|
Name |
Accession |
Description |
Interval |
E-value |
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
61-235 |
9.77e-44 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 150.11 E-value: 9.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 61 LFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYAD 140
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 141 QLRTQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELR 220
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 178757 221 RSLAPYAQDTQEKLN 235
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
188-337 |
8.21e-14 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 69.21 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 188 AKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARI----------- 256
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLepyteelrkrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 257 SASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA----ELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRTKLGPH 332
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLEQNVDALRARLApyaeELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQ 166
|
....*
gi 178757 333 AGDVE 337
Cdd:pfam01442 167 AEDLR 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-274 |
7.83e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 34 YFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELhERLAKDSEKLKEEIGK---ELEELR 110
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKleeALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 111 ARLLPHANEVSQKIGDNLRELQQRLEPYADQLrtQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKI 190
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 191 ---DQNVEELKGRLTPYADEfKVKIDQTVEELRRSLAPyAQDTQEKLNHQLEgltfQMKKNAEELKARISASAEELRQRL 267
Cdd:TIGR02169 864 eelEEELEELEAALRDLESR-LGDLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIE 937
|
....*..
gi 178757 268 APLAEDV 274
Cdd:TIGR02169 938 DPKGEDE 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-306 |
1.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 128 LRELQQRLEPyADQLRTQVNTQAEQLRRQLTPYAQRMERVLRE-NADSLQASLRPHADELkAKIDQN---VEELKGRLtp 203
Cdd:COG4913 619 LAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAEL-ERLDASsddLAALEEQL-- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 204 yaDEFKVKIDQTVEELRRslapyAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAP---------LAEDV 274
Cdd:COG4913 695 --EELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaVEREL 767
|
170 180 190
....*....|....*....|....*....|..
gi 178757 275 RGNLRGNTEGLQKSLAELGGHLDQQVEEFRRR 306
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-308 |
2.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 64 DKLGEVNTYAGDLQKKLVPF--ATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVsqkigDNLRELQQRLEPYADQ 141
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFikRTENIEELIKEKEKELEEVLREINEISSELPELREEL-----EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 142 LrtqvnTQAEQLRRQLTPYAQRMERVLRENADSLqASLRPHADELKAKIdQNVEELKGRLTPYA--DEFKVKIDQTVEEL 219
Cdd:PRK03918 240 I-----EELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKV-KELKELKEKAEEYIklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 220 RRSLAPYAQDTQEkLNHQLEGLTfQMKKNAEELKARIsasaEELRQRLAPLAEDVRG-----NLRGNTEGLQKSLAELG- 293
Cdd:PRK03918 313 EKRLSRLEEEING-IEERIKELE-EKEERLEELKKKL----KELEKRLEELEERHELyeeakAKKEELERLKKRLTGLTp 386
|
250
....*....|....*
gi 178757 294 GHLDQQVEEFRRRVE 308
Cdd:PRK03918 387 EKLEKELEELEKAKE 401
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
61-235 |
9.77e-44 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 150.11 E-value: 9.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 61 LFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYAD 140
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 141 QLRTQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELR 220
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 178757 221 RSLAPYAQDTQEKLN 235
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
146-313 |
6.36e-23 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 94.64 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 146 VNTQAEQLRRQLTPYAQRmervlrenadsLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAP 225
Cdd:pfam01442 9 LSTYAEELQEQLGPVAQE-----------LVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 226 YAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA----ELGGHLDQQVE 301
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLApyaeEVQAQLSQRLQ 157
|
170
....*....|..
gi 178757 302 EFRRRVEPYGEN 313
Cdd:pfam01442 158 ELREKLEPQAED 169
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
188-337 |
8.21e-14 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 69.21 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 188 AKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARI----------- 256
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLepyteelrkrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 257 SASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA----ELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRTKLGPH 332
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLEQNVDALRARLApyaeELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQ 166
|
....*
gi 178757 333 AGDVE 337
Cdd:pfam01442 167 AEDLR 171
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
211-364 |
1.11e-13 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 68.83 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 211 KIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA 290
Cdd:pfam01442 8 ELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 178757 291 elgghldQQVEEFRRRVEPYGENFNKALVQQMEQLRTKLGPHAGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQ 364
Cdd:pfam01442 88 -------ADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQ 154
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
12-168 |
4.00e-10 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 58.43 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 12 LVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKS--ELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHE 89
Cdd:pfam01442 27 LVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNveELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 178757 90 RLAkdseklkeeigKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYADQLRTQVNTQAEQLRRQLTPYAQRMERVL 168
Cdd:pfam01442 107 RLE-----------QNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLREKL 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-274 |
7.83e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 34 YFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELhERLAKDSEKLKEEIGK---ELEELR 110
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKleeALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 111 ARLLPHANEVSQKIGDNLRELQQRLEPYADQLrtQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKI 190
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 191 ---DQNVEELKGRLTPYADEfKVKIDQTVEELRRSLAPyAQDTQEKLNHQLEgltfQMKKNAEELKARISASAEELRQRL 267
Cdd:TIGR02169 864 eelEEELEELEAALRDLESR-LGDLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIE 937
|
....*..
gi 178757 268 APLAEDV 274
Cdd:TIGR02169 938 DPKGEDE 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-306 |
1.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 128 LRELQQRLEPyADQLRTQVNTQAEQLRRQLTPYAQRMERVLRE-NADSLQASLRPHADELkAKIDQN---VEELKGRLtp 203
Cdd:COG4913 619 LAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAEL-ERLDASsddLAALEEQL-- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 204 yaDEFKVKIDQTVEELRRslapyAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAP---------LAEDV 274
Cdd:COG4913 695 --EELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaVEREL 767
|
170 180 190
....*....|....*....|....*....|..
gi 178757 275 RGNLRGNTEGLQKSLAELGGHLDQQVEEFRRR 306
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
53-147 |
2.65e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 53 ELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAkdseklkeeigKELEELRARLLPHANEVSQKIGDNLRELQ 132
Cdd:pfam01442 92 ELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLA-----------ERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
90
....*....|....*
gi 178757 133 QRLEPYADQLRTQVN 147
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
182-308 |
5.47e-04 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 182 HADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAE 261
Cdd:pfam07902 118 HNDTIKTEIVESAEGIATRISEDTDKKLALINETISGIRREYQDADRQLSSSYQAGIEGLKATMASDKIGLQAEIQASAQ 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 178757 262 ELRQR----LAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVE 308
Cdd:pfam07902 198 GLSQRydneIRKLSAKITTTSSGTTEAYESKLDDLRAEFTRSNQGMRTELE 248
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
34-350 |
2.09e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 34 YFSQLSNnAKEAVEHLqKSELtQQLNALFQDKLGEvntyagdLQKKLVPFATELHE------RLAKDSEKLKEEIGKELE 107
Cdd:pfam15921 315 YMRQLSD-LESTVSQL-RSEL-REAKRMYEDKIEE-------LEKQLVLANSELTEarterdQFSQESGNLDDQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 108 EL--RARLLPHANEVSQKIGDN-----------LRELQ------QRLEPYADQLRTQVNTQAEQLRRQLTPYAQRMERVl 168
Cdd:pfam15921 385 DLhkREKELSLEKEQNKRLWDRdtgnsitidhlRRELDdrnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 169 renadslqASLRPHADELKAKIDQNVEELKGRltpyadefkvkiDQTVEELRRSLAPYAQDTQEKlNHQLEGLTFQMKKn 248
Cdd:pfam15921 464 --------SSLTAQLESTKEMLRKVVEELTAK------------KMTLESSERTVSDLTASLQEK-ERAIEATNAEITK- 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 249 aeeLKARISASAEELrQRLAPLAEDVRgNLRGNTEGLQKSLAELgghlDQQVEEFRRRVEpygenfnkalvqQMEQLRTK 328
Cdd:pfam15921 522 ---LRSRVDLKLQEL-QHLKNEGDHLR-NVQTECEALKLQMAEK----DKVIEILRQQIE------------NMTQLVGQ 580
|
330 340
....*....|....*....|..
gi 178757 329 LGPHAGDVEGHLSFLEKDLRDK 350
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDR 602
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-347 |
2.24e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 89 ERLAKDSEKLKE---EIGKELEELRARLLPHANEVSQKigdnlrelqQRLEPYADQLRTQVNTQAEQLRRQLTPYAQRME 165
Cdd:TIGR02168 680 EELEEKIEELEEkiaELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 166 RVLRENAD-----SLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKvKIDQTVEELRRSLapyaQDTQEKLNHQLEG 240
Cdd:TIGR02168 751 QLSKELTEleaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAEL----TLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 241 LTfQMKKNAEELKARISASAEELRQRLAPLAEdVRGNLRGNTEGLQKSLAELGGHLDQ--QVEEFRRRVEPYGENFNKAL 318
Cdd:TIGR02168 826 LE-SLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNEraSLEEALALLRSELEELSEEL 903
|
250 260 270
....*....|....*....|....*....|....*
gi 178757 319 ------VQQMEQLRTKLGPHAGDVEGHLSFLEKDL 347
Cdd:TIGR02168 904 releskRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-305 |
2.48e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 18 ARAEVSADQvatvmwDYFSQLSNNAKEAVEHLQKSELtqqlnalfqdKLGEVNTYAGDLQKKLVPFATELHERLAKDSEK 97
Cdd:pfam12128 483 ANAEVERLQ------SELRQARKRRDQASEALRQASR----------RLEERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 98 LKEEIGKELEE---LRARLLPHANEVSQKIGDNLRELQQRLEpyadqlRTQVNTQA---EQLRRQLTPY--AQRMERVLR 169
Cdd:pfam12128 547 WEQSIGKVISPellHRTDLDPEVWDGSVGGELNLYGVKLDLK------RIDVPEWAaseEELRERLDKAeeALQSAREKQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 170 ENADSLQASLRPHADELKAKID------QNVEELKGRLTPYADEFKVKIDQTVEELRRSlapyAQDTQEKLNHQLEGLTF 243
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDS----ANERLNSLEAQLKQLDK 696
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 178757 244 QMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRR 305
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR 758
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-308 |
2.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 64 DKLGEVNTYAGDLQKKLVPF--ATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVsqkigDNLRELQQRLEPYADQ 141
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFikRTENIEELIKEKEKELEEVLREINEISSELPELREEL-----EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 142 LrtqvnTQAEQLRRQLTPYAQRMERVLRENADSLqASLRPHADELKAKIdQNVEELKGRLTPYA--DEFKVKIDQTVEEL 219
Cdd:PRK03918 240 I-----EELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKV-KELKELKEKAEEYIklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 220 RRSLAPYAQDTQEkLNHQLEGLTfQMKKNAEELKARIsasaEELRQRLAPLAEDVRG-----NLRGNTEGLQKSLAELG- 293
Cdd:PRK03918 313 EKRLSRLEEEING-IEERIKELE-EKEERLEELKKKL----KELEKRLEELEERHELyeeakAKKEELERLKKRLTGLTp 386
|
250
....*....|....*
gi 178757 294 GHLDQQVEEFRRRVE 308
Cdd:PRK03918 387 EKLEKELEELEKAKE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-329 |
3.51e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 99 KEEIGKELEELRARLlphanevsQKIGDNLRELQQRLEP-------------YADQLR-----------TQVNTQAEQLR 154
Cdd:TIGR02168 174 RKETERKLERTRENL--------DRLEDILNELERQLKSlerqaekaerykeLKAELRelelallvlrlEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 155 RQLTPYAQRMERvLRENADSLQASLRPHADElKAKIDQNVEELKGRLTPYADEFKvKIDQTVEELRRSLApYAQDTQEKL 234
Cdd:TIGR02168 246 EELKEAEEELEE-LTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEIS-RLEQQKQILRERLA-NLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 235 NHQLEGLtFQMKKNAEELKARISASAEELRQRLAPLAEDVRgnlrgNTEGLQKSLAELGGHLDQQVEEFRRRVepygenf 314
Cdd:TIGR02168 322 EAQLEEL-ESKLDELAEELAELEEKLEELKEELESLEAELE-----ELEAELEELESRLEELEEQLETLRSKV------- 388
|
250
....*....|....*
gi 178757 315 nKALVQQMEQLRTKL 329
Cdd:TIGR02168 389 -AQLELQIASLNNEI 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-251 |
7.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 44 EAVEHLQKSELTQQLNALF--QDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLkEEIGKELEELRARLLPHANEVs 121
Cdd:COG4717 41 AFIRAMLLERLEKEADELFkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREEL- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 122 qkigDNLRELQQRLEPY-----ADQLRTQVNTQAEQLRRQLTPYAQrmervLRENADSLQASLRPHADELKAKIDQNVEE 196
Cdd:COG4717 119 ----EKLEKLLQLLPLYqeleaLEAELAELPERLEELEERLEELRE-----LEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 178757 197 LKGRLTPYADEFKvKIDQTVEELRRSLApYAQDTQEKLNHQLEGLTFQMKKNAEE 251
Cdd:COG4717 190 TEEELQDLAEELE-ELQQRLAELEEELE-EAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
41-309 |
8.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 41 NAKEAVEHLQK--SELTQQLNALfQDKLGEVNTYAGDLQKKLvpfatELHERLAK------DSEKLKEEIGkELEELRAR 112
Cdd:COG4913 607 DNRAKLAALEAelAELEEELAEA-EERLEALEAELDALQERR-----EALQRLAEyswdeiDVASAEREIA-ELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 113 LLphanevsqKIGDNLRELQQRLEpyadQLRTQVNTQAEQLRRqltpyAQRMERVLRENADSLQASLRPHADELKAKIDQ 192
Cdd:COG4913 680 LD--------ASSDDLAALEEQLE----ELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 178757 193 NVEELKGRLTPYADEfkVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARIS------ASAEELRQR 266
Cdd:COG4913 743 ARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadlESLPEYLAL 820
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 178757 267 LAPLAEDV--------RGNLRGNTEGlqkSLAELGGHLDQQVEEFRRRVEP 309
Cdd:COG4913 821 LDRLEEDGlpeyeerfKELLNENSIE---FVADLLSKLRRAIREIKERIDP 868
|
|
| |
