|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-370 |
1.69e-164 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 464.25 E-value: 1.69e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKELGT 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 81 TKLEIDLGKKGKR-AKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILKQ 159
Cdd:PRK00064 81 LPLGLEIDKKGGRkVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 160 RNNYLKQlqlkeaSDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKFKYVCALKkkhqTNEND 239
Cdd:PRK00064 161 RNALLKQ------ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFELASLSYQSSVE----DDAEK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 240 IYTGLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDVL 319
Cdd:PRK00064 231 IEEDLLEALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 927267543 320 SELDDNRQTHLLKSIQD-KVQTFLTTTSLSGIArDLISDPKVFNISSGQVVE 370
Cdd:PRK00064 311 SELDDGRRAALLERLKGlGAQVFITTTDLEDLA-DLLENAKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-354 |
1.23e-153 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 436.51 E-value: 1.23e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 2 KLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKELGTT 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 82 KLEIDLGKKG-KRAKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILKQR 160
Cdd:COG1195 81 RLGLGLSRGGkKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 161 NNYLKQLQlkeASDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKFKYVCALKKKHQTNENDi 240
Cdd:COG1195 161 NALLKQGR---EADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSGGKEELELRYRSGWLYESAELEEA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 241 ytgLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDVLS 320
Cdd:COG1195 237 ---LLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFA 313
|
330 340 350
....*....|....*....|....*....|....*
gi 927267543 321 ELDDNRQTHLLKSIQDK-VQTFLTTTSLSGIARDL 354
Cdd:COG1195 314 ELDEERREALLELLADLgGQVFITTTDPEDFPALL 348
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-368 |
6.82e-138 |
|
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: 397.11 E-value: 6.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKEL-- 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 79 GTTKLEIDLGKKGKRAKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILK 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 159 QRNNYLKQLQLKEaSDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKFKYvcalkkkhQTNEN 238
Cdd:TIGR00611 161 QRNAALKQAQRQY-GDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFY--------RGELW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 239 DIYTGLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDV 318
Cdd:TIGR00611 232 DKETDYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 927267543 319 LSELDDNRQTHLLKSIQDK-VQTFLTTTSLSGIARDLISDPK---VFNISSGQV 368
Cdd:TIGR00611 312 ASELDDQRRRLLAELLQSLgVQVFVTAISLDHLKEMWDPNRVtiaLVSVDRGTI 365
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-368 |
2.41e-113 |
|
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: 331.18 E-value: 2.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 3 LREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKELGTTK 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 83 LEIDL-GKKGKRAKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILKQRN 161
Cdd:cd03242 81 LELTIrSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 162 NYLKqlqlkeasdklyldvlsdqlaaygaklifqrlellkklqgwaanihaeisqgkeelkfkyvcalkkkhqtnendiy 241
Cdd:cd03242 161 ALLK---------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 242 tglkelfeenkdkeirqgntlyGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDVLSE 321
Cdd:cd03242 165 ----------------------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAE 222
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 927267543 322 LDDNRQTHLLKSIQDKVQTFLTTTSLSGIARDLISDPKVFNISSGQV 368
Cdd:cd03242 223 LDLGRQAALLDAIEGRVQTFVTTTDLADFDALWLRRAQIFRVDAGTL 269
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-46 |
1.44e-07 |
|
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: 52.99 E-value: 1.44e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVL 46
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-370 |
1.69e-164 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 464.25 E-value: 1.69e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKELGT 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 81 TKLEIDLGKKGKR-AKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILKQ 159
Cdd:PRK00064 81 LPLGLEIDKKGGRkVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 160 RNNYLKQlqlkeaSDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKFKYVCALKkkhqTNEND 239
Cdd:PRK00064 161 RNALLKQ------ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFELASLSYQSSVE----DDAEK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 240 IYTGLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDVL 319
Cdd:PRK00064 231 IEEDLLEALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 927267543 320 SELDDNRQTHLLKSIQD-KVQTFLTTTSLSGIArDLISDPKVFNISSGQVVE 370
Cdd:PRK00064 311 SELDDGRRAALLERLKGlGAQVFITTTDLEDLA-DLLENAKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-354 |
1.23e-153 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 436.51 E-value: 1.23e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 2 KLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKELGTT 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 82 KLEIDLGKKG-KRAKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILKQR 160
Cdd:COG1195 81 RLGLGLSRGGkKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 161 NNYLKQLQlkeASDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKFKYVCALKKKHQTNENDi 240
Cdd:COG1195 161 NALLKQGR---EADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSGGKEELELRYRSGWLYESAELEEA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 241 ytgLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDVLS 320
Cdd:COG1195 237 ---LLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFA 313
|
330 340 350
....*....|....*....|....*....|....*
gi 927267543 321 ELDDNRQTHLLKSIQDK-VQTFLTTTSLSGIARDL 354
Cdd:COG1195 314 ELDEERREALLELLADLgGQVFITTTDPEDFPALL 348
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-368 |
6.82e-138 |
|
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: 397.11 E-value: 6.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKEL-- 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 79 GTTKLEIDLGKKGKRAKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILK 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 159 QRNNYLKQLQLKEaSDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKFKYvcalkkkhQTNEN 238
Cdd:TIGR00611 161 QRNAALKQAQRQY-GDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFY--------RGELW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 239 DIYTGLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDV 318
Cdd:TIGR00611 232 DKETDYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 927267543 319 LSELDDNRQTHLLKSIQDK-VQTFLTTTSLSGIARDLISDPK---VFNISSGQV 368
Cdd:TIGR00611 312 ASELDDQRRRLLAELLQSLgVQVFVTAISLDHLKEMWDPNRVtiaLVSVDRGTI 365
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-368 |
2.41e-113 |
|
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: 331.18 E-value: 2.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 3 LREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYGEVEKELGTTK 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 83 LEIDL-GKKGKRAKVNQLEQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRKILKQRN 161
Cdd:cd03242 81 LELTIrSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 162 NYLKqlqlkeasdklyldvlsdqlaaygaklifqrlellkklqgwaanihaeisqgkeelkfkyvcalkkkhqtnendiy 241
Cdd:cd03242 161 ALLK---------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 242 tglkelfeenkdkeirqgntlyGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLLDDVLSE 321
Cdd:cd03242 165 ----------------------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAE 222
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 927267543 322 LDDNRQTHLLKSIQDKVQTFLTTTSLSGIARDLISDPKVFNISSGQV 368
Cdd:cd03242 223 LDLGRQAALLDAIEGRVQTFVTTTDLADFDALWLRRAQIFRVDAGTL 269
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-345 |
1.76e-60 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 198.47 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYvLALTRSHRTNNNRDLINWENENAQVYGEVEKELGT 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIY-LALTGELPNGRLADLVRFGEGEAWVHAEVETGGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 81 TKLEIDLGKKGKRAKVNQL-----EQAKLSSYVgelnviLFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRYLYNNSQYRK 155
Cdd:PRK14079 80 SRLEVGLGPGRRELKLDGVrvslrELARLPGAV------LIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 156 ILKQRNNYLKQLQLKEasdklyLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEelkfkyvCALKKKHQT 235
Cdd:PRK14079 154 AVQQRNAALKSGGGWG------LHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRKP-------LRLELSEST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 236 NENdiytGLKELFEENKDKEIRQGNTLYGPHRDDLQFIINGKDVSTFGSQGQQRTSALSVKLAEIDLMKEETNEYPILLL 315
Cdd:PRK14079 221 APE----GYLAALEARRAEELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLV 296
|
330 340 350
....*....|....*....|....*....|
gi 927267543 316 DDVLSELDDNRQTHLLKSIQDKVQTFLTTT 345
Cdd:PRK14079 297 DDFTAELDPRRRGALLALAASLPQAIVAGT 326
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-102 |
7.18e-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: 65.79 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYvLALTRSHRTNNNRDLINWENENAQVYGEVEKELGT 80
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALR-LLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGS 79
|
90 100
....*....|....*....|..
gi 927267543 81 TKLEIdLGKKGKRAKVNQLEQA 102
Cdd:COG3593 80 LLSRL-LRLLLKEEDKEELEEA 100
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-85 |
4.73e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.79 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 2 KLREIKLRNFRNYSD-VEVQFSPSINVLLGNNAQGKTNMLEAI-YVLALTRSHRTNNNRDLINWENENAQVygEVEKELG 79
Cdd:COG0419 1 KLLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIrYALYGKARSRSKLRSDLINVGSEEASV--ELEFEHG 78
|
....*.
gi 927267543 80 TTKLEI 85
Cdd:COG0419 79 GKRYRI 84
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-47 |
5.19e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 54.17 E-value: 5.19e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 927267543 2 KLREIKLRNFRNYSDVEVQFSPsINVLLGNNAQGKTNMLEAIYVLA 47
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFLS 45
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-46 |
1.44e-07 |
|
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: 52.99 E-value: 1.44e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVL 46
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-45 |
7.47e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 7.47e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYV 45
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILV 45
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-110 |
1.99e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 47.88 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 6 IKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIyVLALTRSHRTNNNRDLINWENENAQVYGEVEKElgtTKLEI 85
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAI-KLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGK---AYVEI 76
|
90 100
....*....|....*....|....*
gi 927267543 86 DLGKKGKRAKVNQLEQAKLSSYVGE 110
Cdd:pfam13476 77 TFENNDGRYTYAIERSRELSKKKGK 101
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-71 |
3.18e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 3.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927267543 3 LREIKLRNFR-NYSDVEVQFSPSINVLLGNNAQGKTNMLEAIyVLALTRSHRTNNN-----RDLINwENEN-AQVY 71
Cdd:cd03240 1 IDKLSIRNIRsFHERSEIEFFSPLTLIVGQNGAGKTTIIEAL-KYALTGELPPNSKggahdPKLIR-EGEVrAQVK 74
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-48 |
8.99e-06 |
|
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: 46.05 E-value: 8.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 927267543 3 LREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIyVLAL 48
Cdd:cd03277 3 IVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAI-CLGL 47
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-55 |
1.02e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 1.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 927267543 5 EIKLRNFRNYSDVE-VQF-SPSINVLLGNNAQGKTNMLEAIYVLALTRSHRTN 55
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFgEGSLTIITGPNGSGKSTILDAIGLALGGAQSATR 53
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-263 |
1.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYVL-------ALTRSHRTNNNRDLINWEN--ENAQVY 71
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMllerlekEADELFKPQGRKPELNLKElkELEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 72 GEVEKELGT-TKLEIDLGKKGKRAKVNQLEQAKLSSYVGELNVILFAPEDLSivkgaptvRRRFMDMEFGQMSSRYlynn 150
Cdd:COG4717 81 KEAEEKEEEyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ--------ELEALEAELAELPERL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 151 sqyrKILKQRNNYLKQLQLKEASDKLYLDVLSDQLAAYGAKLIFQRLELLKKLQGWAANIHAEISQGKEELKfkyvcALK 230
Cdd:COG4717 149 ----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE-----EAQ 219
|
250 260 270
....*....|....*....|....*....|...
gi 927267543 231 KKHQTNENDIYTGLKELFEENKDKEIRQGNTLY 263
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-97 |
1.29e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEAIYvLALTRSHRTNNNRDLINWENENAQVYGEVEKELGT 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIR-FALFTDKRTEKIEDMIKKGKNNLEVELEFRIGGHV 79
|
90
....*....|....*..
gi 927267543 81 TKLEIDLGKKGKRAKVN 97
Cdd:PRK01156 80 YQIRRSIERRGKGSRRE 96
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-257 |
5.20e-05 |
|
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: 45.35 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 2 KLREIKLRNFRNYSD-VEVQFSPSINVLLGNNAQGKTNMLEAI-YVLALT--RSHRTNNNRDLINWENENAQVYGEVE-- 75
Cdd:pfam02463 1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGERsaKSLRSERLSDLIHSKSGAFVNSAEVEit 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 76 -----KELGTTKLEIDLGKKGKRAKVNQL----EQAKLSSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFGQMSSRY 146
Cdd:pfam02463 81 fdnedHELPIDKEEVSIRRRVYRGGDSEYyingKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 147 LYNNSQYRKILKQRNNYLKQLQLKEAsdklylDVLSDQLaaygaKLIFQRLELlkKLQGWAANIHAEISQGKEELKFKYV 226
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLA------ELIIDLE-----ELKLQELKL--KEQAKKALEYYQLKEKLELEEEYLL 227
|
250 260 270
....*....|....*....|....*....|.
gi 927267543 227 CALKKKHQTNENDIYTGLKELFEENKDKEIR 257
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-52 |
8.28e-05 |
|
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: 42.68 E-value: 8.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 927267543 3 LREIKLRNFRNYSDVE-VQFSPSINVLLGNNAQGKTNMLEAI-YVLALTRSH 52
Cdd:cd03239 1 IKQITLKNFKSYRDETvVGGSNSFNAIVGPNGSGKSNIVDAIcFVLGGKAAK 52
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-62 |
8.95e-05 |
|
ATP-binding cassette domain of eukaryotic SMC2 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: 213240 [Multi-domain] Cd Length: 251 Bit Score: 43.44 E-value: 8.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927267543 1 MKLREIKLRNFRNYSD-VEVQ-FSPSINVLLGNNAQGKTNMLEAI-YVLALT--RSHRTNNNRDLIN 62
Cdd:cd03273 1 MHIKEIILDGFKSYATrTVISgFDPQFNAITGLNGSGKSNILDAIcFVLGITnlSTVRASNLQDLIY 67
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-75 |
1.49e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.45 E-value: 1.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927267543 3 LREIKLRNFRNYSD-VEVQFSPSINVLLGNNAQGKTNMLEAI-YVLALTRSH--RTNNNRDLINW--ENENAQVYGEVE 75
Cdd:cd03278 1 LKKLELKGFKSFADkTTIPFPPGLTAIVGPNGSGKSNIIDAIrWVLGEQSAKslRGEKMSDVIFAgsETRKPANFAEVT 79
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-348 |
2.15e-04 |
|
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: 42.76 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 25 INVLLGNNAQGKTNMLEAIYVLALTRSHRTNNNRDLINWENENAQVYG--EVEKELGTTKLEIDLGKKGKRAKVnqleqa 102
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLlnGIDPKEPIEFEISEFLEDGVRYRY------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 103 klsSYVGELNVILFAPEDLSIVKGAPTVRRRFMDMEFgqmsSRYLYNNSQYRKILKQRNNYLKQLQLKEASDKLYLDVLS 182
Cdd:pfam13304 75 ---GLDLEREDVEEKLSSKPTLLEKRLLLREDSEERE----PKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 183 DQLAAYGAKLIFQRLELLKKLQGWAANIHAEISqgKEELKFKYVCALKKkhqtNENDIYTGLKELFEENKDKEIRQGNTL 262
Cdd:pfam13304 148 ISPLSFLLLLDEGLLLEDWAVLDLAADLALFPD--LKELLQRLVRGLKL----ADLNLSDLGEGIEKSLLVDDRLRERGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927267543 263 YGPHRDDLQFIINGKDvstfgSQGQQRTSALSVKLAEIDlmkeetNEYPILLLDDVLSELDDNRQTHLLKSIQDK----V 338
Cdd:pfam13304 222 ILLENGGGGELPAFEL-----SDGTKRLLALLAALLSAL------PKGGLLLIDEPESGLHPKLLRRLLELLKELsrngA 290
|
330
....*....|
gi 927267543 339 QTFLTTTSLS 348
Cdd:pfam13304 291 QLILTTHSPL 300
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-47 |
1.42e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 1.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 927267543 3 LREIKLRNFRNYSDvEVQFS--------PSINVLLGNNAQGKTNMLEAIYVLA 47
Cdd:COG1106 2 LISFSIENFRSFKD-ELTLSmvasglrlLRVNLIYGANASGKSNLLEALYFLR 53
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-42 |
2.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 2.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 927267543 1 MKLREIKLRNFRNYSDVEVQFSPSINVLLGNNAQGKTNMLEA 42
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEA 42
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-46 |
4.54e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 4.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 927267543 3 LREIKLRNFRNYSD--VEVQFSPSINVLLGNNAQGKTNMLEAI-YVL 46
Cdd:cd03272 1 IKQVIIQGFKSYKDqtVIEPFSPKHNVVVGRNGSGKSNFFAAIrFVL 47
|
|
| |
