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Conserved domains on  [gi|50960038|gb|AAH74764|]
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Apolipoprotein A-IV [Homo sapiens]

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 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
 
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
 
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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