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Conserved domains on  [gi|4557321|ref|NP_000030.1|]
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apolipoprotein A-I isoform 1 preproprotein [Homo sapiens]

Protein Classification

Apolipoprotein domain-containing protein (domain architecture ID 12019813)

Apolipoprotein domain-containing protein

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 ...
74-242 4.00e-53

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: 307549  Cd Length: 170  Bit Score: 173.25  E-value: 4.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     74 WDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEG 153
Cdd:pfam01442   1 LDELSAYAAELQEQLGPLTQELIDRLSKETEELRERLQKDLEEVREKLEPYLDELQQKLGQNVEELRQRLEPYTEELRER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321    154 ARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKP 233
Cdd:pfam01442  81 LNADAEELQEKLAPYSEELRERLEQNVDELREQLGPYSEELRQKLDQRLEELKERLAPYAEELKERLSQQVEELREKLEP 160

                  ....*....
gi 4557321    234 ALEDLRQGL 242
Cdd:pfam01442 161 QAEDLREKL 169
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
74-242 4.00e-53

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: 307549  Cd Length: 170  Bit Score: 173.25  E-value: 4.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     74 WDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEG 153
Cdd:pfam01442   1 LDELSAYAAELQEQLGPLTQELIDRLSKETEELRERLQKDLEEVREKLEPYLDELQQKLGQNVEELRQRLEPYTEELRER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321    154 ARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKP 233
Cdd:pfam01442  81 LNADAEELQEKLAPYSEELRERLEQNVDELREQLGPYSEELRQKLDQRLEELKERLAPYAEELKERLSQQVEELREKLEP 160

                  ....*....
gi 4557321    234 ALEDLRQGL 242
Cdd:pfam01442 161 QAEDLREKL 169
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
85-207 9.97e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750  Cd Length: 782  Bit Score: 43.28  E-value: 9.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321    85 REQLGPVTQEFwDNLEKETEGLRQEMSKDLEEVKAKVQPYlDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEK 164
Cdd:PRK00409 508 KKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE 585
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 4557321   165 LSPLGEEMRDRARAHVDALRTHLApysDELRQRLAARLEALKE 207
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHEL---IEARKRLNKANEKKEK 625
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
97-240 5.61e-04

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  Cd Length: 1164  Bit Score: 40.82  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321      97 DNLEKETEGLRqemsKDLEEVKAKVQPYLDDFQKKwQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLGEEMrdra 176
Cdd:TIGR02169  332 DKLLAEIEELE----REIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI---- 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557321     177 rahvDALRTHLAPYSDELRQRLAARLEAlkENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQ 240
Cdd:TIGR02169  402 ----NELKRELDRLQEELQRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
74-242 4.00e-53

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: 307549  Cd Length: 170  Bit Score: 173.25  E-value: 4.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     74 WDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEG 153
Cdd:pfam01442   1 LDELSAYAAELQEQLGPLTQELIDRLSKETEELRERLQKDLEEVREKLEPYLDELQQKLGQNVEELRQRLEPYTEELRER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321    154 ARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKP 233
Cdd:pfam01442  81 LNADAEELQEKLAPYSEELRERLEQNVDELREQLGPYSEELRQKLDQRLEELKERLAPYAEELKERLSQQVEELREKLEP 160

                  ....*....
gi 4557321    234 ALEDLRQGL 242
Cdd:pfam01442 161 QAEDLREKL 169
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
85-207 9.97e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750  Cd Length: 782  Bit Score: 43.28  E-value: 9.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321    85 REQLGPVTQEFwDNLEKETEGLRQEMSKDLEEVKAKVQPYlDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEK 164
Cdd:PRK00409 508 KKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE 585
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 4557321   165 LSPLGEEMRDRARAHVDALRTHLApysDELRQRLAARLEALKE 207
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHEL---IEARKRLNKANEKKEK 625
Exonuc_VII_L pfam02601
Exonuclease VII, large subunit; This family consist of exonuclease VII, large subunit EC:3.1. ...
111-205 1.04e-04

Exonuclease VII, large subunit; This family consist of exonuclease VII, large subunit EC:3.1.11.6 This enzyme catalyzes exonucleolytic cleavage in either 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. This exonuclease VII enzyme is composed of one large subunit and 4 small ones.


Pssm-ID: 308296  Cd Length: 289  Bit Score: 42.44  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321    111 SKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQ------EGARQKLHELQEKLSPLGEEMRDRARAHVDALR 184
Cdd:pfam02601 139 VPDRAELLARLEQLQQRLARAMQRRLERRRQRLDRLARRLPspsrllERQRQRLDELSQRLERALARRLARARQRLERLE 218
                          90       100
                  ....*....|....*....|....*.
gi 4557321    185 THLAPYS--DELRQRL---AARLEAL 205
Cdd:pfam02601 219 QRLKAERllERKRQRLellASRLEAL 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
97-240 5.61e-04

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  Cd Length: 1164  Bit Score: 40.82  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321      97 DNLEKETEGLRqemsKDLEEVKAKVQPYLDDFQKKwQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLGEEMrdra 176
Cdd:TIGR02169  332 DKLLAEIEELE----REIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI---- 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557321     177 rahvDALRTHLAPYSDELRQRLAARLEAlkENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQ 240
Cdd:TIGR02169  402 ----NELKRELDRLQEELQRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
57-238 3.30e-03

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  Cd Length: 1164  Bit Score: 38.51  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321      57 FEGSALGKQLNlKLLDNWDSVTSTFSKLREQLGPVTQEFwDNLEKETEGLRQemskDLEEVKAKVQPYLDDFQKKWQEEM 136
Cdd:TIGR02169  223 YEGYELLKEKE-ALERQKEAIERQLASLEEELEKLTEEI-SELEKRLEEIEQ----LLEELNKKIKDLGEEEQLRVKEKI 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     137 ELYRQKVEPLRAELQEGARQkLHELQEKLSPLgEEMRDRARAHVDALRTHLAPYSDELRQrLAARLEALKENGGARLAEY 216
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERE-LEDAEERLAKL-EAEIDKLLAEIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAEL 373
                          170       180
                   ....*....|....*....|....
gi 4557321     217 HAKATEHLSTLSE--KAKPALEDL 238
Cdd:TIGR02169  374 EEVDKEFAETRDElkDYREKLEKL 397
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
99-266 6.57e-03

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  Cd Length: 1164  Bit Score: 37.74  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321      99 LEKETEGLRQEMSKDLEEVKAkvqpyLDDFQKKWQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLgeeMRDRARA 178
Cdd:TIGR02169  721 IEKEIEQLEQEEEKLKERLEE-----LEEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDL---EARLSHS 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     179 HVDALRTHLAPYSDElRQRLAARLEAL--KENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGlLPVLESFKVSFLSA 256
Cdd:TIGR02169  792 RIPEIQAELSKLEEE-VSRIEARLREIeqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-IENLNGKKEELEEE 869
                          170
                   ....*....|
gi 4557321     257 LEEYTKKLNT 266
Cdd:TIGR02169  870 LEELEAALRD 879
prfA TIGR00019
peptide chain release factor 1; This model describes peptide chain release factor 1 (PrfA, ...
70-174 6.62e-03

peptide chain release factor 1; This model describes peptide chain release factor 1 (PrfA, RF-1), and excludes the related peptide chain release factor 2 (PrfB, RF-2). RF-1 helps recognize and terminate translation at UAA and UAG stop codons. The mitochondrial release factors are prfA-like, although not included above the trusted cutoff for this model. RF-1 does not have a translational frameshift. [Protein synthesis, Translation factors]


Pssm-ID: 129130  Cd Length: 360  Bit Score: 37.37  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     70 LLDNWDSVTSTFSKLREQLGPVT----QEFWDNLEKEteglrqemSKDLEEVKAKVQPYlddfqKKWQEEMELYRQKVEP 145
Cdd:TIGR00019   5 LLEKLESLLERYEELEALLSDPEvisdQDKLRKLSKE--------YSQLEEIVDCYREY-----QQAQEDIKEAKEILEE 71
                          90       100
                  ....*....|....*....|....*....
gi 4557321    146 LRAELQEGARQKLHELQEKLSPLGEEMRD 174
Cdd:TIGR00019  72 SDPEMREMAKEELEELEEKIEELEEQLKV 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-240 8.12e-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  Cd Length: 1179  Bit Score: 37.34  E-value: 8.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321      73 NWDSVTSTFSKLREQLGpVTQEFWDNLEKETEglrqEMSKDLEEVKAKVQPYLDDFqKKWQEEMELYRQKVEPLRAELQE 152
Cdd:TIGR02168  289 ELYALANEISRLEQQKQ-ILRERLANLERQLE----ELEAQLEELESKLDELAEEL-AELEEKLEELKEELESLEAELEE 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557321     153 gARQKLHELQEKLSPLGEEMRDRARA------HVDALRTHLAPYSDELrQRLAARLEALKENGGARLAEYHAKATEHLST 226
Cdd:TIGR02168  363 -LEAELEELESRLEELEEQLETLRSKvaqlelQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQA 440
                          170
                   ....*....|....
gi 4557321     227 LSEKAKPALEDLRQ 240
Cdd:TIGR02168  441 ELEELEEELEELQE 454
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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