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Conserved domains on  [gi|19527130|ref|NP_598679|]
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EMILIN-1 precursor [Mus musculus]

Protein Classification

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 ...
57-128 2.38e-23

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: 94.41  E-value: 2.38e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527130     57 RNWCAYvvtRTVSCVLEDGVETIVKPDYQP----CgWGQPHCSrsiMYRSFLRPRYRVAYKTVTDMEWRCCQGYGG 128
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 ...
870-1011 1.25e-15

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: 74.65  E-value: 1.25e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130     870 PRVAFSAALSLPRSEPG-TVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTgHRHEKVEAVLSRSNLGVARiDSGG 948
Cdd:smart00110    6 PRSAFSVIRSNRPPPPGqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE-SKGRNVKVSLMKNGIQVMS-TYDE 83
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130     949 YEPEGLEnkpvaesQPSPGAlgvfslILPLQVGDTVCI-------DLVMGQLAHSeepltIFSGALLYED 1011
Cdd:smart00110   84 YQKGLYD-------VASGGA------LLQLRQGDQVWLelpdeknGLYAGEYVDS-----TFSGFLLFPD 135
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
639-808 5.02e-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: 57.37  E-value: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    639 SALQALQGELSEVILTFSSLNDSLHELQTTVEGQGADLADLGATKDSIISEINRLQQEATEHVTESEERFRGLEEGQAQA 718
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    719 gqcpslegrlgrlegvcERLDTVAGGLQGLREGLSRHVAGLWAAVRESNSTSLTQAALLEKLLGGQAGLGRRLGALNNSL 798
Cdd:TIGR02168  340 -----------------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170
                   ....*....|
gi 19527130    799 LLLEDRLQQL 808
Cdd:TIGR02168  403 ERLEARLERL 412
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
170-573 2.35e-03

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: 41.68  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  170 GGEGPVESEKVQQLERQVKSL---TKELQGLRGVLQGMNGRLAEdVQRAVDTVFNGRQQPADAAARPGVHETLSEIQQQL 246
Cdd:COG4717   63 GRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  247 QLLDNRVSTHDQELGHLNNHHNGGPGGGGRAsgpvpvpsgpsEELLRQLERQLQESCSVCLTGLDGFRQQQQEDRERLRT 326
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELEELEAEL-----------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  327 LEKLMSSMEERQQQLVGPAMARRPPQEccPPELGRRVSELERRLdVVTGSLTVLSGRRGSELG--------GAAGQGGHP 398
Cdd:COG4717  211 LEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLL-LIAAALLALLGLGGSLLSliltiagvLFLVLGLLA 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  399 PGYTSLASRLSRLEDRFNSTLGPSEE---QEKNWPGGPGRLGHWLPAAPGRLEKLEGLLANVSRELGGRMDLLEE-QVAG 474
Cdd:COG4717  288 LLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEE 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  475 AVRTCGQICSGAPGEQDSRVNEILSALERRVlDSEGRLQLVGSGL--HEAEAAGEAQQAVLEGLQGLLSRLRERMDAQEE 552
Cdd:COG4717  368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEE 446
                        410       420
                 ....*....|....*....|.
gi 19527130  553 TAAEILLRLNLTAAQLSQLEG 573
Cdd:COG4717  447 ELEELREELAELEAELEQLEE 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 ...
57-128 2.38e-23

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: 94.41  E-value: 2.38e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527130     57 RNWCAYvvtRTVSCVLEDGVETIVKPDYQP----CgWGQPHCSrsiMYRSFLRPRYRVAYKTVTDMEWRCCQGYGG 128
Cdd:pfam07546    1 RNVCAY---KVVSCVVVTGTESYVQPVYKPyltwC-AGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
870-1011 1.25e-15

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: 74.65  E-value: 1.25e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130     870 PRVAFSAALSLPRSEPG-TVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTgHRHEKVEAVLSRSNLGVARiDSGG 948
Cdd:smart00110    6 PRSAFSVIRSNRPPPPGqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE-SKGRNVKVSLMKNGIQVMS-TYDE 83
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130     949 YEPEGLEnkpvaesQPSPGAlgvfslILPLQVGDTVCI-------DLVMGQLAHSeepltIFSGALLYED 1011
Cdd:smart00110   84 YQKGLYD-------VASGGA------LLQLRQGDQVWLelpdeknGLYAGEYVDS-----TFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
873-1008 1.94e-11

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: 62.30  E-value: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    873 AFSAALSLPRSEPGT--VPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHrhekveavlSRSNLGVARIDSGgye 950
Cdd:pfam00386    1 AFSAGRTTGLTAPNEqpVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTV---------DGKSLYVSLVKNG--- 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527130    951 peglenKPVA--ESQPSPGALGVFS--LILPLQVGDTVCIDLVMGQLAHSEE--PLTIFSGALL 1008
Cdd:pfam00386   69 ------QEVVsfYDQPQKGSLDVASgsVVLELQRGDEVWLQLTGYNGLYYDGsdTDSTFSGFLL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
639-808 5.02e-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: 57.37  E-value: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    639 SALQALQGELSEVILTFSSLNDSLHELQTTVEGQGADLADLGATKDSIISEINRLQQEATEHVTESEERFRGLEEGQAQA 718
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    719 gqcpslegrlgrlegvcERLDTVAGGLQGLREGLSRHVAGLWAAVRESNSTSLTQAALLEKLLGGQAGLGRRLGALNNSL 798
Cdd:TIGR02168  340 -----------------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170
                   ....*....|
gi 19527130    799 LLLEDRLQQL 808
Cdd:TIGR02168  403 ERLEARLERL 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
170-573 2.35e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  170 GGEGPVESEKVQQLERQVKSL---TKELQGLRGVLQGMNGRLAEdVQRAVDTVFNGRQQPADAAARPGVHETLSEIQQQL 246
Cdd:COG4717   63 GRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  247 QLLDNRVSTHDQELGHLNNHHNGGPGGGGRAsgpvpvpsgpsEELLRQLERQLQESCSVCLTGLDGFRQQQQEDRERLRT 326
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELEELEAEL-----------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  327 LEKLMSSMEERQQQLVGPAMARRPPQEccPPELGRRVSELERRLdVVTGSLTVLSGRRGSELG--------GAAGQGGHP 398
Cdd:COG4717  211 LEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLL-LIAAALLALLGLGGSLLSliltiagvLFLVLGLLA 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  399 PGYTSLASRLSRLEDRFNSTLGPSEE---QEKNWPGGPGRLGHWLPAAPGRLEKLEGLLANVSRELGGRMDLLEE-QVAG 474
Cdd:COG4717  288 LLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEE 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  475 AVRTCGQICSGAPGEQDSRVNEILSALERRVlDSEGRLQLVGSGL--HEAEAAGEAQQAVLEGLQGLLSRLRERMDAQEE 552
Cdd:COG4717  368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEE 446
                        410       420
                 ....*....|....*....|.
gi 19527130  553 TAAEILLRLNLTAAQLSQLEG 573
Cdd:COG4717  447 ELEELREELAELEAELEQLEE 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 ...
57-128 2.38e-23

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: 94.41  E-value: 2.38e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527130     57 RNWCAYvvtRTVSCVLEDGVETIVKPDYQP----CgWGQPHCSrsiMYRSFLRPRYRVAYKTVTDMEWRCCQGYGG 128
Cdd:pfam07546    1 RNVCAY---KVVSCVVVTGTESYVQPVYKPyltwC-AGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
870-1011 1.25e-15

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: 74.65  E-value: 1.25e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130     870 PRVAFSAALSLPRSEPG-TVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTgHRHEKVEAVLSRSNLGVARiDSGG 948
Cdd:smart00110    6 PRSAFSVIRSNRPPPPGqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE-SKGRNVKVSLMKNGIQVMS-TYDE 83
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130     949 YEPEGLEnkpvaesQPSPGAlgvfslILPLQVGDTVCI-------DLVMGQLAHSeepltIFSGALLYED 1011
Cdd:smart00110   84 YQKGLYD-------VASGGA------LLQLRQGDQVWLelpdeknGLYAGEYVDS-----TFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
873-1008 1.94e-11

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: 62.30  E-value: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    873 AFSAALSLPRSEPGT--VPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHrhekveavlSRSNLGVARIDSGgye 950
Cdd:pfam00386    1 AFSAGRTTGLTAPNEqpVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTV---------DGKSLYVSLVKNG--- 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527130    951 peglenKPVA--ESQPSPGALGVFS--LILPLQVGDTVCIDLVMGQLAHSEE--PLTIFSGALL 1008
Cdd:pfam00386   69 ------QEVVsfYDQPQKGSLDVASgsVVLELQRGDEVWLQLTGYNGLYYDGsdTDSTFSGFLL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
639-808 5.02e-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: 57.37  E-value: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    639 SALQALQGELSEVILTFSSLNDSLHELQTTVEGQGADLADLGATKDSIISEINRLQQEATEHVTESEERFRGLEEGQAQA 718
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    719 gqcpslegrlgrlegvcERLDTVAGGLQGLREGLSRHVAGLWAAVRESNSTSLTQAALLEKLLGGQAGLGRRLGALNNSL 798
Cdd:TIGR02168  340 -----------------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170
                   ....*....|
gi 19527130    799 LLLEDRLQQL 808
Cdd:TIGR02168  403 ERLEARLERL 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
178-811 1.86e-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: 48.90  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    178 EKVQQLERQVKSLTKELQGLRGVLQGMNGRLAEDVQRAVDTVFNGRQQPADAAArpgVHETLSEIQQQLQLLDNRVSTHD 257
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAELE 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    258 QELGHLNNHHNGGPGGGGRASGPVPVpsgpSEELLRQLERQLQESCSvcltGLDGFRQQQQEDRERLRTLEKLMSSMEER 337
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLEDR 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    338 QQQLVGPAMARRP-PQECCPPELGRRVSELER-------RLDVVTGSLTVLSGRR---GSELGGAAGQgghppgYTSLAS 406
Cdd:TIGR02168  416 RERLQQEIEELLKkLEEAELKELQAELEELEEeleelqeELERLEEALEELREELeeaEQALDAAERE------LAQLQA 489
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    407 RLSRLEDRFNSTLGPSEE-----QEKNWPGG-----------------------PGRLGHWL---------------PAA 443
Cdd:TIGR02168  490 RLDSLERLQENLEGFSEGvkallKNQSGLSGilgvlselisvdegyeaaieaalGGRLQAVVvenlnaakkaiaflkQNE 569
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    444 PGRLEKLEGLLANVSRELGGRMDLLEEQvAGAVRTCGQICSGAPGEQDSR---------VNEILSALE-RRVLDSEGRL- 512
Cdd:TIGR02168  570 LGRVTFLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRKALsyllggvlvVDDLDNALElAKKLRPGYRIv 648
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    513 ----QLVGSGLHEAEAAGEAQQAVLEgLQGLLSRLRERMDAQEETAAEILLRLNLTAAQLSQLEG---LLQARGDEGCGA 585
Cdd:TIGR02168  649 tldgDLVRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQ 727
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    586 CGGVQEELGRLRDGVERCSCPLLPPRGpgagpgvggpsrgpldgfsvfggssgsALQALQGELSEVILTFSSLNDSLHEL 665
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSK---------------------------ELTELEAEIEELEERLEEAEEELAEA 780
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    666 QTTVEGQGADLADLGATKDSIISEINRLQQEATEHVTESEERFRGLEEGQAQAGQCP-SLEGRLGRLEGVCERLDTVAGG 744
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRLEDLEEQIEELSEDIESLAAE 860
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130    745 LQGLREGLSRHVAGLWAAVRESNSTSLTQAAL---LEKLLGGQAGLGRRLGALNNSLLLLEDRLQQLSLK 811
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLrseLEELSEELRELESKRSELRRELEELREKLAQLELR 930
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
170-573 2.35e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  170 GGEGPVESEKVQQLERQVKSL---TKELQGLRGVLQGMNGRLAEdVQRAVDTVFNGRQQPADAAARPGVHETLSEIQQQL 246
Cdd:COG4717   63 GRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  247 QLLDNRVSTHDQELGHLNNHHNGGPGGGGRAsgpvpvpsgpsEELLRQLERQLQESCSVCLTGLDGFRQQQQEDRERLRT 326
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELEELEAEL-----------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  327 LEKLMSSMEERQQQLVGPAMARRPPQEccPPELGRRVSELERRLdVVTGSLTVLSGRRGSELG--------GAAGQGGHP 398
Cdd:COG4717  211 LEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLL-LIAAALLALLGLGGSLLSliltiagvLFLVLGLLA 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  399 PGYTSLASRLSRLEDRFNSTLGPSEE---QEKNWPGGPGRLGHWLPAAPGRLEKLEGLLANVSRELGGRMDLLEE-QVAG 474
Cdd:COG4717  288 LLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEE 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527130  475 AVRTCGQICSGAPGEQDSRVNEILSALERRVlDSEGRLQLVGSGL--HEAEAAGEAQQAVLEGLQGLLSRLRERMDAQEE 552
Cdd:COG4717  368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEE 446
                        410       420
                 ....*....|....*....|.
gi 19527130  553 TAAEILLRLNLTAAQLSQLEG 573
Cdd:COG4717  447 ELEELREELAELEAELEQLEE 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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