|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
975-1077 |
4.38e-67 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 224.40 E-value: 4.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 975 VKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITP 1054
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 966993023 1055 KLLQNLPYSEKMTVLFVYNGPHM 1077
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
51-196 |
4.22e-58 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 198.97 E-value: 4.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 51 GSIVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRA 130
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966993023 131 SGnlvitreidvaknqsfwfinkksttqkvveeqvaalNIQVGNLCQFLPQDKVGEFAKLSKIELL 196
Cdd:cd03277 81 PG------------------------------------NIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
991-1073 |
3.90e-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: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 991 QSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACkeNTSQYFFITPKLLQNLPYSEKMTVLF 1070
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
...
gi 966993023 1071 VYN 1073
Cdd:cd03239 173 VHG 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-1053 |
3.13e-22 |
|
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: 103.98 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERfyerkrhldliemleakrpwveyenVRQEYEEVKLVRDRVK 293
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAE-------------------------LEEKLEELKEELESLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 294 EEVRKLKEgqipitrRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRI 373
Cdd:TIGR02168 358 AELEELEA-------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 374 SNTRKmiEDLQNELKTTEN-CENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDhivrfdnlmnqk 452
Cdd:TIGR02168 431 EEAEL--KELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER------------ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 453 edkLRQRFRDTYDAVLWLRSNRDKFKQRVcePIMLTINMKDNKNAKYIENHIPSNdLRAFVFESQEDMEV---FLKEvrd 529
Cdd:TIGR02168 497 ---LQENLEGFSEGVKALLKNQSGLSGIL--GVLSELISVDEGYEAAIEAALGGR-LQAVVVENLNAAKKaiaFLKQ--- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 530 NKKLRVNAVIAPKSSYADKAPSRSLNELKQYGFFSYLRELFDAPD---PVMSYLCCQYHI----------------HEVP 590
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPklrKALSYLLGGVLVvddldnalelakklrpGYRI 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 591 V---------------GTEKT--------------RERIERVIQETRLKQI-----------YTAEEKYVVKTSFYSNKI 630
Cdd:TIGR02168 648 VtldgdlvrpggvitgGSAKTnssilerrreieelEEKIEELEEKIAELEKalaelrkeleeLEEELEQLRKELEELSRQ 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 631 ISSNTSLKVAQFLTVTVDLEQRRHLEEQLKEISRKLQAVDSRLIALRETSKHLEHKDNELRQK-----------KKELLE 699
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalREALDE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 700 RKTKKRQLEQKISSKLGSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVIS 779
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 780 EKNKLESDYMAASSQLRlteqhfiELDENRQRLLQKCKELMKRARQVCNlgAEQTLPQEYQTQVPTIPNGHNSSLPMVFQ 859
Cdd:TIGR02168 888 ALALLRSELEELSEELR-------ELESKRSELRRELEELREKLAQLEL--RLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 860 DLPNTLDEIDAL------LTEERSRascFTGLNPTIVQEYtkreeeieqltEELKGKKVELDQYREN-----------IS 922
Cdd:TIGR02168 959 LENKIEDDEEEArrrlkrLENKIKE---LGPVNLAAIEEY-----------EELKERYDFLTAQKEDlteaketleeaIE 1024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 923 QVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKF--RSSTQLHELtphhqSGGERSVST 1000
Cdd:TIGR02168 1025 EIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPpgKKNQNLSLL-----SGGEKALTA 1099
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 966993023 1001 MLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVvntacKE--NTSQYFFIT 1053
Cdd:TIGR02168 1100 LALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLL-----KEfsKNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-1052 |
1.38e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.60 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTYDICEVSP-GPHLNMIIGANGTGKSSIVCAI--CLGLAGKPAFmgRADKVGFFV---KRGCSRGMVEIE 126
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPfSKGFTVISGPNGSGKSNIGDAIlfALGLSSSKAM--RAERLSDLIsngKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 127 LF------RASGNLVITREIDVAKN--QSFWFINKKSTTQKVVEEQVAALNIQVGNLcQFLPQDKVGEFAKLSKIELLEA 198
Cdd:TIGR02169 80 VTfknddgKFPDELEVVRRLKVTDDgkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 199 TEKSIGPPEMHR----YHCELKNFREKEKQLETSCKEKTEYLQKM-VQRN--ERYK--QDVERFYERKRHLDLIEMLEAK 269
Cdd:TIGR02169 159 IDEIAGVAEFDRkkekALEELEEVEENIERLDLIIDEKRQQLERLrREREkaERYQalLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 270 RPWVEYE----------------NVRQEYEEVKLVRDRVKEEVRKLKEG-QIPITRRIEEMENERHNLEARIKEKATDIK 332
Cdd:TIGR02169 239 KEAIERQlasleeeleklteeisELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 333 EASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNEL---------------KTTENCENLQ 397
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaetrdelkDYREKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 398 PQIDAITNDLRRIQDEKALCEGEIID----------------------------KRRERETLEKEKKSVDDHIVRFDNLM 449
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADlnaaiagieakineleeekedkaleikkQEWKLEQLAADLSKYEQELYDLKEEY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 450 NQKEDKL-----------------RQRFRDTYDAVLWLRSNRDKFKQRVCEPIMLtinmkDNKNAKYIENhIPSNDLRAF 512
Cdd:TIGR02169 479 DRVEKELsklqrelaeaeaqarasEERVRGGRAVEEVLKASIQGVHGTVAQLGSV-----GERYATAIEV-AAGNRLNNV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 513 VFESQEDMEV---FLKEVRDNKK--LRVNAViapkssyadKAPSRSLNELKQYGFFSYLRELFDAPD---PVMSYLCCQY 584
Cdd:TIGR02169 553 VVEDDAVAKEaieLLKRRKAGRAtfLPLNKM---------RDERRDLSILSEDGVIGFAVDLVEFDPkyePAFKYVFGDT 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 585 HIHE--------------------------VPVGTEKTRERIERVIQETRLKQIYTAEEKYVVKTSFYS---------NK 629
Cdd:TIGR02169 624 LVVEdieaarrlmgkyrmvtlegelfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrrieNR 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 630 IISSNTSLKVAQFLTVTVDLE------QRRHLEEQLKEISRKLQAVDSRLIALRETSKHLE------------------- 684
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEarieeleedlhkleealnd 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 685 -----------HKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEE-----EERKAS--TKIKEINVQK 746
Cdd:TIGR02169 784 learlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqridlKEQIKSieKEIENLNGKK 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 747 AKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELMKRARQv 826
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE- 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 827 cnlgaeqtlPQEYQTQVPTIPnghnsslpmvfqDLPNTLDEIdalltEERSRAscFTGLNPTIVQEYtkreEEIEQLTEE 906
Cdd:TIGR02169 943 ---------DEEIPEEELSLE------------DVQAELQRV-----EEEIRA--LEPVNMLAIQEY----EEVLKRLDE 990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 907 LKGKKVELDQYRENISQVKERwLNPLK-----ELVEKINEKFSNFFSSMQcAGEVDLHTENEEDYDKYGIRIRVKFRSST 981
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEE-YEKKKrevfmEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKP 1068
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966993023 982 --QLHELtphhqSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVvntacKENTSQYFFI 1052
Cdd:TIGR02169 1069 vqRLEAM-----SGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLI-----REKAGEAQFI 1131
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
53-127 |
6.91e-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: 82.36 E-value: 6.91e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966993023 53 IVRISMENFLTYDICEVSPGP-HLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKV---GFFVKRGCSRGMVEIEL 127
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITF 79
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
989-1077 |
1.39e-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: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 989 HHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKenTSQYFFITPKLLQNLPYSEKMTV 1068
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
|
....*....
gi 966993023 1069 LFVYNGPHM 1077
Cdd:cd03227 154 KKVITGVYK 162
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
53-1053 |
1.20e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.79 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTYDICEVSP-GPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV----KRGCSRGMVEI-- 125
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPfSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEItf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 126 -----ELFRASGNLVITREIdVAKNQSFWFINKKSTTQKVVEEQVAALNIQVGNLCQFLPQDKV---------------- 184
Cdd:pfam02463 82 dnedhELPIDKEEVSIRRRV-YRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIeiiammkperrleiee 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 185 ----GEFAKLSKIELLEATEKSIGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHL 260
Cdd:pfam02463 161 eaagSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 261 DLIEMLEAKRPWVEYENVRQEYEE-----VKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNLEARI----------- 324
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEeklaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKvddeeklkese 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 325 -------KEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKTTENCEN-- 395
Cdd:pfam02463 321 kekkkaeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELElk 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 396 ------------LQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDT 463
Cdd:pfam02463 401 seeekeaqllleLARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 464 ------YDAVLWLRSNRDKFKQRVCEPI--MLTINMKDNKNAKYIENHIPSNDLRAFVFESQEDMEVFLKEVR----DNK 531
Cdd:pfam02463 481 klqeqlELLLSRQKLEERSQKESKARSGlkVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVsataDEV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 532 KLRVNAVIAPKSSYADKAPSRSLNELKQYGFFSYLRELFDAPDPVMSYLCCQYHIHEVPVG----------TEKTRERIE 601
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvvegilkdTELTKLKES 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 602 RVIQETRLKQIYTAEEKYVVK----------------TSFYSNKIISSNTSLKVAQFLTVTVDLEQRRHLEEQLKEISRK 665
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKsevkaslseltkelleIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 666 LQAVDSRLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLM----------------EQDTCNLE 729
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaeerekteklkveeekEEKLKAQE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 730 EEERKASTKIKEINVQKAKLVTELTNL--IKICTSLHIQKVDLILQNTTVISEKNKLESDYMAA---SSQLRLTEQHFIE 804
Cdd:pfam02463 801 EELRALEEELKEEAELLEEEQLLIEQEekIKEEELEELALELKEEQKLEKLAEEELERLEEEITkeeLLQELLLKEEELE 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 805 LDENRQRLLQKCKEL------MKRARQVCNLGAEQTLPQEYQTQVPTIPNGHNSSLPMVFQDLP---------NTLDEID 869
Cdd:pfam02463 881 EQKLKDELESKEEKEkeekkeLEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEadekekeenNKEEEEE 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 870 ALLTEERSRASCFTGLNPTIVQEYTKREEEIEQLTEELKGKKVELDQYRENISQVKERWLNPLKELVEKINEKFSNFFSs 949
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY- 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 950 MQCAGEVDLHTENEEDYDKYGIRIRVKFRSSTQLHELTphhQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPIN 1029
Cdd:pfam02463 1040 LELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDL---LSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQN 1116
|
1130 1140
....*....|....*....|....
gi 966993023 1030 ERRVFEMVVNTAckeNTSQYFFIT 1053
Cdd:pfam02463 1117 VSRVANLLKELS---KNAQFIVIS 1137
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
992-1069 |
2.19e-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: 2.19e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966993023 992 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVL 1069
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
56-235 |
7.16e-13 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 68.29 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 56 ISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV------KRGCSRGMVEIELFR 129
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 130 ASG--------NLVITREIDVAKNQSFWFINKKSTTQKVVEEQVAALNIQVgNLCQFLPQDKVGEFAKLSKIELLEATEK 201
Cdd:pfam13476 81 NDGrytyaierSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180 190
....*....|....*....|....*....|....
gi 966993023 202 SIGppemhryhcELKNFREKEKQLETSCKEKTEY 235
Cdd:pfam13476 160 ALE---------EKEDEKKLLEKLLQLKEKKKEL 184
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
53-127 |
8.23e-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: 68.39 E-value: 8.23e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIEL 127
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTL 75
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
53-476 |
3.37e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRASG 132
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 133 NLVITREIDvaKNQSFWFINKKSTTQKVVEEQVAALNIQVGNLCQFLPQDKV--GEFAKLskIELLEATEKSIGP-PEMH 209
Cdd:PRK03918 83 KYRIVRSFN--RGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLNAIYIrqGEIDAI--LESDESREKVVRQiLGLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 210 RYHCELKNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLI---------EMLEAKRPWVEYENVRQ 280
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIsselpelreELEKLEKEVKELEELKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 281 EYEEVKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNLEAR------IKEKATD---IKEASQKCKQKQDVIERKDKH 351
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEyikLSEFYEEYLDELREIEKRLSR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 352 IEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKrrERETL 431
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK--ELEEL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 966993023 432 EKEKKSVDDHIvrfdNLMNQKEDKLRQRFRDTYDAVLWLRSNRDK 476
Cdd:PRK03918 397 EKAKEEIEEEI----SKITARIGELKKEIKELKKAIEELKKAKGK 437
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
53-138 |
3.96e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 60.79 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTY-DICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAfmGRADKVGFFVKRGCSRGMVEIELFRAS 131
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
....*..
gi 966993023 132 GNLVITR 138
Cdd:COG0419 80 KRYRIER 86
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-825 |
1.59e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 244 ERYKQDVERFYERKRHLDLIEmleakRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQIpiTRRIEEMENERHNLEAR 323
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-----ELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 324 IKEKATDIKEASQKCKQKQDVIERKD-KHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKTT-----ENCENLQ 397
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 398 PQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSvddhivrfdnlmnqkedkLRQRfRDTYDAvlWLRSNRDKF 477
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------------LERR-KSNIPA--RLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 478 KQR----------VCEpiMLTINMKDNK--NA--KYIENH-----IPSNDLRAfvfesqedmevFLKEVRDNK---KLRV 535
Cdd:COG4913 450 AEAlgldeaelpfVGE--LIEVRPEEERwrGAieRVLGGFaltllVPPEHYAA-----------ALRWVNRLHlrgRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 536 NAVIAPKSSYADKAPS-RSL-NEL--KQYGFFSYLRELFDAPdpvMSYLCCQyhihevpvgTEKTRERIERVIQETRL-K 610
Cdd:COG4913 517 ERVRTGLPDPERPRLDpDSLaGKLdfKPHPFRAWLEAELGRR---FDYVCVD---------SPEELRRHPRAITRAGQvK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 611 QIYTAEEKyvvKTSFY--SNKIISSNTSLKVAQFLTVTVDLEQRRH-LEEQLKEISRKLQAVDSRLIALRETSKHLEHkD 687
Cdd:COG4913 585 GNGTRHEK---DDRRRirSRYVLGFDNRAKLAALEAELAELEEELAeAEERLEALEAELDALQERREALQRLAEYSWD-E 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 688 NELRQKKKELLERKTKKRQLEQKiSSKLGSLKLMEQDtcnLEEEERKASTKIKEINVQKAKLVTELTNLikictslhiqk 767
Cdd:COG4913 661 IDVASAEREIAELEAELERLDAS-SDDLAALEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQA----------- 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966993023 768 VDLILQNTTVISEKNKLESDYMAASSQLRL----TEQHFIELDENRQRLLQKCKELMKRARQ 825
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLEERFaaalGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
55-127 |
4.10e-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: 56.60 E-value: 4.10e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966993023 55 RISMENFLTYDICE-VSPG-PHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRadkvGFFVKRGCSRGMVEIEL 127
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR----RSGVKAGCIVAAVSAEL 71
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
53-163 |
5.99e-08 |
|
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: 55.29 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLglagkpAFMGRADKVgfFVKRGCSRGMVEIE------ 126
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSL------LLGGRASAD--LIRSGAEKAVVEGVfdisde 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 966993023 127 ----------LFRASGNLVITREIDvAKNQSFWFINKKSTTQKVVEE 163
Cdd:cd03241 73 eeakalllelGIEDDDDLIIRREIS-RKGRSRYFINGQSVTLKLLRE 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-467 |
1.45e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 136 ITREIDVAKNQsfwfINKKSTTQKVVEEQVAALNIQVGNLCQFLPQDKVGEFAKLSKIELLEATEKSIgPPEMHRYHCEL 215
Cdd:TIGR02168 682 LEEKIEELEEK----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 216 KNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFyeRKRHLDLIEMLEAKRPwvEYENVRQEYEEVKLVRDRVKEE 295
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL--KEELKALREALDELRA--ELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 296 VRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNE--ELDRQRR- 372
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElrELESKRSe 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 373 ----ISNTRKMIEDLQNELKTTENceNLQPQIDAITNDLRR-----------IQDEKALCEGEIIDKRRERETL------ 431
Cdd:TIGR02168 913 lrreLEELREKLAQLELRLEGLEV--RIDNLQERLSEEYSLtleeaealenkIEDDEEEARRRLKRLENKIKELgpvnla 990
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966993023 432 -----EKEKKsvddhivRFDNLMNQKED------KL-----------RQRFRDTYDAV 467
Cdd:TIGR02168 991 aieeyEELKE-------RYDFLTAQKEDlteakeTLeeaieeidreaRERFKDTFDQV 1041
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
306-462 |
2.74e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 306 ITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQN 385
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 386 ELkttencENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRD 462
Cdd:COG1196 317 RL------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-397 |
9.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDliEMLEAKRPWVEYENVRQEYEEVKLVRDRVK 293
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 294 EEVRKLKEGQipitRRIEEMENERHNLEARIKEKATDIKEASQKckQKQDVIERkdkhIEEIQQALTVKQNEELDRQRRI 373
Cdd:COG4717 153 ERLEELRELE----EELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEE----LEELQQRLAELEEELEEAQEEL 222
|
170 180
....*....|....*....|....
gi 966993023 374 SNTRKMIEDLQNELKTTENCENLQ 397
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLK 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
216-458 |
6.20e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 216 KNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQ--EYEEVKLVRDRVK 293
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEakKAEEDKNMALRKA 1583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 294 EEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQ-KQDVIERKDKHIEEIQQALTVKQNEELDRQRR 372
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 373 ISNTRKMIEDLQN--ELKTTENCENLQPQidaitnDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMN 450
Cdd:PTZ00121 1664 AEEAKKAEEDKKKaeEAKKAEEDEKKAAE------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
....*...
gi 966993023 451 QKEDKLRQ 458
Cdd:PTZ00121 1738 EAEEDKKK 1745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
208-478 |
8.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 208 MHRYHCELKNFREKEKQLETSCKE------KTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQE 281
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKlrkelrELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 282 YEEVKLVRDRVKEEVRKLKEgqipITRRIEEMENERHNLEARIKEKATDIKEASQKCkqkqdvIERKDKHIEEIQQALTv 361
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFES------VEELEERLKELEPFYN- 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 362 KQNEELDRQRRISNTRKMIEDLQNEL-KTTENCENLQPQIDAITNDL------------RRIQDEKALCEGEIIDKRRER 428
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELdKAFEELAETEKRLEELRKELeelekkyseeeyEELREEYLELSRELAGLRAEL 682
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 966993023 429 ETLEKEKKSVDDHIvrfDNLMNQKE--DKLRQRFRDTYDAVLWLRSNRDKFK 478
Cdd:PRK03918 683 EELEKRREEIKKTL---EKLKEELEerEKAKKELEKLEKALERVEELREKVK 731
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
261-422 |
9.75e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 261 DLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEgqipitrRIEEMENERHNLEARIKEKATDIKEASQKCKQ 340
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 341 KQDVIERKDKHIEEIQqaltvKQNEELDR-QRRISNTRKMIEDLQNELKTTENCENLQ--------PQIDAITND-LRRI 410
Cdd:COG2433 453 ARSEERREIRKDREIS-----RLDREIERlERELEEERERIEELKRKLERLKELWKLEhsgelvpvKVVEKFTKEaIRRL 527
|
170
....*....|..
gi 966993023 411 QDEKALCEGEII 422
Cdd:COG2433 528 EEEYGLKEGDVV 539
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
53-151 |
1.34e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLT-YDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAG-KPAFMGRADKVGFFVKRGCSRGMVEIELFRA 130
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGeLPPNSKGGAHDPKLIREGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|....*....
gi 966993023 131 SGN-LVITREIDVAKN-------QSFWFI 151
Cdd:cd03240 81 NGKkYTITRSLAILENvifchqgESNWPL 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-453 |
1.58e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 181 QDKVGEFAKLSKIELLEATEKSIGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLQKMVQ---RNERYKQDVERFYERK 257
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 258 RHLDLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKlkegqipITRRIEEMENERHNLEARIKEkatdIKEASQK 337
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK-------ITARIGELKKEIKELKKAIEE----LKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 338 C---------KQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKTTENCEnlqpQIDAITNDLR 408
Cdd:PRK03918 438 CpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLK 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 966993023 409 RIQDEKALCEGEIIDKRRER-ETLEKEKKSVDDHIVRFDNLMNQKE 453
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKlIKLKGEIKSLKKELEKLEELKKKLA 559
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
53-459 |
1.66e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPafmgRADKVGFFVKRGCSRGMVEIElFRASG 132
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELE-FRIGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 133 NLVITReidvaknQSFWFINKKSTTQKVVEEQVAALNIQVGNLCQFLPQDKVGefakLSKIELLEATEKSIGppemhryh 212
Cdd:PRK01156 78 HVYQIR-------RSIERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKNILG----ISKDVFLNSIFVGQG-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 213 celknfrEKEKQLETSCKEKTEYLQKMVQRNErykqdVERFYERKRhlDLIEMLEAKRPwvEYENVRQEYEEVKLVRDRV 292
Cdd:PRK01156 139 -------EMDSLISGDPAQRKKILDEILEINS-----LERNYDKLK--DVIDMLRAEIS--NIDYLEEKLKSSNLELENI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 293 KEEVRKLKEGQIPITRRIEEMENERHNLEarikEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALT------VKQNEE 366
Cdd:PRK01156 203 KKQIADDEKSHSITLKEIERLSIEYNNAM----DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSmeleknNYYKEL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 367 LDRQRRISN-----TRKMIEDLQNELKTTEN----CENLQPQIDAITNDLRRIQDEKALcEGEIIDKRRERETLEKEKKS 437
Cdd:PRK01156 279 EERHMKIINdpvykNRNYINDYFKYKNDIENkkqiLSNIDAEINKYHAIIKKLSVLQKD-YNDYIKKKSRYDDLNNQILE 357
|
410 420
....*....|....*....|..
gi 966993023 438 VDDHIVRFDNLMNQKEDKLRQR 459
Cdd:PRK01156 358 LEGYEMDYNSYLKSIESLKKKI 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
274-723 |
1.93e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEgqipITRRIEEMENERHNLEARIK--EKATDIKEASQKCKQKQDVIERKDKH 351
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 352 IEEIQQALTvkqnEELDRQRRISNTRKMIEDLQNELKTTENCENLQ--PQIDAITNDLRRIQDEKALCEGEIIDKRRERE 429
Cdd:COG4717 148 LEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 430 TLEKEKKSVDDhivrfDNLMNQKEDKLRQrfrdtYDAVLWLRSnrdkfkqrvcepIMLTINMKDNKNAKYIENHIPSNDL 509
Cdd:COG4717 224 ELEEELEQLEN-----ELEAAALEERLKE-----ARLLLLIAA------------ALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 510 RAFVFesqedmeVFLKEVRDNKKLrvnaviAPKSSYADKAPSRSLNELKQYGFFSYLREL----FDAPDPVMSYLCCQYH 585
Cdd:COG4717 282 VLGLL-------ALLFLLLAREKA------SLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 586 IHEVPVGTEKTRERIERVIQETRLKQ---------------IYTAEEKYVVKT---SFYSNKIISSNTSLKVAQFLTVTV 647
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraALEQAEEYQELKeelEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 648 DLEQR-RHLEEQLKEISRKLQAVDSRLIALRETSKHLEhKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQ 723
Cdd:COG4717 429 ELEEElEELEEELEELEEELEELREELAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
280-434 |
3.89e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 280 QEYEEVKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKckqkqdvierkdkhIEEIQQAL 359
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--------------IKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 360 -TVKQNEELDR-QRRISNTRKMIEDLQNELKttenceNLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKE 434
Cdd:COG1579 83 gNVRNNKEYEAlQKEIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
214-450 |
5.66e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDV-------------ERFYERKRHLDLI--EMLEAKRPWV-EYEN 277
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVtellnkysalaikNKFAKTKKDSEIIikEIKDAHKKFIlEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 278 VRQEYEEVKLVRDRVKEEV---RKLKEGQIPITRRIEEMENERHnlearikeKATDIKEASQKCKQKQDVIERKDKHIEE 354
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIEDDAaknDKSNKAAIDIQLSLENFENKFL--------KISDIKKKINDCLKETESIEKKISSFSI 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 355 IQQALTVKQNEELDRQ-----RRISNTRKMIEDLQNELkttencENLQPQIDAITNDlrrIQDEKALCEGEIIDKRRE-- 427
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSlqeflESLKDQKKNIEDKKKEL------DELDSEIEKIEID---VDQHKKNYEIGIIEKIKEia 1709
|
250 260
....*....|....*....|....*.
gi 966993023 428 ---RETLEKEKKSVDDHIVRFDNLMN 450
Cdd:TIGR01612 1710 ianKEEIESIKELIEPTIENLISSFN 1735
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
55-796 |
6.94e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 55 RISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVgffVKRGCSRGMVEIELFRASGNL 134
Cdd:PRK02224 5 RVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLDDV---ITIGAEEAEIELWFEHAGGEY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 135 VITREIDVAKNQSfwfinkkSTTQKV-------------VEEQVAAL---------------NIQVGNLCQFLP---QDK 183
Cdd:PRK02224 82 HIERRVRLSGDRA-------TTAKCVletpegtidgardVREEVTELlrmdaeafvncayvrQGEVNKLINATPsdrQDM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 184 VGEFAKLSKIE---------------LLEATEKSIGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLqkmvqrnERYKQ 248
Cdd:PRK02224 155 IDDLLQLGKLEeyrerasdarlgverVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI-------ERYEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 249 DVERFYERKRHLDliEMLEakrpwvEYENVRQEYEEVKlvrdrvkEEVRKLKEgqipitrRIEEMENERHNLEARIKEKA 328
Cdd:PRK02224 228 QREQARETRDEAD--EVLE------EHEERREELETLE-------AEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 329 TDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKT-TENCENLQPQIDAITNDL 407
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESlREDADDLEERAEELREEA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 408 RRIQDEKALCEGEIIDKRRERETLEKE----KKSVDDHIVRFDNLMNQKEDklrqrfrdtydavlwLRSNRDKFKQRVCE 483
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEE---------------LREERDELREREAE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 484 pimLTINMKDNKNA-----------KYIENHIPSNDL-RAFVFESQEDMEVFLKEVRDNKKLRVNAViapkssyaDKAPS 551
Cdd:PRK02224 431 ---LEATLRTARERveeaealleagKCPECGQPVEGSpHVETIEEDRERVEELEAELEDLEEEVEEV--------EERLE 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 552 RSLNELKQYGFFSYLRELFDAPDPVmsylccqyhIHEVPVGTEKTRERIERvIQETRLKQIYTAEEKYVVKTSFYSNkii 631
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEEL---------IAERRETIEEKRERAEE-LRERAAELEAEAEEKREAAAEAEEE--- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 632 SSNTSLKVAQFLTVTVDLEQRRHLEEQLKEISRKLQAVDSRLIALRETSKHLEHKDNELRQKKKELLERktkKRQLEQKI 711
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER---KRELEAEF 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 712 SSKlgSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTE---LTNLIKICTSLHIQKVDliLQNT-----TVISEKNK 783
Cdd:PRK02224 644 DEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREA--LENRvealeALYDEAEE 719
|
810
....*....|...
gi 966993023 784 LESDYMAASSQLR 796
Cdd:PRK02224 720 LESMYGDLRAELR 732
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
214-436 |
1.53e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSCKEKTEYLQ-KMVQRNERYKQDVE-----RFYERKRHLDLIE-MLEAKRPWVEYENVRQ------ 280
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQmERQQKNERVRQELEaarkvKILEEERQRKIQQqKVEMEQIRAEQEEARQrevrrl 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 281 ------EYEEVKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNlEARIKEKATDIKEasqkckqkQDVIERKDKHIEE 354
Cdd:pfam17380 441 eeerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILE--------KELEERKQAMIEE 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 355 IQQALTVKQNEElDRQRRI--SNTRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIqdekalcegEIIDKRRE--RET 430
Cdd:pfam17380 512 ERKRKLLEKEME-ERQKAIyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL---------EAMEREREmmRQI 581
|
....*.
gi 966993023 431 LEKEKK 436
Cdd:pfam17380 582 VESEKA 587
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
650-825 |
1.66e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 650 EQRRHLEEQLKEISRKLQAVDSRLIALREtskHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKlmeqdtcNLE 729
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-------EAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 730 EEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENR 809
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170
....*....|....*.
gi 966993023 810 QRLLQKCKELMKRARQ 825
Cdd:COG1196 452 AELEEEEEALLELLAE 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-467 |
1.87e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 249 DVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEEVKLVRDRvkeEVRKLKEGQIPITRRIEEMENERHNLEARIKEKA 328
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR---EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 329 TDIKEAsqkcKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKTTENCENLQPQIDAITNDLR 408
Cdd:COG1196 682 EELAER----LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 409 RIQDEKALcEGEIIDKRRERETLEK-------EKKSVDDhivRFDNLMNQKED------KL-----------RQRFRDTY 464
Cdd:COG1196 758 EPPDLEEL-ERELERLEREIEALGPvnllaieEYEELEE---RYDFLSEQREDleeareTLeeaieeidretRERFLETF 833
|
...
gi 966993023 465 DAV 467
Cdd:COG1196 834 DAV 836
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
214-453 |
1.91e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSCKEKTEYLQKmvQRNERYK-QDVERFYERKRHLDLIEMLEAKRPwVEYENVRQEYEEVKLvrdRV 292
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKaEELKKAEEEKKKVEQLKKKEAEEK-KKAEELKKAEEENKI---KA 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 293 KEEVRKLKEGQipitRRIEEMENERHnlEARIKEKATDIKEasqkcKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRR 372
Cdd:PTZ00121 1664 AEEAKKAEEDK----KKAEEAKKAEE--DEKKAAEALKKEA-----EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 373 ISNTRKMIEDLQN--ELKTTENCEN-LQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDdhivRFDNLM 449
Cdd:PTZ00121 1733 EEAKKEAEEDKKKaeEAKKDEEEKKkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD----IFDNFA 1808
|
....
gi 966993023 450 NQKE 453
Cdd:PTZ00121 1809 NIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-519 |
2.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 183 KVGEFAKLSKIELLEATEKSIGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLQKMVQRNE-RYKQDVERFYERKRHLD 261
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAE 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 262 LIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQIpitrRIEEMENERHNLEARIKE-----KATDIKEASQ 336
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKEAeedkkKAEEAKKDEE 1754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 337 KCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQ--RRISNTRKMIEDlqnelkTTENCENLQpqiDAITNDLRRIQDEK 414
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKD------IFDNFANII---EGGKEGNLVINDSK 1825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 415 ALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYdavlwlrsNRDKFKQRVCEPIMltiNMKDN 494
Cdd:PTZ00121 1826 EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKD--------LKEDDEEEIEEADE---IEKID 1894
|
330 340
....*....|....*....|....*
gi 966993023 495 KNAkyIENHIPSNDLRAFVFESQED 519
Cdd:PTZ00121 1895 KDD--IEREIPNNNMAGKNNDIIDD 1917
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
309-458 |
2.37e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 309 RIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELK 388
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 389 TTEN----------------------------------------CENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRER 428
Cdd:COG4942 101 AQKEelaellralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|
gi 966993023 429 ETLEKEKKSVDDHIVRFDNLMNQKEDKLRQ 458
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-1021 |
2.37e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 219 REKEKQLETsckekteyLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRpwvEYENVRQEYEEVKLVRDRVKEEVRK 298
Cdd:COG1196 196 GELERQLEP--------LERQAEKAERYRELKEELKELEAELLLLKLRELEA---ELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 299 LKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRK 378
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 379 MIEDLQNELKTTENC-ENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLR 457
Cdd:COG1196 345 ELEEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 458 QRfrdtYDAVLWLRSNRDKFKQRVCEpimlTINMKDNKNAKYIENHIPSNDLRAfVFESQEDMEVFLKEVRDNKKLRVNA 537
Cdd:COG1196 425 EL----EEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELLE-EAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 538 VIAPKSSYAdkapsrslnelkqyGFFSYLRELFDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQ-------ETRLK 610
Cdd:COG1196 496 LLEAEADYE--------------GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddEVAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 611 QI-YTAEEKYVVKTSFYSNKIISSNTSLKVAQ-------FLTVTVDLEQRRHLEEQLKEISRKLQAVDSRLIALRETSKH 682
Cdd:COG1196 562 AIeYLKAAKAGRATFLPLDKIRARAALAAALArgaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 683 LEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEqdtcnlEEEERKASTKIKEINVQKAKLVTELTNLIKICTS 762
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL------EELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 763 LHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELmKRARQ----VcNLGAEQtlpqE 838
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL-EREIEalgpV-NLLAIE----E 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 839 YQ----------TQvptipnghnsslpmvFQDLpntLDEIDALLTeersrascftglnptIVQEYTKReeeieqlteelk 908
Cdd:COG1196 790 YEeleerydflsEQ---------------REDL---EEARETLEE---------------AIEEIDRE------------ 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 909 gkkveldqyrenisqVKERwlnpLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRV-----KFRSSTQL 983
Cdd:COG1196 825 ---------------TRER----FLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLETGIEIMAqppgkKLQRLSLL 885
|
810 820 830
....*....|....*....|....*....|....*...
gi 966993023 984 heltphhqSGGERSVSTMLYLMALQELNRCPFRVVDEI 1021
Cdd:COG1196 886 --------SGGEKALTALALLFAIFRLNPSPFCVLDEV 915
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
992-1053 |
2.67e-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: 2.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966993023 992 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 1053
Cdd:cd03278 115 SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS---KETQFIVIT 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
274-458 |
3.41e-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: 44.37 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIE 353
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 354 EIQQA-----------LTVKQNEELDRQRRISNTRKMIEDLQNELkttencENLQPQIDAITNDLRRIQDEKALCEGEII 422
Cdd:COG4942 108 ELLRAlyrlgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQA------EELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 966993023 423 DKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQ 458
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-459 |
3.89e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETScKEKTEYLQKMV-QRNERYKQDVERFYE-RKRHLDLIEMLEAKRpwveyenvrQEYEEVKLVRDR 291
Cdd:PRK02224 500 RAEDLVEAEDRIERL-EERREDLEELIaERRETIEEKRERAEElRERAAELEAEAEEKR---------EAAAEAEEEAEE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 292 VKEEVRKLKEGQIPITRRIEEMENERHNLeARIKEKATDIKEASQKCKQKQDV-IERKDKHIE--EIQQALtvkqNEELD 368
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREKREALAELnDERRERLAEkrERKREL----EAEFD 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 369 RQRrisntrkmIEDLQNELKTTEN-CENLQPQIDAITNDLRRIQDEKALCEGEIidkrRERETLEKEKKSVDDHIVRFDN 447
Cdd:PRK02224 645 EAR--------IEEAREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVEALEA 712
|
250 260
....*....|....*....|..
gi 966993023 448 LMNQKED----------KLRQR 459
Cdd:PRK02224 713 LYDEAEElesmygdlraELRQR 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
650-823 |
3.91e-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: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 650 EQRRHLEEQLKEISRKLQAVDSRLIALR-------ETSKHLEHKDNELRQKKKELLERK----TKKRQLEQKISSKLGSL 718
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 719 KLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLT 798
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180
....*....|....*....|....*
gi 966993023 799 EQHFIELDENRQRLLQKCKELMKRA 823
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKL 430
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
222-438 |
4.76e-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: 44.12 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 222 EKQLETSCKEKTEYLQKMVQRN-------ERYKQDVERFYERKRHL--DLIEMLEAKRPWVE-YENVRQEYEEVKLVRDR 291
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANrqrekekERYKRDREQWERQRRELesRVAELKEELRQSREkHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 292 VKEEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQkcKQKQDVIERKDKHIEEIQQALTVKQNEEldRQR 371
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKE--RAKKAGAQRKEEEAERKQLQAKLQQTEE--ELR 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 372 RISNTRKMIEDLQNELKTteNCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSV 438
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDT--QVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
53-95 |
5.35e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 5.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICL 95
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRL 45
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
53-407 |
8.32e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.97 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFmgraDKVGFFVKRGCSRGMVEIELFRASG 132
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKF----FEDDFLVLYLKDVIKIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 133 NLVITREIDVAKnqsfWFinkksttqkVVEEQVAALNIQVGNLCQFLPQDKVGEFAKLSKIELLEATEKSIGPPEMHRYh 212
Cdd:pfam13175 79 NISFSIDIEIDV----EF---------LLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKY- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 213 ceLKNFREKEKQLETSCKEKteYLQKMVQRNERYKQDVERFYERKRHLDlIEMLEAKRPWVEYENVRQEYEEVKLVRDRV 292
Cdd:pfam13175 145 --LKQFKIYIYNNYYLDEKK--NVFDKKSKYELPSLKEEFLNSEKEEIK-VDKEDLKKLINELEKSINYHENVLENLQIK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 293 KEevrklkegqIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTvkqneeldrqrr 372
Cdd:pfam13175 220 KL---------LISADRNASDEDSEKINSLLGALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLA------------ 278
|
330 340 350
....*....|....*....|....*....|....*
gi 966993023 373 iSNTRKMIEDLQNELKTTENCENLQPQIDAITNDL 407
Cdd:pfam13175 279 -EELKNILFKKIDKLKDFGYPPFLNPEIEIKKDDE 312
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
311-386 |
8.63e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966993023 311 EEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNE 386
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
214-390 |
8.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLEtscKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEM-LEAKRP----------WVEYENVRQEY 282
Cdd:COG3883 59 ELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYRSGGSVSYLDVlLGSESFsdfldrlsalSKIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 283 EEVKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVK 362
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170 180
....*....|....*....|....*...
gi 966993023 363 QNEELDRQRRISNTRKMIEDLQNELKTT 390
Cdd:COG3883 216 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
53-117 |
9.17e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.29 E-value: 9.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 53 IVRISMENFLTYDICEV--SPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRG 117
Cdd:COG3950 3 IKSLTIENFRGFEDLEIdfDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNG 69
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-372 |
9.40e-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: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 136 ITREIDVAKNQsfwfINKKSTTQKVVEEQVAALNIQVGNLcqflpQDKVGEFAKlsKIELLEAteksigppemhryhcEL 215
Cdd:COG4942 32 LQQEIAELEKE----LAALKKEEKALLKQLAALERRIAAL-----ARRIRALEQ--ELAALEA---------------EL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 216 KNFREKEKQLETSCKEKTEYLQKMV---QRNERYK--------QDVERFYERKRHLDLIemleakrpwveYENVRQEYEE 284
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLralYRLGRQPplalllspEDFLDAVRRLQYLKYL-----------APARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 285 VKLVRDRVKEEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQN 364
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*...
gi 966993023 365 EELDRQRR 372
Cdd:COG4942 235 EAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
217-440 |
9.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 217 NFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYE--RKRHLDLIEMLEAKRPwveyENVRQEYEEVKLVRDRVKE 294
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEeaKKKAEDARKAEEARKA----EDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 295 EVRKLKEG-QIPITRRIEE---MENERHNLEARikeKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELdrq 370
Cdd:PTZ00121 1156 IARKAEDArKAEEARKAEDakkAEAARKAEEVR---KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV--- 1229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966993023 371 RRISNTRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKAlcegeiiDKRRERETLEK--EKKSVDD 440
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-------EEARKADELKKaeEKKKADE 1294
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
309-459 |
1.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 309 RIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISntrKMIEDLQNELK 388
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---ERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 389 TT----------------ENCENLQP-------QIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRF 445
Cdd:COG3883 101 SVsyldvllgsesfsdflDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170
....*....|....
gi 966993023 446 DNLMNQKEDKLRQR 459
Cdd:COG3883 181 EALLAQLSAEEAAA 194
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
650-749 |
1.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 650 EQRRHLEEQLKEISRKLQAVDSRLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSL----------K 719
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakeI 158
|
90 100 110
....*....|....*....|....*....|.
gi 966993023 720 LMEQdtcnLEEE-ERKASTKIKEInVQKAKL 749
Cdd:PRK12704 159 LLEK----VEEEaRHEAAVLIKEI-EEEAKE 184
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
52-145 |
1.29e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 42.45 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 52 SIVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLgLAgkpafMGRadkvGF-------FVKRGCSRGMVE 124
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-----PGR----SHrtardkeLIRFGAEAAVIH 71
|
90 100
....*....|....*....|.
gi 966993023 125 IELFRASGNLVITREIDVAKN 145
Cdd:PRK00064 72 GRVEKGGRELPLGLEIDKKGG 92
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
53-93 |
1.58e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.23 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 966993023 53 IVRISMENFLTYDICEVSPGPhLNMIIGANGTGKSSIVCAI 93
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDAL 41
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
230-362 |
1.80e-03 |
|
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: 40.66 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 230 KEKTEYLQKMVQRNERYKQDVERfyERKRHLD-----LIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQI 304
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQ--ENKRLTEplqkaQEEVEELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 966993023 305 PITRRIEEMENERHNLEARIKEKatdIKEASQKCKQKQDVIERKdkhIEEIQQALTVK 362
Cdd:pfam13851 110 VLEQRFEKVERERDELYDKFEAA---IQDVQQKTGLKNLLLEKK---LQALGETLEKK 161
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
318-481 |
1.88e-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: 41.06 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 318 HNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNEELDRQRRISNTRKMIEDLQNELKTTENcenlQ 397
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN----N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 398 PQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYDAVLWLRSNRDKF 477
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
....
gi 966993023 478 KQRV 481
Cdd:COG1579 169 AAKI 172
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
651-748 |
2.55e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.25 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 651 QRRHLEEQLKEISRKLQAVDSRLIALRETskhLEHKDNELRQKKKELLERktkkrqlEQKISSKLGSLKLMEQDTCNLEE 730
Cdd:pfam12072 65 LRAEAERELKERRNELQRQERRLLQKEET---LDRKDESLEKKEESLEKK-------EKELEAQQQQLEEKEEELEELIE 134
|
90
....*....|....*...
gi 966993023 731 EERKASTKIKEINVQKAK 748
Cdd:pfam12072 135 EQRQELERISGLTSEEAK 152
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
642-877 |
2.83e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 642 FLTVTVDLEQRRHLEEQLKEISRKLQAVDSRLialretskhlehkdNELRQKKKELLErktKKRQLEQKISSKLGSLKLM 721
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKEL--------------AALKKEEKALLK---QLAALERRIAALARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 722 EQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLI-KICTSLHIQKVDLILQNTTVisekNKLESDYMAASSQLRLTEQ 800
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 801 HFIELDENRQRLLQKCKELMKRARQVCNLGAEQtlpQEYQTQVPTIPNGHNSSLPMVFQDLPNTLDEIDALLTEERS 877
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
219-409 |
3.59e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.17 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 219 REKEKQLETSCKEKTEYLQKMVQRNERYKQDVERfyeRKRHLDLIEmlEAKrpwveyENVRQEYEEVKLVRDRVKEEVRK 298
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELEELKEQNEELEKQYKV---KKKTLDLLP--DAE------ENIAKLQALVDASAQRLVELAGQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 299 LKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKdkhiEEIQQALtVKQNEELDRQ-------R 371
Cdd:pfam05667 424 WEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQK----EELYKQL-VAEYERLPKDvsrsaytR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966993023 372 RI----SNTRKMIEDLQNELKTTencENLQPQIDAITNDLRR 409
Cdd:pfam05667 499 RIleivKNIKKQKEEITKILSDT---KSLQKEINSLTGKLDR 537
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
649-758 |
3.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 649 LEQRRHLEEQLKEISRKLQAVDSRLIALRETskhLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTcnL 728
Cdd:PRK12704 67 HKLRNEFEKELRERRNELQKLEKRLLQKEEN---LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ--L 141
|
90 100 110
....*....|....*....|....*....|....*
gi 966993023 729 EEEERKAS-TK--IKEINVQKAK--LVTELTNLIK 758
Cdd:PRK12704 142 QELERISGlTAeeAKEILLEKVEeeARHEAAVLIK 176
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
76-440 |
3.81e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 76 NMIIGANGTGKSSIVCAICLGLAGKPaFmgRADKVGFFV----KRGCsrgMVEIELFRASGNLVITREI-----DVAKNQ 146
Cdd:PHA02562 30 TLITGKNGAGKSTMLEALTFALFGKP-F--RDIKKGQLInsinKKDL---LVELWFEYGEKEYYIKRGIkpnvfEIYCNG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 147 SFWfiNKKSTT---QKVVeEQVAALN------IQVGNLCQFLPqdkvgeFAKLSKIELLEATEKSIgppemhryhcELKN 217
Cdd:PHA02562 104 KLL--DESASSkdfQKYF-EQMLGMNyksfkqIVVLGTAGYVP------FMQLSAPARRKLVEDLL----------DISV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 218 FREKEKQLETSCKEKTEYLQKMVQRNERYKQDVerfyerKRHLDLIEMLEAK------RPWVEYENVRQEYEEVKLVRDR 291
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQI------KTYNKNIEEQRKKngeniaRKQNKYDELVEEAKTIKAEIEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 292 VKEEVRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIK---------EASQKCKQKQDVIERKDKHIEEIQQALT-- 360
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEkl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 361 -VKQNEELDRQRRISNTRKMIEDLQNELkttencENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVD 439
Cdd:PHA02562 319 dTAIDELEEIMDEFNEQSKKLLELKNKI------STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
.
gi 966993023 440 D 440
Cdd:PHA02562 393 K 393
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
648-767 |
4.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 648 DLEQRRHLEEQLKEISRKLQAVDSRLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKIS-SKLGSLKLMEQDTC 726
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELE 202
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 966993023 727 NLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQK 767
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
214-442 |
4.05e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSC-------KEKTEYLQKMVQRNERYKQDVERFYERK-RHLDLIEMLEAKRpwveyENVRQEYEEV 285
Cdd:pfam05483 479 ELEKEKLKNIELTAHCdklllenKELTQEASDMTLELKKHQEDIINCKKQEeRMLKQIENLEEKE-----MNLRDELESV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 286 KlvrdrvkeevRKLKEGQIPITRRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEEIQQALTVKQNE 365
Cdd:pfam05483 554 R----------EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966993023 366 ELDRQRRISNTRKMIEDLQNELKTTENcenlqpQIDAITNDLRRIQDEKALCEGEIIdkrrerETLEKEKKSVDDHI 442
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQ------KFEEIIDNYQKEIEDKKISEEKLL------EEVEKAKAIADEAV 688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-462 |
4.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 214 ELKNFREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKR--------PWVEYENVRQEYEEV 285
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelerldaSSDDLAALEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 286 KLVRDRVKEEVRKLKegqipitRRIEEMENERHNLEARIKEKATDIKEASQKCK--QKQDVIER-----KDKHIEEIQQA 358
Cdd:COG4913 698 EAELEELEEELDELK-------GEIGRLEKELEQAEEELDELQDRLEAAEDLARleLRALLEERfaaalGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 359 LTvkqnEELDR-QRRISNTRKMIEDLQNELKT--TENCENLQPQIDAIT---NDLRRIQDEKAlcegeiidKRRERETLE 432
Cdd:COG4913 771 LE----ERIDAlRARLNRAEEELERAMRAFNRewPAETADLDADLESLPeylALLDRLEEDGL--------PEYEERFKE 838
|
250 260 270
....*....|....*....|....*....|
gi 966993023 433 KEKKSVDDHIVRFDNLMNQKEDKLRQRFRD 462
Cdd:COG4913 839 LLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
649-822 |
4.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 649 LEQRRHLEEQLKEISRKLQAVDSRLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNL 728
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 729 EEEERKASTKIKEINvQKAKLVTELTNLIKictsLHIQKVDLILQNTTVISEKNKLESDYmaaSSQLRLTEQHFIELDEN 808
Cdd:PRK03918 265 EERIEELKKEIEELE-EKVKELKELKEKAE----EYIKLSEFYEEYLDELREIEKRLSRL---EEEINGIEERIKELEEK 336
|
170
....*....|....*..
gi 966993023 809 RQR---LLQKCKELMKR 822
Cdd:PRK03918 337 EERleeLKKKLKELEKR 353
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
952-1074 |
4.86e-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: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 952 CAGEVDLHTENEEDYDKYGIRIRVKFRSstQLheltphhqSGGERSVSTMLYLMALQelnrCPFRVVDEINQGMDPINER 1031
Cdd:cd00267 52 TSGEILIDGKDIAKLPLEELRRRIGYVP--QL--------SGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRE 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 966993023 1032 RVFEMVVNTACKENTsqYFFITPKLLQNLPYSEKmtVLFVYNG 1074
Cdd:cd00267 118 RLLELLRELAEEGRT--VIIVTHDPELAELAADR--VIVLKDG 156
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
234-481 |
5.17e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 234 EYLQK--MVQRNErYKQDVERFYERK---------RHLDLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEG 302
Cdd:PRK05771 23 EALHElgVVHIED-LKEELSNERLRKlrslltklsEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 303 QIPITRRIEEMENERHNLEARIKE----KATDIKEA--------SQKCKQKQDVIERKDKHIEEIQQALTVKQNEELD-- 368
Cdd:PRK05771 102 IKELEEEISELENEIKELEQEIERlepwGNFDLDLSlllgfkyvSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyv 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 369 ----RQRRISNTRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRREretLEKEKKSVDDHIvr 444
Cdd:PRK05771 182 vvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKK---YLEELLALYEYL-- 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 966993023 445 fDNLMNQKEDKLRQRFRDTYDAVL-WLRSNR-DKFKQRV 481
Cdd:PRK05771 257 -EIELERAEALSKFLKTDKTFAIEgWVPEDRvKKLKELI 294
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
53-172 |
6.37e-03 |
|
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: 39.48 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 53 IVRISMENFLTY-DICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMgRADKVGFFVKRGC------SRGMVEI 125
Cdd:cd03275 1 LKRLELENFKSYkGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHL-RSKNLKDLIYRARvgkpdsNSAYVTA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 966993023 126 ELFRASGN-LVITREIdvAKNQSFWFINKKSTTQKVVEEQVAALNIQV 172
Cdd:cd03275 80 VYEDDDGEeKTFRRII--TGGSSSYRINGKVVSLKEYNEELEKINILV 125
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
53-99 |
8.37e-03 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 39.77 E-value: 8.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966993023 53 IVRISMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAG 99
Cdd:PRK14079 3 LLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTG 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-459 |
8.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 274 EYENVRQEYEEVKLVRDRVKEEVRKLKEgqipitrRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERK----D 349
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966993023 350 KHIEEIQQA----------LTVKQNEE-LDRQRRIS----NTRKMIEDLQNELKTTENCE-NLQPQIDAITNDLRRIQDE 413
Cdd:COG3883 90 ERARALYRSggsvsyldvlLGSESFSDfLDRLSALSkiadADADLLEELKADKAELEAKKaELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966993023 414 KALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQR 459
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| |
