|
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 |
2.38e-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: 148.95 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 61 LFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYAD 140
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 141 QLRTQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELR 220
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 50960038 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 |
4.68e-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: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 188 AKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRL 267
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 268 APLAEDVRGNLRGNTEGLQKSLAelgghldQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDL 347
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLE-------QNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQEL 159
|
170
....*....|....
gi 50960038 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 |
9.82e-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: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 34 YFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELhERLAKDSEKLKEEIGK---ELEELR 110
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKleeALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 111 ARLLPHANEVSQKIGDNLRELQQRLEPYADQLrtQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKI 190
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 191 ---DQNVEELKGRLTPYADEfKVKIDQTVEELRRSLAPyAQDTQEKLNHQLEgltfQMKKNAEELKARISASAEELRQRL 267
Cdd:TIGR02169 864 eelEEELEELEAALRDLESR-LGDLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIE 937
|
....*..
gi 50960038 268 APLAEDV 274
Cdd:TIGR02169 938 DPKGEDE 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-306 |
1.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 128 LRELQQRLEPyADQLRTQVNTQAEQLRRQLTPYAQRMERVLRE-NADSLQASLRPHADELkAKIDQN---VEELKGRLtp 203
Cdd:COG4913 619 LAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAEL-ERLDASsddLAALEEQL-- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 204 yaDEFKVKIDQTVEELRRslapyAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAP---------LAEDV 274
Cdd:COG4913 695 --EELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaVEREL 767
|
170 180 190
....*....|....*....|....*....|..
gi 50960038 275 RGNLRGNTEGLQKSLAELGGHLDQQVEEFRRR 306
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-330 |
2.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 64 DKLGEVNTYAGDLQKKLVPF--ATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVsqkigDNLRELQQRLEPYADQ 141
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFikRTENIEELIKEKEKELEEVLREINEISSELPELREEL-----EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 142 LrtqvnTQAEQLRRQLTPYAQRMERVLRENADSLqASLRPHADELKAKIdQNVEELKGRLTPYA--DEFKVKIDQTVEEL 219
Cdd:PRK03918 240 I-----EELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKV-KELKELKEKAEEYIklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 220 RRSLAPYAQDTQEkLNHQLEGLTfQMKKNAEELKARIsasaEELRQRLAPLAEDVRG-----NLRGNTEGLQKSLAELG- 293
Cdd:PRK03918 313 EKRLSRLEEEING-IEERIKELE-EKEERLEELKKKL----KELEKRLEELEERHELyeeakAKKEELERLKKRLTGLTp 386
|
250 260 270
....*....|....*....|....*....|....*..
gi 50960038 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 |
2.38e-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: 148.95 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 61 LFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYAD 140
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 141 QLRTQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELR 220
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 50960038 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 |
1.09e-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: 93.87 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 146 VNTQAEQLRRQLTPYAQRmervlrenadsLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAP 225
Cdd:pfam01442 9 LSTYAEELQEQLGPVAQE-----------LVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 226 YAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA----ELGGHLDQQVE 301
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLApyaeEVQAQLSQRLQ 157
|
170
....*....|..
gi 50960038 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 |
4.68e-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: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 188 AKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRL 267
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 268 APLAEDVRGNLRGNTEGLQKSLAelgghldQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDL 347
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLE-------QNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQEL 159
|
170
....*....|....
gi 50960038 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 |
2.76e-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: 67.67 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 211 KIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLA 290
Cdd:pfam01442 8 ELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50960038 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 ... |
12-168 |
5.65e-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: 58.04 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 12 LVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKS--ELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHE 89
Cdd:pfam01442 27 LVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNveELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50960038 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 |
9.82e-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: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 34 YFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELhERLAKDSEKLKEEIGK---ELEELR 110
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKleeALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 111 ARLLPHANEVSQKIGDNLRELQQRLEPYADQLrtQVNTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKI 190
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 191 ---DQNVEELKGRLTPYADEfKVKIDQTVEELRRSLAPyAQDTQEKLNHQLEgltfQMKKNAEELKARISASAEELRQRL 267
Cdd:TIGR02169 864 eelEEELEELEAALRDLESR-LGDLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIE 937
|
....*..
gi 50960038 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 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 182 HADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAE 261
Cdd:pfam07902 118 HNDTIKTEIVESAEGIATRISEDTDKKLALINETISGIRREYQDADRQLSSSYQAGIEGLKATMASDKIGLQAEIQASAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 262 ELRQR----LAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVe 337
Cdd:pfam07902 198 GLSQRydneIRKLSAKITTTSSGTTEAYESKLDDLRAEFTRSNQGMRTELESKISGLQSTQQSTAYQISQEISNREGAV- 276
|
170
....*....|
gi 50960038 338 ghlSFLEKDL 347
Cdd:pfam07902 277 ---SRVQQDL 283
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-306 |
1.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 128 LRELQQRLEPyADQLRTQVNTQAEQLRRQLTPYAQRMERVLRE-NADSLQASLRPHADELkAKIDQN---VEELKGRLtp 203
Cdd:COG4913 619 LAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAEL-ERLDASsddLAALEEQL-- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 204 yaDEFKVKIDQTVEELRRslapyAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAP---------LAEDV 274
Cdd:COG4913 695 --EELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaVEREL 767
|
170 180 190
....*....|....*....|....*....|..
gi 50960038 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 |
3.41e-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: 41.10 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 53 ELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAkdseklkeeigKELEELRARLLPHANEVSQKIGDNLRELQ 132
Cdd:pfam01442 92 ELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLA-----------ERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
90
....*....|....*
gi 50960038 133 QRLEPYADQLRTQVN 147
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-347 |
1.23e-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: 41.20 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 89 ERLAKDSEKLKE---EIGKELEELRARLLPHANEVSQKigdnlrelqQRLEPYADQLRTQVNTQAEQLRRQLTPYAQRME 165
Cdd:TIGR02168 680 EELEEKIEELEEkiaELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 166 RVLRENAD-----SLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKvKIDQTVEELRRSLapyaQDTQEKLNHQLEG 240
Cdd:TIGR02168 751 QLSKELTEleaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAEL----TLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 241 LTfQMKKNAEELKARISASAEELRQRLAPLAEdVRGNLRGNTEGLQKSLAELGGHLDQ--QVEEFRRRVEPYGENFNKAL 318
Cdd:TIGR02168 826 LE-SLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNEraSLEEALALLRSELEELSEEL 903
|
250 260 270
....*....|....*....|....*....|....*
gi 50960038 319 ------VQQMEQLRQKLGPHAGDVEGHLSFLEKDL 347
Cdd:TIGR02168 904 releskRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-330 |
2.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 64 DKLGEVNTYAGDLQKKLVPF--ATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVsqkigDNLRELQQRLEPYADQ 141
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFikRTENIEELIKEKEKELEEVLREINEISSELPELREEL-----EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 142 LrtqvnTQAEQLRRQLTPYAQRMERVLRENADSLqASLRPHADELKAKIdQNVEELKGRLTPYA--DEFKVKIDQTVEEL 219
Cdd:PRK03918 240 I-----EELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKV-KELKELKEKAEEYIklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 220 RRSLAPYAQDTQEkLNHQLEGLTfQMKKNAEELKARIsasaEELRQRLAPLAEDVRG-----NLRGNTEGLQKSLAELG- 293
Cdd:PRK03918 313 EKRLSRLEEEING-IEERIKELE-EKEERLEELKKKL----KELEKRLEELEERHELyeeakAKKEELERLKKRLTGLTp 386
|
250 260 270
....*....|....*....|....*....|....*..
gi 50960038 294 GHLDQQVEEFRRRVEPYGENFNKaLVQQMEQLRQKLG 330
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISK-ITARIGELKKEIK 422
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-329 |
2.66e-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: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 18 ARAEVSADQvatvmwDYFSQLSNNAKEAVEHLQKSELtqqlnalfqdKLGEVNTYAGDLQKKLVPFATELHERLAKDSEK 97
Cdd:pfam12128 483 ANAEVERLQ------SELRQARKRRDQASEALRQASR----------RLEERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 98 LKEEIGKELEE---LRARLLPHANEVSQKIGDNLRELQQRLEpyadqlRTQVNTQA---EQLRRQLTPY--AQRMERVLR 169
Cdd:pfam12128 547 WEQSIGKVISPellHRTDLDPEVWDGSVGGELNLYGVKLDLK------RIDVPEWAaseEELRERLDKAeeALQSAREKQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 170 ENADSLQASLRPHADELKAKID------QNVEELKGRLTPYADEFKVKIDQTVEELRRSlapyAQDTQEKLNHQLEGLTF 243
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDS----ANERLNSLEAQLKQLDK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 244 QMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYG--ENFNKALVQQ 321
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGvdPDVIAKLKRE 776
|
....*...
gi 50960038 322 MEQLRQKL 329
Cdd:pfam12128 777 IRTLERKI 784
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-329 |
5.36e-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: 39.27 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 99 KEEIGKELEELRARLlphanevsQKIGDNLRELQQRLEP-------------YADQLR-----------TQVNTQAEQLR 154
Cdd:TIGR02168 174 RKETERKLERTRENL--------DRLEDILNELERQLKSlerqaekaerykeLKAELRelelallvlrlEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 155 RQLTPYAQRMERvLRENADSLQASLRPHADElKAKIDQNVEELKGRLTPYADEFKvKIDQTVEELRRSLApYAQDTQEKL 234
Cdd:TIGR02168 246 EELKEAEEELEE-LTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEIS-RLEQQKQILRERLA-NLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 235 NHQLEGLtFQMKKNAEELKARISASAEELRQRLAPLAEDVRgnlrgNTEGLQKSLAELGGHLDQQVEEFRRRVepygenf 314
Cdd:TIGR02168 322 EAQLEEL-ESKLDELAEELAELEEKLEELKEELESLEAELE-----ELEAELEELESRLEELEEQLETLRSKV------- 388
|
250
....*....|....*
gi 50960038 315 nKALVQQMEQLRQKL 329
Cdd:TIGR02168 389 -AQLELQIASLNNEI 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
41-309 |
9.98e-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: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 41 NAKEAVEHLQK--SELTQQLNALfQDKLGEVNTYAGDLQKKLvpfatELHERLAK------DSEKLKEEIGkELEELRAR 112
Cdd:COG4913 607 DNRAKLAALEAelAELEEELAEA-EERLEALEAELDALQERR-----EALQRLAEyswdeiDVASAEREIA-ELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 113 LLphanevsqKIGDNLRELQQRLEpyadQLRTQVNTQAEQLRRqltpyAQRMERVLRENADSLQASLRPHADELKAKIDQ 192
Cdd:COG4913 680 LD--------ASSDDLAALEEQLE----ELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50960038 193 NVEELKGRLTPYADEfkVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARIS------ASAEELRQR 266
Cdd:COG4913 743 ARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadlESLPEYLAL 820
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50960038 267 LAPLAEDV--------RGNLRGNTEGlqkSLAELGGHLDQQVEEFRRRVEP 309
Cdd:COG4913 821 LDRLEEDGlpeyeerfKELLNENSIE---FVADLLSKLRRAIREIKERIDP 868
|
|
|