NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720366858|ref|XP_030102027|]
View 

SRC kinase signaling inhibitor 1 isoform X17 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AIP3 super family cl38141
Actin interacting protein 3;
211-290 4.44e-06

Actin interacting protein 3;


The actual alignment was detected with superfamily member pfam03915:

Pssm-ID: 427585 [Multi-domain]  Cd Length: 407  Bit Score: 50.99  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  211 FLQFGEETRRVHITHEvssldtlhaliahmfpqkLTMGMLK---------SPNT----AILIKDEARNVFYELEDVRDIQ 277
Cdd:pfam03915    1 FLQLGRKVKKVVLPLP------------------LTIASLRllfvekfaySPGGddfpEIYIQDPVSGVRYELEDLSDVK 62
                           90
                   ....*....|...
gi 1720366858  278 DRSIIKIyRKEPL 290
Cdd:pfam03915   63 DGSVLSL-NIEPL 74
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1096-1447 6.66e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1096 SEVVRPASTPPIMASAikdeddeeRIIAELEVFERSSVSSLPPTPRRQPIPTLLSPQDMGSPGgSALGSPRKAASGPgdf 1175
Cdd:pfam05109  456 TNLTAPASTGPTVSTA--------DVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPT-SAVTTPTPNATSP--- 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1176 cVPQIILTECTPSSPTLPEITleELGPRTVPTPRPrTLAGSGKAWNGPQALLGLAAETlwSRSSSVPGKEPALlQSPHSV 1255
Cdd:pfam05109  524 -TPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNA-TSPTPAVTTPTPNATIPTLGKT--SPTSAVTTPTPNA-TSPTVG 596
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1256 EArvlclrGPSPDETRKTF--TVETHSEETPQNSVcdTQACSRGPQAINSGSTvqdatlrrmDSLEETLQELETTLSEMG 1333
Cdd:pfam05109  597 ET------SPQANTTNHTLggTSSTPVVTSPPKNA--TSAVTTGQHNITSSST---------SSMSLRPSSISETLSPST 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1334 AKSTMTMMmcpgiPQPLHPHPQSGG--SSVPPMKVVTPGASRLKAAQGPAGSPDKGKHGKQRTeymriqaqqqATKPSK- 1410
Cdd:pfam05109  660 SDNSTSHM-----PLLTSAHPTGGEniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST----------STKPGEv 724
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1720366858 1411 ---EVSGPNETSSPgsEKPSGSRTSIPVLTSFGARNSSIS 1447
Cdd:pfam05109  725 nvtKGTPPKNATSP--QAPSGQKTAVPTVTSTGGKANSTT 762
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
722-876 4.23e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 4.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  722 LKRTEAELSMRVSEAARRQEDpLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRlvpgpELEEKALV 801
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAA 876
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366858  802 LKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNL 876
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
 
Name Accession Description Interval E-value
AIP3 pfam03915
Actin interacting protein 3;
211-290 4.44e-06

Actin interacting protein 3;


Pssm-ID: 427585 [Multi-domain]  Cd Length: 407  Bit Score: 50.99  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  211 FLQFGEETRRVHITHEvssldtlhaliahmfpqkLTMGMLK---------SPNT----AILIKDEARNVFYELEDVRDIQ 277
Cdd:pfam03915    1 FLQLGRKVKKVVLPLP------------------LTIASLRllfvekfaySPGGddfpEIYIQDPVSGVRYELEDLSDVK 62
                           90
                   ....*....|...
gi 1720366858  278 DRSIIKIyRKEPL 290
Cdd:pfam03915   63 DGSVLSL-NIEPL 74
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1096-1447 6.66e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1096 SEVVRPASTPPIMASAikdeddeeRIIAELEVFERSSVSSLPPTPRRQPIPTLLSPQDMGSPGgSALGSPRKAASGPgdf 1175
Cdd:pfam05109  456 TNLTAPASTGPTVSTA--------DVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPT-SAVTTPTPNATSP--- 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1176 cVPQIILTECTPSSPTLPEITleELGPRTVPTPRPrTLAGSGKAWNGPQALLGLAAETlwSRSSSVPGKEPALlQSPHSV 1255
Cdd:pfam05109  524 -TPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNA-TSPTPAVTTPTPNATIPTLGKT--SPTSAVTTPTPNA-TSPTVG 596
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1256 EArvlclrGPSPDETRKTF--TVETHSEETPQNSVcdTQACSRGPQAINSGSTvqdatlrrmDSLEETLQELETTLSEMG 1333
Cdd:pfam05109  597 ET------SPQANTTNHTLggTSSTPVVTSPPKNA--TSAVTTGQHNITSSST---------SSMSLRPSSISETLSPST 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1334 AKSTMTMMmcpgiPQPLHPHPQSGG--SSVPPMKVVTPGASRLKAAQGPAGSPDKGKHGKQRTeymriqaqqqATKPSK- 1410
Cdd:pfam05109  660 SDNSTSHM-----PLLTSAHPTGGEniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST----------STKPGEv 724
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1720366858 1411 ---EVSGPNETSSPgsEKPSGSRTSIPVLTSFGARNSSIS 1447
Cdd:pfam05109  725 nvtKGTPPKNATSP--QAPSGQKTAVPTVTSTGGKANSTT 762
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
722-876 4.23e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 4.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  722 LKRTEAELSMRVSEAARRQEDpLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRlvpgpELEEKALV 801
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAA 876
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366858  802 LKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNL 876
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
716-868 8.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  716 ESVRALLKRTEAELSmRVSEAARRQEDPLQRQRTLVEEERLRYLNDEElITQQLNDLEKSVEKIQRDVAhnhrlvpgpEL 795
Cdd:PRK03918   189 ENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELEKELESLEGSKR---------KL 257
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366858  796 EEKalvLKQLGETLTELKAHFPGLQSKMRVVLRVEVEA------VKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEG 868
Cdd:PRK03918   258 EEK---IRELEERIEELKKEIEELEEKVKELKELKEKAeeyiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
 
Name Accession Description Interval E-value
AIP3 pfam03915
Actin interacting protein 3;
211-290 4.44e-06

Actin interacting protein 3;


Pssm-ID: 427585 [Multi-domain]  Cd Length: 407  Bit Score: 50.99  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  211 FLQFGEETRRVHITHEvssldtlhaliahmfpqkLTMGMLK---------SPNT----AILIKDEARNVFYELEDVRDIQ 277
Cdd:pfam03915    1 FLQLGRKVKKVVLPLP------------------LTIASLRllfvekfaySPGGddfpEIYIQDPVSGVRYELEDLSDVK 62
                           90
                   ....*....|...
gi 1720366858  278 DRSIIKIyRKEPL 290
Cdd:pfam03915   63 DGSVLSL-NIEPL 74
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1096-1447 6.66e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1096 SEVVRPASTPPIMASAikdeddeeRIIAELEVFERSSVSSLPPTPRRQPIPTLLSPQDMGSPGgSALGSPRKAASGPgdf 1175
Cdd:pfam05109  456 TNLTAPASTGPTVSTA--------DVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPT-SAVTTPTPNATSP--- 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1176 cVPQIILTECTPSSPTLPEITleELGPRTVPTPRPrTLAGSGKAWNGPQALLGLAAETlwSRSSSVPGKEPALlQSPHSV 1255
Cdd:pfam05109  524 -TPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNA-TSPTPAVTTPTPNATIPTLGKT--SPTSAVTTPTPNA-TSPTVG 596
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1256 EArvlclrGPSPDETRKTF--TVETHSEETPQNSVcdTQACSRGPQAINSGSTvqdatlrrmDSLEETLQELETTLSEMG 1333
Cdd:pfam05109  597 ET------SPQANTTNHTLggTSSTPVVTSPPKNA--TSAVTTGQHNITSSST---------SSMSLRPSSISETLSPST 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858 1334 AKSTMTMMmcpgiPQPLHPHPQSGG--SSVPPMKVVTPGASRLKAAQGPAGSPDKGKHGKQRTeymriqaqqqATKPSK- 1410
Cdd:pfam05109  660 SDNSTSHM-----PLLTSAHPTGGEniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST----------STKPGEv 724
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1720366858 1411 ---EVSGPNETSSPgsEKPSGSRTSIPVLTSFGARNSSIS 1447
Cdd:pfam05109  725 nvtKGTPPKNATSP--QAPSGQKTAVPTVTSTGGKANSTT 762
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
722-876 4.23e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 4.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  722 LKRTEAELSMRVSEAARRQEDpLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRlvpgpELEEKALV 801
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAA 876
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366858  802 LKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNL 876
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
716-868 8.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366858  716 ESVRALLKRTEAELSmRVSEAARRQEDPLQRQRTLVEEERLRYLNDEElITQQLNDLEKSVEKIQRDVAhnhrlvpgpEL 795
Cdd:PRK03918   189 ENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELEKELESLEGSKR---------KL 257
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366858  796 EEKalvLKQLGETLTELKAHFPGLQSKMRVVLRVEVEA------VKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEG 868
Cdd:PRK03918   258 EEK---IRELEERIEELKKEIEELEEKVKELKELKEKAeeyiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH