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Conserved domains on  [gi|2280295597|ref|XP_049672882|]
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upstream-binding protein 1 isoform X1 [Accipiter gentilis]

Protein Classification

SAM domain-containing protein; ACK family non-receptor tyrosine-protein kinase( domain architecture ID 10266809)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation| ACK (activated Cdc42-associated kinase) family non-receptor tyrosine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates; such as TNK1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CP2 super family cl04559
CP2 transcription factor; This family represents a conserved region in the CP2 transcription ...
 49-254 4.93e-59

CP2 transcription factor; This family represents a conserved region in the CP2 transcription factor family.


The actual alignment was detected with superfamily member pfam04516:

Pssm-ID: 461338  Cd Length: 214  Bit Score: 194.95  E-value: 4.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597  49 EDSSLPQENETKHppFQYVMCAATSPAVKLYDETLTYLNQGQSYEIRMldnRKAG--DIPEINGKLVKSIIRVVFHDRRL 126
Cdd:pfam04516   8 EQYAVSGSTENFR--FHYTLEAPTAMIKKVNEIPMTYLNKGQAYSISL---IDTGmnKCSVLPGSKLRSVVRVVFHERKL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597 127 QYTEHQQLEGWKWNRPGDRLLDLDIpmSVGVIDIKTNP------SQLNAVEFLWDPTKCTSAFIQVHCISTEFTPRKhgG 200
Cdd:pfam04516  83 RVEELKCWQLWKEGRPTAAVRIVDP--LYGGYEEQKNTqvniesISFNAFSFTWNPTEECKIFIRVNCLSTDFSHSK--G 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2280295597 201 EKGVPFRIQVDTFkQTENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKR 254
Cdd:pfam04516 159 VKGVPLRLQIKTY-SYGPGSARPAAHRAYCQVKVFRDKGAERKLSNDVAKVKKR 211
SAM_LBP1 cd09588
SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 ...
 369-435 2.52e-42

SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 (also known as UBP1) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate alpha-globin in erythroid cells and P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LPB1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers, apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.


:

Pssm-ID: 188987  Cd Length: 67  Bit Score: 145.52  E-value: 2.52e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2280295597 369 TIQETQQWLLKHRFSTYTRLFSNFSGADLLKLTREDLVQICGPADGIRLYNALKSRSVRPRLTIYVC 435
Cdd:cd09588     1 TIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTREDLVQICGAADGIRLYNALKSRSVRPRLTIYVC 67
 
Name Accession Description Interval E-value
CP2 pfam04516
CP2 transcription factor; This family represents a conserved region in the CP2 transcription ...
 49-254 4.93e-59

CP2 transcription factor; This family represents a conserved region in the CP2 transcription factor family.


Pssm-ID: 461338  Cd Length: 214  Bit Score: 194.95  E-value: 4.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597  49 EDSSLPQENETKHppFQYVMCAATSPAVKLYDETLTYLNQGQSYEIRMldnRKAG--DIPEINGKLVKSIIRVVFHDRRL 126
Cdd:pfam04516   8 EQYAVSGSTENFR--FHYTLEAPTAMIKKVNEIPMTYLNKGQAYSISL---IDTGmnKCSVLPGSKLRSVVRVVFHERKL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597 127 QYTEHQQLEGWKWNRPGDRLLDLDIpmSVGVIDIKTNP------SQLNAVEFLWDPTKCTSAFIQVHCISTEFTPRKhgG 200
Cdd:pfam04516  83 RVEELKCWQLWKEGRPTAAVRIVDP--LYGGYEEQKNTqvniesISFNAFSFTWNPTEECKIFIRVNCLSTDFSHSK--G 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2280295597 201 EKGVPFRIQVDTFkQTENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKR 254
Cdd:pfam04516 159 VKGVPLRLQIKTY-SYGPGSARPAAHRAYCQVKVFRDKGAERKLSNDVAKVKKR 211
SAM_LBP1 cd09588
SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 ...
 369-435 2.52e-42

SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 (also known as UBP1) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate alpha-globin in erythroid cells and P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LPB1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers, apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.


Pssm-ID: 188987  Cd Length: 67  Bit Score: 145.52  E-value: 2.52e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2280295597 369 TIQETQQWLLKHRFSTYTRLFSNFSGADLLKLTREDLVQICGPADGIRLYNALKSRSVRPRLTIYVC 435
Cdd:cd09588     1 TIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTREDLVQICGAADGIRLYNALKSRSVRPRLTIYVC 67
SAM_3 pfam18016
SAM domain (Sterile alpha motif);
363-422 5.09e-22

SAM domain (Sterile alpha motif);


Pssm-ID: 436214  Cd Length: 65  Bit Score: 89.63  E-value: 5.09e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2280295597 363 QLHPSATIQETQQWLLKHRFSTYT-RLFSNFSGADLLKLTREDLVQICGPADGIRLYNALK 422
Cdd:pfam18016   5 NITPKSTPEEVQAWLTAKGFSKKTvKSLGTLSGAQLFSLSKEELKQICGPAEGIRLYSQLL 65
 
Name Accession Description Interval E-value
CP2 pfam04516
CP2 transcription factor; This family represents a conserved region in the CP2 transcription ...
 49-254 4.93e-59

CP2 transcription factor; This family represents a conserved region in the CP2 transcription factor family.


Pssm-ID: 461338  Cd Length: 214  Bit Score: 194.95  E-value: 4.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597  49 EDSSLPQENETKHppFQYVMCAATSPAVKLYDETLTYLNQGQSYEIRMldnRKAG--DIPEINGKLVKSIIRVVFHDRRL 126
Cdd:pfam04516   8 EQYAVSGSTENFR--FHYTLEAPTAMIKKVNEIPMTYLNKGQAYSISL---IDTGmnKCSVLPGSKLRSVVRVVFHERKL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597 127 QYTEHQQLEGWKWNRPGDRLLDLDIpmSVGVIDIKTNP------SQLNAVEFLWDPTKCTSAFIQVHCISTEFTPRKhgG 200
Cdd:pfam04516  83 RVEELKCWQLWKEGRPTAAVRIVDP--LYGGYEEQKNTqvniesISFNAFSFTWNPTEECKIFIRVNCLSTDFSHSK--G 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2280295597 201 EKGVPFRIQVDTFkQTENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKR 254
Cdd:pfam04516 159 VKGVPLRLQIKTY-SYGPGSARPAAHRAYCQVKVFRDKGAERKLSNDVAKVKKR 211
SAM_LBP1 cd09588
SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 ...
 369-435 2.52e-42

SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 (also known as UBP1) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate alpha-globin in erythroid cells and P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LPB1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers, apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.


Pssm-ID: 188987  Cd Length: 67  Bit Score: 145.52  E-value: 2.52e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2280295597 369 TIQETQQWLLKHRFSTYTRLFSNFSGADLLKLTREDLVQICGPADGIRLYNALKSRSVRPRLTIYVC 435
Cdd:cd09588     1 TIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTREDLVQICGAADGIRLYNALKSRSVRPRLTIYVC 67
SAM_CP2-like cd09537
SAM domain of CP2-like transcription factors; SAM (sterile alpha motif) domain of CP2-like ...
 369-435 1.47e-41

SAM domain of CP2-like transcription factors; SAM (sterile alpha motif) domain of CP2-like transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. CP2-like family of transcriptional factors includes three subgroups: LBP1, TFCP2, and LBP9. Members of this family are involved in transcriptional regulation from early development to terminal differentiation. They play a role in regulation of expression of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in placenta, and alpha-globin in erythroid cells. They are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LBP1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.


Pssm-ID: 188936  Cd Length: 67  Bit Score: 143.27  E-value: 1.47e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2280295597 369 TIQETQQWLLKHRFSTYTRLFSNFSGADLLKLTREDLVQICGPADGIRLYNALKSRSVRPRLTIYVC 435
Cdd:cd09537     1 SPQQTTQWLRKNRFGAYLRTFSNFSGADLLRLTRDDLIQICGLADGIRLFNALHSRAIRPRLTLYVC 67
SAM_TFCP2 cd09589
SAM domain of TFCP2 transcription factors; SAM (sterile alpha motif) domain of TFCP2 ...
 369-435 3.14e-36

SAM domain of TFCP2 transcription factors; SAM (sterile alpha motif) domain of TFCP2 transcription factors is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate expression of erythroid cell-specific alpha-globin, fibrinogen, and sex-determining gene SRY as well as lens alpha-crystallin. TFCP2 regulators can interact with NF-E4 proteins forming heteromeric stage selector protein complex (SSP). This complex is able to bind stage selector element (SSE) and regulate embryonic globin expression in fetal-erythroid cells.


Pssm-ID: 188988  Cd Length: 67  Bit Score: 128.94  E-value: 3.14e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2280295597 369 TIQETQQWLLKHRFSTYTRLFSNFSGADLLKLTREDLVQICGPADGIRLYNALKSRSVRPRLTIYVC 435
Cdd:cd09589     1 TPQEAQQWLHRNRFSTFSRLFTNFSGADLLKLTREDVIQICGPADGIRLFNALKGRMVRPRLTIYVC 67
SAM_LBP9 cd09590
SAM domain of LBP9 transcriptional factors; SAM (sterile alpha motif) domain of LBP9 (also ...
 369-435 9.81e-35

SAM domain of LBP9 transcriptional factors; SAM (sterile alpha motif) domain of LBP9 (also known as TFCP2L1 or CRTR-1 (CP2-Related Transcriptional Repressor-1)) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland as well as for regulation of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta.


Pssm-ID: 188989  Cd Length: 67  Bit Score: 125.01  E-value: 9.81e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2280295597 369 TIQETQQWLLKHRFSTYTRLFSNFSGADLLKLTREDLVQICGPADGIRLYNALKSRSVRPRLTIYVC 435
Cdd:cd09590     1 SIQDAQQWLHRNRFSQFCRLFSSFSGADLLKMSRDDFIQICGPADGIRLFNAIKGRNVRPRLTIYVC 67
SAM_3 pfam18016
SAM domain (Sterile alpha motif);
363-422 5.09e-22

SAM domain (Sterile alpha motif);


Pssm-ID: 436214  Cd Length: 65  Bit Score: 89.63  E-value: 5.09e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2280295597 363 QLHPSATIQETQQWLLKHRFSTYT-RLFSNFSGADLLKLTREDLVQICGPADGIRLYNALK 422
Cdd:pfam18016   5 NITPKSTPEEVQAWLTAKGFSKKTvKSLGTLSGAQLFSLSKEELKQICGPAEGIRLYSQLL 65
SAM_EPS8-like cd09540
SAM domain of EPS8-like subfamily; SAM (sterile alpha motif) domain of EPS8-like subfamily is ...
 363-421 5.04e-06

SAM domain of EPS8-like subfamily; SAM (sterile alpha motif) domain of EPS8-like subfamily is a putative protein-protein interaction domain. This subfamily includes epidermal growth factor receptor kinase substrate 8 proteins (EPS8) and epidermal growth factor receptor kinase substrate 8-like (EPSL8) 1, 2, 3 proteins with the SAM domain located in the C-terminal effector region. This region is responsible for intracellular protein localization and is involved in small GTPases (such as Rac and Rab5) activation/inhibition. Proteins belonging to this group participate in coordination and integration of multiple signaling pathways; in particular, they play a role in the control of actin dynamics and in receptor endocytosis. They can form complexes with other proteins; for example, in the actin signaling network they interact with SOS1 and E3b1 (Abl1) proteins as well as with CRIB (via SH3 domains) during the actin filament formation, and in the receptor endocytosis their partner is RN-tre protein.


Pssm-ID: 188939  Cd Length: 66  Bit Score: 44.24  E-value: 5.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280295597 363 QLHPSATIQETQQWLLKHRFSTYT-RLFSNFSGADLLKLTREDLVQICgPADGIRLYNAL 421
Cdd:cd09540     1 PLTYDSSPEEVKAWLQAKGFSKITvRSLGVLTGAQLFSLNKEELKTVC-PEEGARVYSQL 59
 
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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