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Conserved domains on  [gi|1720366877|ref|XP_030102034|]
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SRC kinase signaling inhibitor 1 isoform X29 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AIP3 super family cl38141
Actin interacting protein 3;
273-352 4.31e-06

Actin interacting protein 3;


The actual alignment was detected with superfamily member pfam03915:

Pssm-ID: 427585 [Multi-domain]  Cd Length: 407  Bit Score: 50.61  E-value: 4.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366877  273 FLQFGEETRRVHITHEvssldtlhaliahmfpqkLTMGMLK---------SPNT----AILIKDEARNVFYELEDVRDIQ 339
Cdd:pfam03915    1 FLQLGRKVKKVVLPLP------------------LTIASLRllfvekfaySPGGddfpEIYIQDPVSGVRYELEDLSDVK 62

                           90
                   ....*....|...
gi 1720366877  340 DRSIIKIyRKEPL 352
Cdd:pfam03915   63 DGSVLSL-NIEPL 74
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 783-937 4.66e-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: 44.67  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366877  783 LKRTEAELSMRVSEAARRQEDpLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRlvpgpELEEKALV 862
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAA 876

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366877  863 LKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNL 937
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
 
Name Accession Description Interval E-value
AIP3 pfam03915
Actin interacting protein 3;
273-352 4.31e-06

Actin interacting protein 3;


Pssm-ID: 427585 [Multi-domain]  Cd Length: 407  Bit Score: 50.61  E-value: 4.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366877  273 FLQFGEETRRVHITHEvssldtlhaliahmfpqkLTMGMLK---------SPNT----AILIKDEARNVFYELEDVRDIQ 339
Cdd:pfam03915    1 FLQLGRKVKKVVLPLP------------------LTIASLRllfvekfaySPGGddfpEIYIQDPVSGVRYELEDLSDVK 62

                           90
                   ....*....|...
gi 1720366877  340 DRSIIKIyRKEPL 352
Cdd:pfam03915   63 DGSVLSL-NIEPL 74
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 783-937 4.66e-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: 44.67  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366877  783 LKRTEAELSMRVSEAARRQEDpLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRlvpgpELEEKALV 862
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAA 876

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366877  863 LKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNL 937
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
 273-344 9.98e-03

Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.


Pssm-ID: 214826 [Multi-domain]  Cd Length: 426  Bit Score: 40.04  E-value: 9.98e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366877   273 FLQFGEETRRVHITHEVssldTLHALiahmfpQKLTMGMLK-SPNTA----ILIKDEARNVFYELEDV--RDIQDRSII 344
Cdd:smart00806    1 FLRIGNKTKKVVVSSPL----TFNAL------RLLFIEKFAySPGGDdfpdIYIQDPVSGVSYELEELslHDIKDGSVL 69
 
Name Accession Description Interval E-value
AIP3 pfam03915
Actin interacting protein 3;
273-352 4.31e-06

Actin interacting protein 3;


Pssm-ID: 427585 [Multi-domain]  Cd Length: 407  Bit Score: 50.61  E-value: 4.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366877  273 FLQFGEETRRVHITHEvssldtlhaliahmfpqkLTMGMLK---------SPNT----AILIKDEARNVFYELEDVRDIQ 339
Cdd:pfam03915    1 FLQLGRKVKKVVLPLP------------------LTIASLRllfvekfaySPGGddfpEIYIQDPVSGVRYELEDLSDVK 62

                           90
                   ....*....|...
gi 1720366877  340 DRSIIKIyRKEPL 352
Cdd:pfam03915   63 DGSVLSL-NIEPL 74
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 783-937 4.66e-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: 44.67  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366877  783 LKRTEAELSMRVSEAARRQEDpLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRlvpgpELEEKALV 862
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAA 876

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366877  863 LKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNL 937
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
 273-344 9.98e-03

Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.


Pssm-ID: 214826 [Multi-domain]  Cd Length: 426  Bit Score: 40.04  E-value: 9.98e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366877   273 FLQFGEETRRVHITHEVssldTLHALiahmfpQKLTMGMLK-SPNTA----ILIKDEARNVFYELEDV--RDIQDRSII 344
Cdd:smart00806    1 FLRIGNKTKKVVVSSPL----TFNAL------RLLFIEKFAySPGGDdfpdIYIQDPVSGVSYELEELslHDIKDGSVL 69
 
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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