|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
6-513 |
0e+00 |
|
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: 724.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 6 AWSICLVGMQARPVRVEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSGYDLAM 85
Cdd:COG0606 5 VYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFDLPI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 86 AVSVLAAMGVISRSRAGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKTKILVPQANLAEASLVPGVDVVGVHHLGQVI 165
Cdd:COG0606 85 ALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLLEVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 166 ELLGGDLMMPLPPPeepaeaaegdTTPAPACSLGGDFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTMLASRLPGI 245
Cdd:COG0606 165 AFLRGEQPLPPAEP----------DAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 246 LPPLELDQSVEVTALHSLAGTLSPLDGLIRQPPFQAPHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAPEFGARVL 325
Cdd:COG0606 235 LPPLTEEEALEVTAIHSVAGLLPPDGGLIRRRPFRAPHHTASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFSRRVL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 326 DSLREPLENGEITLHRAAGAAQYPARFQLIMAANPCPCGNAGSRRATCTCTPYSRKRYLERLSGPLLDRMDIQIQVESPG 405
Cdd:COG0606 314 EALRQPLEDGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 406 RGSLAGAKPADTTTVVAARVQRARDVQRERWKGRGWDLNREIPGPFLRQ-----PEGgftRELIgrvDNVVEQGRLSMRG 480
Cdd:COG0606 394 YEELSSAPPGESSAEVRERVAAARERQLERFGGTGIRLNAQLPGRELRKycrldAEA---RALL---ERALERLGLSARA 467
|
490 500 510
....*....|....*....|....*....|...
gi 1839373875 481 AQRVLRLAWTVADLSGKTVPGLPELGTAMTLRR 513
Cdd:COG0606 468 YDRILRVARTIADLAGSERIEREHLAEALQYRR 500
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
7-512 |
5.61e-155 |
|
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]
Pssm-ID: 129465 [Multi-domain] Cd Length: 499 Bit Score: 451.61 E-value: 5.61e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 7 WSICLVGMQARPVRVEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSGYDLAMA 86
Cdd:TIGR00368 2 YSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 87 VSVLAAMGVISRSRAGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKTKILVPQANLAEASLVPGVDVVGVHHLGQVIE 166
Cdd:TIGR00368 82 IGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAEEASLIDGLNIYGADHLKEVVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 167 LLGGDLMMPLPPPEEPAEAaegDTTPAPACSlggDFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTMLASRLPGIL 246
Cdd:TIGR00368 162 FLEGSEKLPPRTNTKPKSI---INKSYIIDL---DLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 247 PPLELDQSVEVTALHSLAGTLSPLdGLIRQPPFQAPHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAPEFGARVLD 326
Cdd:TIGR00368 236 PPLTNEEAIETARIWSLVGKLIDR-KQIKQRPFRSPHHSASKPALVGGGP-IPLPGEISLAHNGVLFLDELPEFKRSVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 327 SLREPLENGEITLHRAAGAAQYPARFQLIMAANPCPCGNAGSRRATCTCTPYSRKRYLERLSGPLLDRMDIQIQVESPGR 406
Cdd:TIGR00368 314 ALREPIEDGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 407 GSLAGAKPADTTTVVAARVQRARDVQRERW-KGRGWDLNREIPGPFLRQ---PEGGFTRELIGRVDNVveqgRLSMRGAQ 482
Cdd:TIGR00368 394 EKLLSTGSGESSAEVKQRVIKAREIQNIRYeKFANINKNADLNSDEIEQfckLSAIDANDLEGALNKL----GLSSRATH 469
|
490 500 510
....*....|....*....|....*....|
gi 1839373875 483 RVLRLAWTVADLSGKTVPGLPELGTAMTLR 512
Cdd:TIGR00368 470 RILKVARTIADLKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
1-496 |
2.06e-124 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 373.55 E-value: 2.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 1 MSSGFAWSICLVGMQARPVRVEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSG 80
Cdd:PRK09862 1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 81 YDLAMAVSVLAAMGVISRSRAGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKtKILVPQANLAEASLVPGVDVVGVHH 160
Cdd:PRK09862 81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGR-KIIVAKDNEDEVGLINGEGCLIADH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 161 LGQVIELLGG--DLMMPLpppeepaeaAEGDTTPApacsLGGDFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTML 238
Cdd:PRK09862 160 LQAVCAFLEGkhALERPK---------PTDAVSRA----LQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTML 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 239 ASRLPGILPPLELDQSVEVTALHSLAGTLSpLDGLIRQPPFQAPHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAP 318
Cdd:PRK09862 227 ASRINGLLPDLSNEEALESAAILSLVNAES-VQKQWRQRPFRSPHHSASLTAMVGGGA-IPGPGEISLAHNGVLFLDELP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 319 EFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANPCPCGNAGSRRAtcTCTPYSRKRYLERLSGPLLDRMDIQ 398
Cdd:PRK09862 305 EFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHN--RCTPEQTLRYLNRLSGPFLDRFDLS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 399 IQVESPGRGSLA-GAKPADTTTVVAARVQRARDVQRERWKgrgwDLNREIPGPFLRQPEGGFTRELIGRVDNVVEQGrLS 477
Cdd:PRK09862 383 LEIPLPPPGILSkTVVPGESSATVKQRVMAARERQFKRQN----KLNAWLDSPEIRQFCKLESEDARWLEETLIHLG-LS 457
|
490
....*....|....*....
gi 1839373875 478 MRGAQRVLRLAWTVADLSG 496
Cdd:PRK09862 458 IRAWQRLLKVARTIADIDQ 476
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
201-409 |
1.25e-117 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 344.90 E-value: 1.25e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 201 DFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTMLASRLPGILPPLELDQSVEVTALHSLAGtLSPLDGLIRQPPFQ 280
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAG-LGGDGGLIRRRPFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 281 APHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANP 360
Cdd:pfam01078 80 APHHSASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1839373875 361 CPCGNAGSRRATCTCTPYSRKRYLERLSGPLLDRMDIQIQVESPGRGSL 409
Cdd:pfam01078 159 CPCGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
224-397 |
1.07e-06 |
|
MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).
Pssm-ID: 350658 [Multi-domain] Cd Length: 311 Bit Score: 50.42 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 224 HLLMIGTPGSGKTMLASRLPGILPpleldQSVEVTALHSLAGTLSpldglirqppfqaphhsATLAAMVGGGSGVPRPGA 303
Cdd:cd17706 43 HILLVGDPGTAKSQILKYVLKIAP-----RGVYTSGKGSSGAGLT-----------------AAVVRDSETGEWYLEAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 304 ASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANPcpcgnAGSRratctctpYSRKRY 383
Cdd:cd17706 101 LVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANP-----KGGR--------YNPKLS 167
|
170
....*....|....*..
gi 1839373875 384 L-ER--LSGPLLDRMDI 397
Cdd:cd17706 168 PiENinLPSPLLSRFDL 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
222-360 |
1.93e-04 |
|
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: 41.98 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 222 GHHLLMIGTPGSGKTMLASRLPGILPPLELDqSVEVTAlhslagtlsplDGLIRQPPFQAPHHSATLAAMVGGGSGVPRp 301
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG-VIYIDG-----------EDILEEVLDQLLLIIVGGKKASGSGELRLR- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839373875 302 GAASLAHR---GVLFLDEApefgARVLDSLREPLENGEITLhRAAGAAQYPARFQLIMAANP 360
Cdd:smart00382 69 LALALARKlkpDVLILDEI----TSLLDAEQEALLLLLEEL-RLLLLLKSEKNLTVILTTND 125
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
6-513 |
0e+00 |
|
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: 724.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 6 AWSICLVGMQARPVRVEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSGYDLAM 85
Cdd:COG0606 5 VYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFDLPI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 86 AVSVLAAMGVISRSRAGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKTKILVPQANLAEASLVPGVDVVGVHHLGQVI 165
Cdd:COG0606 85 ALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLLEVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 166 ELLGGDLMMPLPPPeepaeaaegdTTPAPACSLGGDFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTMLASRLPGI 245
Cdd:COG0606 165 AFLRGEQPLPPAEP----------DAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 246 LPPLELDQSVEVTALHSLAGTLSPLDGLIRQPPFQAPHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAPEFGARVL 325
Cdd:COG0606 235 LPPLTEEEALEVTAIHSVAGLLPPDGGLIRRRPFRAPHHTASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFSRRVL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 326 DSLREPLENGEITLHRAAGAAQYPARFQLIMAANPCPCGNAGSRRATCTCTPYSRKRYLERLSGPLLDRMDIQIQVESPG 405
Cdd:COG0606 314 EALRQPLEDGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 406 RGSLAGAKPADTTTVVAARVQRARDVQRERWKGRGWDLNREIPGPFLRQ-----PEGgftRELIgrvDNVVEQGRLSMRG 480
Cdd:COG0606 394 YEELSSAPPGESSAEVRERVAAARERQLERFGGTGIRLNAQLPGRELRKycrldAEA---RALL---ERALERLGLSARA 467
|
490 500 510
....*....|....*....|....*....|...
gi 1839373875 481 AQRVLRLAWTVADLSGKTVPGLPELGTAMTLRR 513
Cdd:COG0606 468 YDRILRVARTIADLAGSERIEREHLAEALQYRR 500
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
7-512 |
5.61e-155 |
|
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]
Pssm-ID: 129465 [Multi-domain] Cd Length: 499 Bit Score: 451.61 E-value: 5.61e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 7 WSICLVGMQARPVRVEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSGYDLAMA 86
Cdd:TIGR00368 2 YSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 87 VSVLAAMGVISRSRAGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKTKILVPQANLAEASLVPGVDVVGVHHLGQVIE 166
Cdd:TIGR00368 82 IGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAEEASLIDGLNIYGADHLKEVVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 167 LLGGDLMMPLPPPEEPAEAaegDTTPAPACSlggDFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTMLASRLPGIL 246
Cdd:TIGR00368 162 FLEGSEKLPPRTNTKPKSI---INKSYIIDL---DLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 247 PPLELDQSVEVTALHSLAGTLSPLdGLIRQPPFQAPHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAPEFGARVLD 326
Cdd:TIGR00368 236 PPLTNEEAIETARIWSLVGKLIDR-KQIKQRPFRSPHHSASKPALVGGGP-IPLPGEISLAHNGVLFLDELPEFKRSVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 327 SLREPLENGEITLHRAAGAAQYPARFQLIMAANPCPCGNAGSRRATCTCTPYSRKRYLERLSGPLLDRMDIQIQVESPGR 406
Cdd:TIGR00368 314 ALREPIEDGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 407 GSLAGAKPADTTTVVAARVQRARDVQRERW-KGRGWDLNREIPGPFLRQ---PEGGFTRELIGRVDNVveqgRLSMRGAQ 482
Cdd:TIGR00368 394 EKLLSTGSGESSAEVKQRVIKAREIQNIRYeKFANINKNADLNSDEIEQfckLSAIDANDLEGALNKL----GLSSRATH 469
|
490 500 510
....*....|....*....|....*....|
gi 1839373875 483 RVLRLAWTVADLSGKTVPGLPELGTAMTLR 512
Cdd:TIGR00368 470 RILKVARTIADLKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
1-496 |
2.06e-124 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 373.55 E-value: 2.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 1 MSSGFAWSICLVGMQARPVRVEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSG 80
Cdd:PRK09862 1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 81 YDLAMAVSVLAAMGVISRSRAGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKtKILVPQANLAEASLVPGVDVVGVHH 160
Cdd:PRK09862 81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGR-KIIVAKDNEDEVGLINGEGCLIADH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 161 LGQVIELLGG--DLMMPLpppeepaeaAEGDTTPApacsLGGDFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTML 238
Cdd:PRK09862 160 LQAVCAFLEGkhALERPK---------PTDAVSRA----LQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTML 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 239 ASRLPGILPPLELDQSVEVTALHSLAGTLSpLDGLIRQPPFQAPHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAP 318
Cdd:PRK09862 227 ASRINGLLPDLSNEEALESAAILSLVNAES-VQKQWRQRPFRSPHHSASLTAMVGGGA-IPGPGEISLAHNGVLFLDELP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 319 EFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANPCPCGNAGSRRAtcTCTPYSRKRYLERLSGPLLDRMDIQ 398
Cdd:PRK09862 305 EFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHN--RCTPEQTLRYLNRLSGPFLDRFDLS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 399 IQVESPGRGSLA-GAKPADTTTVVAARVQRARDVQRERWKgrgwDLNREIPGPFLRQPEGGFTRELIGRVDNVVEQGrLS 477
Cdd:PRK09862 383 LEIPLPPPGILSkTVVPGESSATVKQRVMAARERQFKRQN----KLNAWLDSPEIRQFCKLESEDARWLEETLIHLG-LS 457
|
490
....*....|....*....
gi 1839373875 478 MRGAQRVLRLAWTVADLSG 496
Cdd:PRK09862 458 IRAWQRLLKVARTIADIDQ 476
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
201-409 |
1.25e-117 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 344.90 E-value: 1.25e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 201 DFSDIRGQAAACQAMEVAAAGGHHLLMIGTPGSGKTMLASRLPGILPPLELDQSVEVTALHSLAGtLSPLDGLIRQPPFQ 280
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAG-LGGDGGLIRRRPFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 281 APHHSATLAAMVGGGSgVPRPGAASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANP 360
Cdd:pfam01078 80 APHHSASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1839373875 361 CPCGNAGSRRATCTCTPYSRKRYLERLSGPLLDRMDIQIQVESPGRGSL 409
Cdd:pfam01078 159 CPCGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
21-143 |
2.49e-46 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 157.61 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 21 VEAHISDGMTAYSLVGLPDTAVREAKDRVRAAVTSCLYEWPGTRIVLNLSPASLPKTGSGYDLAMAVSVLAAMGVIsrSR 100
Cdd:pfam13541 1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFEFPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQI--PV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1839373875 101 AGQCIMLGELGLDGRVIGIRGILPSVIGAMNTGKTKILVPQAN 143
Cdd:pfam13541 79 LEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| Mg_chelatase_C |
pfam13335 |
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative ... |
415-512 |
1.64e-21 |
|
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative bacterial magnesium chelatase subunit ChlI proteins. Most members have the associated pfam01078.
Pssm-ID: 433125 Cd Length: 93 Bit Score: 88.98 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 415 ADTTTVVAARVQRARDVQRERWKGrgwdLNREIPGPFLRQpEGGFTRELIGRVDNVVEQGRLSMRGAQRVLRLAWTVADL 494
Cdd:pfam13335 1 GESSAEVRERVAAARERQAERFGG----ENAQLPGRELRR-FCRLDAAARALLERALERLGLSARAYDRILRVARTIADL 75
|
90
....*....|....*...
gi 1839373875 495 SGKTVPGLPELGTAMTLR 512
Cdd:pfam13335 76 AGSERIGREHLAEALQYR 93
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
224-397 |
1.07e-06 |
|
MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).
Pssm-ID: 350658 [Multi-domain] Cd Length: 311 Bit Score: 50.42 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 224 HLLMIGTPGSGKTMLASRLPGILPpleldQSVEVTALHSLAGTLSpldglirqppfqaphhsATLAAMVGGGSGVPRPGA 303
Cdd:cd17706 43 HILLVGDPGTAKSQILKYVLKIAP-----RGVYTSGKGSSGAGLT-----------------AAVVRDSETGEWYLEAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 304 ASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANPcpcgnAGSRratctctpYSRKRY 383
Cdd:cd17706 101 LVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANP-----KGGR--------YNPKLS 167
|
170
....*....|....*..
gi 1839373875 384 L-ER--LSGPLLDRMDI 397
Cdd:cd17706 168 PiENinLPSPLLSRFDL 184
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
224-395 |
5.79e-06 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 45.75 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 224 HLLMIGTPGSGKTMLASRLPGILPPleldQSVEVTALHslAGTlSPLDglIRQPpfqaphhsatLAAMVGGGSGVPRPGA 303
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSN----RPVFYVQLT--RDT-TEED--LFGR----------RNIDPGGASWVDGPLV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 304 ASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPA-RFQLIMAANPCPcgnagsrratctctpysrkR 382
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLD-------------------R 122
|
170
....*....|...
gi 1839373875 383 YLERLSGPLLDRM 395
Cdd:pfam07728 123 GLNELSPALRSRF 135
|
|
| MCM |
pfam00493 |
MCM P-loop domain; |
224-397 |
2.77e-05 |
|
MCM P-loop domain;
Pssm-ID: 459830 [Multi-domain] Cd Length: 224 Bit Score: 45.60 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 224 HLLMIGTPGSGKTMLASRLPGILPPleldqSVEVTALHSLAGTLSPldGLIRQPPfqaphhsatlaamvgGGSGVPRPGA 303
Cdd:pfam00493 59 NVLLVGDPGTAKSQLLKYVEKIAPR-----AVYTSGKGSSAAGLTA--AVVRDPV---------------TGEFVLEAGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 304 ASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANPcpcgnAGSRratctctpYSRKRY 383
Cdd:pfam00493 117 LVLADGGVCCIDEFDKMNDEDRVALHEAMEQQTISIAKAGIVATLNARCSILAAANP-----IFGR--------YDPKKS 183
|
170
....*....|....*..
gi 1839373875 384 LE---RLSGPLLDRMDI 397
Cdd:pfam00493 184 IAeniNLPPPLLSRFDL 200
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
222-360 |
3.11e-05 |
|
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: 44.06 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 222 GHHLLMIGTPGSGKTMLAsrlpgilppleldqsvevtalHSLAGTLSpldglIRQPPFQAPHHSATLAAMVGGG-----S 296
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLA---------------------RAIANELF-----RPGAPFLYLNASDLLEGLVVAElfghfL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1839373875 297 GVPRPGAASLAHRGVLFLDEAPEFGARVLDSLREplengeiTLHRAAGAAQYPARFQLIMAANP 360
Cdd:cd00009 73 VRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLR-------VLETLNDLRIDRENVRVIGATNR 129
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
75-168 |
9.33e-05 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 43.77 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 75 PKTGSGYDLAMAVSVLAAM-GVISRSRAGqciMLGELGLDGRVIGIRGILPSVIGAMNTGKTKILVPQANLAEASLVP-- 151
Cdd:pfam05362 106 PKDGPSAGVTMATALVSALtGIPVRKDVA---MTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLEDIPen 182
|
90 100
....*....|....*....|
gi 1839373875 152 ---GVDVVGVHHLGQVIELL 168
Cdd:pfam05362 183 vreGLEIIPVEHVDEVLKHA 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
222-360 |
1.93e-04 |
|
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: 41.98 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 222 GHHLLMIGTPGSGKTMLASRLPGILPPLELDqSVEVTAlhslagtlsplDGLIRQPPFQAPHHSATLAAMVGGGSGVPRp 301
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG-VIYIDG-----------EDILEEVLDQLLLIIVGGKKASGSGELRLR- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839373875 302 GAASLAHR---GVLFLDEApefgARVLDSLREPLENGEITLhRAAGAAQYPARFQLIMAANP 360
Cdd:smart00382 69 LALALARKlkpDVLILDEI----TSLLDAEQEALLLLLEEL-RLLLLLKSEKNLTVILTTND 125
|
|
| MCM_arch |
cd17761 |
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ... |
221-360 |
8.23e-04 |
|
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork
Pssm-ID: 350667 [Multi-domain] Cd Length: 308 Bit Score: 41.67 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839373875 221 GGHHLLMIGTPGSGKTMLASRLPGILPpleldQSVEVTALHSLAGTLSpldglirqppfqaphhsatlAAMV---GGGSG 297
Cdd:cd17761 41 GDIHILLVGDPGTAKSQLLKYVSKVAP-----RAVYTTGKGSTAAGLT--------------------AAVVrdeGTGEW 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1839373875 298 VPRPGAASLAHRGVLFLDEAPEFGARVLDSLREPLENGEITLHRAAGAAQYPARFQLIMAANP 360
Cdd:cd17761 96 YLEAGALVLADKGIAVVDEIDKMRKEDRSALHEAMEQQTISIAKAGIVATLNARAAVLAAANP 158
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
223-267 |
4.68e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 38.71 E-value: 4.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1839373875 223 HHLLMIGTPGSGKTMLASRLPGilpplELDQSVEVTALHSLAGTL 267
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAG-----ELKLPLLTVRLDSLIGSY 75
|
|
| |
