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Conserved domains on  [gi|18412822|ref|NP_567290|]
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Octicosapeptide/Phox/Bem1p family protein [Arabidopsis thaliana]

Protein Classification

PB1 domain-containing protein( domain architecture ID 10157399)

PB1 domain-containing protein may mediate specific protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PB1_UP2 cd06410
Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific ...
62-161 1.13e-48

Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions.


:

Pssm-ID: 99731  Cd Length: 97  Bit Score: 162.00  E-value: 1.13e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822  62 MCTFGGRILPRPPDNQLCYVGGDNRMVAVHRHTTFASLLSKLAKLSGKSN-ISVKYQLPNEDLDALISVSTDEDVENMMD 140
Cdd:cd06410   1 LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVvVTLKYQLPDEDLDALISVSNDEDLKNMME 80
                        90       100
                ....*....|....*....|.
gi 18412822 141 EYDRVaqnqNPRASRLRLFLF 161
Cdd:cd06410  81 EYDRL----SGGSARLRVFLF 97
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
288-424 1.95e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.87  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822   288 MRISTPELPPPvfikpESPEPVSTPKSNPQPEQVMQQSNLPVNSQWQYA---PGPGQQVHYQGH--TIHQSPVYYVPGSV 362
Cdd:pfam09770 203 MRAQAKKPAQQ-----PAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPqqqPQQPQQHPGQGHpvTILQRPQSPQPDPA 277
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18412822   363 PGNHMVQQGNHMVQPGNHMVQPVQ------MPGQYLQQYHHVPMGYHQPQTHQMAGPGQVYGGTVRPV 424
Cdd:pfam09770 278 QPSIQPQAQQFHQQPPPVPVQPTQilqnpnRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI 345
 
Name Accession Description Interval E-value
PB1_UP2 cd06410
Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific ...
62-161 1.13e-48

Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions.


Pssm-ID: 99731  Cd Length: 97  Bit Score: 162.00  E-value: 1.13e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822  62 MCTFGGRILPRPPDNQLCYVGGDNRMVAVHRHTTFASLLSKLAKLSGKSN-ISVKYQLPNEDLDALISVSTDEDVENMMD 140
Cdd:cd06410   1 LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVvVTLKYQLPDEDLDALISVSNDEDLKNMME 80
                        90       100
                ....*....|....*....|.
gi 18412822 141 EYDRVaqnqNPRASRLRLFLF 161
Cdd:cd06410  81 EYDRL----SGGSARLRVFLF 97
PB1 pfam00564
PB1 domain;
73-161 4.57e-17

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 75.79  E-value: 4.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822    73 PPDNQLCYVGGDNRMVAVHRHTTFASLLSKLAKLSGKSNISVKYQLPNEDLDaLISVSTDEDVENMMDEYDRVAQNqnpr 152
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGD-LVSLTSDEDLEEALEEARSLGSK---- 75

                  ....*....
gi 18412822   153 asRLRLFLF 161
Cdd:pfam00564  76 --SLRLHVF 82
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
73-161 4.99e-17

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 75.70  E-value: 4.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822     73 PPDNQLCYvGGDNRMVAVHRHTTFASLLSKLAKLSG--KSNISVKYQlpNEDLDaLISVSTDEDVENMMDEYDRVAQNqn 150
Cdd:smart00666   1 TVDVKLRY-GGETRRLSVPRDISFEDLRSKVAKRFGldNQSFTLKYQ--DEDGD-LVSLTSDEDLEEAIEEYDSLGSK-- 74
                           90
                   ....*....|.
gi 18412822    151 prasRLRLFLF 161
Cdd:smart00666  75 ----KLRLHVF 81
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
288-424 1.95e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.87  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822   288 MRISTPELPPPvfikpESPEPVSTPKSNPQPEQVMQQSNLPVNSQWQYA---PGPGQQVHYQGH--TIHQSPVYYVPGSV 362
Cdd:pfam09770 203 MRAQAKKPAQQ-----PAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPqqqPQQPQQHPGQGHpvTILQRPQSPQPDPA 277
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18412822   363 PGNHMVQQGNHMVQPGNHMVQPVQ------MPGQYLQQYHHVPMGYHQPQTHQMAGPGQVYGGTVRPV 424
Cdd:pfam09770 278 QPSIQPQAQQFHQQPPPVPVQPTQilqnpnRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI 345
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
337-457 1.04e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 41.18  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822 337 PGPGQQVHYQGHTIHQSPVYYVPGSVPGNHMVQQGNHMvQPGNHMVQPVQMPGQYLQQYHHVPMGYHQPQTHQMAGPGQv 416
Cdd:cd22056 203 FMGQQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGG-PDCHLLHSSHHHHHHHHLQYQYMNAPYPPHYAHQGAPQFH- 280
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18412822 417 yggtvrpvmmavdgmnrtGYYGMKT-PGPVQMYQHHTGMVVP 457
Cdd:cd22056 281 ------------------GQYSVFRePMRVHHQGHPGSMLTP 304
PHA03247 PHA03247
large tegument protein UL36; Provisional
244-363 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822   244 APPHELRDRDPRAKIQREVSTLSDPGSPRRDVPSPYGSTSSAPVmristPELPPPVFIKPESPEPVSTPKSNPQPEQVMQ 323
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL-----PPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 18412822   324 QSNLPVNSQWQYAPGPGQQVHYQGHTIHQSPV--YYVPGSVP 363
Cdd:PHA03247 2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgALVPGRVA 2973
 
Name Accession Description Interval E-value
PB1_UP2 cd06410
Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific ...
62-161 1.13e-48

Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions.


Pssm-ID: 99731  Cd Length: 97  Bit Score: 162.00  E-value: 1.13e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822  62 MCTFGGRILPRPPDNQLCYVGGDNRMVAVHRHTTFASLLSKLAKLSGKSN-ISVKYQLPNEDLDALISVSTDEDVENMMD 140
Cdd:cd06410   1 LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVvVTLKYQLPDEDLDALISVSNDEDLKNMME 80
                        90       100
                ....*....|....*....|.
gi 18412822 141 EYDRVaqnqNPRASRLRLFLF 161
Cdd:cd06410  81 EYDRL----SGGSARLRVFLF 97
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
77-161 1.13e-18

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 80.40  E-value: 1.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822  77 QLCYVGGDNRMVAVHRHTTFASLLSKLAKLSGKSNISVKYQLPNEDLDaLISVSTDEDVENMMDEYDRvaqnqnPRASRL 156
Cdd:cd05992   4 KVKYGGEIRRFVVVSRSISFEDLRSKIAEKFGLDAVSFKLKYPDEDGD-LVTISSDEDLEEAIEEARR------SGSKKL 76

                ....*
gi 18412822 157 RLFLF 161
Cdd:cd05992  77 RLFVF 81
PB1 pfam00564
PB1 domain;
73-161 4.57e-17

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 75.79  E-value: 4.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822    73 PPDNQLCYVGGDNRMVAVHRHTTFASLLSKLAKLSGKSNISVKYQLPNEDLDaLISVSTDEDVENMMDEYDRVAQNqnpr 152
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGD-LVSLTSDEDLEEALEEARSLGSK---- 75

                  ....*....
gi 18412822   153 asRLRLFLF 161
Cdd:pfam00564  76 --SLRLHVF 82
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
73-161 4.99e-17

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 75.70  E-value: 4.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822     73 PPDNQLCYvGGDNRMVAVHRHTTFASLLSKLAKLSG--KSNISVKYQlpNEDLDaLISVSTDEDVENMMDEYDRVAQNqn 150
Cdd:smart00666   1 TVDVKLRY-GGETRRLSVPRDISFEDLRSKVAKRFGldNQSFTLKYQ--DEDGD-LVSLTSDEDLEEAIEEYDSLGSK-- 74
                           90
                   ....*....|.
gi 18412822    151 prasRLRLFLF 161
Cdd:smart00666  75 ----KLRLHVF 81
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
288-424 1.95e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.87  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822   288 MRISTPELPPPvfikpESPEPVSTPKSNPQPEQVMQQSNLPVNSQWQYA---PGPGQQVHYQGH--TIHQSPVYYVPGSV 362
Cdd:pfam09770 203 MRAQAKKPAQQ-----PAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPqqqPQQPQQHPGQGHpvTILQRPQSPQPDPA 277
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18412822   363 PGNHMVQQGNHMVQPGNHMVQPVQ------MPGQYLQQYHHVPMGYHQPQTHQMAGPGQVYGGTVRPV 424
Cdd:pfam09770 278 QPSIQPQAQQFHQQPPPVPVQPTQilqnpnRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI 345
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
337-457 1.04e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 41.18  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822 337 PGPGQQVHYQGHTIHQSPVYYVPGSVPGNHMVQQGNHMvQPGNHMVQPVQMPGQYLQQYHHVPMGYHQPQTHQMAGPGQv 416
Cdd:cd22056 203 FMGQQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGG-PDCHLLHSSHHHHHHHHLQYQYMNAPYPPHYAHQGAPQFH- 280
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18412822 417 yggtvrpvmmavdgmnrtGYYGMKT-PGPVQMYQHHTGMVVP 457
Cdd:cd22056 281 ------------------GQYSVFRePMRVHHQGHPGSMLTP 304
PHA03247 PHA03247
large tegument protein UL36; Provisional
244-363 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412822   244 APPHELRDRDPRAKIQREVSTLSDPGSPRRDVPSPYGSTSSAPVmristPELPPPVFIKPESPEPVSTPKSNPQPEQVMQ 323
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL-----PPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 18412822   324 QSNLPVNSQWQYAPGPGQQVHYQGHTIHQSPV--YYVPGSVP 363
Cdd:PHA03247 2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgALVPGRVA 2973
 
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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