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Conserved domains on  [gi|20127519|ref|NP_036244|]
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targeting protein for Xklp2 [Homo sapiens]

Protein Classification

Aurora-A_bind and TPX2_importin domain-containing protein( domain architecture ID 10557231)

protein containing domains Aurora-A_bind, TPX2_importin, and TPX2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aurora-A_bind pfam09041
Aurora-A binding; The Aurora-A binding domain binds to two distinct sites on the Aurora kinase: ...
 1-68 4.07e-44

Aurora-A binding; The Aurora-A binding domain binds to two distinct sites on the Aurora kinase: the upstream residues bind at the N-terminal lobe, whilst the downstream residues bind in an alpha-helical conformation between the N- and C-terminal lobes. The two Aurora-A binding motifs are connected by a flexible linker that is variable in length and sequence across species. Binding of the domain results strong activation of Aurora-A and protection from deactivating dephosphorylation by phosphatase PP1.


:

Pssm-ID: 430383  Cd Length: 68  Bit Score: 152.68  E-value: 4.07e-44
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20127519     1 MSQVKSSYSYDAPSDFINFSSLDDEGDTQNIDSWFEEKANLENKLLGKNGTGGLFQGKTPLRKANLQQ 68
Cdd:pfam09041   1 MSQVKTSYSFDAPTDFINFTSLDDEEDTENIDSWFEEKANLENKFPGKNGTGGLFQGKTPLRKANLQQ 68
TPX2_importin pfam12214
Cell cycle regulated microtubule associated protein; This domain is found in eukaryotes. This ...
 367-489 1.08e-37

Cell cycle regulated microtubule associated protein; This domain is found in eukaryotes. This domain is typically between 127 to 182 amino acids in length. This domain is found associated with pfam06886. This domain is found in the protein TPX2 (a.k.a p100) which is involved in cell cycling. It is only expressed between the start of the S phase and completion of cytokinesis. The microtubule-associated protein TPX2 has been reported to be crucial for mitotic spindle formation. This domain is close to the C terminal of TPX2. The protein importin alpha regulates the activity of TPX2 by binding to the nuclear localization signal in this domain.


:

Pssm-ID: 463495 [Multi-domain]  Cd Length: 129  Bit Score: 136.67  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127519   367 PQTPVLQTKHRARAVTCKSTAELEAEELEKLQQYKFKARELDPRILEGGPILPKKPPVKPPTEPIGFDLEIEKRIQERES 446
Cdd:pfam12214   1 PKEPELETAQRARPVRVKSSAELEAEELEKIQQYKFKARPLNRKILEAPSLPLKKPSTPRLTEFQEFHLETEKRAQQRSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 20127519   447 KKKTEDE----HFEFHSRPCPTKILE--DVVGVPEKKVLPITVPKSPAF 489
Cdd:pfam12214  81 KKSTSEEelekKHKFKARPLNKKILEskGVVGVFEKKKLPTTVPKEPAF 129
TPX2 pfam06886
Targeting protein for Xklp2 (TPX2) domain; This family represents a conserved region ...
 660-732 4.95e-11

Targeting protein for Xklp2 (TPX2) domain; This family represents a conserved region approximately 60 residues long within the eukaryotic targeting protein for Xklp2 (TPX2). Xklp2 is a kinesin-like protein localized on centrosomes throughout the cell cycle and on spindle pole microtubules during metaphase. In Xenopus, it has been shown that Xklp2 protein is required for centrosome separation and maintenance of spindle bi-polarity. TPX2 is a microtubule-associated protein that mediates the binding of the C-terminal domain of Xklp2 to microtubules. It is phosphorylated during mitosis in a microtubule-dependent way. The TPX domain appears to be truncated in fungal species.


:

Pssm-ID: 462029 [Multi-domain]  Cd Length: 77  Bit Score: 59.13  E-value: 4.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20127519   660 FQLATEKRAKERQELEKRMAEVEAQKAQQLEEARLQEEEQKKEELARLRRELVHKANPIRKYQGLEIKSSDQP 732
Cdd:pfam06886   1 FKLHTDERAEERKEFDKKLEEKEQAKEAEKEERERKRKEEEEEEIKQLRKELVFKAQPMPHFYRVFIPPSKKP 73
 
Name Accession Description Interval E-value
Aurora-A_bind pfam09041
Aurora-A binding; The Aurora-A binding domain binds to two distinct sites on the Aurora kinase: ...
 1-68 4.07e-44

Aurora-A binding; The Aurora-A binding domain binds to two distinct sites on the Aurora kinase: the upstream residues bind at the N-terminal lobe, whilst the downstream residues bind in an alpha-helical conformation between the N- and C-terminal lobes. The two Aurora-A binding motifs are connected by a flexible linker that is variable in length and sequence across species. Binding of the domain results strong activation of Aurora-A and protection from deactivating dephosphorylation by phosphatase PP1.


Pssm-ID: 430383  Cd Length: 68  Bit Score: 152.68  E-value: 4.07e-44
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20127519     1 MSQVKSSYSYDAPSDFINFSSLDDEGDTQNIDSWFEEKANLENKLLGKNGTGGLFQGKTPLRKANLQQ 68
Cdd:pfam09041   1 MSQVKTSYSFDAPTDFINFTSLDDEEDTENIDSWFEEKANLENKFPGKNGTGGLFQGKTPLRKANLQQ 68
TPX2_importin pfam12214
Cell cycle regulated microtubule associated protein; This domain is found in eukaryotes. This ...
 367-489 1.08e-37

Cell cycle regulated microtubule associated protein; This domain is found in eukaryotes. This domain is typically between 127 to 182 amino acids in length. This domain is found associated with pfam06886. This domain is found in the protein TPX2 (a.k.a p100) which is involved in cell cycling. It is only expressed between the start of the S phase and completion of cytokinesis. The microtubule-associated protein TPX2 has been reported to be crucial for mitotic spindle formation. This domain is close to the C terminal of TPX2. The protein importin alpha regulates the activity of TPX2 by binding to the nuclear localization signal in this domain.


Pssm-ID: 463495 [Multi-domain]  Cd Length: 129  Bit Score: 136.67  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127519   367 PQTPVLQTKHRARAVTCKSTAELEAEELEKLQQYKFKARELDPRILEGGPILPKKPPVKPPTEPIGFDLEIEKRIQERES 446
Cdd:pfam12214   1 PKEPELETAQRARPVRVKSSAELEAEELEKIQQYKFKARPLNRKILEAPSLPLKKPSTPRLTEFQEFHLETEKRAQQRSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 20127519   447 KKKTEDE----HFEFHSRPCPTKILE--DVVGVPEKKVLPITVPKSPAF 489
Cdd:pfam12214  81 KKSTSEEelekKHKFKARPLNKKILEskGVVGVFEKKKLPTTVPKEPAF 129
TPX2 pfam06886
Targeting protein for Xklp2 (TPX2) domain; This family represents a conserved region ...
 660-732 4.95e-11

Targeting protein for Xklp2 (TPX2) domain; This family represents a conserved region approximately 60 residues long within the eukaryotic targeting protein for Xklp2 (TPX2). Xklp2 is a kinesin-like protein localized on centrosomes throughout the cell cycle and on spindle pole microtubules during metaphase. In Xenopus, it has been shown that Xklp2 protein is required for centrosome separation and maintenance of spindle bi-polarity. TPX2 is a microtubule-associated protein that mediates the binding of the C-terminal domain of Xklp2 to microtubules. It is phosphorylated during mitosis in a microtubule-dependent way. The TPX domain appears to be truncated in fungal species.


Pssm-ID: 462029 [Multi-domain]  Cd Length: 77  Bit Score: 59.13  E-value: 4.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20127519   660 FQLATEKRAKERQELEKRMAEVEAQKAQQLEEARLQEEEQKKEELARLRRELVHKANPIRKYQGLEIKSSDQP 732
Cdd:pfam06886   1 FKLHTDERAEERKEFDKKLEEKEQAKEAEKEERERKRKEEEEEEIKQLRKELVFKAQPMPHFYRVFIPPSKKP 73
 
Name Accession Description Interval E-value
Aurora-A_bind pfam09041
Aurora-A binding; The Aurora-A binding domain binds to two distinct sites on the Aurora kinase: ...
 1-68 4.07e-44

Aurora-A binding; The Aurora-A binding domain binds to two distinct sites on the Aurora kinase: the upstream residues bind at the N-terminal lobe, whilst the downstream residues bind in an alpha-helical conformation between the N- and C-terminal lobes. The two Aurora-A binding motifs are connected by a flexible linker that is variable in length and sequence across species. Binding of the domain results strong activation of Aurora-A and protection from deactivating dephosphorylation by phosphatase PP1.


Pssm-ID: 430383  Cd Length: 68  Bit Score: 152.68  E-value: 4.07e-44
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20127519     1 MSQVKSSYSYDAPSDFINFSSLDDEGDTQNIDSWFEEKANLENKLLGKNGTGGLFQGKTPLRKANLQQ 68
Cdd:pfam09041   1 MSQVKTSYSFDAPTDFINFTSLDDEEDTENIDSWFEEKANLENKFPGKNGTGGLFQGKTPLRKANLQQ 68
TPX2_importin pfam12214
Cell cycle regulated microtubule associated protein; This domain is found in eukaryotes. This ...
 367-489 1.08e-37

Cell cycle regulated microtubule associated protein; This domain is found in eukaryotes. This domain is typically between 127 to 182 amino acids in length. This domain is found associated with pfam06886. This domain is found in the protein TPX2 (a.k.a p100) which is involved in cell cycling. It is only expressed between the start of the S phase and completion of cytokinesis. The microtubule-associated protein TPX2 has been reported to be crucial for mitotic spindle formation. This domain is close to the C terminal of TPX2. The protein importin alpha regulates the activity of TPX2 by binding to the nuclear localization signal in this domain.


Pssm-ID: 463495 [Multi-domain]  Cd Length: 129  Bit Score: 136.67  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127519   367 PQTPVLQTKHRARAVTCKSTAELEAEELEKLQQYKFKARELDPRILEGGPILPKKPPVKPPTEPIGFDLEIEKRIQERES 446
Cdd:pfam12214   1 PKEPELETAQRARPVRVKSSAELEAEELEKIQQYKFKARPLNRKILEAPSLPLKKPSTPRLTEFQEFHLETEKRAQQRSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 20127519   447 KKKTEDE----HFEFHSRPCPTKILE--DVVGVPEKKVLPITVPKSPAF 489
Cdd:pfam12214  81 KKSTSEEelekKHKFKARPLNKKILEskGVVGVFEKKKLPTTVPKEPAF 129
TPX2 pfam06886
Targeting protein for Xklp2 (TPX2) domain; This family represents a conserved region ...
 660-732 4.95e-11

Targeting protein for Xklp2 (TPX2) domain; This family represents a conserved region approximately 60 residues long within the eukaryotic targeting protein for Xklp2 (TPX2). Xklp2 is a kinesin-like protein localized on centrosomes throughout the cell cycle and on spindle pole microtubules during metaphase. In Xenopus, it has been shown that Xklp2 protein is required for centrosome separation and maintenance of spindle bi-polarity. TPX2 is a microtubule-associated protein that mediates the binding of the C-terminal domain of Xklp2 to microtubules. It is phosphorylated during mitosis in a microtubule-dependent way. The TPX domain appears to be truncated in fungal species.


Pssm-ID: 462029 [Multi-domain]  Cd Length: 77  Bit Score: 59.13  E-value: 4.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20127519   660 FQLATEKRAKERQELEKRMAEVEAQKAQQLEEARLQEEEQKKEELARLRRELVHKANPIRKYQGLEIKSSDQP 732
Cdd:pfam06886   1 FKLHTDERAEERKEFDKKLEEKEQAKEAEKEERERKRKEEEEEEIKQLRKELVFKAQPMPHFYRVFIPPSKKP 73
 
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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