|
Name |
Accession |
Description |
Interval |
E-value |
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
1-452 |
0e+00 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 823.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 1 MAKKKVIFECMACGYQSPKWMGKCPNCGAWNQM-EEIVEKAANPKHGVKTKELAGKVQKLNSIKHETTPRVLTDSAEFNR 79
Cdd:COG1066 1 MAKTKTVYVCQECGYESPKWLGRCPECGAWNTLvEEVVAKAKKGRAASGAAGRASKPVPLSEVEAEEEPRISTGIGELDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 80 VLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQK-KKVLYITGEESLSQTKLRAERLDEDSSELQVLAETDLEVIYQT 158
Cdd:COG1066 81 VLGGGLVPGSVVLIGGEPGIGKSTLLLQVAARLAKKgGKVLYVSGEESASQIKLRAERLGLLSDNLYLLAETDLEAILAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 159 VKEEQPDLLVVDSIQTIYHPEISSAPGSVSQVRESTQSLMNIAKQMNIATFIVGHVTKEGQIAGPRLLEHMVDTVLYFEG 238
Cdd:COG1066 161 IEELKPDLLVIDSIQTMYSEELESAPGSVSQVRECAAELIRLAKETGIAVFLVGHVTKEGSIAGPRVLEHMVDTVLYFEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 239 DEHHAYRILRAVKNRFGSTNEMGIFEMKQSGLKGVNNPSEMFLEERSTNVPGSTIVATMEGTRPLLIEVQALVTPTTFNN 318
Cdd:COG1066 241 DRHSRYRILRAVKNRFGSTNEIGVFEMTEKGLREVSNPSELFLSERDEPVPGSAVTVTMEGTRPLLVEVQALVSPSSFGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 319 PRRMATGIDHNRLSLLMAVLEKKENYLLQQQDAYIKVAGGVKLTEPAVDLSVIVATASSFKDKAVDGLDCYIGEVGLTGE 398
Cdd:COG1066 321 PRRTAVGLDSNRLAMLLAVLEKRAGLPLGDQDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGEVGLTGE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 613363400 399 VRRVSRIEQRVQEAAKLGFKRVIIPKNNIGGWTyPEGIQVIGVTTVHEALSFAL 452
Cdd:COG1066 401 IRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKLK-PKGIEIIGVSTLEEALEALF 453
|
|
| sms |
TIGR00416 |
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved ... |
1-448 |
0e+00 |
|
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved in both DNA repair and degradation of proteins, peptides, glycopeptides. Also known as sms. Residues 11-28 of the SEED alignment contain a putative Zn binding domain. Residues 110-117 of the seed contain a putative ATP binding site both documented in Haemophilus (SP:P45266) and in Listeria monocytogenes (SP:Q48761) . for E.coli see ( J. BACTERIOL. 178:5045-5048(1996)). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273067 [Multi-domain] Cd Length: 454 Bit Score: 632.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 1 MAKKKVIFECMACGYQSPKWMGKCPNCGAWNQMEEIV---------EKAANPKHGVKTkelAGKVQKLNSIKHETTPRVL 71
Cdd:TIGR00416 1 MAKAKSKFVCQHCGADSPKWQGKCPACHAWNTITEERlhrslgaqkNRRNSGKAGIPQ---AQKSQTISAIELEEVPRFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 72 TDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQKK-KVLYITGEESLSQTKLRAERLDEDSSELQVLAET 150
Cdd:TIGR00416 78 SGFGELDRVLGGGIVPGSLILIGGDPGIGKSTLLLQVACQLAKNQmKVLYVSGEESLQQIKMRAIRLGLPEPNLYVLSET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 151 DLEVIYQTVKEEQPDLLVVDSIQTIYHPEISSAPGSVSQVRESTQSLMNIAKQMNIATFIVGHVTKEGQIAGPRLLEHMV 230
Cdd:TIGR00416 158 NWEQICANIEEENPQACVIDSIQTLYSPDISSAPGSVSQVRECTAELMRLAKTRGIAIFIVGHVTKEGSIAGPKVLEHMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 231 DTVLYFEGDEHHAYRILRAVKNRFGSTNEMGIFEMKQSGLKGVNNPSEMFLEERSTNVPGSTIVATMEGTRPLLIEVQAL 310
Cdd:TIGR00416 238 DTVLYFEGDRDSRFRILRSVKNRFGATNEIGIFEMTEQGLREVLNPSAIFLSRREEPMSGSSITVTWEGTRPLLVEIQAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 311 VTPTTFNNPRRMATGIDHNRLSLLMAVLEKKENYLLQQQDAYIKVAGGVKLTEPAVDLSVIVATASSFKDKAVDGLDCYI 390
Cdd:TIGR00416 318 VSPTSFANPRRVATGLDQNRLALLLAVLEKRLGLPLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 613363400 391 GEVGLTGEVRRVSRIEQRVQEAAKLGFKRVIIPKNNIGGwTYPEGIQVIGVTTVHEAL 448
Cdd:TIGR00416 398 GEVGLAGEIRPVPSLEERLKEAAKLGFKRAIVPKANSPK-TAPEGIKVIGVKKVGDAL 454
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
8-273 |
1.98e-167 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 471.25 E-value: 1.98e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 8 FECMACGYQSPKWMGKCPNCGAWNQMEEIVEKAANPKHGVKTKELA-GKVQKLNSIKHETTPRVLTDSAEFNRVLGGGIV 86
Cdd:cd01121 1 YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSSASRRASASPSpSKPLPLSDVEAEEEERISTGIGELDRVLGGGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 87 SGSLVLIGGDPGIGKSTLLLQICASLSQK-KKVLYITGEESLSQTKLRAERLDEDSSELQVLAETDLEVIYQTVKEEQPD 165
Cdd:cd01121 81 PGSVVLIGGDPGIGKSTLLLQVAARLAQRgGKVLYVSGEESLSQIKLRAERLGLGSDNLYLLAETNLEAILAEIEELKPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 166 LLVVDSIQTIYHPEISSAPGSVSQVRESTQSLMNIAKQMNIATFIVGHVTKEGQIAGPRLLEHMVDTVLYFEGDEHHAYR 245
Cdd:cd01121 161 LVVIDSIQTVYSPELTSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVTKDGAIAGPKVLEHMVDTVLYFEGDRGSSYR 240
|
250 260
....*....|....*....|....*...
gi 613363400 246 ILRAVKNRFGSTNEMGIFEMKQSGLKGV 273
Cdd:cd01121 241 ILRSVKNRFGPTNEIGVFEMTENGLREV 268
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
69-265 |
5.93e-28 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 110.39 E-value: 5.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 69 RVLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQ-ICASLSQKKKVLYITGEESLSQTKLRAERL---------- 137
Cdd:COG0467 1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQfLAEGLRRGEKGLYVSFEESPEQLLRRAESLgldleeyies 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 138 ------DEDSSELQVLAETDLEVIYQTVKEEQPDLLVVDSIQTIYhpeisSAPGSVSQVRESTQSLMNIAKQMNIATFIV 211
Cdd:COG0467 81 gllriiDLSPEELGLDLEELLARLREAVEEFGAKRVVIDSLSGLL-----LALPDPERLREFLHRLLRYLKKRGVTTLLT 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613363400 212 GHVTKEGQIAGPRLLEHMVDTVLYFEGDEHHA--YRILRAVKNRfGSTNEMGIFEM 265
Cdd:COG0467 156 SETGGLEDEATEGGLSYLADGVILLRYVELGGelRRALSVLKMR-GSAHDRTIREF 210
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
85-255 |
4.10e-20 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 90.73 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 85 IVSGSLVLIGGDPGIGKSTLLLQICASLS----------QKKKVLYITGEESLSQTKLR---------------AERLDE 139
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAaggpwlgrrvPPGKVLYLAAEDDRGELRRRlkalgadlglpfadlDGRLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 140 DSSELQVLAETDLEVIYQTVKEEQPDLLVVDSIQTIYHPEISSApgsvSQVRESTQSLMNIAKQMNIATFIVGHVTKEGQ 219
Cdd:COG3598 90 LSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLARVFGGDENDA----EEMRAFLNPLDRLAERTGAAVLLVHHTGKGGA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 613363400 220 IAGPRL-------LEHMVDTVLYFEGDEHHAYRILRAVKNRFG 255
Cdd:COG3598 166 GKDSGDrargssaLRGAARSVLVLSREKGEDLRVLTRAKSNYG 208
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
77-266 |
3.75e-19 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 77 FNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQ-ICASLSQKKKVLYITGEESLSQTKLRAERL--DEDSSEL--------Q 145
Cdd:cd01124 8 LDELLGGGIPKGSVTLLTGGPGTGKTLFGLQfLYAGAKNGEPGLFFTFEESPERLLRNAKSFgwDFDEMEDegkliivdA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 146 VLAETD-------LEVIYQTVKEEQPDLLVVDSIQTIYhpEISSAPgsvSQVRESTQSLMNIAKQMNIATFIVG--HVTK 216
Cdd:cd01124 88 PPTEAGrfsldelLSRILSIIKSFKAKRVVIDSLSGLR--RAKEDQ---MRARRIVIALLNELRAAGVTTIFTSemRSFL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613363400 217 EGQIAGPRLLEHMVDTV--LYFEGDEHHAYRILRAVKNRFGStNEMGIFEMK 266
Cdd:cd01124 163 SSESAGGGDVSFIVDGVilLRYVEIEGELRRTIRVLKMRGTG-HDTGTHPFE 213
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
80-219 |
3.57e-14 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 70.87 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 80 VLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQKK------------KVLYITGEESLSQTKLRAE------------ 135
Cdd:pfam13481 25 LIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKpwlggprvpeqgKVLYVSAEGPADELRRRLRaagadldlparl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 136 ---------RLDEDSSELQVLAEtDLEVIYQTVKE-EQPDLLVVDSIQTIYHPEISSApgsvSQVRESTQSLMNIAKQMN 205
Cdd:pfam13481 105 lflslveslPLFFLDRGGPLLDA-DVDALEAALEEvEDPDLVVIDPLARALGGDENSN----SDVGRLVKALDRLARRTG 179
|
170
....*....|....
gi 613363400 206 IATFIVGHVTKEGQ 219
Cdd:pfam13481 180 ATVLLVHHVGKDGA 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
87-237 |
6.80e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.86 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 87 SGSLVLIGGDPGIGKSTLLLQICASLSQK-KKVLYITGEESLSQTKLRAERLDEDSSELQVLAETDLEVIYQTVKEEQPD 165
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613363400 166 LLVVDSIQTIYHPEISSApgsvSQVRESTQSLMNIAKQMNIATFIVGHVTKegqIAGPRLLEHMVDTVLYFE 237
Cdd:smart00382 81 VLILDEITSLLDAEQEAL----LLLLEELRLLLLLKSEKNLTVILTTNDEK---DLGPALLRRRFDRRIVLL 145
|
|
| Rubredoxin_2 |
pfam18073 |
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ... |
8-35 |
1.19e-12 |
|
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found in Interest in lipopolysaccharide (LPS) assembly protein B (LapB). Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo. Other family members include RadA proteins which play a role in DNA damage repair. In E. coli, a protein known as RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain.
Pssm-ID: 436248 [Multi-domain] Cd Length: 28 Bit Score: 61.79 E-value: 1.19e-12
10 20
....*....|....*....|....*...
gi 613363400 8 FECMACGYQSPKWMGKCPNCGAWNQMEE 35
Cdd:pfam18073 1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
70-214 |
1.57e-12 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 66.57 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 70 VLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQI-CASLSQKKKVLYITgEESLSQTKLRA---ERLDEDSSELQ 145
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLaVEAAKQGKKVVYID-TEGLSPERFQQiagERFESIASNII 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613363400 146 VLAETDLE-------VIYQTVKEEQPDLLVVDSIQTIYHPEISSAPGSVSQVRESTQSLMNIAKQMNIATFIVGHV 214
Cdd:cd01394 80 VFEPYSFDeqgvaiqEAEKLLKSDKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLSIARKYDIPVVITNQV 155
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
77-271 |
2.52e-11 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 63.42 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 77 FNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQ--ICASLSQKKKVLYITGEESLSQTKLRAERLD------EDSSELQVL- 147
Cdd:pfam06745 8 LDEILKGGFPEGRVVLITGGPGTGKTIFGLQflYNGALKYGEPGVFVTLEEPPEDLRENARSFGwdleklEEEGKLAIId 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 148 AETD----------------LEVIYQTVKEEQPDLLVVDSIQTIYHPEissapgSVSQVRESTQSLMNIAKQMNIATFIV 211
Cdd:pfam06745 88 ASTSgigiaevedrfdleelIERLREAIREIGAKRVVIDSITTLFYLL------KPAVAREILRRLKRVLKGLGVTAIFT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363400 212 GHVTK-EGQIAGPRLLEHMVDTV--LYFEGDEHHAYRILRAVKNRfGSTNEMG--IFEMKQSGLK 271
Cdd:pfam06745 162 SEKPSgEGGIGGYGVEEFIVDGVirLDLKEIEEERVRTIEIVKMR-GTPHSMKryPFEITDNGIV 225
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
76-271 |
2.53e-10 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 60.01 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 76 EFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQ-ICASLSQKKKVLYITGEESLSQTKLRAERLD------EDSSELQVLA 148
Cdd:cd19487 7 ELDELLGGGLERGTSTLLIGPAGVGKSTLALQfAKAAAARGERSVLFSFDESIGTLFERSEALGidlramVEKGLLSIEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 149 ETDLEV--------IYQTVKEEQPDLLVVDSIqTIYhpeISSAPGSVSQVREsTQSLMNIAKQMNIATFIVG--HVTKEG 218
Cdd:cd19487 87 IDPAELspgefaqrVRTSVEQEDARVVVIDSL-NGY---LNAMPDERFLILQ-MHELLSYLNNQGVTTLLIVaqHGLLGG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613363400 219 QIAGPRLLEHMVDTVL---YFEgdehHAYRILRA---VKNRFGsTNEMGI--FEMKQSGLK 271
Cdd:cd19487 162 DMGTPVDISYLADTVVllrYFE----AEGEVRKAisvLKKRTG-DHERTIreFRITRSGLK 217
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
69-209 |
4.69e-10 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 61.43 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 69 RVLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQ-ICASLSQKKKVLYITGEESLSQTkLRAER---LD----ED 140
Cdd:PRK09302 254 RISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLASKfAEAACRRGERCLLFAFEESRAQL-IRNARswgIDlekmEE 332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613363400 141 SSELQVLA--------ETDLEVIYQTVKEEQPDLLVVDSIQTIYhpeissAPGSVSQVRESTQSLMNIAKQMNIATF 209
Cdd:PRK09302 333 KGLLKIICarpesyglEDHLIIIKREIEEFKPSRVAIDPLSALA------RGGSLNEFRQFVIRLTDYLKSEEITGL 403
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
69-214 |
1.18e-09 |
|
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.
Pssm-ID: 462471 [Multi-domain] Cd Length: 255 Bit Score: 58.85 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 69 RVLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICAS----LSQ---KKKVLYITGEESLSQTKLR--AERLDE 139
Cdd:pfam08423 18 QITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTcqlpLEMgggEGKALYIDTEGTFRPERLVaiAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 140 DSSElqVL----------AETDLEVIYQ---TVKEEQPDLLVVDSIQTIYHPEISSApGSVS----QVRESTQSLMNIAK 202
Cdd:pfam08423 98 DPED--VLdnvayaraynSEHQMQLLQQaaaMMSESRFALLIVDSATALYRTDFSGR-GELAerqqHLAKFLRTLQRLAD 174
|
170
....*....|..
gi 613363400 203 QMNIATFIVGHV 214
Cdd:pfam08423 175 EFGVAVVITNQV 186
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
81-274 |
1.52e-09 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 57.95 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 81 LGGGIVSGSLVLIGGDPGIGKSTLLLQI-CASLSQKKKVLYI-TgeESLSQTKLRA---ERLDEDSSELQVLAETDLEVI 155
Cdd:PRK09361 16 LGGGFERGTITQIYGPPGSGKTNICLQLaVEAAKNGKKVIYIdT--EGLSPERFKQiagEDFEELLSNIIIFEPSSFEEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 156 YQTVKEEQP------DLLVVDSIQTIYHPEISSAPGSVSQVREST---QSLMNIAKQMNIATFIVGHV---TKEGQI--A 221
Cdd:PRK09361 94 SEAIRKAEKlakenvGLIVLDSATSLYRLELEDEEDNSKLNRELGrqlTHLLKLARKHDLAVVITNQVysdIDSDGLrpL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613363400 222 GPRLLEHMVDTVLYFEGDEhHAYRILRAVKNRFGSTNEMGIFEMKQSGLKGVN 274
Cdd:PRK09361 174 GGHTLEHWSKTILRLEKFR-NGKRRATLEKHRSRPEGESAEFRITDRGIEIID 225
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
88-215 |
1.76e-09 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 56.98 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 88 GSLVLIGGDPGIGKSTLLLQICA-SLSQKKKVLYITGE---------ESLSQTKLRAERLDEDSSELQVLAETD----LE 153
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAAnALLLGGGVVWIDTEgafppsrlvQILEASPSSELELAEALSRLLYFRPPDtlahLL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613363400 154 VIYQTVKEEQP----DLLVVDSIQTIYHPEISSAPGSVSQVREST-------QSLMNIAKQMNIATFIVGHVT 215
Cdd:cd01393 81 ALDSLPESLFPppntSLVVVDSVSALFRKAFPRGGDGDSSSSLRArllsqlaRALQKLAAQFNLAVVVTNQVT 153
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
72-124 |
2.49e-09 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 57.53 E-value: 2.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 613363400 72 TDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQIC-ASLSQKKKVLYITGE 124
Cdd:COG2874 5 TGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAyGALENGLSVTYISTE 58
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
72-176 |
2.86e-09 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 57.29 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 72 TDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQIC-ASLSQKKKVLYITGEES----LSQTK--------------- 131
Cdd:PRK06067 9 TGNEELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFVyGALKQGKKVYVITTENTsksyLKQMEsvkidisdfflwgyl 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 613363400 132 ----LRAERLDEDSSELQVLaetdLEVIYQTVKEEQPDLLVVDS--IQTIY 176
Cdd:PRK06067 89 rifpLNTEGFEWNSTLANKL----LELIIEFIKSKREDVIIIDSltIFATY 135
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
70-172 |
3.03e-09 |
|
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410896 [Multi-domain] Cd Length: 225 Bit Score: 56.97 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 70 VLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQ-ICASLSQKKKVLYITGEESLSQTKLRAER----LD------ 138
Cdd:cd19488 1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQfLLEGAANGETGLYITLSETEQELRAVALShgwsLDgihife 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 613363400 139 --------EDSSELQVLAETDLEV------IYQTVKEEQPDLLVVDSI 172
Cdd:cd19488 81 lspsesalDAAQQYTILHPSELELsettrlIFERVERLKPSRVVIDSL 128
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
78-252 |
4.62e-09 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 56.56 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 78 NRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQKKK-------VLYITGEESLSQTKLRA---------------- 134
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARkggldggVLYIDTESKFSAERLAEiaearfpeafsgfmee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 135 -ERLDEDSSELQVLAETDLEVIYQTVKEEQPD-------LLVVDSIQTIYHPEISSAPGSVSQVRESTQSLMNIAKQM-- 204
Cdd:cd19493 81 nERAEEMLKRVAVVRVTTLAQLLERLPNLEEHilssgvrLVVIDSIAALVRREFGGSDGEVTERHNALAREASSLKRLae 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 205 ---------NIATFIVGHVTKEGQIAGPRL---LEHMVDTVLYFEGDEHHAYRILRAVKN 252
Cdd:cd19493 161 efriavlvtNQATTHFGDAGDGSSGVTAALgdaWAHAVNTRLRLERCLLQLRRVLEIVKS 220
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
72-209 |
5.99e-09 |
|
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410892 [Multi-domain] Cd Length: 218 Bit Score: 56.18 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 72 TDSAEFNRVL-GGGIVSGSLVLIGGDPGIGKSTLLLQ-ICASLSQKKKVLYITGEESLSQT--KLRAERLD----EDSSE 143
Cdd:cd19484 3 TGIPRLDAMLgGGGFFRGSSILVSGATGTGKTLLAASfADAACRRGERCLYFAFEESPAQLirNAKSIGIDleqmERKGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613363400 144 LQVLA----ETDLEVIYQTVKEE----QPDLLVVDSIQTIyhpeisSAPGSVSQVRESTQSLMNIAKQMNIATF 209
Cdd:cd19484 83 LKIICarpeLYGLEDHLIIIKSEinefKPSRVIVDPLSAL------ARGGSLNEVKEFVIRLIDYLKSQEITGL 150
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
72-239 |
1.55e-08 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 55.23 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 72 TDSAEFNRVLGGGIVSGSLVLIGGDPGIGKStlllQICASLS-----------QKKKVLYITGEESLSQTKLR--AER-- 136
Cdd:cd01123 3 TGSKELDKLLGGGIETGSITEMFGEFRTGKT----QLCHTLAvtcqlpidrggGEGKAIYIDTEGTFRPERLRaiAQRfg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 137 LDEDSSELQVL------AETDLEVIYQT---VKEEQPDLLVVDSIQTIYHPEISSApGSVS----QVRESTQSLMNIAKQ 203
Cdd:cd01123 79 LDPDDVLDNVAyarafnSDHQTQLLDQAaamMVESRFKLLIVDSATALYRTDYSGR-GELSarqmHLAKFLRMLQRLADE 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 613363400 204 MNIATFIVGHVTKEgqiagprllehmVDTVLYFEGD 239
Cdd:cd01123 158 FGVAVVVTNQVVAQ------------VDGAMMFAAD 181
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
79-215 |
2.84e-08 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 54.61 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 79 RVLGGGIVSGSLVLIGGDPGIGKSTLLLQIC--ASLS-----QKKKVLYITGEESLSQTKLRA-----ERLDEDSSELQV 146
Cdd:cd19491 3 ELLGGGIPVGGITEIAGESGAGKTQLCLQLAltVQLPrelggLGGGAVYICTESSFPSKRLQQlasslPKRYHLEKAKNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 147 L----------AETDLEVIYQTVK---EEQP-DLLVVDSIQTIYHPEI-SSAPGSVSQVRESTQ---SLMNIAKQMNIAT 208
Cdd:cd19491 83 LdnifvehvadLETLEHCLNYQLPallERGPiRLVVIDSIAALFRSEFdTSRSDLVERAKYLRRladHLKRLADKYNLAV 162
|
....*..
gi 613363400 209 FIVGHVT 215
Cdd:cd19491 163 VVVNQVT 169
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
83-206 |
4.82e-08 |
|
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 410864 [Multi-domain] Cd Length: 256 Bit Score: 54.06 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 83 GGIVSGSLVLIGGDPGIGKSTLLLQIC--ASLSQKKKVLYITGEES--------------LSQTKLRAERL-DEDSSELQ 145
Cdd:cd00984 14 GGLQPGDLIIIAARPSMGKTAFALNIAenIALDEGLPVLFFSLEMSaeqlaerllssesgVSLSKLRTGRLdDEDWERLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 146 ----VLAETDL-----------EVIYQT--VKEEQP--DLLVVDSIQTIYHPEISSapGSVSQVRESTQSLMNIAKQMNI 206
Cdd:cd00984 94 aamgELSELPLyiddtpgltvdEIRAKArrLKREHGglGLIVIDYLQLIRGSKRAE--NRQQEVAEISRSLKALAKELNV 171
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
91-217 |
6.35e-08 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 50.96 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 91 VLIGGDPGIGKSTLLLQICA-SLSQKKKVLYITgeeslsqtklraerldedsselqvLAETDLEVIYQTVKEEQPDLLVV 169
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEqALLSDEPVIFIS------------------------FLDTILEAIEDLIEEKKLDIIII 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 613363400 170 DSIQTIYHPEIssaPGSVSQVRESTQSLMNIAKQMNIATFIVGHVTKE 217
Cdd:cd01120 57 DSLSSLARASQ---GDRSSELLEDLAKLLRAARNTGITVIATIHSDKF 101
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
69-214 |
8.97e-08 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 53.85 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 69 RVLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQIC--ASLSQKK-----KVLYITGEESLSQTKLR--AERLDE 139
Cdd:PTZ00035 99 RITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCvtCQLPIEQgggegKVLYIDTEGTFRPERIVqiAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 140 DSSElqVLA----------ETDLEVIYQTVK---EEQPDLLVVDSIQTIYHPEISSApGSVSQvREST-----QSLMNIA 201
Cdd:PTZ00035 179 DPED--VLDniayaraynhEHQMQLLSQAAAkmaEERFALLIVDSATALFRVDYSGR-GELAE-RQQHlgkflRALQKLA 254
|
170
....*....|...
gi 613363400 202 KQMNIATFIVGHV 214
Cdd:PTZ00035 255 DEFNVAVVITNQV 267
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
77-263 |
1.92e-06 |
|
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410893 [Multi-domain] Cd Length: 226 Bit Score: 48.90 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 77 FNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQK--KKVLYITGEES------------------LSQTKLRAER 136
Cdd:cd19485 8 FDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEfgEPGVFVTFEESpediiknmasfgwdlpklVAEGKLLILD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 137 LDEDSSELQVLAETDLEV----IYQTVKEEQPDLLVVDSIQTIYHpEISSApgsvSQVRESTQSLMNIAKQMNIATFIVG 212
Cdd:cd19485 88 ASPEPSEEEVTGEYDLEAllirIEYAIRKIGAKRVSLDSLEAVFS-GLSDS----AVVRAELLRLFAWLKQKGVTAIMTG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613363400 213 HVTKEGQIAGPRLLEHMVDTV--LYFEGDEHHAYRILRAVKNRfGSTNEMGIF 263
Cdd:cd19485 163 ERGEDGPLTRYGVEEYVSDCVviLRNVLEGERRRRTLEILKYR-GSSHGKGEY 214
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
72-215 |
5.07e-06 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 47.74 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 72 TDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQIC--ASLSQKK-----KVLYITGEESLSQTKLR--AER--LDED 140
Cdd:cd19514 3 TGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCvtAQLPGSMgggggKVAYIDTEGTFRPDRIRpiAERfgVDHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 141 ------------SSELQVlaETDLEVIYQTVKEEQPDLLVVDSIQTIYHPEISSApGSVSQvRESTQS-----LMNIAKQ 203
Cdd:cd19514 83 avldnilyarayTSEHQM--ELLDYVAAKFHEEAVFRLLIIDSIMALFRVDFSGR-GELAE-RQQKLAqmlsrLQKISEE 158
|
170
....*....|..
gi 613363400 204 MNIATFIVGHVT 215
Cdd:cd19514 159 YNVAVFITNQVT 170
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
48-215 |
6.21e-06 |
|
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.
Pssm-ID: 131292 [Multi-domain] Cd Length: 313 Bit Score: 47.85 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 48 KTKELAGKVQKLN-------SIKHETTPRVLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQKK---- 116
Cdd:TIGR02238 49 KIKEAASKIINPGfitafeiSQKRKKVLKITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPRemgg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 117 ---KVLYITGEESLSQTKLR--AER--LDEDSSELQVL------AETDLEVIYQT---VKEEQPDLLVVDSIQTIYHPEI 180
Cdd:TIGR02238 129 gngKVAYIDTEGTFRPDRIRaiAERfgVDPDAVLDNILyaraytSEHQMELLDYLaakFSEEPFRLLIVDSIMALFRVDF 208
|
170 180 190
....*....|....*....|....*....|....*....
gi 613363400 181 SSApGSVSQVRESTQSLMN----IAKQMNIATFIVGHVT 215
Cdd:TIGR02238 209 SGR-GELSERQQKLAQMLSrlnkISEEFNVAVFVTNQVQ 246
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
88-219 |
9.63e-06 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 46.61 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 88 GSLVLIGGDPGIGKSTLLLQICASLS-----------QKKKVLYITGEESLS---------------QTKLRAERLDEDS 141
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVAtgrdwlgerrvKQGRVVYLAAEDPRDglrrrlkaigahlgdEDAALAENLVIEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 142 -SELQVLAETDLEVIYQTVKEEQP-DLLVVDSIQTIYH--PEISSAP-GSVSQVREStqslmnIAKQMNIATFIVGHVTK 216
Cdd:cd01125 81 lRGKPVSIDAEAPELERIIEELEGvRLIIIDTLARVLHggDENDAADmGAFVAGLDR------IARETGAAVLLVHHTGK 154
|
...
gi 613363400 217 EGQ 219
Cdd:cd01125 155 DAA 157
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
390-450 |
1.42e-05 |
|
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440371 [Multi-domain] Cd Length: 502 Bit Score: 47.34 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613363400 390 IGEVGLTGEVRRVSRIEQRVQEAAKLGFKRVIIPKNNIGGWTYPEGIQVIGVTTVHEALSF 450
Cdd:COG0606 106 LGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLLEVVAF 166
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
364-426 |
1.64e-05 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 43.98 E-value: 1.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613363400 364 PAVDLSVIVATASSFKDKAVDGLDCYIGEVGLTGEVRRVSRIEQRVQEAAKLGFKRVIIPKNN 426
Cdd:pfam13541 59 SSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| PRK05973 |
PRK05973 |
replicative DNA helicase; Provisional |
85-191 |
2.66e-05 |
|
replicative DNA helicase; Provisional
Pssm-ID: 168322 [Multi-domain] Cd Length: 237 Bit Score: 45.41 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 85 IVSGSLVLIGGDPGIGKSTLLLQIC-ASLSQKKKVLYITGEESLSQTKLRAERLDEDSSELQVLAETDLE-------VIY 156
Cdd:PRK05973 61 LKPGDLVLLGARPGHGKTLLGLELAvEAMKSGRTGVFFTLEYTEQDVRDRLRALGADRAQFADLFEFDTSdaicadyIIA 140
|
90 100 110
....*....|....*....|....*....|....*....
gi 613363400 157 QTVKEEQPDLLVVDSIQTI----YHPEISsapgsvSQVR 191
Cdd:PRK05973 141 RLASAPRGTLVVIDYLQLLdqrrEKPDLS------VQVR 173
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
88-215 |
3.11e-05 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 44.14 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 88 GSLVLIGGDPGIGKSTLLLQICASLSQKK-------KVLYITGEESLSQTKLRAERLDEDSSELQVLaetdleviyQTVK 160
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIPKcfgglagEAIYIDTEGSFNIHYFRVHDYVELLALINSL---------PKFL 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 613363400 161 EEQPD--LLVVDSI-QTIYHpEISSAPGSVSQVRESTQSLMNIAKQMNIATFIVGHVT 215
Cdd:cd19492 72 EDHPKvkLIVVDSIaFPFRH-DFDDLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVT 128
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
91-266 |
3.73e-05 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410891 [Multi-domain] Cd Length: 231 Bit Score: 44.87 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 91 VLIGGDPGIGKSTLLLQICASL--SQKKKVLYITGEESLSQT-------------KLRAERLDEDSSELQVLAETD---- 151
Cdd:cd19483 1 VTIGAGSGIGKSTIVRELAYHLitEHGEKVGIISLEESVEETakglagkhlgkpePLELPRDDITEEEEDDAFDNElgsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 152 ----------------LEVIYQTVKEEQPDLLVVDSIQTIyhpeisSAPGSVSQVRESTQSLM----NIAKQMNIATFIV 211
Cdd:cd19483 81 rfflydhfgsldwdnlKEKIRYMVKVLGCKVIVLDHLTIL------VSGLDSSDERKELDEIMtelaALVKELGVTIILV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613363400 212 GHVTK--------------EGQIAGPRLLEHMVDTVLYFEGDEHHAYRI------LRAVKNR-FGSTNEMGIFEMK 266
Cdd:cd19483 155 SHLRRpgggkgheeggevsESDLRGSSAIAQLSDYVIGLERNKQADDPVernttrVRVLKNRfTGETGIAGTLYYD 230
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
50-206 |
5.07e-05 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 45.45 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 50 KELAGKVQKLNSIKHETTpRVLTDSAEFNRVLGGgIVSGSLVLIGGDPGIGKSTLLLQIC--ASLSQKKKVLYITGE--- 124
Cdd:COG0305 155 KEALERIEELYKNGGGIT-GVPTGFTDLDKLTGG-LQPGDLIILAARPSMGKTAFALNIArnAAIKEGKPVAIFSLEmsa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 125 ESL-----------SQTKLRAERLDED-----SSELQVLAETDLeVIYQT---------------VKEEQPDLLVVDSIQ 173
Cdd:COG0305 233 EQLvmrllsseariDSSKLRTGKLSDEdwerlSSAAGELSEAPI-YIDDTpgltiaeirakarrlKREHGLGLIVIDYLQ 311
|
170 180 190
....*....|....*....|....*....|....
gi 613363400 174 TIyhpEISSAPGS-VSQVRESTQSLMNIAKQMNI 206
Cdd:COG0305 312 LM---SGSGRSENrQQEISEISRSLKALAKELNV 342
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
82-243 |
8.73e-05 |
|
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410897 [Multi-domain] Cd Length: 209 Bit Score: 43.39 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 82 GGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQKK--KVLYI-TG--------EESLSQTKLRAERLDEDSSELQVLAET 150
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSgqNVLYIdTKssfsarrlAQILKSRAQDAEEIDKALQRIRVVRVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 151 D-------LEVIYQTVKEEQ------PDLLVVDSIQTIYHPEISSapgsvSQVRESTQSLMNIAKQMN-------IATFI 210
Cdd:cd19489 81 DpyelldlLEELRNTLSQQQenlysrLKLVIIDSLSALISPLLGG-----SKHSEGHALLASLARLLKklaaeyqIAVLV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613363400 211 VGHVTKEGQIAGPRLL--------EHMVDTVLYFEGDEHHA 243
Cdd:cd19489 156 TNLTVRGGDGGQQGSTkpalgeywESVPSTRLLLSRDENDP 196
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
70-215 |
1.01e-04 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 44.33 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 70 VLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKStlllQICASL--------SQK---KKVLYITGEESLSQTKLR--AER 136
Cdd:TIGR02239 78 LTTGSKELDKLLGGGIETGSITEIFGEFRTGKT----QLCHTLavtcqlpiDQGggeGKALYIDTEGTFRPERLLaiAER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 137 LDEDSSElqVL----------AETDLEVIYQT---VKEEQPDLLVVDSIQTIYHPEISSApGSVSqVRES-----TQSLM 198
Cdd:TIGR02239 154 YGLNPED--VLdnvayaraynTDHQLQLLQQAaamMSESRFALLIVDSATALYRTDFSGR-GELS-ARQMhlarfLRSLQ 229
|
170
....*....|....*..
gi 613363400 199 NIAKQMNIATFIVGHVT 215
Cdd:TIGR02239 230 RLADEFGVAVVITNQVV 246
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
72-215 |
1.67e-04 |
|
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.
Pssm-ID: 410921 [Multi-domain] Cd Length: 235 Bit Score: 43.08 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 72 TDSAEFNRVLGGGIVSGSLVLIGGDPGIGKStlllQICASLS---Q--------KKKVLYITGEESLSQTKLR--AERLD 138
Cdd:cd19513 3 TGSKELDKLLGGGIETGSITELFGEFRTGKT----QLCHTLAvtcQlpidqgggEGKALYIDTEGTFRPERLLaiAERYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 139 EDSSElqVL----------AETDLEVIYQ---TVKEEQPDLLVVDSIQTIYHPEISSApGSVSQvRES-----TQSLMNI 200
Cdd:cd19513 79 LNGED--VLdnvayaraynTDHQMQLLIQasaMMAESRYALLIVDSATALYRTDYSGR-GELSA-RQMhlakfLRMLQRL 154
|
170
....*....|....*
gi 613363400 201 AKQMNIATFIVGHVT 215
Cdd:cd19513 155 ADEFGVAVVITNQVV 169
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
77-166 |
2.28e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 41.72 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 77 FNRVLGGgivSGSLVLIGGDPGIGKSTLLLQICASLSqKKKVLYITGE-----------ESLSQTKLRAERLDEDSSELQ 145
Cdd:pfam13191 16 LDRVRSG---RPPSVLLTGEAGTGKTTLLRELLRALE-RDGGYFLRGKcdenlpyspllEALTREGLLRQLLDELESSLL 91
|
90 100
....*....|....*....|.
gi 613363400 146 VLAETDLEVIYQTVKEEQPDL 166
Cdd:pfam13191 92 EAWRAALLEALAPVPELPGDL 112
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
91-176 |
2.42e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.36 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 91 VLIGGDPGIGKSTLLLQICASLS-QKKKVLYITGEESLSQTKLRAERLDEDSSELQVLAEtdleviyqtvkEEQPDLLVV 169
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAE-----------KAKPGVLFI 90
|
....*..
gi 613363400 170 DSIQTIY 176
Cdd:cd00009 91 DEIDSLS 97
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
75-114 |
2.93e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 2.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 613363400 75 AEFNRVLGGgivSGSLVLIGGDPGIGKSTLLLQICASLSQ 114
Cdd:COG3899 301 AALERARAG---RGELVLVSGEAGIGKSRLVRELARRARA 337
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
90-183 |
3.00e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 40.65 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 90 LVLIGgdP-GIGKSTLLLQICASLSQKKKVLYITGEEslsqtklraerldedsSELQVLAETDLEVIYQTVKEEQPDLLV 168
Cdd:pfam13173 5 LVITG--PrQVGKTTLLLQLIKELLPPENILYINLDD----------------PRLLKLADFELLELFLELLYPGKTYLF 66
|
90
....*....|....*
gi 613363400 169 VDSIQtiYHPEISSA 183
Cdd:pfam13173 67 LDEIQ--RVPDWELA 79
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
91-182 |
4.14e-04 |
|
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.
Pssm-ID: 396860 Cd Length: 179 Bit Score: 41.08 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 91 VLIGGDPGIGKSTLLLQICASLSQKKKVLYITGEesLSQTKLRAERLDEDSSELQVLAE--------TDLEV-IYQTV-K 160
Cdd:pfam02492 3 TVITGFLGSGKTTLLNHLLKQNRAGLRIAVIVNE--FGETGIDAELLSETGVLIVELSNgcicctirEDLSMaLEALLeR 80
|
90 100 110
....*....|....*....|....*....|.
gi 613363400 161 EEQPDLLVVDS---------IQTIYHPEISS 182
Cdd:pfam02492 81 EGRLDVIFIETtglaepapvAQTFLSPELRS 111
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
97-170 |
1.81e-03 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 40.78 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 97 PGIGKSTLLLQICASLSQKKKVLYIT-GEESLSQTKLRAERLDEDSSELQVLAETDLEVI---YQTVK--------EEQP 164
Cdd:COG1061 109 TGTGKTVLALALAAELLRGKRVLVLVpRRELLEQWAEELRRFLGDPLAGGGKKDSDAPITvatYQSLArrahldelGDRF 188
|
....*.
gi 613363400 165 DLLVVD 170
Cdd:COG1061 189 GLVIID 194
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
67-116 |
2.50e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 40.56 E-value: 2.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 613363400 67 TPRVLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICASLSQKK 116
Cdd:COG5635 159 VPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERY 208
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
90-183 |
3.10e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 39.54 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 90 LVLIGgdP-GIGKSTLLLQICASLsqkKKVLYITgeeslsqtklraerLDEDssELQVLAETDLEVIYQTVKE--EQPDL 166
Cdd:COG1373 23 VVITG--PrQVGKTTLLKQLAKEL---ENILYIN--------------LDDP--RLRALAEEDPDDLLEALKElyPGKTY 81
|
90
....*....|....*..
gi 613363400 167 LVVDSIQTIyhPEISSA 183
Cdd:COG1373 82 LFLDEIQRV--PEWEDA 96
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
81-171 |
3.24e-03 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 39.38 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 81 LG-GGIVSGSLVLIGGDPGIGKSTLLLQICASLsQKK--KVLYITGEESLSQTklRAERLDEDSSELQVL----AETDLE 153
Cdd:COG0468 55 LGvGGLPRGRIVEIYGPESSGKTTLALHAIAEA-QKAggIAAFIDAEHALDPE--YAKKLGVDIDNLLVSqpdtGEQALE 131
|
90
....*....|....*...
gi 613363400 154 VIYQTVKEEQPDLLVVDS 171
Cdd:COG0468 132 IAETLVRSGAVDLIVVDS 149
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
70-225 |
4.40e-03 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 38.95 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 70 VLTDSAEFNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICAS----LSQ---KKKVLYITGE-----ESLSQTklrAERL 137
Cdd:PLN03186 105 ITTGSRELDKILEGGIETGSITEIYGEFRTGKTQLCHTLCVTcqlpLDQgggEGKAMYIDTEgtfrpQRLIQI---AERF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363400 138 DEDSSElqVLAETDLEVIYQTvkEEQPDLL---------------VVDSIQTIYHPEISSApGSVS----QVRESTQSLM 198
Cdd:PLN03186 182 GLNGAD--VLENVAYARAYNT--DHQSELLleaasmmaetrfalmIVDSATALYRTEFSGR-GELSarqmHLGKFLRSLQ 256
|
170 180 190
....*....|....*....|....*....|.
gi 613363400 199 NIAKQMNIATFI----VGHVTKEGQIAGPRL 225
Cdd:PLN03186 257 RLADEFGVAVVItnqvVAQVDGSAFFAGPQL 287
|
|
| 41 |
PHA02542 |
41 helicase; Provisional |
77-138 |
5.19e-03 |
|
41 helicase; Provisional
Pssm-ID: 222864 [Multi-domain] Cd Length: 473 Bit Score: 39.27 E-value: 5.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613363400 77 FNRVLGGGIVSGSLVLIGGDPGIGKSTLLLQICAS-LSQKKKVLYITGEesLSQTKLrAERLD 138
Cdd:PHA02542 179 LNKITKGGAERKTLNVLLAGVNVGKSLGLCSLAADyLQQGYNVLYISME--MAEEVI-AKRID 238
|
|
| PRK08533 |
PRK08533 |
flagellar accessory protein FlaH; Reviewed |
76-104 |
8.93e-03 |
|
flagellar accessory protein FlaH; Reviewed
Pssm-ID: 181459 Cd Length: 230 Bit Score: 37.74 E-value: 8.93e-03
10 20
....*....|....*....|....*....
gi 613363400 76 EFNRVLGGGIVSGSLVLIGGDPGIGKSTL 104
Cdd:PRK08533 12 ELHKRLGGGIPAGSLILIEGDESTGKSIL 40
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| COG2888 |
COG2888 |
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ... |
4-29 |
9.98e-03 |
|
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];
Pssm-ID: 442134 [Multi-domain] Cd Length: 52 Bit Score: 34.32 E-value: 9.98e-03
10 20
....*....|....*....|....*.
gi 613363400 4 KKVIFECMACGYQSPKWmGKCPNCGA 29
Cdd:COG2888 25 EALIIRCPKCRKQSNAL-YFCPKCGF 49
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