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Conserved domains on  [gi|1954572292|gb|KAG1559636|]
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hypothetical protein G6F49_003419 [Rhizopus delemar]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 711-849 1.78e-44

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


:

Pssm-ID: 434701  Cd Length: 118  Bit Score: 156.43  E-value: 1.78e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  711 YKEGIVIRKHLLENASQKA--KHREWKECYLEVgKNGELCMYQVQEqapqdkslfRHSSAHFTDRKSntlgghtkwVNNA 788
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTprGKRSWKMVYAVL-KDLVLYLYKDEH---------PPESSQFEDKKS---------LKNA 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954572292  789 qLMGKIALNHTLSNPlpPPGYNRqRPHVFAIQQPDGGVYLFQTTSSEQAQEWVSTCNYWAA 849
Cdd:pfam15410   62 -PVGKIRLHHALATP--APDYTK-KSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
 418-593 1.11e-35

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.


:

Pssm-ID: 460178  Cd Length: 183  Bit Score: 133.74  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  418 EAKAKETAQRLWNEDEsiVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEAQQIDRILEAF 497
Cdd:pfam01369   30 EDDPESIAKFLFETPG--LDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAF 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  498 ANRYWECNTDcLLGSSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgNRRpqSDDHRTWE 577
Cdd:pfam01369  108 AERYYEQNPG-VFANADAAYVLAYSIIMLNTDLHNPNVKK-KMTLEDFIRN----------------LRG--INDGKDFP 167

                          170
                   ....*....|....*.
gi 1954572292  578 MEvenYLKEMYTSVKQ 593
Cdd:pfam01369  168 DE---YLEEIYDSIKK 180
 
Name Accession Description Interval E-value
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 711-849 1.78e-44

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 156.43  E-value: 1.78e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  711 YKEGIVIRKHLLENASQKA--KHREWKECYLEVgKNGELCMYQVQEqapqdkslfRHSSAHFTDRKSntlgghtkwVNNA 788
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTprGKRSWKMVYAVL-KDLVLYLYKDEH---------PPESSQFEDKKS---------LKNA 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954572292  789 qLMGKIALNHTLSNPlpPPGYNRqRPHVFAIQQPDGGVYLFQTTSSEQAQEWVSTCNYWAA 849
Cdd:pfam15410   62 -PVGKIRLHHALATP--APDYTK-KSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
 418-593 1.11e-35

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.


Pssm-ID: 460178  Cd Length: 183  Bit Score: 133.74  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  418 EAKAKETAQRLWNEDEsiVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEAQQIDRILEAF 497
Cdd:pfam01369   30 EDDPESIAKFLFETPG--LDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAF 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  498 ANRYWECNTDcLLGSSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgNRRpqSDDHRTWE 577
Cdd:pfam01369  108 AERYYEQNPG-VFANADAAYVLAYSIIMLNTDLHNPNVKK-KMTLEDFIRN----------------LRG--INDGKDFP 167

                          170
                   ....*....|....*.
gi 1954572292  578 MEvenYLKEMYTSVKQ 593
Cdd:pfam01369  168 DE---YLEEIYDSIKK 180
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
 408-592 1.82e-35

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


Pssm-ID: 238100  Cd Length: 185  Bit Score: 133.12  E-value: 1.82e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  408 DLMAKEDEDQEAkAKETAQRLWNEDEsiVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEA 487
Cdd:cd00171     22 FLIEKGFLEDDS-PKEIAKFLYETEG--LNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFRLPGEA 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  488 QQIDRILEAFANRYWECNTDCLLGSSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNTMstvldqkeheeslgnrr 567
Cdd:cd00171     99 QKIDRLLEKFSERYCECNPGIFSSSADAAYTLAYSIIMLNTDLHNPNVKK-KMTLEDFIKNLR----------------- 160

                          170       180
                   ....*....|....*....|....*
gi 1954572292  568 pQSDDHRTWEMEvenYLKEMYTSVK 592
Cdd:cd00171    161 -GINDGEDFPRE---FLKELYDSIK 181
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
 407-592 2.74e-28

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors).


Pssm-ID: 214569 [Multi-domain]  Cd Length: 189  Bit Score: 112.77  E-value: 2.74e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292   407 DDLMAKEDeDQEAKAKETAQRLwnEDESIVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAE 486
Cdd:smart00222   24 QSLQEKGF-LANEDPQDVADFL--SKNEGLNKKAIGDYLGEHDEFNRLVLHAFVDLFDFSAKDLDQALREFLESFRLPGE 100

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292   487 AQQIDRILEAFANRYWECNTDCLLGSS-DVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgN 565
Cdd:smart00222  101 AQKIDRLLEAFSSRYCECNPGVFSKANaDAAYTLAYSLIMLNTDLHNPNVKK-KMTLEDFIKN----------------V 163

                           170       180
                    ....*....|....*....|....*..
gi 1954572292   566 RRpqSDDHRTWEMEvenYLKEMYTSVK 592
Cdd:smart00222  164 RG--SNDGEDLPRE---FLEELYDSIK 185
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
 432-651 5.84e-17

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 86.80  E-value: 5.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  432 DESIVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEAQQIDRILEAFANRYWECNTDClLG 511
Cdd:PLN03076   657 DASGLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIMEKFAERYCKCNPKA-FS 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  512 SSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgNRrpQSDDHRTWEmevENYLKEMYTSV 591
Cdd:PLN03076   736 SADTAYVLAYSVIMLNTDAHNPMVKN-KMSADDFIRN----------------NR--GIDDGKDLP---EEFMRSLYERI 793

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  592 KQYQIlqPLKRKTSLVKRGSILGNRRVAGLKRSVNSIIRKSGIVDSMIIPEDFYPAIQPR 651
Cdd:PLN03076   794 SKNEI--KMKEDDLVPQQKQSANSNRILGLDSILNIVIRKRGEDSYMETSDDLIKHMQEQ 851
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 713-842 2.26e-10

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 58.39  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  713 EGIVIRKHLLENASQKAKHREWKECYLeVGKNGELCMYQVQEQAPQDKSLFRHSSahftdrksntlgghtkwVNNAQLMG 792
Cdd:cd10571      2 EGFLERKHEWESGGKKASNRSWKNVYT-VLRGQELSFYKDQKAAKSGITYAAEPP-----------------LNLYNAVC 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1954572292  793 KIALNHTlsnplpppgynrQRPHVFAIQQPDGGVYLFQTTSSEQAQEWVS 842
Cdd:cd10571     64 EVASDYT------------KKKHVFRLKLSDGAEFLFQAKDEEEMNQWVK 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 711-845 5.74e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 37.53  E-value: 5.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292   711 YKEGIVIRKHllenasqKAKHREWKECYLEVgKNGELCMYqvqeqapqdkslfrhssahftdrKSNtlgghtKWVNNAQL 790
Cdd:smart00233    2 IKEGWLYKKS-------GGGKKSWKKRYFVL-FNSTLLYY-----------------------KSK------KDKKSYKP 44

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1954572292   791 MGKIALNHTLSNPlPPPGYNRQRPHVFAIQQPDGGVYLFQTTSSEQAQEWVSTCN 845
Cdd:smart00233   45 KGSIDLSGCTVRE-APDPDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALR 98
 
Name Accession Description Interval E-value
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 711-849 1.78e-44

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 156.43  E-value: 1.78e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  711 YKEGIVIRKHLLENASQKA--KHREWKECYLEVgKNGELCMYQVQEqapqdkslfRHSSAHFTDRKSntlgghtkwVNNA 788
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTprGKRSWKMVYAVL-KDLVLYLYKDEH---------PPESSQFEDKKS---------LKNA 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954572292  789 qLMGKIALNHTLSNPlpPPGYNRqRPHVFAIQQPDGGVYLFQTTSSEQAQEWVSTCNYWAA 849
Cdd:pfam15410   62 -PVGKIRLHHALATP--APDYTK-KSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
 418-593 1.11e-35

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.


Pssm-ID: 460178  Cd Length: 183  Bit Score: 133.74  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  418 EAKAKETAQRLWNEDEsiVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEAQQIDRILEAF 497
Cdd:pfam01369   30 EDDPESIAKFLFETPG--LDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAF 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  498 ANRYWECNTDcLLGSSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgNRRpqSDDHRTWE 577
Cdd:pfam01369  108 AERYYEQNPG-VFANADAAYVLAYSIIMLNTDLHNPNVKK-KMTLEDFIRN----------------LRG--INDGKDFP 167

                          170
                   ....*....|....*.
gi 1954572292  578 MEvenYLKEMYTSVKQ 593
Cdd:pfam01369  168 DE---YLEEIYDSIKK 180
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
 408-592 1.82e-35

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


Pssm-ID: 238100  Cd Length: 185  Bit Score: 133.12  E-value: 1.82e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  408 DLMAKEDEDQEAkAKETAQRLWNEDEsiVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEA 487
Cdd:cd00171     22 FLIEKGFLEDDS-PKEIAKFLYETEG--LNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFRLPGEA 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  488 QQIDRILEAFANRYWECNTDCLLGSSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNTMstvldqkeheeslgnrr 567
Cdd:cd00171     99 QKIDRLLEKFSERYCECNPGIFSSSADAAYTLAYSIIMLNTDLHNPNVKK-KMTLEDFIKNLR----------------- 160

                          170       180
                   ....*....|....*....|....*
gi 1954572292  568 pQSDDHRTWEMEvenYLKEMYTSVK 592
Cdd:cd00171    161 -GINDGEDFPRE---FLKELYDSIK 181
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
 407-592 2.74e-28

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors).


Pssm-ID: 214569 [Multi-domain]  Cd Length: 189  Bit Score: 112.77  E-value: 2.74e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292   407 DDLMAKEDeDQEAKAKETAQRLwnEDESIVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAE 486
Cdd:smart00222   24 QSLQEKGF-LANEDPQDVADFL--SKNEGLNKKAIGDYLGEHDEFNRLVLHAFVDLFDFSAKDLDQALREFLESFRLPGE 100

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292   487 AQQIDRILEAFANRYWECNTDCLLGSS-DVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgN 565
Cdd:smart00222  101 AQKIDRLLEAFSSRYCECNPGVFSKANaDAAYTLAYSLIMLNTDLHNPNVKK-KMTLEDFIKN----------------V 163

                           170       180
                    ....*....|....*....|....*..
gi 1954572292   566 RRpqSDDHRTWEMEvenYLKEMYTSVK 592
Cdd:smart00222  164 RG--SNDGEDLPRE---FLEELYDSIK 185
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
 432-651 5.84e-17

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 86.80  E-value: 5.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  432 DESIVSKEKMAEWLGQGKAFNSTVLAHYMQYFNFDDMRLDTGFRKLCSKLYFKAEAQQIDRILEAFANRYWECNTDClLG 511
Cdd:PLN03076   657 DASGLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIMEKFAERYCKCNPKA-FS 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  512 SSDVVYAVVYSLLLLNTDLHVAQGKHvRMTRSEFIRNtmstvldqkeheeslgNRrpQSDDHRTWEmevENYLKEMYTSV 591
Cdd:PLN03076   736 SADTAYVLAYSVIMLNTDAHNPMVKN-KMSADDFIRN----------------NR--GIDDGKDLP---EEFMRSLYERI 793

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  592 KQYQIlqPLKRKTSLVKRGSILGNRRVAGLKRSVNSIIRKSGIVDSMIIPEDFYPAIQPR 651
Cdd:PLN03076   794 SKNEI--KMKEDDLVPQQKQSANSNRILGLDSILNIVIRKRGEDSYMETSDDLIKHMQEQ 851
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 713-842 2.26e-10

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 58.39  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292  713 EGIVIRKHLLENASQKAKHREWKECYLeVGKNGELCMYQVQEQAPQDKSLFRHSSahftdrksntlgghtkwVNNAQLMG 792
Cdd:cd10571      2 EGFLERKHEWESGGKKASNRSWKNVYT-VLRGQELSFYKDQKAAKSGITYAAEPP-----------------LNLYNAVC 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1954572292  793 KIALNHTlsnplpppgynrQRPHVFAIQQPDGGVYLFQTTSSEQAQEWVS 842
Cdd:cd10571     64 EVASDYT------------KKKHVFRLKLSDGAEFLFQAKDEEEMNQWVK 101
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 794-856 3.50e-10

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270107  Cd Length: 126  Bit Score: 58.49  E-value: 3.50e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954572292  794 IALNHTLSnpLPPPGYNRqRPHVFAIQQPDGGVYLFQTTSSEQAQEWVSTCNYWAARNSKEPL 856
Cdd:cd13295     66 ISVHHSLA--TKATDYTK-KPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPL 125
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 711-845 5.74e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 37.53  E-value: 5.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954572292   711 YKEGIVIRKHllenasqKAKHREWKECYLEVgKNGELCMYqvqeqapqdkslfrhssahftdrKSNtlgghtKWVNNAQL 790
Cdd:smart00233    2 IKEGWLYKKS-------GGGKKSWKKRYFVL-FNSTLLYY-----------------------KSK------KDKKSYKP 44

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1954572292   791 MGKIALNHTLSNPlPPPGYNRQRPHVFAIQQPDGGVYLFQTTSSEQAQEWVSTCN 845
Cdd:smart00233   45 KGSIDLSGCTVRE-APDPDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALR 98
 
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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