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Conserved domains on  [gi|762005996|ref|NP_001292113|]
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actin filament-associated protein 1-like 2 [Rattus norvegicus]

Protein Classification

AFAP1 family PH domain-containing protein( domain architecture ID 10193118)

AFAP1 family Pleckstrin homology (PH) domain-containing protein similar to mammalian actin filament-associated protein 1 (AFAP1) that can cross-link actin filaments into both network and bundle structures

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  15493994|22728242
SCOP:  3000134

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH1_AFAP cd13306
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1; There are ...
 184-290 7.12e-60

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. The amino terminal PH1 domain of AFAP1 has been known to function in intra-molecular regulation of AFAP1. In addition, the PH1 domain is a binding partner for PKCa and phospholipids. This cd is the first PH domain of AFAP. 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: 270116  Cd Length: 107  Bit Score: 198.48  E-value: 7.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 184 SPEASIELMRDARICAFLWRKKWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLLGSSVVHKEKQVRKKEHKLKIMPM 263
Cdd:cd13306    1 SEEASMELVKDARICAFLLRKKRFGQWAKQLCVIKDNRLLCYKSSKDQQPQLELPLLGCSVIYVPKDGRRKKHELKFTPP 80

                         90       100
                 ....*....|....*....|....*..
gi 762005996 264 NADVIVLGLQSKDQAEQWLRVIQEVSG 290
Cdd:cd13306   81 GAEALVLAVQSKEQAEQWLKVIREVSS 107
PH2_AFAP cd13307
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are ...
 372-472 1.02e-56

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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: 270117  Cd Length: 101  Bit Score: 189.51  E-value: 1.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 372 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRGKMAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 451
Cdd:cd13307    1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                         90       100
                 ....*....|....*....|.
gi 762005996 452 EEMGHWLGLLLSESGSKTDPE 472
Cdd:cd13307   81 EDMGRWLGVLLAETGSATDPE 101
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 675-779 2.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 675 DKLRVTSAEIKLGKNRTEAEVKRYTEEKRRLERSKEEIRGHLAQLRREKRELKETLLRCTDKgvVAKLEQALKRIDEECR 754
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERRR 312

                         90       100
                 ....*....|....*....|....*
gi 762005996 755 LEESRRVDLELSIVEVKDNLKKAEA 779
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEE 337
 
Name Accession Description Interval E-value
PH1_AFAP cd13306
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1; There are ...
 184-290 7.12e-60

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. The amino terminal PH1 domain of AFAP1 has been known to function in intra-molecular regulation of AFAP1. In addition, the PH1 domain is a binding partner for PKCa and phospholipids. This cd is the first PH domain of AFAP. 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: 270116  Cd Length: 107  Bit Score: 198.48  E-value: 7.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 184 SPEASIELMRDARICAFLWRKKWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLLGSSVVHKEKQVRKKEHKLKIMPM 263
Cdd:cd13306    1 SEEASMELVKDARICAFLLRKKRFGQWAKQLCVIKDNRLLCYKSSKDQQPQLELPLLGCSVIYVPKDGRRKKHELKFTPP 80

                         90       100
                 ....*....|....*....|....*..
gi 762005996 264 NADVIVLGLQSKDQAEQWLRVIQEVSG 290
Cdd:cd13306   81 GAEALVLAVQSKEQAEQWLKVIREVSS 107
PH2_AFAP cd13307
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are ...
 372-472 1.02e-56

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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: 270117  Cd Length: 101  Bit Score: 189.51  E-value: 1.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 372 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRGKMAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 451
Cdd:cd13307    1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                         90       100
                 ....*....|....*....|.
gi 762005996 452 EEMGHWLGLLLSESGSKTDPE 472
Cdd:cd13307   81 EDMGRWLGVLLAETGSATDPE 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 384-458 4.95e-10

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: 57.17  E-value: 4.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996   384 NSQWKSRWCFVRDSHLHFYQDR--NRGKMAQQPLSLVGCDVLPDPSPDHL---YSFRILHNGEELAKLEAKSSEEMGHWL 458
Cdd:smart00233  15 KKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGSIDLSGCTVREAPDPDSSkkpHCFEIKTSDRKTLLLQAESEEEREKWV 94
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 200-289 1.17e-07

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: 50.62  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996   200 FLWRKKW--LGQWAKQLCVIRDTRLLCYKSSK---DHSPQLDVNLLGSSVVH-KEKQVRKKEHKLKIMPMNADVIVLGLQ 273
Cdd:smart00233   6 WLYKKSGggKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKTLLLQAE 85

                           90
                   ....*....|....*.
gi 762005996   274 SKDQAEQWLRVIQEVS 289
Cdd:smart00233  86 SEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 385-458 2.99e-06

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.79  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996  385 SQWKSRWCFVRDSHLHFYQDRNRGKMA--QQPLSLVGC---DVLPDPSPDHLYSFRILH---NGEELAKLEAKSSEEMGH 456
Cdd:pfam00169  16 KSWKKRYFVLFDGSLLYYKDDKSGKSKepKGSISLSGCevvEVVASDSPKRKFCFELRTgerTGKRTYLLQAESEEERKD 95


                  ..
gi 762005996  457 WL 458
Cdd:pfam00169  96 WI 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 190-289 3.24e-06

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.40  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996  190 ELMRDARICAFLWRKKWlgqwakqlCVIRDTRLLCYKSS---KDHSPQLDVNLLGSSVVHKEKQVR-KKEHKLKI---MP 262
Cdd:pfam00169   6 WLLKKGGGKKKSWKKRY--------FVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSpKRKFCFELrtgER 77

                          90       100
                  ....*....|....*....|....*..
gi 762005996  263 MNADVIVLGLQSKDQAEQWLRVIQEVS 289
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSAI 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 675-779 2.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 675 DKLRVTSAEIKLGKNRTEAEVKRYTEEKRRLERSKEEIRGHLAQLRREKRELKETLLRCTDKgvVAKLEQALKRIDEECR 754
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERRR 312

                         90       100
                 ....*....|....*....|....*
gi 762005996 755 LEESRRVDLELSIVEVKDNLKKAEA 779
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEE 337
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
688-778 4.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 688 KNRTEAEVKRYTEEKRR---LERSKEEIRGHLAQLRREKRELKETLLRCTDKGV-VAKLEQALKRIDEECRLEESRRVDL 763
Cdd:PRK03918 192 EELIKEKEKELEEVLREineISSELPELREELEKLEKEVKELEELKEEIEELEKeLESLEGSKRKLEEKIRELEERIEEL 271

                         90
                 ....*....|....*
gi 762005996 764 ELSIVEVKDNLKKAE 778
Cdd:PRK03918 272 KKEIEELEEKVKELK 286
 
Name Accession Description Interval E-value
PH1_AFAP cd13306
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1; There are ...
 184-290 7.12e-60

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. The amino terminal PH1 domain of AFAP1 has been known to function in intra-molecular regulation of AFAP1. In addition, the PH1 domain is a binding partner for PKCa and phospholipids. This cd is the first PH domain of AFAP. 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: 270116  Cd Length: 107  Bit Score: 198.48  E-value: 7.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 184 SPEASIELMRDARICAFLWRKKWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLLGSSVVHKEKQVRKKEHKLKIMPM 263
Cdd:cd13306    1 SEEASMELVKDARICAFLLRKKRFGQWAKQLCVIKDNRLLCYKSSKDQQPQLELPLLGCSVIYVPKDGRRKKHELKFTPP 80

                         90       100
                 ....*....|....*....|....*..
gi 762005996 264 NADVIVLGLQSKDQAEQWLRVIQEVSG 290
Cdd:cd13306   81 GAEALVLAVQSKEQAEQWLKVIREVSS 107
PH2_AFAP cd13307
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are ...
 372-472 1.02e-56

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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: 270117  Cd Length: 101  Bit Score: 189.51  E-value: 1.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 372 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRGKMAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 451
Cdd:cd13307    1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                         90       100
                 ....*....|....*....|.
gi 762005996 452 EEMGHWLGLLLSESGSKTDPE 472
Cdd:cd13307   81 EDMGRWLGVLLAETGSATDPE 101
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 384-461 6.74e-11

Pleckstrin homology (PH) domain; 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: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 59.48  E-value: 6.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 384 NSQWKSRWCFVRDSHLHFYQDRN-RGKMAQQPLSLVG-CDVLPDPSPDHLYSFRILHNGEELAKLEAKSSEEMGHWLGLL 461
Cdd:cd00821   13 LKSWKKRWFVLFEGVLLYYKSKKdSSYKPKGSIPLSGiLEVEEVSPKERPHCFELVTPDGRTYYLQADSEEERQEWLKAL 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 384-458 4.95e-10

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: 57.17  E-value: 4.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996   384 NSQWKSRWCFVRDSHLHFYQDR--NRGKMAQQPLSLVGCDVLPDPSPDHL---YSFRILHNGEELAKLEAKSSEEMGHWL 458
Cdd:smart00233  15 KKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGSIDLSGCTVREAPDPDSSkkpHCFEIKTSDRKTLLLQAESEEEREKWV 94
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 200-289 1.17e-07

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: 50.62  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996   200 FLWRKKW--LGQWAKQLCVIRDTRLLCYKSSK---DHSPQLDVNLLGSSVVH-KEKQVRKKEHKLKIMPMNADVIVLGLQ 273
Cdd:smart00233   6 WLYKKSGggKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKTLLLQAE 85

                           90
                   ....*....|....*.
gi 762005996   274 SKDQAEQWLRVIQEVS 289
Cdd:smart00233  86 SEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 385-458 2.99e-06

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.79  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996  385 SQWKSRWCFVRDSHLHFYQDRNRGKMA--QQPLSLVGC---DVLPDPSPDHLYSFRILH---NGEELAKLEAKSSEEMGH 456
Cdd:pfam00169  16 KSWKKRYFVLFDGSLLYYKDDKSGKSKepKGSISLSGCevvEVVASDSPKRKFCFELRTgerTGKRTYLLQAESEEERKD 95


                  ..
gi 762005996  457 WL 458
Cdd:pfam00169  96 WI 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 190-289 3.24e-06

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.40  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996  190 ELMRDARICAFLWRKKWlgqwakqlCVIRDTRLLCYKSS---KDHSPQLDVNLLGSSVVHKEKQVR-KKEHKLKI---MP 262
Cdd:pfam00169   6 WLLKKGGGKKKSWKKRY--------FVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSpKRKFCFELrtgER 77

                          90       100
                  ....*....|....*....|....*..
gi 762005996  263 MNADVIVLGLQSKDQAEQWLRVIQEVS 289
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSAI 104
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
 187-290 8.65e-06

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. 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: 270118  Cd Length: 113  Bit Score: 45.47  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 187 ASIELMRDARICAFLWRK----KWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLLGSSVVHKEKQVRKKEHKLKIMP 262
Cdd:cd13308    1 QLLTLPRDVIHSGTLTKKggsqKTLQNWQLRYVIIHQGCVYYYKNDQSAKPKGVFSLNGYNRRAAEERTSKLKFVFKIIH 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 762005996 263 MNADVIVLGLQSKDQAEQ--WLRVIQEVSG 290
Cdd:cd13308   81 LSPDHRTWYFAAKSEDEMseWMEYIRREID 110
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 370-458 1.82e-04

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: 41.44  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 370 DRSLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDR-----NRGKMAQQPLSLVG--CDVLPDpspdhlY-----SFRI- 436
Cdd:cd10571    6 ERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQkaaksGITYAAEPPLNLYNavCEVASD------YtkkkhVFRLk 79

                         90       100
                 ....*....|....*....|..
gi 762005996 437 LHNGEELAkLEAKSSEEMGHWL 458
Cdd:cd10571   80 LSDGAEFL-FQAKDEEEMNQWV 100
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 201-285 5.10e-04

Pleckstrin homology (PH) domain; 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: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 39.83  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 201 LWRKKWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLD--VNLLGSSVVhKEKQVRKKEHKLKIMPMNADVIVLGLQSKDQA 278
Cdd:cd00821    7 KRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKgsIPLSGILEV-EEVSPKERPHCFELVTPDGRTYYLQADSEEER 85


                 ....*..
gi 762005996 279 EQWLRVI 285
Cdd:cd00821   86 QEWLKAL 92
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 386-458 5.90e-04

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 39.95  E-value: 5.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 762005996 386 QWKSRWCFVRDSHLHFYQDRNRGKmAQQPLSLVGCDVLPDPSPDHL---YSFRILHNGEELAKLEAKSSEEMGHWL 458
Cdd:cd13248   23 NWRKRWFVLKDNCLYYYKDPEEEK-ALGSILLPSYTISPAPPSDEIsrkFAFKAEHANMRTYYFAADTAEEMEQWM 97
PH_fermitin cd01237
Fermitin family pleckstrin homology (PH) domain; Fermitin functions as a mediator of integrin ...
 387-458 8.86e-04

Fermitin family pleckstrin homology (PH) domain; Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. 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: 269943  Cd Length: 125  Bit Score: 40.07  E-value: 8.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 762005996 387 WKSRWCFVRDSHLHFYQDRN-RGKMAQQPLSLVGCDVLPDPSpdhlysfriLHNGEELAKLEAKSSEEM-GHWL 458
Cdd:cd01237   20 YKRYWFVFKDTHLSYYKSKEeSNGAPIQQINLKGCEVTPDVN---------VSQQKFCIKLLVPSPEGMsEVWL 84
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 385-472 1.45e-03

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. 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: 270110  Cd Length: 106  Bit Score: 38.76  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 385 SQWKSRWCFVRDSHLHFYQDRNRGKM-AQQPLS-LVGCDVLPDPSPDH---LYS-FRILHngeelakLEAKSSEEMGHWL 458
Cdd:cd13298   20 KNWKKRWVVLRPCQLSYYKDEKEYKLrRVINLSeLLAVAPLKDKKRKNvfgIYTpSKNLH-------FRATSEKDANEWV 92

                         90
                 ....*....|....
gi 762005996 459 GLLLSESGSKTDPE 472
Cdd:cd13298   93 EALREEFRLDDEEE 106
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 675-779 2.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 675 DKLRVTSAEIKLGKNRTEAEVKRYTEEKRRLERSKEEIRGHLAQLRREKRELKETLLRCTDKgvVAKLEQALKRIDEECR 754
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERRR 312

                         90       100
                 ....*....|....*....|....*
gi 762005996 755 LEESRRVDLELSIVEVKDNLKKAEA 779
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEE 337
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 201-289 3.36e-03

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 38.02  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 201 LWRKKWlgqwakqlCVIRDTRLLCYKSSKDHSPQLDVNLLGSSV--VHKEKQVRKKeHKLKIMPMNADVIVLGLQSKDQA 278
Cdd:cd13248   23 NWRKRW--------FVLKDNCLYYYKDPEEEKALGSILLPSYTIspAPPSDEISRK-FAFKAEHANMRTYYFAADTAEEM 93

                         90
                 ....*....|.
gi 762005996 279 EQWLRVIQEVS 289
Cdd:cd13248   94 EQWMNAMSLAA 104
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
688-778 4.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 688 KNRTEAEVKRYTEEKRR---LERSKEEIRGHLAQLRREKRELKETLLRCTDKGV-VAKLEQALKRIDEECRLEESRRVDL 763
Cdd:PRK03918 192 EELIKEKEKELEEVLREineISSELPELREELEKLEKEVKELEELKEEIEELEKeLESLEGSKRKLEEKIRELEERIEEL 271

                         90
                 ....*....|....*
gi 762005996 764 ELSIVEVKDNLKKAE 778
Cdd:PRK03918 272 KKEIEELEEKVKELK 286
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
688-776 7.38e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762005996 688 KNRTEAEVKRYTEEKRRLERSKEEIRGHLAQLRREKRELKETLlrctdkgvvAKLEQALKRIDEECRLEEsrRVDLELSI 767
Cdd:COG2433  401 KEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI---------ERLERELSEARSEERREI--RKDREISR 469

                         90
                 ....*....|
gi 762005996 768 VEVK-DNLKK 776
Cdd:COG2433  470 LDREiERLER 479
 
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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