|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
951-1053 |
5.19e-67 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 224.01 E-value: 5.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 951 VKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITP 1030
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 530390803 1031 KLLQNLPYSEKMTVLFVYNGPHM 1053
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
51-196 |
1.36e-57 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 197.43 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 51 GSIVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRA 130
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530390803 131 SGnlvitreidvaknqsfwfinkksttqkiveekvaalNIQVGNLCQFLPQDKVGEFAKLSKIELL 196
Cdd:cd03277 81 PG------------------------------------NIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
967-1049 |
3.80e-28 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 112.02 E-value: 3.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 967 QSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACkeNTSQYFFITPKLLQNLPYSEKMTVLF 1046
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
...
gi 530390803 1047 VYN 1049
Cdd:cd03239 173 VHG 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-1029 |
2.84e-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: 97.43 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERfyerkrhldliemLEAKrpwveYENVRQEYEEvklVRDRVK 293
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAE-------------LEEK-----LEELKEELES---LEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 294 EEVRKLkegqipvtcriEEMENERHNLEarikEKIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTENcENLQ 373
Cdd:TIGR02168 362 ELEAEL-----------EELESRLEELE----EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 374 PQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQ-------------RFRDTY 440
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerlqeNLEGFS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 441 DAVLWLRNNRDKFKQRVcePIMLTINMKDNKNAKYIENHIPSNdLRAFVFESQEDMEV---FLKEvrdNKKLRVNAVIAP 517
Cdd:TIGR02168 506 EGVKALLKNQSGLSGIL--GVLSELISVDEGYEAAIEAALGGR-LQAVVVENLNAAKKaiaFLKQ---NELGRVTFLPLD 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 518 KSSYADKAPSRSLNELKQYGFFSYLRELFDAPD---PVMSYLCCQYHI----------------HEVPV----------- 567
Cdd:TIGR02168 580 SIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPklrKALSYLLGGVLVvddldnalelakklrpGYRIVtldgdlvrpgg 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 568 ----GTEKT--------------RERIERVIQETRLKQI-----------YTAEEKYVVKTSFYSNKVISSNTSLKVAQF 618
Cdd:TIGR02168 660 vitgGSAKTnssilerrreieelEEKIEELEEKIAELEKalaelrkeleeLEEELEQLRKELEELSRQISALRKDLARLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 619 LTVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQK-----------KKELLERKTKKRQLEQKI 687
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalREALDELRAELTLLNEEA 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 688 SSKLGSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAA 767
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 768 SSQLRlteqhfiELDENRQRLLQKCKELMKRARQVCNlgAEQTLPQEYQTQVPTIPNGHNSSLPMVFQDLPNTLDEIDAL 847
Cdd:TIGR02168 900 SEELR-------ELESKRSELRRELEELREKLAQLEL--RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 848 ------LTEERSRascFTGLNPTIVQEYtkreeeieqltEELKGKKVELDQYREN-----------ISQVKERWLNPLKE 910
Cdd:TIGR02168 971 rrrlkrLENKIKE---LGPVNLAAIEEY-----------EELKERYDFLTAQKEDlteaketleeaIEEIDREARERFKD 1036
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 911 LVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKF--RSSTQLHELtphhqSGGERSVSTMLYLMALQELNR 988
Cdd:TIGR02168 1037 TFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPpgKKNQNLSLL-----SGGEKALTALALLFAIFKVKP 1111
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 530390803 989 CPFRVVDEINQGMDPINERRVFEMVvntacKE--NTSQYFFIT 1029
Cdd:TIGR02168 1112 APFCILDEVDAPLDDANVERFANLL-----KEfsKNTQFIVIT 1149
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
53-127 |
3.94e-18 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 83.13 E-value: 3.94e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530390803 53 IVRISMENFLTYDICEVSPGP-HLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKV---GFFVKRGCSRGMVEIEL 127
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITF 79
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
965-1053 |
1.36e-17 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 81.25 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 965 HHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKenTSQYFFITPKLLQNLPYSEKMTV 1044
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
|
....*....
gi 530390803 1045 LFVYNGPHM 1053
Cdd:cd03227 154 KKVITGVYK 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-1028 |
4.58e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.05 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTYDICEVSP-GPHLNMIVGANGTGKSSIVCAI--CLGLAGKPAFmgRADKVGFFV---KRGCSRGMVEIE 126
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPfSKGFTVISGPNGSGKSNIGDAIlfALGLSSSKAM--RAERLSDLIsngKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 127 LF------RASGNLVITREIDVAKN--QSFWFINKKSTTQKIVEEKVAALNIQVGNLcQFLPQDKVGEFAKLSKIELLEA 198
Cdd:TIGR02169 80 VTfknddgKFPDELEVVRRLKVTDDgkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 199 TEKSIGPPE----MHKYHCELKNLREKEKQLETSCKEKTEYLQKM-VQRN--ERYK--QDVERFYERKRHLDLIEMLEAK 269
Cdd:TIGR02169 159 IDEIAGVAEfdrkKEKALEELEEVEENIERLDLIIDEKRQQLERLrREREkaERYQalLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 270 RPWVEYE----------------NVRQEYEEVKLVRDRVKEEVRKLKEG-QIPVTCRIEEMENERHNLEARIKEKIEELQ 332
Cdd:TIGR02169 239 KEAIERQlasleeeleklteeisELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 333 QA--LIVKQNEELDRQR----------------------RIGNTRKMIEDLQNEL---------------KTTENCENLQ 373
Cdd:TIGR02169 319 DAeeRLAKLEAEIDKLLaeieelereieeerkrrdklteEYAELKEELEDLRAELeevdkefaetrdelkDYREKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 374 PQIDAITNDLRRIQDEKALCEGEIID----------------------------KRRERETLEKEKKSVDDHIVRFDNLM 425
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADlnaaiagieakineleeekedkaleikkQEWKLEQLAADLSKYEQELYDLKEEY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 426 NQKEDKLRQRFRDtYDAVLwlrNNRDKFKQRVCEPIMLTINMKDNKNA---------KYIENHI------PSNDLRAFVF 490
Cdd:TIGR02169 479 DRVEKELSKLQRE-LAEAE---AQARASEERVRGGRAVEEVLKASIQGvhgtvaqlgSVGERYAtaievaAGNRLNNVVV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 491 ESQEDMEV---FLKEVRDNKK--LRVNAViapkssyadKAPSRSLNELKQYGFFSYLRELFDAPD---PVMSY------- 555
Cdd:TIGR02169 555 EDDAVAKEaieLLKRRKAGRAtfLPLNKM---------RDERRDLSILSEDGVIGFAVDLVEFDPkyePAFKYvfgdtlv 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 556 ---------LCCQYH-------IHE---VPVGTEKTRERIERVIQETRLKQIYTAEEKYVVKTSFYS---------NKVI 607
Cdd:TIGR02169 626 vedieaarrLMGKYRmvtlegeLFEksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrrieNRLD 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 608 SSNTSLKVAQFLTVTVDLE------QRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLE--------------------- 660
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEarieeleedlhkleealndle 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 661 ---------HKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEE-----EERKAS--TKIKEINVQKAK 724
Cdd:TIGR02169 786 arlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqridlKEQIKSieKEIENLNGKKEE 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 725 LVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELMKRARQvcn 804
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--- 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 805 lgaeqtlPQEYQTQVPTIPnghnsslpmvfqDLPNTLDEIdalltEERSRAscFTGLNPTIVQEYtkreEEIEQLTEELK 884
Cdd:TIGR02169 943 -------DEEIPEEELSLE------------DVQAELQRV-----EEEIRA--LEPVNMLAIQEY----EEVLKRLDELK 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 885 GKKVELDQYRENISQVKERwLNPLK-----ELVEKINEKFSNFFSSMQcAGEVDLHTENEEDYDKYGIRIRVKFRSST-- 957
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEE-YEKKKrevfmEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPvq 1070
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530390803 958 QLHELtphhqSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVvntacKENTSQYFFI 1028
Cdd:TIGR02169 1071 RLEAM-----SGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLI-----REKAGEAQFI 1131
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
56-238 |
1.78e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 72.91 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 56 ISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV------KRGCSRGMVEIELFR 129
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 130 ASG--------NLVITREIDVAKNQSFWFINKKSTTQKIVEEKVAALNIQVgNLCQFLPQDKVGEFAKLSKIELLEATEK 201
Cdd:pfam13476 81 NDGrytyaierSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 530390803 202 SIgppemhKYHCELKNLREKEKQLETSCKEKTEYLQK 238
Cdd:pfam13476 160 AL------EEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
214-1029 |
6.22e-14 |
|
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: 76.55 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLiemlEAKRPWVEYENVRQEYEEVKLVRDRVK 293
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA----KKKLESERLSSAAKLKEEELELKSEEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 294 EEVRKLKEgqipVTCRIEEMENERHNLEARIKEKIEELQQAL-----IVKQNEELDRQRRIGNTR--KMIEDLQNELKTT 366
Cdd:pfam02463 405 KEAQLLLE----LARQLEDLLKEEKKEELEILEEEEESIELKqgkltEEKEELEKQELKLLKDELelKKSEDLLKETQLV 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 367 ENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTY---DAV 443
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSataDEV 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 444 LWLRNNRDKFKQRVCEPIMLTINMKDNKNAKYIENHIPSNDLRAFVFESQEDMEVFLKEVRDN-----------KKLRVN 512
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKvvegilkdtelTKLKES 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 513 AVIAPKSSYADKAPSRSLNELKQYgffSYLRELFDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQETRLKQIYTAE 592
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEV---KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 593 EKYVVKTSFYSNKVISSNTSLKVAQfltvtvdLEQRRHLEEQLKEIHRKLQAVDSgLIALRETSKHLEHKDNELRQKKKE 672
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLK-------QKIDEEEEEEEKSRLKKEEKEEE-KSELSLKEKELAEEREKTEKLKVE 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 673 LLERKTKKRQLEQKISSKLGSLKLMEQDTcNLEEEERKASTKIKEINVQKAKLVTELTNLIKictsLHIQKVDLILQNTT 752
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLE-EEQLLIEQEEKIKEEELEELALELKEEQKLEK----LAEEELERLEEEIT 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 753 VISEKNKLESDymaassQLRLTEQHFIELDENRQRLLQKCKELMKRARQVCNLGAEQTLPQEYQTQVPTIPNGHNSSLPM 832
Cdd:pfam02463 865 KEELLQELLLK------EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 833 VFQDLP---------NTLDEIDALLTEERSRASCFTGLNPTIVQEYTKREEEIEQLTEELKGKKVELDQYRENISQVKER 903
Cdd:pfam02463 939 ELLLEEadekekeenNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 904 WLNPLKELVEKINEKFSNFFSsMQCAGEVDLHTENEEDYDKYGIRIRVKFRSSTQLHELTphhQSGGERSVSTMLYLMAL 983
Cdd:pfam02463 1019 LKEFLELFVSINKGWNKVFFY-LELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDL---LSGGEKTLVALALIFAI 1094
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 530390803 984 QELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 1029
Cdd:pfam02463 1095 QKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS---KNAQFIVIS 1137
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
968-1045 |
2.00e-13 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 69.93 E-value: 2.00e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530390803 968 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVL 1045
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
53-127 |
3.44e-13 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 69.55 E-value: 3.44e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530390803 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIEL 127
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTL 75
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-801 |
4.61e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETScKEKTEYLQKMVQRNERYKQDVERfyerkrhldlIEMLEAKRPWVEYENVRQEYEEVKLVRDRVK 293
Cdd:COG4913 233 HFDDLERAHEALEDA-REQIELLEPIRELAERYAAARER----------LAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 294 EEVRKLKEGQIPVTCRIEEMENERHNLEARIKE----KIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTT--- 366
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaee 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 367 --ENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSvddhivrfdnlmnqkedkLRQRfRDTYDAvl 444
Cdd:COG4913 382 faALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------------LERR-KSNIPA-- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 445 WLRNNRDKFKQR----------VCEpiMLTINMKDNK--NA--KYIENH-----IPSNDLRAfvfesqedmevFLKEVRD 505
Cdd:COG4913 441 RLLALRDALAEAlgldeaelpfVGE--LIEVRPEEERwrGAieRVLGGFaltllVPPEHYAA-----------ALRWVNR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 506 NK---KLRVNAVIAPKSSYADKAPS-RSL-NEL--KQYGFFSYLRELFDAPdpvMSYLCCQyhihevpvgTEKTRERIER 578
Cdd:COG4913 508 LHlrgRLVYERVRTGLPDPERPRLDpDSLaGKLdfKPHPFRAWLEAELGRR---FDYVCVD---------SPEELRRHPR 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 579 VIQETRL-KQIYTAEEKyvvKTSFY--SNKVISSNTSLKVAQFLTVTVDLEQRRH-LEEQLKEIHRKLQAVDSGLIALRE 654
Cdd:COG4913 576 AITRAGQvKGNGTRHEK---DDRRRirSRYVLGFDNRAKLAALEAELAELEEELAeAEERLEALEAELDALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 655 TSKHLEHkDNELRQKKKELLERKTKKRQLEQKiSSKLGSLKLMEQDtcnLEEEERKASTKIKEINVQKAKLVTELTNLik 734
Cdd:COG4913 653 LAEYSWD-EIDVASAEREIAELEAELERLDAS-SDDLAALEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQA-- 725
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530390803 735 ictslhiqkVDLILQNTTVISEKNKLESDYMAASSQLRL----TEQHFIELDENRQRLLQKCKELMKRARQ 801
Cdd:COG4913 726 ---------EEELDELQDRLEAAEDLARLELRALLEERFaaalGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
53-138 |
2.03e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 61.56 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTY-DICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAfmGRADKVGFFVKRGCSRGMVEIELFRAS 131
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
....*..
gi 530390803 132 GNLVITR 138
Cdd:COG0419 80 KRYRIER 86
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
55-127 |
1.81e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 57.75 E-value: 1.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530390803 55 RISMENFLTYDICE-VSPG-PHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRadkvGFFVKRGCSRGMVEIEL 127
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR----RSGVKAGCIVAAVSAEL 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
53-452 |
1.14e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRASG 132
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 133 NLVITREIDvaKNQSFWFINKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKV--GEFAKLskIELLEATEKSIGP-PEMH 209
Cdd:PRK03918 83 KYRIVRSFN--RGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLNAIYIrqGEIDAI--LESDESREKVVRQiLGLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 210 KYHCELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLI---------EMLEAKRPWVEYENVRQ 280
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIsselpelreELEKLEKEVKELEELKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 281 EYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKE---------------------------------K 327
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyiklsefyeeyldelreiekrlsR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 328 IEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKrrERETL 407
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK--ELEEL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 530390803 408 EKEKKSVDDHIvrfdNLMNQKEDKLRQRFRDTYDAVLWLRNNRDK 452
Cdd:PRK03918 397 EKAKEEIEEEI----SKITARIGELKKEIKELKKAIEELKKAKGK 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-398 |
9.71e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLE---TSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDliEMLEAKRPWVEYENVRQEYEEVKLVRD 290
Cdd:COG4717 72 ELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 291 RVKEEVRKLKEGQIpvtcRIEEMENERHNLEARIKEKIEELQQAlivKQNEELDRQRRIGNTRKMIEDLQNELKTTEN-C 369
Cdd:COG4717 150 ELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEeL 222
|
170 180
....*....|....*....|....*....
gi 530390803 370 ENLQPQIDAITNDLRRIQDEKALCEGEII 398
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLL 251
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
53-163 |
2.43e-07 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 53.36 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLglagkpAFMGRADKVgfFVKRGCSRGMVEIE------ 126
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSL------LLGGRASAD--LIRSGAEKAVVEGVfdisde 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530390803 127 ----------LFRASGNLVITREIDvAKNQSFWFINKKSTTQKIVEE 163
Cdd:cd03241 73 eeakalllelGIEDDDDLIIRREIS-RKGRSRYFINGQSVTLKLLRE 118
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
53-435 |
3.84e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPafmgRADKVGFFVKRGCSRGMVEIELFRASG 132
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 133 NLVITREID-----------VAKNQSFWFINKKSTTqKIVEEKVAALNIQVGNLCQFLPQDKV-----GEFAKLSKI--E 194
Cdd:PRK01156 79 VYQIRRSIErrgkgsrreayIKKDGSIIAEGFDDTT-KYIEKNILGISKDVFLNSIFVGQGEMdslisGDPAQRKKIldE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 195 LLEATEKSIGPPEMHK----YHCELKNLREKEKQLETSCKEkTEYLQKMVQRNERYKQDVERfyerkrhldliemlEAKR 270
Cdd:PRK01156 158 ILEINSLERNYDKLKDvidmLRAEISNIDYLEEKLKSSNLE-LENIKKQIADDEKSHSITLK--------------EIER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 271 PWVEYENVRQEYEEVK--LVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDR--- 345
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKsaLNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDyfk 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 346 -QRRIGNTRKMIEDLQNELKttencenlqpQIDAITNDLRRIQDEKAlcegEIIDKRRERETLEKEKKSVDDHIVRFDNL 424
Cdd:PRK01156 303 yKNDIENKKQILSNIDAEIN----------KYHAIIKKLSVLQKDYN----DYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
410
....*....|.
gi 530390803 425 MNQKEDKLRQR 435
Cdd:PRK01156 369 LKSIESLKKKI 379
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
53-151 |
4.69e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLT-YDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAG-KPAFMGRADKVGFFVKRGCSRGMVEIELFRA 130
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGeLPPNSKGGAHDPKLIREGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|....*....
gi 530390803 131 SGN-LVITREIDVAKN-------QSFWFI 151
Cdd:cd03240 81 NGKkYTITRSLAILENvifchqgESNWPL 109
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
76-416 |
1.94e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 76 NMIVGANGTGKSSIVCAICLGLAGKPaFmgRADKVGFFV----KRGCsrgMVEIELFRASGNLVITR-------EIDV-- 142
Cdd:PHA02562 30 TLITGKNGAGKSTMLEALTFALFGKP-F--RDIKKGQLInsinKKDL---LVELWFEYGEKEYYIKRgikpnvfEIYCng 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 143 --------AKNQSFWF-----INKKSTTQ---------------------KIVEEkvaALNIQVgnlcqflpqdkVGEFA 188
Cdd:PHA02562 104 klldesasSKDFQKYFeqmlgMNYKSFKQivvlgtagyvpfmqlsaparrKLVED---LLDISV-----------LSEMD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 189 KLSKIELLEATEKsIGPPEMHKYHCE--LKNLREKEKQLETSCKEKTEYLQKMVQRN----ERYKQDVERFYErkrhldl 262
Cdd:PHA02562 170 KLNKDKIRELNQQ-IQTLDMKIDHIQqqIKTYNKNIEEQRKKNGENIARKQNKYDELveeaKTIKAEIEELTD------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 263 iEMLEAKRPWVEYEN----VRQEYEEVKLVRDRVKEEVRKLKEGQIPVTC---------RIEEMENERHNLEARIkEKIE 329
Cdd:PHA02562 242 -ELLNLVMDIEDPSAalnkLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCtqqisegpdRITKIKDKLKELQHSL-EKLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 330 ELQQALIVKQNEELDRQRRIgntrkmiEDLQNELkttencENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEK 409
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKKL-------LELKNKI------STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
....*..
gi 530390803 410 EKKSVDD 416
Cdd:PHA02562 387 ELDKIVK 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-437 |
3.55e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 194 ELLEATEKSIgppeMHKYHCELKNLREKEKQLEtsckEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWV 273
Cdd:PRK03918 444 ELTEEHRKEL----LEEYTAELKRIEKELKEIE----EKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 274 EYENVRQEYEEVKLVRDR---VKEEVRKLKEGqipvTCRIEEMENERHNLEARIKEKIEELQqalivkqnEELDRQRRIG 350
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKlikLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELA--------ELLKELEELG 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 351 ntRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKE- 429
Cdd:PRK03918 584 --FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEy 661
|
....*...
gi 530390803 430 DKLRQRFR 437
Cdd:PRK03918 662 EELREEYL 669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
214-435 |
6.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHL-DLIEMLEAKRpwveyENVRQEYEEVKLVRDRV 292
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeERLEELEEEL-----AELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 293 KEEVRKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQAlivkQNEELDRQRRIGNTRKMIEDLQNELkttencENL 372
Cdd:COG1196 343 EEELEEAEE-------ELEEAEAELAEAEEALLEAEAELAEA----EEELEELAEELLEALRAAAELAAQL------EEL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530390803 373 QPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQR 435
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-997 |
8.99e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 218 LREKEKQLETsckekteyLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRpwvEYENVRQEYEEVKLVRDRVKEEVR 297
Cdd:COG1196 195 LGELERQLEP--------LERQAEKAERYRELKEELKELEAELLLLKLRELEA---ELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 298 KLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQALI----VKQNEELDRQRRIGNTRKMIEDLQNELKTTENCENLQ 373
Cdd:COG1196 264 ELEA-------ELEELRLELEELELELEEAQAEEYELLAelarLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 374 PQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRF-DNLMNQKEDKLRQRFRDTYDAVLWLRNNRDK 452
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 453 FKQRVcEPIMLTINMKDNKNAKyIENHIPSNDLRAFVFESQEDMEVFLKEVRDNKK---LRVNAVIAPKSSYADKAPSRS 529
Cdd:COG1196 417 ERLEE-ELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEEEEALLELLAELLEeaaLLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 530 L--NELKQY-GFFSYLRELFDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQETRLKQIYTAEE--KYVVKT----- 599
Cdd:COG1196 495 LllEAEADYeGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaiEYLKAAkagra 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 600 SFYSNKVISSNTSLKVAQ--------FLTVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKK 671
Cdd:COG1196 575 TFLPLDKIRARAALAAALargaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 672 ELLERKTKKRQLEQKISSKLGSLKLMEqdtcnlEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNT 751
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAEL------EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 752 TVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELmKRARQ----VcNLGAEQtlpqEYQ----------T 817
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL-EREIEalgpV-NLLAIE----EYEeleerydflsE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 818 QvptipnghnsslpmvFQDLpntLDEIDALLTeersrascftglnptIVQEYTKReeeieqlteelkgkkveldqyreni 897
Cdd:COG1196 803 Q---------------REDL---EEARETLEE---------------AIEEIDRE------------------------- 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 898 sqVKERwlnpLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRV-----KFRSSTQLheltphhqSGGER 972
Cdd:COG1196 825 --TRER----FLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLETGIEIMAqppgkKLQRLSLL--------SGGEK 890
|
810 820
....*....|....*....|....*
gi 530390803 973 SVSTMLYLMALQELNRCPFRVVDEI 997
Cdd:COG1196 891 ALTALALLFAIFRLNPSPFCVLDEV 915
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
214-429 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETSCKEKTEYLQKMvqrnERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVK 293
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRL----EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 294 EEVRKLKEgqipvtcRIEEMENERhnleARIKEKIEELQQA------------------LIVKQNEELDR-QRRIGNTRK 354
Cdd:PRK03918 405 EEISKITA-------RIGELKKEI----KELKKAIEELKKAkgkcpvcgrelteehrkeLLEEYTAELKRiEKELKEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 355 MIEDLQNELKTTENCENLQP----------QIDAITNDLRRIQDEKALCEGEIIDKRRER-ETLEKEKKSVDDHIVRFDN 423
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESeliklkelaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEIKSLKKELEKLEE 553
|
....*.
gi 530390803 424 LMNQKE 429
Cdd:PRK03918 554 LKKKLA 559
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-459 |
1.17e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETSCKEKTEYLqkmvqrnERYKQDVERFYERKRHLDliEMLEakrpwvEYENVRQEYEEVKlvrdrvk 293
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEAD--EVLE------EHEERREELETLE------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 294 EEVRKLKEgqipvtcRIEEMENERHNLEARI---KEKIEELQQALivkqNEELDRQRRIGNTRKMIEDLQNEL-----KT 365
Cdd:PRK02224 258 AEIEDLRE-------TIAETEREREELAEEVrdlRERLEELEEER----DDLLAEAGLDDADAEAVEARREELedrdeEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 366 TENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKE----KKSVDDHIVRFDNLMNQKEDkLRQRFRDT-- 439
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEleeaREAVEDRREEIEELEEEIEE-LRERFGDApv 405
|
250 260
....*....|....*....|....*
gi 530390803 440 -----YDAVLWLRNNRDKFKQRVCE 459
Cdd:PRK02224 406 dlgnaEDFLEELREERDELREREAE 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-368 |
2.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 214 ELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKrhldliEMLEAKRpwveyENVRQEYEEVKLVR-DRV 292
Cdd:PRK02224 583 ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR------ERLAEKR-----ERKRELEAEFDEARiEEA 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 293 KEEVRKLKEGQIPVTCRIEEMENERHNLEARI---KEKIEELqqalivkqnEEL-DRQRRIGNTRKMIEDLQNELKTTEN 368
Cdd:PRK02224 652 REDKERAEEYLEQVEEKLDELREERDDLQAEIgavENELEEL---------EELrERREALENRVEALEALYDEAEELES 722
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
968-1029 |
2.61e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 2.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530390803 968 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 1029
Cdd:cd03278 115 SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS---KETQFIVIT 173
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
261-398 |
3.17e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 261 DLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEgqipvtcRIEEMENERHNLEARIKEK---IEELQQAL-- 335
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKderIERLERELse 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 336 --------------IVKQNEELDR-QRRIGNTRKMIEDLQNELKTTENCENLQ--------PQIDAITND-LRRIQDEKA 391
Cdd:COG2433 453 arseerreirkdreISRLDREIERlERELEEERERIEELKRKLERLKELWKLEhsgelvpvKVVEKFTKEaIRRLEEEYG 532
|
....*..
gi 530390803 392 LCEGEII 398
Cdd:COG2433 533 LKEGDVV 539
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
230-390 |
3.50e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 230 KEKTEYLQKMVQRNERYKQDVERfyERKRHLD-----LIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQI 304
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQ--ENKRLTEplqkaQEEVEELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 305 PVTCRIEEMENERHNLEARIKEKIEELQQAlIVKQNEELdrQRRIGNTRKMIEDLQNELKTTENCENLQP-QIDAITNDL 383
Cdd:pfam13851 110 VLEQRFEKVERERDELYDKFEAAIQDVQQK-TGLKNLLL--EKKLQALGETLEKKEAQLNEVLAAANLDPdALQAVTEKL 186
|
....*..
gi 530390803 384 RRIQDEK 390
Cdd:pfam13851 187 EDVLESK 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
626-799 |
3.71e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 626 EQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERK----TKKRQLEQKISSKLGSLKLMEQDT 701
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 702 CNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIEL 781
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
170
....*....|....*...
gi 530390803 782 DENRQRLLQKCKELMKRA 799
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
194-772 |
3.79e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 194 ELLEATEKSIGPPEMHKYHCELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERkrhLDLIEMLEAkrpwv 273
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER---REELETLEA----- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEgqipvtcRIEEMENERHnlEARIKEKIEELQQALIVKQNEELDR-----QRR 348
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRE-------RLEELEEERD--DLLAEAGLDDADAEAVEARREELEDrdeelRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 349 IGNTRKMIEDLQNELKT-TENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKE----KKSVDDHIVRFDN 423
Cdd:PRK02224 330 LEECRVAAQAHNEEAESlREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 424 LMNQKE------DKLRQRFRDTYDAVLWLRNNRDKFKQRVCE--------PImltinmKDNKNAKYIEnhipsnDLRAFV 489
Cdd:PRK02224 410 AEDFLEelreerDELREREAELEATLRTARERVEEAEALLEAgkcpecgqPV------EGSPHVETIE------EDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 490 FESQEDMEVfLKEVRDNKKLRVNAVIAPKSsyADKAPSRSLNELKQygffsyLRELfdapdpvmsylccqyhIHEVPVGT 569
Cdd:PRK02224 478 EELEAELED-LEEEVEEVEERLERAEDLVE--AEDRIERLEERRED------LEEL----------------IAERRETI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 570 EKTRERIERvIQETRLKQIYTAEEKYVVKTSFYSNkviSSNTSLKVAQFLTVTVDLEQRRHLEEQLKEIHRKLQAVDSGL 649
Cdd:PRK02224 533 EEKRERAEE-LRERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 650 IALRETSKHLEHKDNELRQKKKELLERktkKRQLEQKISSKlgSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTE- 728
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRER---KRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEi 683
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 530390803 729 --LTNLIKICTSLHIQKVDliLQNT-----TVISEKNKLESDYMAASSQLR 772
Cdd:PRK02224 684 gaVENELEELEELRERREA--LENRvealeALYDEAEELESMYGDLRAELR 732
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
53-95 |
5.22e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 5.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530390803 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICL 95
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRL 45
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
53-117 |
7.03e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 7.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530390803 53 IVRISMENFLTYDICEV--SPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRG 117
Cdd:COG3950 3 IKSLTIENFRGFEDLEIdfDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNG 69
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
222-367 |
9.23e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 222 EKQLETSCKEKTEYLQKMVQRN-------ERYKQDVERFYERKRHL--DLIEMLEAKRPWVE-YENVRQEYEEVKLVRDR 291
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANrqrekekERYKRDREQWERQRRELesRVAELKEELRQSREkHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 292 VKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKIEELQQaliVKqneelDRQRRIGNTRKMIE----DLQNELKTTE 367
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER---MK-----ERAKKAGAQRKEEEaerkQLQAKLQQTE 184
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-420 |
9.91e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 326 EKIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTENcenlqpQIDAITNDLRRIQDEKALCEGEIIDKRRERE 405
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER------RIAALARRIRALEQELAALEAELAELEKEIA 93
|
90
....*....|....*
gi 530390803 406 TLEKEKKSVDDHIVR 420
Cdd:COG4942 94 ELRAELEAQKEELAE 108
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
52-145 |
1.09e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 42.45 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 52 SIVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLgLAgkpafMGRadkvGF-------FVKRGCSRGMVE 124
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-----PGR----SHrtardkeLIRFGAEAAVIH 71
|
90 100
....*....|....*....|.
gi 530390803 125 IELFRASGNLVITREIDVAKN 145
Cdd:PRK00064 72 GRVEKGGRELPLGLEIDKKGG 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
274-823 |
1.75e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERH----NLEARIKEKIEELQQALIV---------KQN 340
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHerkqVLEKELKHLREALQQTQQShayltqkreAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 341 EELDRQRRIGNTRKMIEDLQNELKTTencENLQPQIDAITNDLRRIQDEKALCEgeiIDKRRER--ETLEKEKKSVDDHI 418
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVL---EETQERINRARKAAPLAAHIKAVTQ---IEQQAQRihTELQSKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 419 VRFDNLMNQKEDKLRQRfrdtyDAVLWLRNNRDKFKQRVCEPimlTINMKDNKNAKYIENHIPSNDLRAFVFESQEDMEV 498
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQR-----RLLQTLHSQEIHIRDAHEVA---TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 499 FLKEVRDNKKLRVNAVIAPKSSY-ADKAPSRSLNELKQygffsylrelfdapdpvMSYLCCQYHIhevpvgTEKTRERIE 577
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLqGQLAHAKKQQELQQ-----------------RYAELCAAAI------TCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 578 RVIQETRLKQIYTAEEKYVVKTSFYSNKVISSNT-SLKVAQFLTvtvdlEQRRHLEEQLKEIHRKLQAVD---------- 646
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAvVLARLLELQ-----EEPCPLCGSCIHPNPARQDIDnpgpltrrmq 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 647 ---SGLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEEEERKASTKIKEINVQKA 723
Cdd:TIGR00618 532 rgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 724 KLVTELtnLIKICTSLHIQKVDLILQNttvISEKNKLESDYMAAsSQLRLTEQhfielDENRQRLLQKCKELMKRARQVC 803
Cdd:TIGR00618 612 CEQHAL--LRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHA-LQLTLTQE-----RVREHALSIRVLPKELLASRQL 680
|
570 580
....*....|....*....|
gi 530390803 804 NLGAEQTLPQEYQTQVPTIP 823
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLA 700
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
274-749 |
1.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEGQIpvtcRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDRQRRIGNTR 353
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEE----ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 354 kmIEDLQNELKTTEN----CENLQPQIDAITNDLRRIQDEKAL-CEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQK 428
Cdd:COG4717 148 --LEELEERLEELREleeeLEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 429 EDKLRQRFRDTYDAVLWLRNNRDKFKQRVcEPIMLTINMKDNKNAKYIENHIPSNDLRAFVFesqedmeVFLKEVRDNKK 508
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLI-AAALLALLGLGGSLLSLILTIAGVLFLVLGLL-------ALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 509 LrvnaviAPKSSYADKAPSRSLNELKQYGFFSYLREL----FDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQETR 584
Cdd:COG4717 298 A------SLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 585 LKQIytaeekyvvktsFYSNKVISsntslkVAQFLTVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDn 664
Cdd:COG4717 372 IAAL------------LAEAGVED------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 665 ELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTC--NLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQ 742
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
....*..
gi 530390803 743 KVDLILQ 749
Cdd:COG4717 513 RLPPVLE 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-403 |
2.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 192 KIELLEAteksigppemhkyhcELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKR- 270
Cdd:COG4913 611 KLAALEA---------------ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEa 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 271 -------PWVEYENVRQEYEEVKLVRDRVKEEVRKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQALIVKQNEEL 343
Cdd:COG4913 676 elerldaSSDDLAALEEQLEELEAELEELEEELDELKG-------EIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 344 drqrrigntrkmiEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRE 403
Cdd:COG4913 749 -------------ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
53-93 |
2.28e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 2.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 530390803 53 IVRISMENFLTYDICEVSPGPhLNMIVGANGTGKSSIVCAI 93
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDAL 41
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
53-99 |
3.08e-03 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 40.92 E-value: 3.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530390803 53 IVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAG 99
Cdd:PRK14079 3 LLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTG 49
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
53-204 |
4.03e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 40.32 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTY-DICEVSP-GPHLNMIVGANGTGKSSIVCAICLGLAGkpAFMG-RADKVGFFVKRGCSR----GMVEI 125
Cdd:cd03272 1 IKQVIIQGFKSYkDQTVIEPfSPKHNVVVGRNGSGKSNFFAAIRFVLSD--EYTHlREEQRQALLHEGSGPsvmsAYVEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 126 eLFRASGN--------LVITREIDVAKNQsfWFINKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKVGEFAKLSKIELLE 197
Cdd:cd03272 79 -IFDNSDNrfpidkeeVRLRRTIGLKKDE--YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQE 155
|
....*..
gi 530390803 198 ATEKSIG 204
Cdd:cd03272 156 MQQLSGG 162
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
928-1050 |
4.74e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.77 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 928 CAGEVDLHTENEEDYDKYGIRIRVKFRSstQLheltphhqSGGERSVSTMLYLMALQelnrCPFRVVDEINQGMDPINER 1007
Cdd:cd00267 52 TSGEILIDGKDIAKLPLEELRRRIGYVP--QL--------SGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRE 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530390803 1008 RVFEMVVNTACKENTsqYFFITPKLLQNLPYSEKmtVLFVYNG 1050
Cdd:cd00267 118 RLLELLRELAEEGRT--VIIVTHDPELAELAADR--VIVLKDG 156
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
290-457 |
5.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 290 DRVKEEVRKLKEgqipvtcRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDrqrrIGNTRKMIEDLQNELKTTENc 369
Cdd:COG1579 20 DRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 370 enlQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYDAVLWLRNN 449
Cdd:COG1579 88 ---NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*...
gi 530390803 450 RDKFKQRV 457
Cdd:COG1579 165 REELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
618-853 |
5.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 618 FLTVTVDLEQRRHLEEQLKEIHRKLQAvdsglialretskhLEHKDNELRQKKKELLErktKKRQLEQKISSKLGSLKLM 697
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAE--------------LEKELAALKKEEKALLK---QLAALERRIAALARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 698 EQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLI-KICTSLHIQKVDLILQNTTVisekNKLESDYMAASSQLRLTEQ 776
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530390803 777 HFIELDENRQRLLQKCKELMKRARQVCNLGAEQtlpQEYQTQVPTIPNGHNSSLPMVFQDLPNTLDEIDALLTEERS 853
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
53-190 |
5.81e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.56 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 53 IVRISMENFLTY------DICEVSPGPhLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIE 126
Cdd:cd03279 3 PLKLELKNFGPFreeqviDFTGLDNNG-LFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFT 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530390803 127 lFRASGNLV-ITREIDVAKNQsfwFINkksttqkiveekvaalniqvgnlCQFLPQdkvGEFAKL 190
Cdd:cd03279 82 -FQLGGKKYrVERSRGLDYDQ---FTR-----------------------IVLLPQ---GEFDRF 116
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
626-822 |
6.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 626 EQRRHLEEQLKEIHRKLQAVDSgliALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLE 705
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLRE---ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 706 EEERKASTKIKEINvqkaklvTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDEnr 785
Cdd:COG4372 108 EEAEELQEELEELQ-------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE-- 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 530390803 786 QRLLQKCKELMKRARQVCNLGAEQTLPQEYQTQVPTI 822
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
626-725 |
6.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 626 EQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSL----------K 695
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakeI 158
|
90 100 110
....*....|....*....|....*....|.
gi 530390803 696 LMEQdtcnLEEE-ERKASTKIKEInVQKAKL 725
Cdd:PRK12704 159 LLEK----VEEEaRHEAAVLIKEI-EEEAKE 184
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
190-429 |
6.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 190 LSKIELLEATEKSIGPPEMHKYHCELKNLREKEKQLETScKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEak 269
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE-- 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 270 rpwvEYENVRQEYEEVKLVRDRVK-EEVRKLKEGqipvtcriEEMENERHNLEARIKEKIEEL--------QQALIVKQN 340
Cdd:PTZ00121 1657 ----EENKIKAAEEAKKAEEDKKKaEEAKKAEED--------EKKAAEALKKEAEEAKKAEELkkkeaeekKKAEELKKA 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 341 EELDRQRRIGNTRKMIEDLQN--ELKTTENCEN-LQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDdh 417
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKaeEAKKDEEEKKkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD-- 1802
|
250
....*....|..
gi 530390803 418 ivRFDNLMNQKE 429
Cdd:PTZ00121 1803 --IFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
194-416 |
9.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 194 ELLEATEKSIGPPEMHKYHCELKNLREKEKQLETScKEKTEYLQKMVQrnERYKQDVERFYERKRHLDLIEMLEAKRpwv 273
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA-KKKADEAKKAAE--AKKKADEAKKAEEAKKADEAKKAEEAK--- 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390803 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKIEELQQALIVKQNEELDRQ-----RR 348
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeeaKK 1614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530390803 349 IGNTRKMIEDLQNELKTTENCENLQPQIDaitNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDD 416
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
|
| |
