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Conserved domains on  [gi|5901944|ref|NP_008977|]
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EMILIN-1 precursor [Homo sapiens]

Protein Classification

EMI and C1q domain-containing protein( domain architecture ID 13728153)

protein containing domains EMI, Smc, SMC_prok_B, and C1q

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
57-126 3.56e-22

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 90.94  E-value: 3.56e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5901944      57 RNWCAYvvtRTVSCVLEDGVETYVK--YQP----CaWGQPQCPqsiMYRRFLRPRYRVAYKTVTDMEWRCCQGYGG 126
Cdd:pfam07546    1 RNVCAY---KVVSCVVVTGTESYVQpvYKPyltwC-AGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
C1q super family cl23878
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
869-1010 3.11e-14

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


The actual alignment was detected with superfamily member smart00110:

Pssm-ID: 420072  Cd Length: 135  Bit Score: 70.41  E-value: 3.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944      869 PQVAFSAALSLPRSEPG-TVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTgHRHEKVEAVLSRSNQGVArvdsgg 947
Cdd:smart00110    6 PRSAFSVIRSNRPPPPGqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE-SKGRNVKVSLMKNGIQVM------ 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5901944      948 YEPEGLENkpvaesqpspGTLGVFS--LILPLQAGDTVCV-------DLVMGQLAHSeepltIFSGALLYGD 1010
Cdd:smart00110   79 STYDEYQK----------GLYDVASggALLQLRQGDQVWLelpdeknGLYAGEYVDS-----TFSGFLLFPD 135
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
638-807 2.22e-08

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     638 SALQALQGELSEVILSFSSLNDSLNELQTTVEGQGADLADLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQA 717
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     718 gqcpslegrlgrlegvcERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSL 797
Cdd:TIGR02168  340 -----------------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170
                   ....*....|
gi 5901944     798 QLLEDRLHQL 807
Cdd:TIGR02168  403 ERLEARLERL 412
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-572 5.89e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   176 EKVQQLEEQVQSL---TKELQGLRGVLQGLSGRLAEdVQRAVETAFNGRQQPADAAARPGVHETLNEIQHQLQLLDTRVS 252
Cdd:COG4717   71 KELKELEEELKEAeekEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   253 THDQELGHLNNHHGGSSSSGGSRapapasappgpsEELLRQLEQRLQESCSVCLAGLDGFRRQQQEDRERLRAMEKLLAS 332
Cdd:COG4717  150 ELEERLEELRELEEELEELEAEL------------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   333 VEERQRHLAglAVGRRPPQECCSPELGRRLAELERRLDVVAGSVTVLS------GRRGTELGGAAGQGGHPPGYTSLASR 406
Cdd:COG4717  218 AQEELEELE--EELEQLENELEAAALEERLKEARLLLLIAAALLALLGlggsllSLILTIAGVLFLVLGLLALLFLLLAR 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   407 ----LSRLEDRFNSTLGPSEEQEESWPGAPGGLSHWLPAARGRLEQLGGLLANVSGELGGRLDLLEE-QVAGAMQACGQL 481
Cdd:COG4717  296 ekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAAL 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   482 CSGAPGEQDSQVSEILSA------LERRVLDSEGQLRLVGSGLHTveaagEARQATLEGLQEVVGRLQDRVDAQDETAAE 555
Cdd:COG4717  376 LAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEE-----LLEALDEEELEEELEELEEELEELEEELEE 450
                        410
                 ....*....|....*..
gi 5901944   556 FTLRLNLTAARLGQLEG 572
Cdd:COG4717  451 LREELAELEAELEQLEE 467
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
57-126 3.56e-22

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 90.94  E-value: 3.56e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5901944      57 RNWCAYvvtRTVSCVLEDGVETYVK--YQP----CaWGQPQCPqsiMYRRFLRPRYRVAYKTVTDMEWRCCQGYGG 126
Cdd:pfam07546    1 RNVCAY---KVVSCVVVTGTESYVQpvYKPyltwC-AGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
869-1010 3.11e-14

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 70.41  E-value: 3.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944      869 PQVAFSAALSLPRSEPG-TVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTgHRHEKVEAVLSRSNQGVArvdsgg 947
Cdd:smart00110    6 PRSAFSVIRSNRPPPPGqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE-SKGRNVKVSLMKNGIQVM------ 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5901944      948 YEPEGLENkpvaesqpspGTLGVFS--LILPLQAGDTVCV-------DLVMGQLAHSeepltIFSGALLYGD 1010
Cdd:smart00110   79 STYDEYQK----------GLYDVASggALLQLRQGDQVWLelpdeknGLYAGEYVDS-----TFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
872-1007 3.85e-12

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 64.23  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     872 AFSAALSLPRSEPGT--VPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHRHEKVEAVLSRSNQGVARVdsggye 949
Cdd:pfam00386    1 AFSAGRTTGLTAPNEqpVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSF------ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5901944     950 peglenkpvaESQPSPGTLGVFS--LILPLQAGDTVCVDLVMGQLAHSEE--PLTIFSGALL 1007
Cdd:pfam00386   75 ----------YDQPQKGSLDVASgsVVLELQRGDEVWLQLTGYNGLYYDGsdTDSTFSGFLL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
638-807 2.22e-08

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: 58.53  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     638 SALQALQGELSEVILSFSSLNDSLNELQTTVEGQGADLADLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQA 717
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     718 gqcpslegrlgrlegvcERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSL 797
Cdd:TIGR02168  340 -----------------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170
                   ....*....|
gi 5901944     798 QLLEDRLHQL 807
Cdd:TIGR02168  403 ERLEARLERL 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-572 5.89e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   176 EKVQQLEEQVQSL---TKELQGLRGVLQGLSGRLAEdVQRAVETAFNGRQQPADAAARPGVHETLNEIQHQLQLLDTRVS 252
Cdd:COG4717   71 KELKELEEELKEAeekEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   253 THDQELGHLNNHHGGSSSSGGSRapapasappgpsEELLRQLEQRLQESCSVCLAGLDGFRRQQQEDRERLRAMEKLLAS 332
Cdd:COG4717  150 ELEERLEELRELEEELEELEAEL------------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   333 VEERQRHLAglAVGRRPPQECCSPELGRRLAELERRLDVVAGSVTVLS------GRRGTELGGAAGQGGHPPGYTSLASR 406
Cdd:COG4717  218 AQEELEELE--EELEQLENELEAAALEERLKEARLLLLIAAALLALLGlggsllSLILTIAGVLFLVLGLLALLFLLLAR 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   407 ----LSRLEDRFNSTLGPSEEQEESWPGAPGGLSHWLPAARGRLEQLGGLLANVSGELGGRLDLLEE-QVAGAMQACGQL 481
Cdd:COG4717  296 ekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAAL 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   482 CSGAPGEQDSQVSEILSA------LERRVLDSEGQLRLVGSGLHTveaagEARQATLEGLQEVVGRLQDRVDAQDETAAE 555
Cdd:COG4717  376 LAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEE-----LLEALDEEELEEELEELEEELEELEEELEE 450
                        410
                 ....*....|....*..
gi 5901944   556 FTLRLNLTAARLGQLEG 572
Cdd:COG4717  451 LREELAELEAELEQLEE 467
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
57-126 3.56e-22

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 90.94  E-value: 3.56e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5901944      57 RNWCAYvvtRTVSCVLEDGVETYVK--YQP----CaWGQPQCPqsiMYRRFLRPRYRVAYKTVTDMEWRCCQGYGG 126
Cdd:pfam07546    1 RNVCAY---KVVSCVVVTGTESYVQpvYKPyltwC-AGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
869-1010 3.11e-14

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 70.41  E-value: 3.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944      869 PQVAFSAALSLPRSEPG-TVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTgHRHEKVEAVLSRSNQGVArvdsgg 947
Cdd:smart00110    6 PRSAFSVIRSNRPPPPGqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE-SKGRNVKVSLMKNGIQVM------ 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5901944      948 YEPEGLENkpvaesqpspGTLGVFS--LILPLQAGDTVCV-------DLVMGQLAHSeepltIFSGALLYGD 1010
Cdd:smart00110   79 STYDEYQK----------GLYDVASggALLQLRQGDQVWLelpdeknGLYAGEYVDS-----TFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
872-1007 3.85e-12

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 64.23  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     872 AFSAALSLPRSEPGT--VPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHRHEKVEAVLSRSNQGVARVdsggye 949
Cdd:pfam00386    1 AFSAGRTTGLTAPNEqpVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSF------ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5901944     950 peglenkpvaESQPSPGTLGVFS--LILPLQAGDTVCVDLVMGQLAHSEE--PLTIFSGALL 1007
Cdd:pfam00386   75 ----------YDQPQKGSLDVASgsVVLELQRGDEVWLQLTGYNGLYYDGsdTDSTFSGFLL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
638-807 2.22e-08

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: 58.53  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     638 SALQALQGELSEVILSFSSLNDSLNELQTTVEGQGADLADLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQA 717
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     718 gqcpslegrlgrlegvcERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSL 797
Cdd:TIGR02168  340 -----------------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170
                   ....*....|
gi 5901944     798 QLLEDRLHQL 807
Cdd:TIGR02168  403 ERLEARLERL 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
176-810 8.42e-05

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: 46.59  E-value: 8.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     176 EKVQQLEEQVQSLTKELQGLRGVLQGLSGRLAEDVqravetafngrqqpadaAARPGVHETLNEIQHQLQLLDTRVSTHD 255
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELR-----------------LEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     256 QELGHLNnhhggssssggsrapapasappgpseELLRQLEQRLQESCsvclAGLDGFRRQQQEDRERLRAMEKLLASVEE 335
Cdd:TIGR02168  302 QQKQILR--------------------------ERLANLERQLEELE----AQLEELESKLDELAEELAELEEKLEELKE 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     336 RQRHLAGLAVGRRPPQEccspELGRRLAELERRLDvvagsvTVLSGRRGTELGGAagqgghppgytSLASRLSRLEDRFN 415
Cdd:TIGR02168  352 ELESLEAELEELEAELE----ELESRLEELEEQLE------TLRSKVAQLELQIA-----------SLNNEIERLEARLE 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     416 STLGPSEEQEESWPGAPGGLS-HWLPAARGRLEQLGGLLANVSGELG---GRLDLLEEQVAGAMQACGQLcsgapGEQDS 491
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELErleEALEELREELEEAEQALDAA-----ERELA 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     492 QVSEILSALERRVLDSEGQLRlvgsGLHTVEAAGEarqatleGLQEVVGRLQD--RVDAQDETAAEFTLRLNLTA----- 564
Cdd:TIGR02168  486 QLQARLDSLERLQENLEGFSE----GVKALLKNQS-------GLSGILGVLSEliSVDEGYEAAIEAALGGRLQAvvven 554
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     565 -------------ARLG---------------QLEGLLQAHGDEGC-GACGGVQEELGRLRDGVErcscPLLPPRGPGAG 615
Cdd:TIGR02168  555 lnaakkaiaflkqNELGrvtflpldsikgteiQGNDREILKNIEGFlGVAKDLVKFDPKLRKALS----YLLGGVLVVDD 630
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     616 PGVGGPSRGPLD---------------GFSVFGGSSGSALQALqgelsevilsfsSLNDSLNELQTTVEGQGADLADLGA 680
Cdd:TIGR02168  631 LDNALELAKKLRpgyrivtldgdlvrpGGVITGGSAKTNSSIL------------ERRREIEELEEKIEELEEKIAELEK 698
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944     681 TKDRIISEINRLQQEATEHATESEERFRGLEEGQAQAGQcpsLEGRLGRLEGVCERLDTVAGGLQGLREGLSRHVAGLWA 760
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR---LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 5901944     761 GLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSLQLLEDRLHQLSLK 810
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-572 5.89e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   176 EKVQQLEEQVQSL---TKELQGLRGVLQGLSGRLAEdVQRAVETAFNGRQQPADAAARPGVHETLNEIQHQLQLLDTRVS 252
Cdd:COG4717   71 KELKELEEELKEAeekEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   253 THDQELGHLNNHHGGSSSSGGSRapapasappgpsEELLRQLEQRLQESCSVCLAGLDGFRRQQQEDRERLRAMEKLLAS 332
Cdd:COG4717  150 ELEERLEELRELEEELEELEAEL------------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   333 VEERQRHLAglAVGRRPPQECCSPELGRRLAELERRLDVVAGSVTVLS------GRRGTELGGAAGQGGHPPGYTSLASR 406
Cdd:COG4717  218 AQEELEELE--EELEQLENELEAAALEERLKEARLLLLIAAALLALLGlggsllSLILTIAGVLFLVLGLLALLFLLLAR 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   407 ----LSRLEDRFNSTLGPSEEQEESWPGAPGGLSHWLPAARGRLEQLGGLLANVSGELGGRLDLLEE-QVAGAMQACGQL 481
Cdd:COG4717  296 ekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAAL 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901944   482 CSGAPGEQDSQVSEILSA------LERRVLDSEGQLRLVGSGLHTveaagEARQATLEGLQEVVGRLQDRVDAQDETAAE 555
Cdd:COG4717  376 LAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEE-----LLEALDEEELEEELEELEEELEELEEELEE 450
                        410
                 ....*....|....*..
gi 5901944   556 FTLRLNLTAARLGQLEG 572
Cdd:COG4717  451 LREELAELEAELEQLEE 467
 
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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