|
Name |
Accession |
Description |
Interval |
E-value |
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-355 |
2.05e-176 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 494.18 E-value: 2.05e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERE 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 81 TAI---GLTKDKQGDSKVRIDGTDghKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKRL 157
Cdd:TIGR00611 81 VTIpleGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 158 LKQRNAALRQVTRY----AQLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQFLPEFSLTFSFQRG--WEKETDYA 231
Cdd:TIGR00611 159 LKQRNAALKQAQRQygdrTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 232 EVLERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDA 311
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 850375193 312 RRGLLASRLKATQSQVFVSAISAEHVIDMSDENSK---MFTVEKGKI 355
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVtiaLVSVDRGTI 365
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-357 |
6.96e-157 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 444.22 E-value: 6.96e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERE 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 81 TAIGLTKDKQGDSKVRIDGTDGHKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKRLLKQ 160
Cdd:PRK00064 81 LPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 161 RNAALRQvTRYAQLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQFLPEF-SLTFSFQRGWEK-----ETDYAEVL 234
Cdd:PRK00064 161 RNALLKQ-ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFeLASLSYQSSVEDdaekiEEDLLEAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 235 ERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRG 314
Cdd:PRK00064 240 AKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGRRA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 850375193 315 LLASRLKATQSQVFVSAISAEHVIDMSdENSKMFTVEKGKITD 357
Cdd:PRK00064 320 ALLERLKGLGAQVFITTTDLEDLADLL-ENAKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-343 |
1.84e-131 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 379.50 E-value: 1.84e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERETA 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 83 IGLTKDKQGDSKVRIDGTDGHKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKRLLKQRN 162
Cdd:COG1195 82 LGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQRN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 163 AALRQ--VTRYAQLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQF-LPEFSLTFSFQRGWEKET-----DYAEVL 234
Cdd:COG1195 162 ALLKQgrEADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALsGGKEELELRYRSGWLYESaeleeALLEAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 235 ERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRG 314
Cdd:COG1195 242 AENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERRE 321
|
330 340
....*....|....*....|....*....
gi 850375193 315 LLASRLKATQSQVFVSAISAEHVIDMSDE 343
Cdd:COG1195 322 ALLELLADLGGQVFITTTDPEDFPALLER 350
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-356 |
5.04e-37 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 134.35 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERETA 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 83 IGLTKDKQGDSKVRIDGTDGHKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDwgcfhneagffnawsnlkRLLKQRN 162
Cdd:cd03242 81 LELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLD------------------RLLGQLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 163 AalrqvtRYAQLRpwdmeliplaeqisrwraeysagiaedmadtckqflpefsltfsfqrgwekeTDYAEVLErsfERDR 242
Cdd:cd03242 143 P------AYAHVL----------------------------------------------------SEYQKALR---QRNA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 243 MLTytahGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRGLLASRLKA 322
Cdd:cd03242 162 LLK----GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAIEG 237
|
330 340 350
....*....|....*....|....*....|....
gi 850375193 323 TQsQVFVSAISAEHVIDMSDENSKMFTVEKGKIT 356
Cdd:cd03242 238 RV-QTFVTTTDLADFDALWLRRAQIFRVDAGTLS 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-194 |
2.25e-35 |
|
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: 137.03 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNI-ESADLALSPGFNFLVGANGSGKTSVLEAI-YTLG--HGRAFRSLQIGRVIRHEQESFVLHGRLQG-- 76
Cdd:pfam02463 2 LKRIEIEGFKSYaKTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGerSAKSLRSERLSDLIHSKSGAFVNSAEVEItf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 77 ---------EERETAIGLTKDKQGDSKVRIDGTDGHKvAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGF 147
Cdd:pfam02463 82 dnedhelpiDKEEVSIRRRVYRGGDSEYYINGKNVTK-KEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 850375193 148 FNAWSNLKRLLKQRNAALRQVTRYAQLRPWDMELIPLAEQISRWRAE 194
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-355 |
2.05e-176 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 494.18 E-value: 2.05e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERE 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 81 TAI---GLTKDKQGDSKVRIDGTDghKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKRL 157
Cdd:TIGR00611 81 VTIpleGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 158 LKQRNAALRQVTRY----AQLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQFLPEFSLTFSFQRG--WEKETDYA 231
Cdd:TIGR00611 159 LKQRNAALKQAQRQygdrTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 232 EVLERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDA 311
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 850375193 312 RRGLLASRLKATQSQVFVSAISAEHVIDMSDENSK---MFTVEKGKI 355
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVtiaLVSVDRGTI 365
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-357 |
6.96e-157 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 444.22 E-value: 6.96e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERE 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 81 TAIGLTKDKQGDSKVRIDGTDGHKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKRLLKQ 160
Cdd:PRK00064 81 LPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 161 RNAALRQvTRYAQLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQFLPEF-SLTFSFQRGWEK-----ETDYAEVL 234
Cdd:PRK00064 161 RNALLKQ-ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFeLASLSYQSSVEDdaekiEEDLLEAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 235 ERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRG 314
Cdd:PRK00064 240 AKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGRRA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 850375193 315 LLASRLKATQSQVFVSAISAEHVIDMSdENSKMFTVEKGKITD 357
Cdd:PRK00064 320 ALLERLKGLGAQVFITTTDLEDLADLL-ENAKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-343 |
1.84e-131 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 379.50 E-value: 1.84e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERETA 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 83 IGLTKDKQGDSKVRIDGTDGHKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKRLLKQRN 162
Cdd:COG1195 82 LGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQRN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 163 AALRQ--VTRYAQLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQF-LPEFSLTFSFQRGWEKET-----DYAEVL 234
Cdd:COG1195 162 ALLKQgrEADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALsGGKEELELRYRSGWLYESaeleeALLEAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 235 ERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRG 314
Cdd:COG1195 242 AENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERRE 321
|
330 340
....*....|....*....|....*....
gi 850375193 315 LLASRLKATQSQVFVSAISAEHVIDMSDE 343
Cdd:COG1195 322 ALLELLADLGGQVFITTTDPEDFPALLER 350
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-356 |
5.04e-37 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 134.35 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQESFVLHGRLQGEERETA 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 83 IGLTKDKQGDSKVRIDGTDGHKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDwgcfhneagffnawsnlkRLLKQRN 162
Cdd:cd03242 81 LELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLD------------------RLLGQLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 163 AalrqvtRYAQLRpwdmeliplaeqisrwraeysagiaedmadtckqflpefsltfsfqrgwekeTDYAEVLErsfERDR 242
Cdd:cd03242 143 P------AYAHVL----------------------------------------------------SEYQKALR---QRNA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 243 MLTytahGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRGLLASRLKA 322
Cdd:cd03242 162 LLK----GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAIEG 237
|
330 340 350
....*....|....*....|....*....|....
gi 850375193 323 TQsQVFVSAISAEHVIDMSDENSKMFTVEKGKIT 356
Cdd:cd03242 238 RV-QTFVTTTDLADFDALWLRRAQIFRVDAGTLS 270
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-334 |
1.93e-36 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 134.91 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYtLGHGRAFRSLQIGRVIRHEQESFVLHGRLqgeerE 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIY-LALTGELPNGRLADLVRFGEGEAWVHAEV-----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 81 TAIGLTKDK----QGDSKVRIDGTDGhKVAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFNAWSNLKR 156
Cdd:PRK14079 75 TGGGLSRLEvglgPGRRELKLDGVRV-SLRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 157 LLKQRNAALRQVTRYAqLRPWDMELIPLAEQISRWRAEYSAGIAEDMADTCKQFLPEFSLTFSFQRGWEKETdYAEVLER 236
Cdd:PRK14079 154 AVQQRNAALKSGGGWG-LHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRKPLRLELSESTAPEG-YLAALEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 237 SFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRGLL 316
Cdd:PRK14079 232 RRAEELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLVDDFTAELDPRRRGAL 311
|
330
....*....|....*...
gi 850375193 317 ASrLKATQSQVFVSAISA 334
Cdd:PRK14079 312 LA-LAASLPQAIVAGTEA 328
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-194 |
2.25e-35 |
|
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: 137.03 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNI-ESADLALSPGFNFLVGANGSGKTSVLEAI-YTLG--HGRAFRSLQIGRVIRHEQESFVLHGRLQG-- 76
Cdd:pfam02463 2 LKRIEIEGFKSYaKTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGerSAKSLRSERLSDLIHSKSGAFVNSAEVEItf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 77 ---------EERETAIGLTKDKQGDSKVRIDGTDGHKvAELALLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGF 147
Cdd:pfam02463 82 dnedhelpiDKEEVSIRRRVYRGGDSEYYINGKNVTK-KEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 850375193 148 FNAWSNLKRLLKQRNAALRQVTRYAQLRPWDMELIPLAEQISRWRAE 194
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK 207
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
186-356 |
8.36e-23 |
|
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: 100.05 E-value: 8.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 186 EQISRWRAEYSAGIAEDMADTCKQFLPEFSLTFSFQRGWEKETDYAEVLERSFERDRMLTYTAHGPHKADFRIRADGAPV 265
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKN 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 266 EDTLSRGQLKLLMCALRLAqgeflTRESGRRCLYLIDDFASELDDARRGLLASRLKA--TQSQVFVSAISAEHVIDMsDE 343
Cdd:pfam02463 1075 LDLLSGGEKTLVALALIFA-----IQKYKPAPFYLLDEIDAALDDQNVSRVANLLKElsKNAQFIVISLREEMLEKA-DK 1148
|
170
....*....|...
gi 850375193 344 NSKMFTVEKGKIT 356
Cdd:pfam02463 1149 LVGVTMVENGVST 1161
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-46 |
5.65e-12 |
|
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: 66.18 E-value: 5.65e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTL 46
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLL 46
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-100 |
2.21e-11 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 63.48 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 1 MSLTRLLIRDFRNIESADLALS--PGFNFLVGANGSGKTSVLEAIYTLGHG-------RAFRSLQIGRVIRHEQESFVLH 71
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDnpPRLTVLVGENGSGKTTLLEAIALALSGllsrlddVKFRKLLIRNGEFGDSAKLILY 80
|
90 100 110
....*....|....*....|....*....|..
gi 850375193 72 ---GRLQGEERETAIGLTKDKQGDSKVRIDGT 100
Cdd:COG3950 81 ygtSRLLLDGPLKKLERLKEEYFSRLDGYDSL 112
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-48 |
2.21e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 2.21e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 850375193 3 LTRLLIRDFRNIESADLALSPgFNFLVGANGSGKTSVLEAIYTLGH 48
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFLSD 46
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-44 |
5.14e-09 |
|
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: 57.22 E-value: 5.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIY 44
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALD 44
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-147 |
4.23e-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: 53.75 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLqigrvIRHEQESFVLHGRLQGEERETA 82
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADL-----IRSGAEKAVVEGVFDISDEEEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 83 IGLTKDKQGD----------------SKVRIDGTdghkVAELALLmpmQLITPEGFT---------LLNggPKYRRAFLD 137
Cdd:cd03241 76 KALLLELGIEddddliirreisrkgrSRYFINGQ----SVTLKLL---RELGSLLVDihgqhdhqnLLN--PERQLDLLD 146
|
170
....*....|
gi 850375193 138 WGCFHNEAGF 147
Cdd:cd03241 147 GGLDDVEFLF 156
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-43 |
7.57e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 49.03 E-value: 7.57e-07
10 20 30
....*....|....*....|....*....|....*...
gi 850375193 6 LLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAI 43
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAI 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-62 |
7.69e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 7.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAIYT---LGHGRAFRSLQIGRVIR 62
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVglyWGHGSKPKGLKKDDFTR 65
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-125 |
6.78e-06 |
|
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: 46.15 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIesADLALSPG---FNFLVGANGSGKTSVLEAI-YTLGhgraFRSLQIGRvirhEQESFVLHGRLQGEE 78
Cdd:cd03239 1 IKQITLKNFKSY--RDETVVGGsnsFNAIVGPNGSGKSNIVDAIcFVLG----GKAAKLRR----GSLLFLAGGGVKAGI 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 850375193 79 RETAIGLTKDK------QGDSKVRIDGtdGHK-VAELALLMPMQLITPEGFTLL 125
Cdd:cd03239 71 NSASVEITFDKsyflvlQGKVEQILSG--GEKsLSALALIFALQEIKPSPFYVL 122
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-330 |
1.14e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 46.61 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 25 FNFLVGANGSGKTSVLEAIYTLGHG-RAFRSLQIGRVIRHEQESFVLHGRLQGEERETAIGLTKDKQGDSKVRIDGTDGH 103
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFdALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 104 KVAELALlmpMQLITPEGFTLL---NGGPKYRRAFLDWGCFH-NEAGFFNAWSNLKRLLKQRNAALRQ--VTRYAQLRPW 177
Cdd:pfam13304 81 EDVEEKL---SSKPTLLEKRLLlreDSEEREPKFPPEAEELRlGLDVEERIELSLSELSDLISGLLLLsiISPLSFLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 178 DMELIPLAEQISRWRAEYSAGIaeDMADTCKQFLPEFSLT-FSFQRGWEKETDYAEVLERSFERDRmltYTAHGPHKADF 256
Cdd:pfam13304 158 DEGLLLEDWAVLDLAADLALFP--DLKELLQRLVRGLKLAdLNLSDLGEGIEKSLLVDDRLRERGL---ILLENGGGGEL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 850375193 257 RIRAdgapvedtLSRGQLKLLmcALRLAQgeFLTRESGRrcLYLIDDFASELDDARRGLLASRLKAT---QSQVFVS 330
Cdd:pfam13304 233 PAFE--------LSDGTKRLL--ALLAAL--LSALPKGG--LLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILT 295
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-46 |
1.78e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 45.73 E-value: 1.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 850375193 3 LTRLLIRDFRNIESADLALSPgFNFLVGANGSGKTSVLEAIYTL 46
Cdd:COG4938 1 IKSISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLIQALLLL 43
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-70 |
3.08e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 45.42 E-value: 3.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 850375193 3 LTRLLIRDFRNI-ESADLALSPG------FNFLVGANGSGKTSVLEAIYTLgHGRAFRSLQIGRVIRheqESFVL 70
Cdd:COG1106 2 LISFSIENFRSFkDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFL-RNLVLNSSQPGDKLV---EPFLL 72
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-43 |
5.75e-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: 43.75 E-value: 5.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 850375193 3 LTRLLIRDFRNI-ESADLALSPGFNFLVGANGSGKTSVLEAI 43
Cdd:cd03240 1 IDKLSIRNIRSFhERSEIEFFSPLTLIVGQNGAGKTTIIEAL 42
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-80 |
6.54e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 850375193 3 LTRLLIRDFRNIESAD-LALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGR--------------VIRHEQES 67
Cdd:COG0419 2 LLRLRLENFRSYRDTEtIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSdlinvgseeasvelEFEHGGKR 81
|
90
....*....|...
gi 850375193 68 FVLHgRLQGEERE 80
Cdd:COG0419 82 YRIE-RRQGEFAE 93
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
3-73 |
1.88e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 850375193 3 LTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAI-YTLGhGRAFRSLqigrvIRHEQESFVLHGR 73
Cdd:COG0497 2 LTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALgLLLG-GRADASL-----VRHGADKAEVEAV 67
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
2-69 |
2.05e-04 |
|
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: 42.20 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 850375193 2 SLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAI-YTLGHGRAF--RSLQIGRVIRH-EQESFV 69
Cdd:cd03277 2 SIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAIcLGLGGKPKLlgRAKKVGEFVKRgCDEGTI 73
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-42 |
2.21e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEA 42
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEA 42
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-43 |
3.47e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 3.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAI 43
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAI 43
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
19-49 |
1.57e-03 |
|
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: 39.12 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|.
gi 850375193 19 LALSPGFNFLVGANGSGKTSVLEAIyTLGHG 49
Cdd:cd03276 17 IEFGPRVNFIVGNNGSGKSAILTAL-TIGLG 46
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
11-43 |
4.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.21 E-value: 4.01e-03
10 20 30
....*....|....*....|....*....|...
gi 850375193 11 FRNIESadLALSPGFNFLVGANGSGKTSVLEAI 43
Cdd:COG3910 27 VRNLEG--LEFHPPVTFFVGENGSGKSTLLEAI 57
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-43 |
5.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 5.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 850375193 1 MSLTRLLIRDFRNIESADLALSPGFNFLVGANGSGKTSVLEAI 43
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFI 43
|
|
| |
