEGNFNLSFVQDVLDKLESEIAMV 880
Cdd:pfam02463 873 llkeeeleeqklkdELESKEEKEKEEKKELEEESQKLNlleEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEE 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 881 NHDE----------SAVTILDQVTAELRELEHTVPQQSKDLETIKAKLKEDHAVLEPKLDDIVSKISARFARLFN----- 945
Cdd:pfam02463 953 NNKEeeeernkrllLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVsinkg 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 946 --------NVGSAGAVRLEKPKDYAEWKIEIMVKFRdNAPLKKLDShtQSGGERAVSTVLYMIALQEFTSAPFRVVDEIN 1017
Cdd:pfam02463 1033 wnkvffylELGGSAELRLEDPDDPFSGGIEISARPP-GKGVKNLDL--LSGGEKTLVALALIFAIQKYKPAPFYLLDEID 1109
|
1130
....*....|.
gi 6324539 1018 QGMDSRNERIV 1028
Cdd:pfam02463 1110 AALDDQNVSRV 1120
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
45-227 |
1.65e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 73.30 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 45 IRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVE------DFIKNGQDVSKIEITLKN 118
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGfvkgdiRIGLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 119 spnvTDIEYIDARDETIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNIQLdNLCQFLSQERVEEFARLKSVKLLV 198
Cdd:pfam13476 81 ----NDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLE 155
|
170 180 190
....*....|....*....|....*....|.
gi 6324539 199 ETIRSID--ASLLDVLDELRELQGNEQSLQK 227
Cdd:pfam13476 156 ELEKALEekEDEKKLLEKLLQLKEKKKELEE 186
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
42-219 |
3.01e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 69.65 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY-TLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEyiGRSKKVEDFIKNGQDVSKIEITLKNSP 120
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 121 NvtdiEYIDARDETIKITRIITRSKRRSDYL-----INDYQVSESVVKTLVAQLNIQLDNL--CQFLSQERVEEFARLKS 193
Cdd:COG0419 80 K----RYRIERRQGEFAEFLEAKPSERKEALkrllgLEIYEELKERLKELEEALESALEELaeLQKLKQEILAQLSGLDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6324539 194 VKLLV--ETIR--------------SIDA-SLLDVLDELRELQ 219
Cdd:COG0419 156 IETLSggERLRlaladllslildfgSLDEeRLERLLDALEELA 198
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-421 |
3.00e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEITLKN--- 118
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKngr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 119 --------SPNVTDIEYIDARDETI----------------------------KITRIITRSKRRSDYL-----INDYQV 157
Cdd:PRK03918 83 kyrivrsfNRGESYLKYLDGSEVLEegdssvrewverlipyhvflnaiyirqgEIDAILESDESREKVVrqilgLDDYEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 158 SESVVKTLVAQLNIQLDNLCQFLSQ-ERVEEfaRLKSV-KLLVETIRSIDaSLLDVLDELRELQGNEQSLQKDLDFKKAK 235
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRtENIEE--LIKEKeKELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 236 IVHLRQESDKLRKSVESL----RDFQNKKGEIELHSQLLPYvKVKDHKEkLNIYKEEYERAKANLRAILKDKKPFANTKK 311
Cdd:PRK03918 240 IEELEKELESLEGSKRKLeekiRELEERIEELKKEIEELEE-KVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 312 TLENQVEELTEKCSlktdEFLKAKEKINEIFEKLNTIRDEVIK-KKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAQT 390
Cdd:PRK03918 318 RLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEElEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
410 420 430
....*....|....*....|....*....|.
gi 6324539 391 HLPEKSVfEDIDIKRKEIINKEGEIRDLISE 421
Cdd:PRK03918 394 EELEKAK-EEIEEEISKITARIGELKKEIKE 423
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-470 |
4.31e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 56 TEFNLSPSLNMIIGPNGSGKSTFVCAV--CLGLAG-KpeyIGRSKKVEDFIKNGQDVSK------IEITLKNSPNVTDIE 126
Cdd:COG1196 18 TTIPFEPGITAIVGPNGSGKSNIVDAIrwVLGEQSaK---SLRGGKMEDVIFAGSSSRKplgraeVSLTFDNSDGTLPID 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 127 YidardETIKITRIITRSKrRSDYLINDYQVSESVVKTLVAQLNI-----------QLDNLCQFLSQER---VEEFA--- 189
Cdd:COG1196 95 Y-----DEVTITRRLYRSG-ESEYYINGKPCRLKDIQDLFLDTGLgpesysiigqgMIDRIIEAKPEERraiIEEAAgis 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 190 -----------RLKSV-------------------------------KLLVETIRSIDASLLdvLDELRELQGNEQSLQK 227
Cdd:COG1196 169 kykerkeeaerKLEATeenlerledilgelerqleplerqaekaeryRELKEELKELEAELL--LLKLRELEAELEELEA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 228 DLDFKKAKIVHLRQESDKLRKSVESLRDFQNKKGEielhsqllpyvKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFA 307
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELEL-----------ELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 308 NTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEIL 387
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 388 AQTHLPEKSVFEDIDIKRKEIINKEGEIRDLISEIDAKANAI----NHEMRSIQRQAESKTKSLTTTDKIGILNQDQDLK 463
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeeeEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
....*..
gi 6324539 464 EVRDAVL 470
Cdd:COG1196 476 EAALAEL 482
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
47-173 |
5.94e-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: 43.50 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 47 LQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVC-LGLAGKpeyiGRSKKVEDFIKNGQDVSKIEITLKNSpnvtdi 125
Cdd:TIGR00611 8 LTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYyLALGRS----HRTSRDKPLIRFGAEAFVIEGRVSKG------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6324539 126 eyidarDETIKITRIITRSKRRSDYLINdyQVSESVVKTLVAQLNIQL 173
Cdd:TIGR00611 78 ------DREVTIPLEGLLKKKGKKAKVN--IDGQDKLSDLAGLLPMQL 117
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
44-151 |
1.87e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 41.68 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 44 KIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLgLAgkpeyIGRSKKV---EDFIKNGQDVSKIEITL--KN 118
Cdd:PRK00064 5 RLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-----PGRSHRTardKELIRFGAEAAVIHGRVekGG 78
|
90 100 110
....*....|....*....|....*....|...
gi 6324539 119 SPNVTDIEYIDARDETIKITRIitRSKRRSDYL 151
Cdd:PRK00064 79 RELPLGLEIDKKGGRKVRINGE--PQRKLAELA 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
956-1072 |
4.85e-66 |
|
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: 221.70 E-value: 4.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 956 EKPKDYAEW-KIEIMVKFRDNAPLKKLDSHTQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVE 1034
Cdd:cd03277 96 DRVGEFAKLsPIELLVKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVE 175
|
90 100 110
....*....|....*....|....*....|....*...
gi 6324539 1035 NACAENTSQYFLITPKLLTGLHYHEKMRIHCVMAGSWI 1072
Cdd:cd03277 176 TACKEGTSQYFLITPKLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
40-198 |
4.54e-54 |
|
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: 187.80 E-value: 4.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 40 GSIIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEITLKNS 119
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324539 120 PNvtdieyidardetikitriitrskrrsdylindyqvsesvvktlvaqlNIQLDNLCQFLSQERVEEFARLKSVKLLV 198
Cdd:cd03277 81 PG------------------------------------------------NIQVDNLCQFLPQDRVGEFAKLSPIELLV 111
|
|
| Smc5_CC_C |
cd22879 |
C-terminal coiled-coil domain of Saccharomyces cerevisiae structural maintenance of ... |
739-811 |
1.48e-25 |
|
C-terminal coiled-coil domain of Saccharomyces cerevisiae structural maintenance of chromosomes protein 5 (Smc5) and similar proteins; Smc5 acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. It functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Smc5 is a component of the Smc5-Smc6 complex which plays a critical role in chromosome stability maintenance, DNA replication, homologous recombination, and double-stranded DNA damage repair. Smc5 contains N- and C-terminal coiled-coil (CC) domains, which wrap together to form an intertwined coiled-coil structure. The model corresponds to the C-terminal CC domain of Smc5.
Pssm-ID: 467855 [Multi-domain] Cd Length: 73 Bit Score: 100.77 E-value: 1.48e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324539 739 DVSQKIKDIDDQIQQLLLKQRHLLSKMASSMKSLKNCQKELISTQILQFEAQNMDVSMNDVIGFFNEREADLK 811
Cdd:cd22879 1 DVSQKIKDCEAQIASLLKKQTKLLREMVEFMKKLQDCQKELLEADIAYFEARNLERSMNEVIGFFNEKEEELR 73
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-1048 |
8.55e-23 |
|
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: 105.54 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY-TLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSK-----IEIT 115
Cdd:TIGR02169 2 IERIELENFKSFgKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSgneayVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 116 LKNSPNVTDIEYidardeTIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNIQLD--------NLCQFLS---QER 184
Cdd:TIGR02169 82 FKNDDGKFPDEL------EVVRRLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEgynvvlqgDVTDFISmspVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 185 ---------VEEFAR--------LKSVKLLVETIRSIDASLLDVLD-----------------ELRELQGNE-------- 222
Cdd:TIGR02169 156 rkiideiagVAEFDRkkekaleeLEEVEENIERLDLIIDEKRQQLErlrrerekaeryqallkEKREYEGYEllkekeal 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 223 -----------QSLQKDLDFKKAKIVHLRQESDKLRKSVESLRDFQNKKGEIE----------LHSQLLPYV-------- 273
Cdd:TIGR02169 236 erqkeaierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkekigeLEAEIASLErsiaeker 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 274 KVKDHKEKLNIYKEEYERAKANLRAILKD-----------KKPFANTKKTLE---NQVEELTEKCSLKTDEFLKAKEKIN 339
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREieeerkrrdklTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYREKLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 340 EIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILaqthlpeksvfEDIDIKRKEIINKEGEIRDLI 419
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-----------EDKALEIKKQEWKLEQLAADL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 420 SEIDAKANAINHEMRSIQRQAESKTKSLTTTDKigilnqdqDLKEVRDAVLMVREHPEMKDKILEPPIMTVSAINAQFAA 499
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEA--------QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 500 YLAQC-VDYNTSKALTVVDSDSYKLFANPILDKFKVN------LRELSSADTTPPVPAETvrdlGFEGYLSDFITGDKR- 571
Cdd:TIGR02169 537 YATAIeVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGratflpLNKMRDERRDLSILSED----GVIGFAVDLVEFDPKy 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 572 ---VMKMLCQTSKIHTIPVSRRELTPAQIKKL----------IT---PRPNGKILFKRIIHGN--RLVDIKQSAYGSKQV 633
Cdd:TIGR02169 613 epaFKYVFGDTLVVEDIEAARRLMGKYRMVTLegelfeksgaMTggsRAPRGGILFSRSEPAElqRLRERLEGLKRELSS 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 634 FPTDV-SIKQTNFYQGSIMSNEQK--IRIENEIINLKNEYN-------DRKSTLDALSNQKSGYRHELSELASKNDDINR 703
Cdd:TIGR02169 693 LQSELrRIENRLDELSQELSDASRkiGEIEKEIEQLEQEEEklkerleELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 704 EAHQ----LNEIRKKYTMrkSTIETLREKLDQLKREaRKDVSQKIKDIDDQIQQLLLKQRHLLSKMassmkslKNCQKEL 779
Cdd:TIGR02169 773 DLHKleeaLNDLEARLSH--SRIPEIQAELSKLEEE-VSRIEARLREIEQKLNRLTLEKEYLEKEI-------QELQEQR 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 780 IstqilqfEAQNMDVSMNDVIGFFNEREADLKSQYEDKKKFVKEM--------RDTPEFQSWMREIRSYDQDTKEKLNKv 851
Cdd:TIGR02169 843 I-------DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlgdlkKERDELEAQLRELERKIEELEAQIEK- 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 852 AEKYEEEGNFNLSFVQDVLDKLESEIAMVNHDESAVTILDQVTAELRELEHTV----------PQQSKDLETIKAKLKED 921
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIralepvnmlaIQEYEEVLKRLDELKEK 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 922 HAVLEPKLDDIV------------------SKISARFARLFNNV-GSAGAVRLEKPKDYAEWKIEIMVKFRDNaPLKKLD 982
Cdd:TIGR02169 995 RAKLEEERKAILerieeyekkkrevfmeafEAINENFNEIFAELsGGTGELILENPDDPFAGGLELSAKPKGK-PVQRLE 1073
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324539 983 ShtQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVENAcaeNTSQYFLIT 1048
Cdd:TIGR02169 1074 A--MSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKA---GEAQFIVVS 1134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-968 |
6.93e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 96.28 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYT-LTEFNLSPSLNMIIGPNGSGKSTFVCAV--CLGLAGKPEYigRSKKVEDFIKNG------QDVSKI 112
Cdd:TIGR02168 2 LKKLELAGFKSFAdPTTINFDKGITGIVGPNGCGKSNIVDAIrwVLGEQSAKAL--RGGKMEDVIFNGsetrkpLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 113 EITLKNSPNVTDIeyidARDETIKITRIITRSkRRSDYLIND---------------------Y------QVSESV---- 161
Cdd:TIGR02168 80 ELVFDNSDGLLPG----ADYSEISITRRLYRD-GESEYFINGqpcrlkdiqdlfldtglgkrsYsiieqgKISEIIeakp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 162 ------------------------------------VKTLVAQLNIQLDNLcqFLSQERVEEFARLK------------- 192
Cdd:TIGR02168 155 eerraifeeaagiskykerrketerklertrenldrLEDILNELERQLKSL--ERQAEKAERYKELKaelrelelallvl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 193 SVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSVESLR-DFQNKKGEIELHSQLLP 271
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 272 YVKVK---------DHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIF 342
Cdd:TIGR02168 313 NLERQleeleaqleELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 343 EKLNTIRDEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAQTHLPE-KSVFEDIDIKRKEIINKEGEIRDLISE 421
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEElEEELEELQEELERLEEALEELREELEE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 422 IDAKANAINHEMRSIQrqaeSKTKSLTTtdkigILNQDQDLKEVRDAVLMVRE-----HPEMKDKIlEPPIMTVSAINAQ 496
Cdd:TIGR02168 473 AEQALDAAERELAQLQ----ARLDSLER-----LQENLEGFSEGVKALLKNQSglsgiLGVLSELI-SVDEGYEAAIEAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 497 FAAYLAQCVDYNTSKALTVVDSDSYKlfanpilDKFKVNLRELSSADTTPPVPAETVRDLGFEGYLSdfitgdkrvmkml 576
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKAIAFLKQN-------ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG------------- 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 577 cqtskihtiPVSRRELTPAQIKKLITPRPNGKILFKRIIHGNRLvdIKQSAYGS-------KQVFPTDVSIKQTNFYQGS 649
Cdd:TIGR02168 603 ---------VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL--AKKLRPGYrivtldgDLVRPGGVITGGSAKTNSS 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 650 IMSNEQKI-RIENEIINLKNEYNDRKSTLDALSNQKSGYRHELSELASKNDDINReahQLNEIRKKYTMRKSTIETLREK 728
Cdd:TIGR02168 672 ILERRREIeELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR---QISALRKDLARLEAEVEQLEER 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 729 LDQLKREaRKDVSQKIKDIDDQIQQLLLKQRHLLSKMASSMKSLKNcQKELISTQILQFEAQNMDVS-MNDVIGFFNERE 807
Cdd:TIGR02168 749 IAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-LKEELKALREALDELRAELTlLNEEAANLRERL 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 808 ADLKSQYEDKKkfvKEMRDTPEFQSWMREIRSYDQDTKEKLNKVAEKYEEEgnfnLSFVQDVLDKLESEIAMVNHDesav 887
Cdd:TIGR02168 827 ESLERRIAATE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE----LEALLNERASLEEALALLRSE---- 895
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 888 tiLDQVTAELRELEHTVP---QQSKDLETIKAKLKEDHAVLEPKLDDIVSKISARFARLFNNvgsAGAVRLEKPKDYAEW 964
Cdd:TIGR02168 896 --LEELSEELRELESKRSelrRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEA 970
|
....
gi 6324539 965 KIEI 968
Cdd:TIGR02168 971 RRRL 974
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
42-1028 |
4.15e-19 |
|
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: 93.50 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY-TLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFI--KNGQDVSK--IEITL 116
Cdd:pfam02463 2 LKRIEIEGFKSYaKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsKSGAFVNSaeVEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 117 KNSPNVTDIEyidarDETIKITRIITRSKrRSDYLINDYQVSESVVKTLVAQLNIQLDNLcQFLSQERVEEFARLKSVKL 196
Cdd:pfam02463 82 DNEDHELPID-----KEEVSIRRRVYRGG-DSEYYINGKNVTKKEVAELLESQGISPEAY-NFLVQGGKIEIIAMMKPER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 197 LVETIRSIDASLLDV-----LDELRELQGNEQSLQ-KDLDFKKAKIVHLRQESDKLRKSVESLRDFqnKKGEIELHSQLL 270
Cdd:pfam02463 155 RLEIEEEAAGSRLKRkkkeaLKKLIEETENLAELIiDLEELKLQELKLKEQAKKALEYYQLKEKLE--LEEEYLLYLDYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 271 PYVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKT-LENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIR 349
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 350 DEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAQTHLPEKSVFEDID---------------------IKRKEI 408
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQekleqleeellakkkleserlSSAAKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 409 INKEGEIRDL----ISEIDAKANAINHEMRSIQRQAESKTKSLT--TTDKIGILNQDQDLKEVRDAVLMVREHPEMKDKI 482
Cdd:pfam02463 393 KEEELELKSEeekeAQLLLELARQLEDLLKEEKKEELEILEEEEesIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 483 LEPPIMTVS---------AINAQFAAYLAQCVDYNTSKALTVVDSDSYKLFAN----------PILDKFKV-NLRELSSA 542
Cdd:pfam02463 473 LLKETQLVKlqeqlelllSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIsahgrlgdlgVAVENYKVaISTAVIVE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 543 DTTPPVPAETVRDLGFEGYLSDFITGDKRVMKMLCQTSKIHTIPVSRRELTPAQIKKLITPRPNGKILFKRIIHGNRLVD 622
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 623 IKQSAYGSKQVFPTDVSIKQTNFYQGSIMS----------------NEQKIRIENEIINLKNEYNDRKSTLDALSNQKSG 686
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSevkaslseltkelleiQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 687 YRHELSELASKNDDINREAHQLNEIRKKYTMRKSTIETLREKLDQLKREARKD----VSQKIKDIDDQIQQLLLK----Q 758
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEkselSLKEKELAEEREKTEKLKveeeK 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 759 RHLLSKMASSMKSLKNCQK----------------ELISTQILQFEAQNMDVSMNDVIGFFNEREADLKSQYEDK----- 817
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKeeaelleeeqllieqeEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEllqel 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 818 --------------KKFVKEMRDTPEFQSWMREIRSYD---QDTKEKLNKVAEKYEEEGNFNLSFVQDVLDKLESEIAMV 880
Cdd:pfam02463 873 llkeeeleeqklkdELESKEEKEKEEKKELEEESQKLNlleEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEE 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 881 NHDE----------SAVTILDQVTAELRELEHTVPQQSKDLETIKAKLKEDHAVLEPKLDDIVSKISARFARLFN----- 945
Cdd:pfam02463 953 NNKEeeeernkrllLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVsinkg 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 946 --------NVGSAGAVRLEKPKDYAEWKIEIMVKFRdNAPLKKLDShtQSGGERAVSTVLYMIALQEFTSAPFRVVDEIN 1017
Cdd:pfam02463 1033 wnkvffylELGGSAELRLEDPDDPFSGGIEISARPP-GKGVKNLDL--LSGGEKTLVALALIFAIQKYKPAPFYLLDEID 1109
|
1130
....*....|.
gi 6324539 1018 QGMDSRNERIV 1028
Cdd:pfam02463 1110 AALDDQNVSRV 1120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
986-1066 |
9.09e-19 |
|
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: 85.05 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 986 QSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVENACaeNTSQYFLITPKLLTGLHYHEKMRIHC 1065
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
.
gi 6324539 1066 V 1066
Cdd:cd03239 173 V 173
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
42-119 |
4.27e-16 |
|
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: 78.02 E-value: 4.27e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEITLKNS 119
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTLKNQ 78
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
45-227 |
1.65e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 73.30 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 45 IRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVE------DFIKNGQDVSKIEITLKN 118
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGfvkgdiRIGLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 119 spnvTDIEYIDARDETIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNIQLdNLCQFLSQERVEEFARLKSVKLLV 198
Cdd:pfam13476 81 ----NDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLE 155
|
170 180 190
....*....|....*....|....*....|.
gi 6324539 199 ETIRSID--ASLLDVLDELRELQGNEQSLQK 227
Cdd:pfam13476 156 ELEKALEekEDEKKLLEKLLQLKEKKKELEE 186
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
42-219 |
3.01e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 69.65 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY-TLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEyiGRSKKVEDFIKNGQDVSKIEITLKNSP 120
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 121 NvtdiEYIDARDETIKITRIITRSKRRSDYL-----INDYQVSESVVKTLVAQLNIQLDNL--CQFLSQERVEEFARLKS 193
Cdd:COG0419 80 K----RYRIERRQGEFAEFLEAKPSERKEALkrllgLEIYEELKERLKELEEALESALEELaeLQKLKQEILAQLSGLDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6324539 194 VKLLV--ETIR--------------SIDA-SLLDVLDELRELQ 219
Cdd:COG0419 156 IETLSggERLRlaladllslildfgSLDEeRLERLLDALEELA 198
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
42-119 |
7.37e-13 |
|
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: 68.10 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEF-NLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVED---FIKNGQDVSKIEITLK 117
Cdd:cd03239 1 IKQITLKNFKSYRDETVvGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLaggGVKAGINSASVEITFD 80
|
..
gi 6324539 118 NS 119
Cdd:cd03239 81 KS 82
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-421 |
3.00e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEITLKN--- 118
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKngr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 119 --------SPNVTDIEYIDARDETI----------------------------KITRIITRSKRRSDYL-----INDYQV 157
Cdd:PRK03918 83 kyrivrsfNRGESYLKYLDGSEVLEegdssvrewverlipyhvflnaiyirqgEIDAILESDESREKVVrqilgLDDYEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 158 SESVVKTLVAQLNIQLDNLCQFLSQ-ERVEEfaRLKSV-KLLVETIRSIDaSLLDVLDELRELQGNEQSLQKDLDFKKAK 235
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRtENIEE--LIKEKeKELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 236 IVHLRQESDKLRKSVESL----RDFQNKKGEIELHSQLLPYvKVKDHKEkLNIYKEEYERAKANLRAILKDKKPFANTKK 311
Cdd:PRK03918 240 IEELEKELESLEGSKRKLeekiRELEERIEELKKEIEELEE-KVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 312 TLENQVEELTEKCSlktdEFLKAKEKINEIFEKLNTIRDEVIK-KKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAQT 390
Cdd:PRK03918 318 RLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEElEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
410 420 430
....*....|....*....|....*....|.
gi 6324539 391 HLPEKSVfEDIDIKRKEIINKEGEIRDLISE 421
Cdd:PRK03918 394 EELEKAK-EEIEEEISKITARIGELKKEIKE 423
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-470 |
4.31e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 56 TEFNLSPSLNMIIGPNGSGKSTFVCAV--CLGLAG-KpeyIGRSKKVEDFIKNGQDVSK------IEITLKNSPNVTDIE 126
Cdd:COG1196 18 TTIPFEPGITAIVGPNGSGKSNIVDAIrwVLGEQSaK---SLRGGKMEDVIFAGSSSRKplgraeVSLTFDNSDGTLPID 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 127 YidardETIKITRIITRSKrRSDYLINDYQVSESVVKTLVAQLNI-----------QLDNLCQFLSQER---VEEFA--- 189
Cdd:COG1196 95 Y-----DEVTITRRLYRSG-ESEYYINGKPCRLKDIQDLFLDTGLgpesysiigqgMIDRIIEAKPEERraiIEEAAgis 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 190 -----------RLKSV-------------------------------KLLVETIRSIDASLLdvLDELRELQGNEQSLQK 227
Cdd:COG1196 169 kykerkeeaerKLEATeenlerledilgelerqleplerqaekaeryRELKEELKELEAELL--LLKLRELEAELEELEA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 228 DLDFKKAKIVHLRQESDKLRKSVESLRDFQNKKGEielhsqllpyvKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFA 307
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELEL-----------ELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 308 NTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEIL 387
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 388 AQTHLPEKSVFEDIDIKRKEIINKEGEIRDLISEIDAKANAI----NHEMRSIQRQAESKTKSLTTTDKIGILNQDQDLK 463
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeeeEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
....*..
gi 6324539 464 EVRDAVL 470
Cdd:COG1196 476 EAALAEL 482
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
984-1069 |
7.25e-12 |
|
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: 64.69 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 984 HTQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVENACaeNTSQYFLITPKLLTGLHYHEKMRI 1063
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV--KGAQVIVITHLPELAELADKLIHI 153
|
....*.
gi 6324539 1064 HCVMAG 1069
Cdd:cd03227 154 KKVITG 159
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
985-1064 |
2.70e-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: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 985 TQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGMDSRNERIVHKAMVENACAENTSQYFLITPKLLTGLHYHEKMRIH 1064
Cdd:cd03276 109 TLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
42-447 |
4.02e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 67.23 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPeyigRSKKVEDFIKNGQDVSKIEITLKNSPN 121
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 122 VTDI--------EYIDARDETIKITRIITRS-KRRSDYL-INDYQVSESVVKTLVAQLNIQLDNLCQFLSQERVEEFARL 191
Cdd:PRK01156 79 VYQIrrsierrgKGSRREAYIKKDGSIIAEGfDDTTKYIeKNILGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 192 KSVKLLVETIrsidASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSvESLRDFQNKKGEIELHSQLLP 271
Cdd:PRK01156 159 LEINSLERNY----DKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKS-HSITLKEIERLSIEYNNAMDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 272 YVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEkcsLKTDEFLKAKEKINEIFeklntirde 351
Cdd:PRK01156 234 YNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMK---IINDPVYKNRNYINDYF--------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 352 viKKKNQNEYYRGRTKKLQATiISTKEDFLRSQEILAQTH---LPEKSVFEDIDIKRKEIINKEGEIRDLISEIDAKANA 428
Cdd:PRK01156 302 --KYKNDIENKKQILSNIDAE-INKYHAIIKKLSVLQKDYndyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK 378
|
410
....*....|....*....
gi 6324539 429 INHEMRSIQRQAESKTKSL 447
Cdd:PRK01156 379 IEEYSKNIERMSAFISEIL 397
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
42-171 |
1.51e-08 |
|
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: 56.81 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY----TLTEFNlspSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIgRSKKVEDFIKNGqdvsKIEITLK 117
Cdd:cd03275 1 LKRLELENFKSYkgrhVIGPFD---RFTCIIGPNGSGKSNLMDAISFVLGEKSSHL-RSKNLKDLIYRA----RVGKPDS 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6324539 118 NSPNVTdIEYIDARDETIKITRIITRSkrRSDYLINDYQVSESVVKTLVAQLNI 171
Cdd:cd03275 73 NSAYVT-AVYEDDDGEEKTFRRIITGG--SSSYRINGKVVSLKEYNEELEKINI 123
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
61-116 |
1.27e-07 |
|
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: 52.36 E-value: 1.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324539 61 SPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKkvedFIKNGQDVSKIEITL 116
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS----GVKAGCIVAAVSAEL 71
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
42-380 |
2.12e-07 |
|
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: 54.53 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYigrsKKVEDFIKNGQDVSKIEITLKNSPN 121
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKF----FEDDFLVLYLKDVIKIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 122 VTDIEyidaRDETIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNIQLDNLCQFLSQERVEEFARLKSVKLLVETI 201
Cdd:pfam13175 79 NISFS----IDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 202 RSIDASLLDVLDelrelqgnEQSLQKDLDFKkakivHLRQESDKlrksVESLRDFQNKKgeiELHSQLLPYVKVKDHKEK 281
Cdd:pfam13175 155 NYYLDEKKNVFD--------KKSKYELPSLK-----EEFLNSEK----EEIKVDKEDLK---KLINELEKSINYHENVLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 282 LNIYKEEYERAKANLRAILKDKKPFANTkKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEY 361
Cdd:pfam13175 215 NLQIKKLLISADRNASDEDSEKINSLLG-ALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKIDKLK 293
|
330
....*....|....*....
gi 6324539 362 YRGRTKKLQATIISTKEDF 380
Cdd:pfam13175 294 DFGYPPFLNPEIEIKKDDE 312
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-901 |
2.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 57 EFNLSPSLNMIIGPNGSGKSTFVCAVCLGL--AGKPEY------IGRSKK-----VEDFIKNGQDVSKIEIT-LKNSPNV 122
Cdd:COG4913 19 TIDFDGRGTLLTGDNGSGKSTLLDAIQTLLvpAKRPRFnkaandAGKSDRtllsyVRGKYGSERDEAGTRPVyLRPGDTW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 123 TDI--EY-IDARDETIKITRII-------TRSKRRSDYLINDYQVSESVVKTLVAQLNIqlDNLCQFLSQERVEEF---- 188
Cdd:COG4913 99 SAIaaTFaNDGSGQTVTLAQVFwlkgdasSLGDVKRFFVIADGPLDLEDFEEFAHGFDI--RALKARLKKQGVEFFdsfs 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 189 ---ARL---------KSVKLLVET-----IRSIDASLLD-VLDElRELQGNEQSLQKDLDfkkaKIVHLRQESDKLRKSV 250
Cdd:COG4913 177 aylARLrrrlgigseKALRLLHKTqsfkpIGDLDDFVREyMLEE-PDTFEAADALVEHFD----DLERAHEALEDAREQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 251 ESLR-------DFQNKKGEIELHSQLLPYVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEK 323
Cdd:COG4913 252 ELLEpirelaeRYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 324 C-SLKTDEFLKAKEKIneifEKLNTIRDEVIKKKNQneyYRGRTKKLQATIISTKEDFLRSQEILAQThlpeksvFEDID 402
Cdd:COG4913 332 IrGNGGDRLEQLEREI----ERLERELEERERRRAR---LEALLAALGLPLPASAEEFAALRAEAAAL-------LEALE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 403 IKRKEIINKEGEIRDLISEIDAKANAINHEMRSIQRQAesktksltttdkigiLNQDQDLKEVRDAVlmvREHpeMKDKI 482
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRK---------------SNIPARLLALRDAL---AEA--LGLDE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 483 LEPPI----MTVS--------AINAqfaaYLAqcvdyntSKALT-VVDSDSYKLFA---NPILDKFKVNLRELSSADTTP 546
Cdd:COG4913 458 AELPFvgelIEVRpeeerwrgAIER----VLG-------GFALTlLVPPEHYAAALrwvNRLHLRGRLVYERVRTGLPDP 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 547 PVPAE---------TVRDLGFEGYLSDFITGDKRVMKmlCQTSK--IHTipvsRRELTPA-QIKklitprpngkilfkri 614
Cdd:COG4913 527 ERPRLdpdslagklDFKPHPFRAWLEAELGRRFDYVC--VDSPEelRRH----PRAITRAgQVK---------------- 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 615 iHGNRLVDI-KQSAYGSKQVFptdvsikqtnfyqGSimSNEQKI--------RIENEIINLKNEYNDRKSTLDALSNQKS 685
Cdd:COG4913 585 -GNGTRHEKdDRRRIRSRYVL-------------GF--DNRAKLaaleaelaELEEELAEAEERLEALEAELDALQERRE 648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 686 GYRHeLSELASKNDDINREAHQLNEIRKKYT-MRKS--TIETLREKLDQLK------REARKDVSQKIKDIDDQIQQLLL 756
Cdd:COG4913 649 ALQR-LAEYSWDEIDVASAEREIAELEAELErLDASsdDLAALEEQLEELEaeleelEEELDELKGEIGRLEKELEQAEE 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 757 KQRHLLSKMASsmkSLKNCQKELISTQILQFEAQNMDVSMNDVIGFFNEREADLKSQYEDK-KKFVKEMRD-----TPEF 830
Cdd:COG4913 728 ELDELQDRLEA---AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAeEELERAMRAfnrewPAET 804
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 831 QSWMREIRSYDqDTKEKLNKVAE----KYEEE-----GNFNLSFVQDVLDKLESEIamvnhdESAVTILDQVTAELRELE 901
Cdd:COG4913 805 ADLDADLESLP-EYLALLDRLEEdglpEYEERfkellNENSIEFVADLLSKLRRAI------REIKERIDPLNDSLKRIP 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-378 |
2.52e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 212 LDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSVESLRDfqnkkgeieLHSQLLPYVKVKDHKEKLNIYKEEYER 291
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK---------LLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 292 AKANLRAI--LKDKKPFANTK-KTLENQVEELTEKCSLKT-DEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEYYRGRTK 367
Cdd:COG4717 151 LEERLEELreLEEELEELEAElAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|.
gi 6324539 368 KLQATIISTKE 378
Cdd:COG4717 231 QLENELEAAAL 241
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
59-171 |
3.41e-06 |
|
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: 49.60 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 59 NLSPSLNMIIGPNGSGKSTFVCAVC--LGLAGKPEYigRSKKVEDFI-KNGQD-VSK--IEITLKNS-PNVTDIEYIDAR 131
Cdd:cd03273 22 GFDPQFNAITGLNGSGKSNILDAICfvLGITNLSTV--RASNLQDLIyKRGQAgITKasVTIVFDNSdKSQSPIGFENYP 99
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6324539 132 deTIKITRIITRSkRRSDYLINDYQVSESVVKTLV--AQLNI 171
Cdd:cd03273 100 --EITVTRQIVLG-GTNKYLINGHRAQQQRVQDLFqsVQLNV 138
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
42-119 |
3.52e-06 |
|
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: 49.00 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYT-LTEFNLSPSLNMIIGPNGSGKSTFVCAV--CLGLAGKPEYigRSKKVEDFIKNG------QDVSKI 112
Cdd:cd03278 1 LKKLELKGFKSFAdKTTIPFPPGLTAIVGPNGSGKSNIIDAIrwVLGEQSAKSL--RGEKMSDVIFAGsetrkpANFAEV 78
|
....*..
gi 6324539 113 EITLKNS 119
Cdd:cd03278 79 TLTFDNS 85
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
42-214 |
3.74e-06 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 50.54 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKpeyiG-RSKKVEDFIKNGQDVSKIEITLKNsp 120
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGR----SfRTARDAELIRFGADGFRVRAEVER-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 121 nvtdieyiDARDETIKITriITRSKRRSdYLINDyqvsESVVKT--LVAQLNIQ--------------------LDNLCQ 178
Cdd:COG1195 76 --------DGREVRLGLG--LSRGGKKR-VRING----KPVRRLsdLAGLLPVVlfspedlrlvkggpserrrfLDRLLF 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6324539 179 FLSQERVEEFARLKSV-----KLLvETIRSIDASLLDVLDE 214
Cdd:COG1195 141 QLDPRYLDALSRYERAlkqrnALL-KQGREADLALLDVWDE 180
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
64-436 |
9.83e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 49.73 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 64 LNMIIGPNGSGKSTFVCAV-CLGLAGKPEYIGRSKKVE-DFIKNGQDVS---------KIEITLKNSPNVTDIEY-IDAR 131
Cdd:COG4694 26 LNLIYGENGSGKSTLSRILrSLELGDTSSEVIAEFEIEaGGSAPNPSVRvfnrdfveeNLRSGEEIKGIFTLGEEnIELE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 132 DETIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQL-----------------NIQLDNLCQFLSQERVEEFARLKSV 194
Cdd:COG4694 106 EEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLaksikddlkklfassgrNYRKANLEKKLSALKSSSEDELKEK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 195 KLLVETIRSIDASLLDVLDELREL-QGNEQSLQKDLdfKKAKIVHLRQESDKLRKS--VESLRDF------------QNK 259
Cdd:COG4694 186 LKLLKEEEPEPIAPITPLPDLKALlSEAETLLEKSA--VSSAIEELAALIQNPGNSdwVEQGLAYhkeeeddtcpfcQQE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 260 KGEiELHSQLLPYVK--VKDHKEKLNIYKEEYERAKANLRAILKD---------KKPFANTKKTLENQVEELTEK----- 323
Cdd:COG4694 264 LAA-ERIEALEAYFDdeYEKLLAALKDLLEELESAINALSALLLEilrtllpsaKEDLKAALEALNALLETLLAAleeki 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 324 ----------CSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEyyrgrtKKLQATIISTKEDFLRSQEILAQTHLP 393
Cdd:COG4694 343 anpstsidldDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEAR------KKLEAHELAELKEDLSRYKAEVEELIE 416
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 6324539 394 EKSVFEDIDIKRKEIINKEGEIRDLISEIDAKANAINHEMRSI 436
Cdd:COG4694 417 ELKTIKALKKALEDLKTEISELEAELSSVDEAADEINEELKAL 459
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-317 |
1.22e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYigrsKKVEDFIKNGQdvskieitlknspn 121
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEK----EADELFKPQGR-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 122 vTDIEYIDARDETIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNiqldnlcqfLSQERVEEFARLKSVKLLVETI 201
Cdd:COG4717 65 -KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE---------ELREELEKLEKLLQLLPLYQEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 202 RSIDASLLDVLDELRELQGNEQ---SLQKDLDFKKAKIVHLRQESDKLRK--SVESLRDFQNKKGEIELHSQllpyvKVK 276
Cdd:COG4717 135 EALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEELEELQQ-----RLA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6324539 277 DHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQV 317
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
42-165 |
2.53e-05 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 46.87 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTY---TLTEFnLSPSLNMIIGPNGSGKSTFVCAVCLGLAGkpEYIG-RSKKVEDFIKNGQDVSKI----E 113
Cdd:cd03272 1 IKQVIIQGFKSYkdqTVIEP-FSPKHNVVVGRNGSGKSNFFAAIRFVLSD--EYTHlREEQRQALLHEGSGPSVMsayvE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6324539 114 ITLKNSPNvtdieYIDARDETIKITRIItrSKRRSDYLINDYQVSESVVKTL 165
Cdd:cd03272 78 IIFDNSDN-----RFPIDKEEVRLRRTI--GLKKDEYFLDKKNVTKNDVMNL 122
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
188-484 |
2.89e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 188 FARLKSVKLLVETIRSIDASLLDVLDELRELQGNEqsLQKDLdfKKAKIVHLRQESDKLRKSVESLRDFQNKKGEIElhs 267
Cdd:PRK05771 1 LAPVRMKKVLIVTLKSYKDEVLEALHELGVVHIED--LKEEL--SNERLRKLRSLLTKLSEALDKLRSYLPKLNPLR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 268 QLLPYVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEKCSLKTD-EFLKAKEKINEIFEKLN 346
Cdd:PRK05771 74 EEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDlSLLLGFKYVSVFVGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 347 TIRDEVIK--KKNQNEYYRGRTKKLQATIISTKEDFLRSQEilaqthlpekSVFEDIDIKRKEIiNKEGEIRDLISEIDA 424
Cdd:PRK05771 154 EDKLEELKleSDVENVEYISTDKGYVYVVVVVLKELSDEVE----------EELKKLGFERLEL-EEEGTPSELIREIKE 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 425 KANAINHEMRSIQRQAESKTKSLTttdkigilnqdQDLKEVRDAVLMVREHPEMKDKILE 484
Cdd:PRK05771 223 ELEEIEKERESLLEELKELAKKYL-----------EELLALYEYLEIELERAEALSKFLK 271
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
57-225 |
4.62e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.53 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 57 EFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEItlknspnvtdIEYIDA-RDETI 135
Cdd:COG3950 20 DFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKL----------ILYYGTsRLLLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 136 KITRIITRSKRRSDYLINDYQ---VSESVVKTLVAQLNIQLDNLCQFLSQERVEEFARLKSV-KLLVETIRSIDASLLDV 211
Cdd:COG3950 90 GPLKKLERLKEEYFSRLDGYDsllDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREAlNKLLPDFKDIRIDRDPG 169
|
170
....*....|....
gi 6324539 212 LDELRELQGNEQSL 225
Cdd:COG3950 170 RLVILDKNGEELPL 183
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-373 |
5.68e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 167 AQLNIQLDNLCQFLSQERVEEFARLKSVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKL 246
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 247 RKSVESLRDFQNKKGEIELHSQLLPYVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEKCSL 326
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324539 327 KTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQATI 373
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
647-857 |
9.62e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 647 QGSIMSNEQKIRIENEIINLKNEYNDRKSTLDALSNqksgyrhELSELASKNDDINREAHQL-NEIRKKYTMRKSTIETL 725
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE-------ELKELAEKRDELNAQVKELrEEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 726 REkldqlKREARKDVSQKIKDIDDQIQQLllkqRHLLSKMASSMKSLKNCQKEListQILQFEAQNMDVSMNDVIGFFnE 805
Cdd:COG1340 74 KE-----LKEERDELNEKLNELREELDEL----RKELAELNKAGGSIDKLRKEI---ERLEWRQQTEVLSPEEEKELV-E 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324539 806 READLKSQYEDKKKFVKEMRDTPEFQSWMREIRSYDQDTKEKLNKVAEKYEE 857
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
42-151 |
1.17e-04 |
|
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: 45.37 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEyigRSKKVEDFIKNGQDVSKIEITL--KNS 119
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSH---RTSRDKELIRWGAEEAKISAVLerQGG 77
|
90 100 110
....*....|....*....|....*....|..
gi 6324539 120 PNVTDIEYIDARDETIKITRIITRskRRSDYL 151
Cdd:cd03242 78 ELALELTIRSGGGRKARLNGIKVR--RLSDLL 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
691-958 |
1.17e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 691 LSELASKNDDINREAHQLNEIRKKytmrkstIETLREKLDQLKREaRKDVSQKIKDIDDQIQQLLLKQRHLLSKMASSMK 770
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQE-------IAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 771 SLKNCQKElISTQILQFEAQNMDVSMNDVIGFFNEREADLK---SQyEDKKKFVKEMRDTPEFQSWMREIRSYDQDTKEK 847
Cdd:COG4942 84 ELAELEKE-IAELRAELEAQKEELAELLRALYRLGRQPPLAlllSP-EDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 848 LNKVAEKYEEEgnfnlsfvQDVLDKLESEIamvnhdESAVTILDQVTAELRELEHTVPQQSKDLETIKAKLKEDHAVLEP 927
Cdd:COG4942 162 LAALRAELEAE--------RAELEALLAEL------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260 270
....*....|....*....|....*....|.
gi 6324539 928 KLDDIVSKISARFARLFNNVGSAGAVRLEKP 958
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALKGKLPWP 258
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
42-94 |
2.13e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.57 E-value: 2.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPsLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIG 94
Cdd:COG4938 1 IKSISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLIQALLLLLQSNFIYLP 52
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
275-450 |
2.76e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 275 VKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEKCSL---KTDEFL----KAKEKINEIFEKLNT 347
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQElreKRDELNekvkELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 348 IRDEVIKKKNQNEYYRGRT---KKLQATIistkEDFLRSQEILAQTHLPEKSVFEDID------IKRKEIINKEGEIRDL 418
Cdd:COG1340 90 LREELDELRKELAELNKAGgsiDKLRKEI----ERLEWRQQTEVLSPEEEKELVEKIKelekelEKAKKALEKNEKLKEL 165
|
170 180 190
....*....|....*....|....*....|....*
gi 6324539 419 ISEIDA---KANAINHEMRSIQRQAESKTKSLTTT 450
Cdd:COG1340 166 RAELKElrkEAEEIHKKIKELAEEAQELHEEMIEL 200
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
667-1025 |
2.84e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 667 KNEYNDRKSTLDALS----NQKSGYRHELSELASKNDDINreahqlNEIRKKYTMRKSTIETLREKL----DQLK--REA 736
Cdd:pfam15921 291 RSQANSIQSQLEIIQeqarNQNSMYMRQLSDLESTVSQLR------SELREAKRMYEDKIEELEKQLvlanSELTeaRTE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 737 RKDVSQKIKDIDDQIQQLLLKqrhlLSKMASSMKSLKNCQKEL--------ISTQILQFEAQNMDVSMNDVIGFFNEREA 808
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLAD----LHKREKELSLEKEQNKRLwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 809 DLKSQYEDKKKFVKEMRDTPEFQSwmrEIRSYDQDTKEKLNKVAEKYE------EEGNFNLSFVQDVLDKLESEIAMVNh 882
Cdd:pfam15921 441 ECQGQMERQMAAIQGKNESLEKVS---SLTAQLESTKEMLRKVVEELTakkmtlESSERTVSDLTASLQEKERAIEATN- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 883 deSAVTIL-DQVTAELRELEHTVPQQ------SKDLETIKAKLKEDHAVLEpklddIVSKISARFARLFNNVG-SAGAVR 954
Cdd:pfam15921 517 --AEITKLrSRVDLKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIE-----ILRQQIENMTQLVGQHGrTAGAMQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 955 LEKP---KDYAEWKIEI----MVKFRDNAPLKKLDShtqsggeRAVSTVLYMIALQEFTSAPFRVVDEINQGMD------ 1021
Cdd:pfam15921 590 VEKAqleKEINDRRLELqefkILKDKKDAKIRELEA-------RVSDLELEKVKLVNAGSERLRAVKDIKQERDqllnev 662
|
....*.
gi 6324539 1022 --SRNE 1025
Cdd:pfam15921 663 ktSRNE 668
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
57-231 |
4.30e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 57 EFNLSPSLNMIIGPNGSGKSTFVCAvcLGLA-GkpeyiGRSKKveDFIKNGQDvsKIEIT----LKNSPNVTDI--EY-I 128
Cdd:COG0497 17 ELEFGPGLTVLTGETGAGKSILLDA--LGLLlG-----GRADA--SLVRHGAD--KAEVEavfdLSDDPPLAAWleENgL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 129 DARDETIKITRIITRSKRrSDYLINDYQVSESVVKTLVAQL-NI--QLDNLcQFLSQER----VEEFARLKSvklLVETI 201
Cdd:COG0497 86 DLDDGELILRREISADGR-SRAFINGRPVTLSQLRELGELLvDIhgQHEHQ-SLLDPDAqrelLDAFAGLEE---LLEEY 160
|
170 180 190
....*....|....*....|....*....|
gi 6324539 202 RSIDASLLDVLDELRELQGNEQSLQKDLDF 231
Cdd:COG0497 161 REAYRAWRALKKELEELRADEAERARELDL 190
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
47-173 |
5.94e-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: 43.50 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 47 LQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVC-LGLAGKpeyiGRSKKVEDFIKNGQDVSKIEITLKNSpnvtdi 125
Cdd:TIGR00611 8 LTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYyLALGRS----HRTSRDKPLIRFGAEAFVIEGRVSKG------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6324539 126 eyidarDETIKITRIITRSKRRSDYLINdyQVSESVVKTLVAQLNIQL 173
Cdd:TIGR00611 78 ------DREVTIPLEGLLKKKGKKAKVN--IDGQDKLSDLAGLLPMQL 117
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
43-421 |
6.28e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 43 IKIRLQDFV----TYTLTEFNLSPSlNMIIGPNGSGKSTFVCAVCLGLAGKPeyiGRSKKVEDFIK--NGQDVsKIEITL 116
Cdd:PHA02562 5 KKIRYKNILsvgnQPIEIQLDKVKK-TLITGKNGAGKSTMLEALTFALFGKP---FRDIKKGQLINsiNKKDL-LVELWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 117 KNSPNvtdiEYIDARDETIKITRIITRSKR-RSDYLINDYQvsesvvKTLVAQLNIQLDNLCQF--LSQERVEEFARLKS 193
Cdd:PHA02562 80 EYGEK----EYYIKRGIKPNVFEIYCNGKLlDESASSKDFQ------KYFEQMLGMNYKSFKQIvvLGTAGYVPFMQLSA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 194 V--KLLVETIRSIDA-SLLDVL--DELRELQGNEQSLQKDLDFKKAKI-VHLRQESDKLRKSVESLRDFQNK-------- 259
Cdd:PHA02562 150 ParRKLVEDLLDISVlSEMDKLnkDKIRELNQQIQTLDMKIDHIQQQIkTYNKNIEEQRKKNGENIARKQNKydelveea 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 260 ---KGEI-ELHSQLLPYVK-VKDHKEKLNIYKEEYERAKANLRAILKDKKPF---------ANTKKTLENQVEELTEKCS 325
Cdd:PHA02562 230 ktiKAEIeELTDELLNLVMdIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITKIKDKLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 326 LKTDEFLKAKEKINEIFEKLNTIRDEVIKKK-NQNEY---------YRGRTKKLQATIISTKEDFLRSQEILAQThlpeK 395
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLeLKNKIstnkqslitLVDKAKKVKAAIEELQAEFVDNAEELAKL----Q 385
|
410 420
....*....|....*....|....*.
gi 6324539 396 SVFEDIDIKRKEIInKEGEIRDLISE 421
Cdd:PHA02562 386 DELDKIVKTKSELV-KEKYHRGIVTD 410
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-449 |
1.03e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 158 SESVVKtlVAQLNIQLDNLCQFLSQERVEEFARLKSVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIV 237
Cdd:pfam15921 457 NESLEK--VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 238 HLRQESDKLRK---SVESLR-DFQNKKGEIELHSQLLPYVK--VKDHK--------EKLNIYKEEYERaKANLR--AILK 301
Cdd:pfam15921 535 HLKNEGDHLRNvqtECEALKlQMAEKDKVIEILRQQIENMTqlVGQHGrtagamqvEKAQLEKEINDR-RLELQefKILK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 302 DKKpfaNTK-KTLENQVEELT-EKCSL--KTDEFLKA----KEKINEIFEKLNTIRD---------EVIKK--KNQNEYY 362
Cdd:pfam15921 614 DKK---DAKiRELEARVSDLElEKVKLvnAGSERLRAvkdiKQERDQLLNEVKTSRNelnslsedyEVLKRnfRNKSEEM 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 363 RGRTKKLQATIISTKEDFLRSQEILAQTHLPEKSVFEDIDIKRKEIINKEGEIRDLISEI----DAKANAiNHEMRSIQR 438
Cdd:pfam15921 691 ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIqfleEAMTNA-NKEKHFLKE 769
|
330
....*....|.
gi 6324539 439 QAESKTKSLTT 449
Cdd:pfam15921 770 EKNKLSQELST 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-439 |
1.53e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 152 INDYQVSESVVKTLVAQLNIQLDNLCQFLSQERVEEFARLKSVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDF 231
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 232 KKAKIVHLRQESDKLRKSVESLRD-FQNKKGEIELHSqllpyVKVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTK 310
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREaLDELRAELTLLN-----EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 311 KTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAQT 390
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6324539 391 HLPEKSVFEDIdikRKEIINKEGEIRDLISEIDAKANAINHEMRSIQRQ 439
Cdd:TIGR02168 935 EVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
651-767 |
1.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 651 MSNEQKIRIENEIINLKNEYNDRKSTLDALSNQKSGYRHELSEL------ASKNDDINREAHQLNEIRKKYTMRKSTIET 724
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 6324539 725 LREKLDQLKREARKDVSQKIKDIDDQIQQLLLKQRHLLSKMAS 767
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
44-151 |
1.87e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 41.68 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 44 KIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLgLAgkpeyIGRSKKV---EDFIKNGQDVSKIEITL--KN 118
Cdd:PRK00064 5 RLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-----PGRSHRTardKELIRFGAEAAVIHGRVekGG 78
|
90 100 110
....*....|....*....|....*....|...
gi 6324539 119 SPNVTDIEYIDARDETIKITRIitRSKRRSDYL 151
Cdd:PRK00064 79 RELPLGLEIDKKGGRKVRINGE--PQRKLAELA 109
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
281-422 |
1.94e-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: 41.72 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 281 KLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTekcslKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNE 360
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELT-----RVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLE 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 361 --------YYRGRTKKLQatiiSTKEDFLRSQEILAQthLPEKSVFEDidikrKEIINKEGEIRDLISEI 422
Cdd:pfam15905 170 akmkevmaKQEGMEGKLQ----VTQKNLEHSKGKVAQ--LEEKLVSTE-----KEKIEEKSETEKLLEYI 228
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
194-502 |
1.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 194 VKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSVESLRDFQNKKGEielhsqllpyv 273
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 274 KVKDHKEKLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVI 353
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 354 KKKNQNEYYRGRTKKLQATIISTKEDFLRSQEILAqthlPEKSVFEDIDIKRKEIINKEGEIRDLISEIDAKANAINHEM 433
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI----ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324539 434 RSIQRQAESKTKSLTTTDKIGILNQDQDLKEVRDAVLMVREHPEMKDKILEPPIMTVSAINAQFAAYLA 502
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
191-425 |
3.44e-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: 41.54 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 191 LKSVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSVESLrdfQNKKGEIELHSQLL 270
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL---TNQDSVKELIIKNL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 271 PYVKvKDHKEKLNIYKEEYERAKANLRAI---LKDK----KPFANTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFE 343
Cdd:TIGR04523 460 DNTR-ESLETQLKVLSRSINKIKQNLEQKqkeLKSKekelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 344 KLNTIRDEVIKKKNQNEYYRGRTKKLQatiistkedflrSQEILAQTHLPEKSVFEDIDIKRKEIINKEGEIRDLISEID 423
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKENLEKEIDE------------KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
..
gi 6324539 424 AK 425
Cdd:TIGR04523 607 EK 608
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
42-117 |
3.66e-03 |
|
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: 40.76 E-value: 3.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPSLNMIIGPNGSGKSTFVCAVCLGLAGKpeyIGRSKKVEDFIKNGQDVSK---IEITLK 117
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS---SSRKFDEEDFYLGDDPDLPeieIELTFG 78
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
691-857 |
3.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 691 LSELASKNDDINREAHQLNEIRKKYTMRKSTIETLREKLDQLKrEARKDVSQKIKDIDDQIQQLLLKQRHLLSKM--ASS 768
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAK-TELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 769 MKSLKNCQKEListqilqfEAQNMDVS-MNDVIGFFNEREADLKSQYEDKKKFVKEMRDtpEFQSWMREIRSYDQDTKEK 847
Cdd:COG1579 88 NKEYEALQKEI--------ESLKRRISdLEDEILELMERIEELEEELAELEAELAELEA--ELEEKKAELDEELAELEAE 157
|
170
....*....|
gi 6324539 848 LNKVAEKYEE 857
Cdd:COG1579 158 LEELEAEREE 167
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
64-287 |
4.79e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 64 LNMIIGPNGSGKSTF-----VCAVCLGLAGKPEYIGRSKKVEDFIKNGQDV------SKIEITLKNSPNVtDIEYIDARD 132
Cdd:pfam13304 1 INVLIGPNGSGKSNLlealrFLADFDALVIGLTDERSRNGGIGGIPSLLNGidpkepIEFEISEFLEDGV-RYRYGLDLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 133 ETIKITRIITRSKRRSDYLINDYQVSESVVKTlvaqlNIQLDNLCQFLSQERVEEFARLKSVKLLVETIRSIDASLLDVL 212
Cdd:pfam13304 80 REDVEEKLSSKPTLLEKRLLLREDSEEREPKF-----PPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 213 DELRELQGNEQSLQKDLD---FKKAKIVHLRQESDKLRKSVE---SLRDFQNKKGEIELHSQLLPYV--KVKDHKEKLNI 284
Cdd:pfam13304 155 LLLDEGLLLEDWAVLDLAadlALFPDLKELLQRLVRGLKLADlnlSDLGEGIEKSLLVDDRLRERGLilLENGGGGELPA 234
|
...
gi 6324539 285 YKE 287
Cdd:pfam13304 235 FEL 237
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
42-79 |
5.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 5.11e-03
10 20 30
....*....|....*....|....*....|....*...
gi 6324539 42 IIKIRLQDFVTYTLTEFNLSPsLNMIIGPNGSGKSTFV 79
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLL 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-447 |
5.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 186 EEFARLKSVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSVESLRDFQNKKGEIEL 265
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 266 HSQLLPYVKVK-----DHKEKLNIYK--------EEYERAKA----NLRAILKDKKPFANTKKTLENQVEELTE---KCS 325
Cdd:PRK03918 360 RHELYEEAKAKkeeleRLKKRLTGLTpeklekelEELEKAKEeieeEISKITARIGELKKEIKELKKAIEELKKakgKCP 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 326 LKTDEFLKAKEK--INEIFEKLNTIRDEVIKKKNQNEYYRGRTKKLQaTIISTKEDFLRSQEILAQTHLPEKSVfEDIDI 403
Cdd:PRK03918 440 VCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLKELAEQLKELEEKL-KKYNL 517
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324539 404 K------------RKEIINKEGEIRDLISEIDaKANAINHEMRSIQRQAESKTKSL 447
Cdd:PRK03918 518 EelekkaeeyeklKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEEL 572
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
654-781 |
6.92e-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: 40.39 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 654 EQKIRIENEIINLKNEYNDRKSTLDALSNQKSGYRHELSELASKNDDINReahQLNEIRKKYTMRKSTIETLREKLDQLK 733
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKE 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6324539 734 RE------ARKDVSQKIKDIDDQIQQLLLKQRHLLSKMASSMKSLKNCQKELIS 781
Cdd:TIGR04523 496 KElkklneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
204-358 |
9.50e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 204 IDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLRQESDKLRKSVeslrdfQNKKGEIELHSQLLPYVK-----VKDH 278
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI------KRLELEIEEVEARIKKYEeqlgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 279 KEkLNIYKEEYERAKANLRAILKDKKPFANTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQ 358
Cdd:COG1579 89 KE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
66-191 |
9.85e-03 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 39.97 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 66 MIIGPNGSGKSTFVCAVCLGLAGK--PEYIgrSKKVEDFIKNGQdvskieITLKNSPNVTDIEYIDARDETIKITRIIT- 142
Cdd:TIGR03928 814 AIFGSPGYGKSTFLQTLIMSLARQhsPEQL--HFYLFDFGTNGL------LPLKKLPHVADYFTLDEEEKIEKLIRRIKk 885
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6324539 143 ----RSKRRSDYLINDYQVSESVVKTLVAQLNIQLDNLCQFLSQERVEEFARL 191
Cdd:TIGR03928 886 eidrRKKLFSEYGVASISMYNKASGEKLPQIVIIIDNYDAVKEEPFYEDFEEL 938
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
654-753 |
1.00e-02 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324539 654 EQKIRIENEIINLKN----EYNDRKSTLDALSNQ----KSGYRHELSELASKNDDINREAHQLNEIRKKYTMRKSTIETL 725
Cdd:PRK12704 57 EALLEAKEEIHKLRNefekELRERRNELQKLEKRllqkEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6324539 726 REK--------------------LDQLKREARKDVSQKIKDIDDQIQQ 753
Cdd:PRK12704 137 IEEqlqelerisgltaeeakeilLEKVEEEARHEAAVLIKEIEEEAKE 184
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