|
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 |
5.22e-43 |
|
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: 148.18 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 61 LFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYAD 140
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 141 QLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELR 220
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 1859630655 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 ... |
188-361 |
5.26e-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: 69.60 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 188 AKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRL 267
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 268 APLAEDVRGNLRGNTEGLQKSLAelgghldQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDL 347
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLE-------QNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQEL 159
|
170
....*....|....
gi 1859630655 348 RDKVNSFFSTFKEK 361
Cdd:pfam01442 160 REKLEPQAEDLREK 173
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-274 |
5.78e-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: 51.61 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 34 YFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELhERLAKDSEKLKEEIGK---ELEELR 110
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKleeALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 111 ARLLPHANEVSQKIGDNLRELQQRLEPYADQLrtQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKI 190
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 191 ---DQNVEELKGRLTPYADEfKVKIDQTVEELRRSLAPyAQDTQEKLNHQLEgltfQMKKNAEELKARISASAEELRQRL 267
Cdd:TIGR02169 864 eelEEELEELEAALRDLESR-LGDLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIE 937
|
....*..
gi 1859630655 268 APLAEDV 274
Cdd:TIGR02169 938 DPKGEDE 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-306 |
2.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 128 LRELQQRLEPyADQLRTQVSTQAEQLRRQLTPYAQRMERVLRE-NADSLQASLRPHADELkAKIDQN---VEELKGRLtp 203
Cdd:COG4913 619 LAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAEL-ERLDASsddLAALEEQL-- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 204 yaDEFKVKIDQTVEELRRslapyAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAP---------LAEDV 274
Cdd:COG4913 695 --EELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaVEREL 767
|
170 180 190
....*....|....*....|....*....|..
gi 1859630655 275 RGNLRGNTEGLQKSLAELGGHLDQQVEEFRRR 306
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-330 |
2.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 64 DKLGEVNTYAGDLQKKLVPF--ATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVsqkigDNLRELQQRLEPYADQ 141
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFikRTENIEELIKEKEKELEEVLREINEISSELPELREEL-----EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 142 LrtqvsTQAEQLRRQLTPYAQRMERVLRENADSLqASLRPHADELKAKIdQNVEELKGRLTPYA--DEFKVKIDQTVEEL 219
Cdd:PRK03918 240 I-----EELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKV-KELKELKEKAEEYIklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 220 RRSLAPYAQDTQEkLNHQLEGLTfQMKKNAEELKARIsasaEELRQRLAPLAEDVRG-----NLRGNTEGLQKSLAELG- 293
Cdd:PRK03918 313 EKRLSRLEEEING-IEERIKELE-EKEERLEELKKKL----KELEKRLEELEERHELyeeakAKKEELERLKKRLTGLTp 386
|
250 260 270
....*....|....*....|....*....|....*..
gi 1859630655 294 GHLDQQVEEFRRRVEPYGENFNKaLVQQMEQLRQKLG 330
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISK-ITARIGELKKEIK 422
|
|
|
|
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 |
5.22e-43 |
|
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: 148.18 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 61 LFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYAD 140
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 141 QLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELR 220
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 1859630655 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 |
1.58e-22 |
|
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: 93.48 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 146 VSTQAEQLRRQLTPYAQRmervlrenadsLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAP 225
Cdd:pfam01442 9 LSTYAEELQEQLGPVAQE-----------LVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 226 YAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA----ELGGHLDQQVE 301
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLApyaeEVQAQLSQRLQ 157
|
170
....*....|..
gi 1859630655 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 ... |
188-361 |
5.26e-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: 69.60 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 188 AKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRL 267
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 268 APLAEDVRGNLRGNTEGLQKSLAelgghldQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDL 347
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLE-------QNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQEL 159
|
170
....*....|....
gi 1859630655 348 RDKVNSFFSTFKEK 361
Cdd:pfam01442 160 REKLEPQAEDLREK 173
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
211-364 |
3.16e-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: 67.29 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 211 KIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA 290
Cdd:pfam01442 8 ELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1859630655 291 elgghldQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQ 364
Cdd:pfam01442 88 -------ADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQ 154
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
52-147 |
1.41e-07 |
|
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: 51.11 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 52 SELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLREL 131
Cdd:pfam01442 80 EELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQEL 159
|
90
....*....|....*.
gi 1859630655 132 QQRLEPYADQLRTQVS 147
Cdd:pfam01442 160 REKLEPQAEDLREKLD 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-274 |
5.78e-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: 51.61 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 34 YFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELhERLAKDSEKLKEEIGK---ELEELR 110
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKleeALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 111 ARLLPHANEVSQKIGDNLRELQQRLEPYADQLrtQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKI 190
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 191 ---DQNVEELKGRLTPYADEfKVKIDQTVEELRRSLAPyAQDTQEKLNHQLEgltfQMKKNAEELKARISASAEELRQRL 267
Cdd:TIGR02169 864 eelEEELEELEAALRDLESR-LGDLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIE 937
|
....*..
gi 1859630655 268 APLAEDV 274
Cdd:TIGR02169 938 DPKGEDE 944
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
182-347 |
1.06e-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: 44.18 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 182 HADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAE 261
Cdd:pfam07902 118 HNDTIKTEIVESAEGIATRISEDTDKKLALINETISGIRREYQDADRQLSSSYQAGIEGLKATMASDKIGLQAEIQASAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 262 ELRQR----LAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVe 337
Cdd:pfam07902 198 GLSQRydneIRKLSAKITTTSSGTTEAYESKLDDLRAEFTRSNQGMRTELESKISGLQSTQQSTAYQISQEISNREGAV- 276
|
170
....*....|
gi 1859630655 338 ghlSFLEKDL 347
Cdd:pfam07902 277 ---SRVQQDL 283
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-306 |
2.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 128 LRELQQRLEPyADQLRTQVSTQAEQLRRQLTPYAQRMERVLRE-NADSLQASLRPHADELkAKIDQN---VEELKGRLtp 203
Cdd:COG4913 619 LAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAEL-ERLDASsddLAALEEQL-- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 204 yaDEFKVKIDQTVEELRRslapyAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAP---------LAEDV 274
Cdd:COG4913 695 --EELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaVEREL 767
|
170 180 190
....*....|....*....|....*....|..
gi 1859630655 275 RGNLRGNTEGLQKSLAELGGHLDQQVEEFRRR 306
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-347 |
1.54e-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: 40.81 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 89 ERLAKDSEKLKE---EIGKELEELRARLLPHANEVSQKigdnlrelqQRLEPYADQLRTQVSTQAEQLRRQLTPYAQRME 165
Cdd:TIGR02168 680 EELEEKIEELEEkiaELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 166 RVLRENAD-----SLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKvKIDQTVEELRRSLapyaQDTQEKLNHQLEG 240
Cdd:TIGR02168 751 QLSKELTEleaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAEL----TLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 241 LTfQMKKNAEELKARISASAEELRQRLAPLAEdVRGNLRGNTEGLQKSLAELGGHLDQ--QVEEFRRRVEPYGENFNKAL 318
Cdd:TIGR02168 826 LE-SLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNEraSLEEALALLRSELEELSEEL 903
|
250 260 270
....*....|....*....|....*....|....*
gi 1859630655 319 ------VQQMEQLRQKLGPHAGDVEGHLSFLEKDL 347
Cdd:TIGR02168 904 releskRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-330 |
2.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 64 DKLGEVNTYAGDLQKKLVPF--ATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVsqkigDNLRELQQRLEPYADQ 141
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFikRTENIEELIKEKEKELEEVLREINEISSELPELREEL-----EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 142 LrtqvsTQAEQLRRQLTPYAQRMERVLRENADSLqASLRPHADELKAKIdQNVEELKGRLTPYA--DEFKVKIDQTVEEL 219
Cdd:PRK03918 240 I-----EELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKV-KELKELKEKAEEYIklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 220 RRSLAPYAQDTQEkLNHQLEGLTfQMKKNAEELKARIsasaEELRQRLAPLAEDVRG-----NLRGNTEGLQKSLAELG- 293
Cdd:PRK03918 313 EKRLSRLEEEING-IEERIKELE-EKEERLEELKKKL----KELEKRLEELEERHELyeeakAKKEELERLKKRLTGLTp 386
|
250 260 270
....*....|....*....|....*....|....*..
gi 1859630655 294 GHLDQQVEEFRRRVEPYGENFNKaLVQQMEQLRQKLG 330
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISK-ITARIGELKKEIK 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-329 |
7.06e-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: 38.88 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 99 KEEIGKELEELRARLlphanevsQKIGDNLRELQQRLEPyadqLRTQVStQAEQLRR--------QLTPYAQRMERvLRE 170
Cdd:TIGR02168 174 RKETERKLERTRENL--------DRLEDILNELERQLKS----LERQAE-KAERYKElkaelrelELALLVLRLEE-LRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 171 NADSLQASLRPHADELKA------KIDQNVEELKGRLTPYADEFKV-------------KIDQTVEELRRSLApYAQDTQ 231
Cdd:TIGR02168 240 ELEELQEELKEAEEELEEltaelqELEEKLEELRLEVSELEEEIEElqkelyalaneisRLEQQKQILRERLA-NLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 232 EKLNHQLEGLtFQMKKNAEELKARISASAEELRQRLAPLAEDVRgnlrgNTEGLQKSLAELGGHLDQQVEEFRRRVepyg 311
Cdd:TIGR02168 319 EELEAQLEEL-ESKLDELAEELAELEEKLEELKEELESLEAELE-----ELEAELEELESRLEELEEQLETLRSKV---- 388
|
250
....*....|....*...
gi 1859630655 312 enfnKALVQQMEQLRQKL 329
Cdd:TIGR02168 389 ----AQLELQIASLNNEI 402
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-329 |
8.16e-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: 38.67 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 18 ARAEVSADQvatvmwDYFSQLSNNAKEAVEHLQKSELtqqlnalfqdKLGEVNTYAGDLQKKLVPFATELHERLAKDSEK 97
Cdd:pfam12128 483 ANAEVERLQ------SELRQARKRRDQASEALRQASR----------RLEERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 98 LKEEIGKELEE---LRARLLPHANEVSQKIGDNLRELQQRLEpyadqlRTQVSTQA---EQLRRQLTPY--AQRMERVLR 169
Cdd:pfam12128 547 WEQSIGKVISPellHRTDLDPEVWDGSVGGELNLYGVKLDLK------RIDVPEWAaseEELRERLDKAeeALQSAREKQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 170 ENADSLQASLRPHADELKAKID------QNVEELKGRLTPYADEFKVKIDQTVEELRRSlapyAQDTQEKLNHQLEGLTF 243
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDS----ANERLNSLEAQLKQLDK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859630655 244 QMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYG--ENFNKALVQQ 321
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGvdPDVIAKLKRE 776
|
....*...
gi 1859630655 322 MEQLRQKL 329
Cdd:pfam12128 777 IRTLERKI 784
|
|
|