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Conserved domains on  [gi|1859630655|sp|P06727|]
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RecName: Full=Apolipoprotein A-IV; Short=Apo-AIV; Short=ApoA-IV; AltName: Full=Apolipoprotein A4; Flags: Precursor

Protein Classification

apolipoprotein A1/A4/E family protein( domain architecture ID 12019813)

apolipoprotein A1/A4/E family protein associates with lipid particles and may function in lipoprotein-mediated lipid transport

Graphical summary

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List of domain hits

 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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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