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Conserved domains on  [gi|767981142|ref|XP_011535311|]
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pleckstrin homology domain-containing family H member 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
1024-1130 8.39e-72

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17178:

Pssm-ID: 475130  Cd Length: 106  Bit Score: 234.47  E-value: 8.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRKPSHSGFALFTDDPSGRDLEHCLQGSVKICDAISKWEQAMKE 1103
Cdd:cd17178     1 PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRKPSHSGFALFTDDPSGKDLEHCLQGSVKICDVISKWEQALKE 80
                          90       100
                  ....*....|....*....|....*..
gi 767981142 1104 LHPGKSEgGTRVVKLMYKNRLYFRSQV 1130
Cdd:cd17178    81 LHPGKYE-GTRTVRLTYKSRLYFRAQA 106
FERM_C-lobe_PLEKHH1_PLEKHH2 cd13206
FERM domain C-lobe of Pleckstrin homology domain-containing family H; PLEKHH1 and PLEKHH2 ...
1254-1356 2.81e-56

FERM domain C-lobe of Pleckstrin homology domain-containing family H; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 241360  Cd Length: 100  Bit Score: 189.95  E-value: 2.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1254 GAKLFAAQPAQLSSKENALVWIAVNEDGVSILDHNTMQVHITYPYSSVTTFGGCRDDFMLVIRSIPDKssgKSHIEKLIF 1333
Cdd:cd13206     1 GAKLFAAKPKTPSSLENTVVWLAVNEDGISILDYNTMRLVVTYPYSSVMTFGGCQDDFMLVVNSIKDK---KKPTEKLLF 77
                          90       100
                  ....*....|....*....|...
gi 767981142 1334 RMAAPKIAEATFIMASYMNHCTT 1356
Cdd:cd13206    78 AMAKPKILEITLLIASYINAFHQ 100
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
581-676 6.85e-55

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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: 241436  Cd Length: 96  Bit Score: 185.58  E-value: 6.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLNSRCQIVRGEGSQTFQLISEKKTYYLTADSPSLL 660
Cdd:cd13282     1 KAGYLTKLGGKVKTWKRRWFVLKNGELFYYKSPNDVIRKPQGQIALDGSCEIARAEGAQTFEIVTEKRTYYLTADSENDL 80
                          90
                  ....*....|....*.
gi 767981142  661 EEWIRVLQSLLKVQAT 676
Cdd:cd13282    81 DEWIRVIQNVLRRQAS 96
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
860-1014 1.41e-54

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 214535  Cd Length: 152  Bit Score: 187.18  E-value: 1.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    860 YSKDGLYASLTTLPSEALQTEALKLFKSCQLFIN-VPVEaaSVDYHVSLAQTALQVCLVHPELQSEIYCQLMKQTSCRPP 938
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGdIPLP--RPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767981142    939 QkYSLMQCWQLLALCAPLFLPQHHFLWYVKQQLQRHADPRSeTGQYATYCQRAVERTLRTGEREARPSRMEVVSIL 1014
Cdd:smart00139   79 R-QSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADPGS-EQGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1027-1258 1.95e-27

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 111.23  E-value: 1.95e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   1027 IPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRkpSHSGFALFTDDPSGrDLEHCLQGSVKICDAISKWEQAmkelhp 1106
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIR--ESEYFGLQFEDPDE-DLRHWLDPAKTLLDQDVKSEPL------ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   1107 gkseggtrvvKLMYKNRLYFRSQVKGETDRERL-LLASQTSREIVAGRFPINKELALEMAALMAQVEYGDlekpalpgpg 1185
Cdd:smart00295   73 ----------TLYFRVKFYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGD---------- 132
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767981142   1186 gTSPAKAQHLLQQVLDRFHPRRYRHGAPAEQLRhlaDMLTTKWATLQGCSPPECIRIYLTVARKWPFFGAKLF 1258
Cdd:smart00295  133 -YDEELHDLRGELSLKRFLPKQLLDSRKLKEWR---ERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
20-171 5.99e-09

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 58.01  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   20 TLETQLFRFRlqasKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKnVDSEGSLHRKYQELLKAIKGK 99
Cdd:COG1579    14 ELDSELDRLE----HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEARIKKYEEQLGNVRNN 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767981142  100 DE---LISQLEAqLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG1579    89 KEyeaLQKEIES-LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
 
Name Accession Description Interval E-value
FERM_F1_PLEKHH1 cd17178
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1024-1130 8.39e-72

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 1 (PLEKHH1); PLEKHH1 is a homolog of Caenorhabditis elegans MAX-1 that has been implicated in motor neuron axon guidance. PLEKHH1 is critical in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH1 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340698  Cd Length: 106  Bit Score: 234.47  E-value: 8.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRKPSHSGFALFTDDPSGRDLEHCLQGSVKICDAISKWEQAMKE 1103
Cdd:cd17178     1 PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRKPSHSGFALFTDDPSGKDLEHCLQGSVKICDVISKWEQALKE 80
                          90       100
                  ....*....|....*....|....*..
gi 767981142 1104 LHPGKSEgGTRVVKLMYKNRLYFRSQV 1130
Cdd:cd17178    81 LHPGKYE-GTRTVRLTYKSRLYFRAQA 106
FERM_C-lobe_PLEKHH1_PLEKHH2 cd13206
FERM domain C-lobe of Pleckstrin homology domain-containing family H; PLEKHH1 and PLEKHH2 ...
1254-1356 2.81e-56

FERM domain C-lobe of Pleckstrin homology domain-containing family H; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 241360  Cd Length: 100  Bit Score: 189.95  E-value: 2.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1254 GAKLFAAQPAQLSSKENALVWIAVNEDGVSILDHNTMQVHITYPYSSVTTFGGCRDDFMLVIRSIPDKssgKSHIEKLIF 1333
Cdd:cd13206     1 GAKLFAAKPKTPSSLENTVVWLAVNEDGISILDYNTMRLVVTYPYSSVMTFGGCQDDFMLVVNSIKDK---KKPTEKLLF 77
                          90       100
                  ....*....|....*....|...
gi 767981142 1334 RMAAPKIAEATFIMASYMNHCTT 1356
Cdd:cd13206    78 AMAKPKILEITLLIASYINAFHQ 100
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
581-676 6.85e-55

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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: 241436  Cd Length: 96  Bit Score: 185.58  E-value: 6.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLNSRCQIVRGEGSQTFQLISEKKTYYLTADSPSLL 660
Cdd:cd13282     1 KAGYLTKLGGKVKTWKRRWFVLKNGELFYYKSPNDVIRKPQGQIALDGSCEIARAEGAQTFEIVTEKRTYYLTADSENDL 80
                          90
                  ....*....|....*.
gi 767981142  661 EEWIRVLQSLLKVQAT 676
Cdd:cd13282    81 DEWIRVIQNVLRRQAS 96
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
860-1014 1.41e-54

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 187.18  E-value: 1.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    860 YSKDGLYASLTTLPSEALQTEALKLFKSCQLFIN-VPVEaaSVDYHVSLAQTALQVCLVHPELQSEIYCQLMKQTSCRPP 938
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGdIPLP--RPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767981142    939 QkYSLMQCWQLLALCAPLFLPQHHFLWYVKQQLQRHADPRSeTGQYATYCQRAVERTLRTGEREARPSRMEVVSIL 1014
Cdd:smart00139   79 R-QSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADPGS-EQGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
908-1012 1.21e-38

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 139.64  E-value: 1.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   908 AQTALQVCLVHPELQSEIYCQLMKQTScRPPQKYSLMQCWQLLALCAPLFLPQHHFLWYVKQQLQRHADPRS-ETGQYAT 986
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTT-NNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADDPSrEVGKYAQ 79
                           90       100
                   ....*....|....*....|....*.
gi 767981142   987 YCQRAVERTLRTGEREARPSRMEVVS 1012
Cdd:pfam00784   80 FCLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1027-1258 1.95e-27

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 111.23  E-value: 1.95e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   1027 IPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRkpSHSGFALFTDDPSGrDLEHCLQGSVKICDAISKWEQAmkelhp 1106
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIR--ESEYFGLQFEDPDE-DLRHWLDPAKTLLDQDVKSEPL------ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   1107 gkseggtrvvKLMYKNRLYFRSQVKGETDRERL-LLASQTSREIVAGRFPINKELALEMAALMAQVEYGDlekpalpgpg 1185
Cdd:smart00295   73 ----------TLYFRVKFYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGD---------- 132
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767981142   1186 gTSPAKAQHLLQQVLDRFHPRRYRHGAPAEQLRhlaDMLTTKWATLQGCSPPECIRIYLTVARKWPFFGAKLF 1258
Cdd:smart00295  133 -YDEELHDLRGELSLKRFLPKQLLDSRKLKEWR---ERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
579-672 6.26e-18

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: 80.29  E-value: 6.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    579 LEKSGYLLKMGSQV-KTWKRRWFVLRQGQIMYYKSPSDV-IRKPQGQVDLNSrCQIVRGEGSQ------TFQLIS-EKKT 649
Cdd:smart00233    1 VIKEGWLYKKSGGGkKSWKKRYFVLFNSTLLYYKSKKDKkSYKPKGSIDLSG-CTVREAPDPDsskkphCFEIKTsDRKT 79
                            90       100
                    ....*....|....*....|...
gi 767981142    650 YYLTADSPSLLEEWIRVLQSLLK 672
Cdd:smart00233   80 LLLQAESEEEREKWVEALRKAIA 102
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
1133-1258 1.77e-17

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 79.62  E-value: 1.77e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  1133 ETDRERLLLASQTSREIVAGRFPINKELALEMAALMAQVEYGDLEKpalpgpggtspaKAQHLLQQVLDRFHPRRYRHGA 1212
Cdd:pfam00373    7 QDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQP------------SSHTSEYLSLESFLPKQLLRKM 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767981142  1213 PAEQLRhlaDMLTTKWATLQGCSPPECIRIYLTVARKWPFFGAKLF 1258
Cdd:pfam00373   75 KSKELE---KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PH pfam00169
PH domain; PH stands for pleckstrin homology.
579-672 3.46e-17

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 78.37  E-value: 3.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   579 LEKSGYLLKMGSQVK-TWKRRWFVLRQGQIMYYKSPSDVI-RKPQGQVDLNSrCQIVR------GEGSQTFQLI----SE 646
Cdd:pfam00169    1 VVKEGWLLKKGGGKKkSWKKRYFVLFDGSLLYYKDDKSGKsKEPKGSISLSG-CEVVEvvasdsPKRKFCFELRtgerTG 79
                           90       100
                   ....*....|....*....|....*.
gi 767981142   647 KKTYYLTADSPSLLEEWIRVLQSLLK 672
Cdd:pfam00169   80 KRTYLLQAESEEERKDWIKAIQSAIR 105
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
1137-1250 7.19e-14

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 68.81  E-value: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1137 ERLLLASQTSREIVAGRFPINKELALEMAALMAQVEYGDLEKPALPGpggtspakaqhlLQQVLDRFHPRRYRHGAPAEQ 1216
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKP------------KYLSLKRFLPKQLLKQRKPEE 68
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767981142 1217 LRhlaDMLTTKWATLQGCSPPECIRIYLTVARKW 1250
Cdd:cd14473    69 WE---KRIVELHKKLRGLSPAEAKLKYLKIARKL 99
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
20-171 5.99e-09

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 58.01  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   20 TLETQLFRFRlqasKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKnVDSEGSLHRKYQELLKAIKGK 99
Cdd:COG1579    14 ELDSELDRLE----HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEARIKKYEEQLGNVRNN 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767981142  100 DE---LISQLEAqLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG1579    89 KEyeaLQKEIES-LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
22-171 1.67e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 1.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    22 ETQLFRFRLQASKIRELLADKMQELEQrlleAEQRAENAETQVGvmEEKVKLSNLKNVDSEGsLHRKYQELLKAIKGK-- 99
Cdd:TIGR04523  252 QTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQLN--QLKSEISDLNNQKEQD-WNKELKSELKNQEKKle 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   100 ---------DELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTlKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAI 170
Cdd:TIGR04523  325 eiqnqisqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-EIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403

                   .
gi 767981142   171 Q 171
Cdd:TIGR04523  404 E 404
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-173 5.76e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   33 SKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKV-KLSNLKNVDSEgsLHRKYQELLKAIKgKDELISQLEAQLE 111
Cdd:PRK03918  299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEeRLEELKKKLKE--LEKRLEELEERHE-LYEEAKAKKEELE 375
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767981142  112 KQKQMRA----EEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKShnqrlveQVGSLQDALEAIQIA 173
Cdd:PRK03918  376 RLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKK-------EIKELKKAIEELKKA 434
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
37-133 6.29e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.94  E-value: 6.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    37 ELLADKMQELEQRL------LEAE----QRAENAETQvgvMEEKVKLSNLKNVDSEGSLHRKYQELLKAIKGKdelISQL 106
Cdd:pfam01576  906 ELLNDRLRKSTLQVeqltteLAAErstsQKSESARQQ---LERQNKELKAKLQEMEGTVKSKFKSSIAALEAK---IAQL 979
                           90       100
                   ....*....|....*....|....*..
gi 767981142   107 EAQLEKQKQMRAEEAKTVQEKAAKIKE 133
Cdd:pfam01576  980 EEQLEQESRERQAANKLVRRTEKKLKE 1006
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
91-166 9.68e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.47  E-value: 9.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   91 ELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIK----EWVTL---------KLAKLEMENQHLKshnQRLV 157
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEilndELIALqiennlleeKLRKLQEENDELV---ERWM 77

                  ....*....
gi 767981142  158 EQVGslQDA 166
Cdd:cd22887    78 AKKQ--QEA 84
 
Name Accession Description Interval E-value
FERM_F1_PLEKHH1 cd17178
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1024-1130 8.39e-72

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 1 (PLEKHH1); PLEKHH1 is a homolog of Caenorhabditis elegans MAX-1 that has been implicated in motor neuron axon guidance. PLEKHH1 is critical in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH1 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340698  Cd Length: 106  Bit Score: 234.47  E-value: 8.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRKPSHSGFALFTDDPSGRDLEHCLQGSVKICDAISKWEQAMKE 1103
Cdd:cd17178     1 PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRKPSHSGFALFTDDPSGKDLEHCLQGSVKICDVISKWEQALKE 80
                          90       100
                  ....*....|....*....|....*..
gi 767981142 1104 LHPGKSEgGTRVVKLMYKNRLYFRSQV 1130
Cdd:cd17178    81 LHPGKYE-GTRTVRLTYKSRLYFRAQA 106
FERM_F1_Max1_like cd17094
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Caenorhabditis ...
1024-1126 1.77e-60

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Caenorhabditis elegans max-1 and its homologs PLEKHH1 and PLEKHH2; Caenorhabditis elegans max-1 is expressed and functions in motor neurons. MAX-1 protein plays a possible role in netrin-induced axon repulsion by modulating the UNC-5 receptor signaling pathway. PLEKHH1 is critically required in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH2 is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. It is involved in matrix adhesion and actin dynamics. Members in this family all contain two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340614  Cd Length: 102  Bit Score: 201.70  E-value: 1.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRKPSHSGFALFTDDPSGRDLEHCLQGSVKICDAISKWEQAMKE 1103
Cdd:cd17094     1 PISIPVHLPNGTYQVVGFDGSTTVEEFLQTLNLELGIRPPSQSGFALFSDDPIGKDIEHCLQPSVKICDVISKWERASRE 80
                          90       100
                  ....*....|....*....|...
gi 767981142 1104 LHPGKSEgGTRVVKLMYKNRLYF 1126
Cdd:cd17094    81 AHSGKVD-SSRVIRLTYKNRLYF 102
FERM_F1_PLEKHH2 cd17179
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1024-1126 7.02e-59

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 2 (PLEKHH2); PLEKHH2 is a novel podocyte protein downregulated in human focal segmental glomerulosclerosis. It is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. PLEKHH2 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PLEKHH2 is involved in matrix adhesion and actin dynamics. It directly interacts through its FERM domain with the focal adhesion protein Hic-5 and actin.


Pssm-ID: 340699  Cd Length: 103  Bit Score: 197.50  E-value: 7.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRKPSHSGFALFTDDPSGRDLEHCLQGSVKICDAISKWEQAMKE 1103
Cdd:cd17179     1 PFSIPVHFMNGTYQVVGFDASTTVEEFLNTLNQDTGMRKPGQSGFALFTDDPSGKDLEHCLQGNIKICDIISKWEQASKE 80
                          90       100
                  ....*....|....*....|...
gi 767981142 1104 LHPGKSEgGTRVVKLMYKNRLYF 1126
Cdd:cd17179    81 QHPGKCE-GTRTVRLTYKNRLYF 102
FERM_C-lobe_PLEKHH1_PLEKHH2 cd13206
FERM domain C-lobe of Pleckstrin homology domain-containing family H; PLEKHH1 and PLEKHH2 ...
1254-1356 2.81e-56

FERM domain C-lobe of Pleckstrin homology domain-containing family H; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 241360  Cd Length: 100  Bit Score: 189.95  E-value: 2.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1254 GAKLFAAQPAQLSSKENALVWIAVNEDGVSILDHNTMQVHITYPYSSVTTFGGCRDDFMLVIRSIPDKssgKSHIEKLIF 1333
Cdd:cd13206     1 GAKLFAAKPKTPSSLENTVVWLAVNEDGISILDYNTMRLVVTYPYSSVMTFGGCQDDFMLVVNSIKDK---KKPTEKLLF 77
                          90       100
                  ....*....|....*....|...
gi 767981142 1334 RMAAPKIAEATFIMASYMNHCTT 1356
Cdd:cd13206    78 AMAKPKILEITLLIASYINAFHQ 100
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
581-676 6.85e-55

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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: 241436  Cd Length: 96  Bit Score: 185.58  E-value: 6.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLNSRCQIVRGEGSQTFQLISEKKTYYLTADSPSLL 660
Cdd:cd13282     1 KAGYLTKLGGKVKTWKRRWFVLKNGELFYYKSPNDVIRKPQGQIALDGSCEIARAEGAQTFEIVTEKRTYYLTADSENDL 80
                          90
                  ....*....|....*.
gi 767981142  661 EEWIRVLQSLLKVQAT 676
Cdd:cd13282    81 DEWIRVIQNVLRRQAS 96
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
860-1014 1.41e-54

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 187.18  E-value: 1.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    860 YSKDGLYASLTTLPSEALQTEALKLFKSCQLFIN-VPVEaaSVDYHVSLAQTALQVCLVHPELQSEIYCQLMKQTSCRPP 938
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGdIPLP--RPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767981142    939 QkYSLMQCWQLLALCAPLFLPQHHFLWYVKQQLQRHADPRSeTGQYATYCQRAVERTLRTGEREARPSRMEVVSIL 1014
Cdd:smart00139   79 R-QSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADPGS-EQGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
908-1012 1.21e-38

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 139.64  E-value: 1.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   908 AQTALQVCLVHPELQSEIYCQLMKQTScRPPQKYSLMQCWQLLALCAPLFLPQHHFLWYVKQQLQRHADPRS-ETGQYAT 986
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTT-NNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADDPSrEVGKYAQ 79
                           90       100
                   ....*....|....*....|....*.
gi 767981142   987 YCQRAVERTLRTGEREARPSRMEVVS 1012
Cdd:pfam00784   80 FCLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1027-1258 1.95e-27

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 111.23  E-value: 1.95e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   1027 IPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRkpSHSGFALFTDDPSGrDLEHCLQGSVKICDAISKWEQAmkelhp 1106
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIR--ESEYFGLQFEDPDE-DLRHWLDPAKTLLDQDVKSEPL------ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   1107 gkseggtrvvKLMYKNRLYFRSQVKGETDRERL-LLASQTSREIVAGRFPINKELALEMAALMAQVEYGDlekpalpgpg 1185
Cdd:smart00295   73 ----------TLYFRVKFYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGD---------- 132
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767981142   1186 gTSPAKAQHLLQQVLDRFHPRRYRHGAPAEQLRhlaDMLTTKWATLQGCSPPECIRIYLTVARKWPFFGAKLF 1258
Cdd:smart00295  133 -YDEELHDLRGELSLKRFLPKQLLDSRKLKEWR---ERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
581-667 4.71e-21

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: 89.14  E-value: 4.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGS-QVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLNSRCQIV---RGEGSQTFQLI-SEKKTYYLTAD 655
Cdd:cd00821     1 KEGYLLKRGGgGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIPLSGILEVEevsPKERPHCFELVtPDGRTYYLQAD 80
                          90
                  ....*....|..
gi 767981142  656 SPSLLEEWIRVL 667
Cdd:cd00821    81 SEEERQEWLKAL 92
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
577-667 2.11e-18

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. 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: 270075  Cd Length: 110  Bit Score: 82.08  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  577 ESLEKSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSD--VIRkpqgQVDLN-----SRCQIVRGEgsQTFQLISEKKT 649
Cdd:cd13255     4 EAVLKAGYLEKKGERRKTWKKRWFVLRPTKLAYYKNDKEyrLLR----LIDLTdihtcTEVQLKKHD--NTFGIVTPART 77
                          90
                  ....*....|....*...
gi 767981142  650 YYLTADSPSLLEEWIRVL 667
Cdd:cd13255    78 FYVQADSKAEMESWISAI 95
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
579-672 6.26e-18

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: 80.29  E-value: 6.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    579 LEKSGYLLKMGSQV-KTWKRRWFVLRQGQIMYYKSPSDV-IRKPQGQVDLNSrCQIVRGEGSQ------TFQLIS-EKKT 649
Cdd:smart00233    1 VIKEGWLYKKSGGGkKSWKKRYFVLFNSTLLYYKSKKDKkSYKPKGSIDLSG-CTVREAPDPDsskkphCFEIKTsDRKT 79
                            90       100
                    ....*....|....*....|...
gi 767981142    650 YYLTADSPSLLEEWIRVLQSLLK 672
Cdd:smart00233   80 LLLQAESEEEREKWVEALRKAIA 102
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
1133-1258 1.77e-17

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 79.62  E-value: 1.77e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  1133 ETDRERLLLASQTSREIVAGRFPINKELALEMAALMAQVEYGDLEKpalpgpggtspaKAQHLLQQVLDRFHPRRYRHGA 1212
Cdd:pfam00373    7 QDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQP------------SSHTSEYLSLESFLPKQLLRKM 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767981142  1213 PAEQLRhlaDMLTTKWATLQGCSPPECIRIYLTVARKWPFFGAKLF 1258
Cdd:pfam00373   75 KSKELE---KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
581-671 2.27e-17

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. 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: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 78.52  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVirKPQGQVDLNsRCQIVRGEGSQ----TFQLISEKKTYYLTADS 656
Cdd:cd10573     5 KEGYLTKLGGIVKNWKTRWFVLRRNELKYFKTRGDT--KPIRVLDLR-ECSSVQRDYSQgkvnCFCLVFPERTFYMYANT 81
                          90
                  ....*....|....*
gi 767981142  657 PSLLEEWIRVLQSLL 671
Cdd:cd10573    82 EEEADEWVKLLKWKL 96
PH pfam00169
PH domain; PH stands for pleckstrin homology.
579-672 3.46e-17

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 78.37  E-value: 3.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   579 LEKSGYLLKMGSQVK-TWKRRWFVLRQGQIMYYKSPSDVI-RKPQGQVDLNSrCQIVR------GEGSQTFQLI----SE 646
Cdd:pfam00169    1 VVKEGWLLKKGGGKKkSWKKRYFVLFDGSLLYYKDDKSGKsKEPKGSISLSG-CEVVEvvasdsPKRKFCFELRtgerTG 79
                           90       100
                   ....*....|....*....|....*.
gi 767981142   647 KKTYYLTADSPSLLEEWIRVLQSLLK 672
Cdd:pfam00169   80 KRTYLLQAESEEERKDWIKAIQSAIR 105
PH2_MyoX cd13296
Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular ...
581-669 1.94e-16

Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the second 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: 270108  Cd Length: 103  Bit Score: 76.35  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQV-----KTWKRRWFVLRQGQIMYYKSPSDViRKPQGQVDLNSRCQIV-RGEGSQTFQLISEKKTYYLTA 654
Cdd:cd13296     1 KSGWLTKKGGGSstlsrRNWKSRWFVLRDTVLKYYENDQEG-EKLLGTIDIRSAKEIVdNDPKENRLSITTEERTYHLVA 79
                          90
                  ....*....|....*
gi 767981142  655 DSPSLLEEWIRVLQS 669
Cdd:cd13296    80 ESPEDASQWVNVLTR 94
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
581-677 4.85e-16

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal 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: 270092  Cd Length: 110  Bit Score: 75.41  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLNSRCQI----VRGEGSQTFQLISEKKTYYLTADS 656
Cdd:cd13273    10 KKGYLWKKGHLLPTWTERWFVLKPNSLSYYKSEDL--KEKKGEIALDSNCCVeslpDREGKKCRFLVKTPDKTYELSASD 87
                          90       100
                  ....*....|....*....|.
gi 767981142  657 PSLLEEWIRVLQSLLKVQATG 677
Cdd:cd13273    88 HKTRQEWIAAIQTAIRLSQEG 108
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
1029-1126 5.31e-16

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340728  Cd Length: 98  Bit Score: 74.59  E-value: 5.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1029 VHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRkPSHSGFALFTDDPsgrDLEHCLQGSVKICDAISKWEQAMKELhpgK 1108
Cdd:cd17208     8 FYFLDGQFKALEFDSAATAAEVLEQLKQKIGLR-STADGFALYEVFG---GIERAILPEEKVADVLSKWEKLQRTM---A 80
                          90
                  ....*....|....*...
gi 767981142 1109 SEGGTRVVKLMYKNRLYF 1126
Cdd:cd17208    81 SCAAQQAVKFVFKKRLFF 98
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
581-667 6.71e-16

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: 74.62  E-value: 6.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKM-GSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLNS---RCQIVRGEGSQTFQLISEK---KTYYLT 653
Cdd:cd13248     9 MSGWLHKQgGSGLKNWRKRWFVLKDNCLYYYKDPEE--EKALGSILLPSytiSPAPPSDEISRKFAFKAEHanmRTYYFA 86
                          90
                  ....*....|....
gi 767981142  654 ADSPSLLEEWIRVL 667
Cdd:cd13248    87 ADTAEEMEQWMNAM 100
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
581-674 6.92e-16

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but 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: 275402  Cd Length: 116  Bit Score: 74.97  E-value: 6.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDvIRKPQGQVDLN--SRCQIVRGEGSQT--FQLISEKKTYYLTADS 656
Cdd:cd13215    23 KSGYLSKRSKRTLRYTRYWFVLKGDTLSWYNSSTD-LYFPAGTIDLRyaTSIELSKSNGEATtsFKIVTNSRTYKFKADS 101
                          90
                  ....*....|....*...
gi 767981142  657 PSLLEEWIRVLQsllKVQ 674
Cdd:cd13215   102 ETSADEWVKALK---KQI 116
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
581-669 1.28e-15

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. 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: 270070  Cd Length: 98  Bit Score: 73.79  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQV-KTWKRRWFVLRQGQIMYYKSPSDV--------IR----KPQGQVDLNSrCqivrgegsqtFQLISEK 647
Cdd:cd13250     1 KEGYLFKRSSNAfKTWKRRWFSLQNGQLYYQKRDKKDeptvmvedLRlctvKPTEDSDRRF-C----------FEVISPT 69
                          90       100
                  ....*....|....*....|..
gi 767981142  648 KTYYLTADSPSLLEEWIRVLQS 669
Cdd:cd13250    70 KSYMLQAESEEDRQAWIQAIQS 91
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
581-670 3.57e-15

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: 72.66  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLN--SRCQIVRGEGSQ-TFQLISEKKTYYLTADSP 657
Cdd:cd13298     8 KSGYLLKRSRKTKNWKKRWVVLRPCQLSYYKDEKE--YKLRRVINLSelLAVAPLKDKKRKnVFGIYTPSKNLHFRATSE 85
                          90
                  ....*....|...
gi 767981142  658 SLLEEWIRVLQSL 670
Cdd:cd13298    86 KDANEWVEALREE 98
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
581-667 1.06e-14

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 270083  Cd Length: 114  Bit Score: 71.65  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVirKPQGQVDLnSRCQI------VRGEGSQTFQLI---------S 645
Cdd:cd13263     5 KSGWLKKQGSIVKNWQQRWFVLRGDQLYYYKDEDDT--KPQGTIPL-PGNKVkevpfnPEEPGKFLFEIIpggggdrmtS 81
                          90       100
                  ....*....|....*....|..
gi 767981142  646 EKKTYYLTADSPSLLEEWIRVL 667
Cdd:cd13263    82 NHDSYLLMANSQAEMEEWVKVI 103
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
581-664 2.91e-14

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. 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: 270095  Cd Length: 106  Bit Score: 70.04  E-value: 2.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPsDVIR--KPQGQVDLNSrCQIVRGEGSQT-----FQLISEKKTYYLT 653
Cdd:cd13276     1 KAGWLEKQGEFIKTWRRRWFVLKQGKLFWFKEP-DVTPysKPRGVIDLSK-CLTVKSAEDATnkenaFELSTPEETFYFI 78
                          90
                  ....*....|.
gi 767981142  654 ADSPSLLEEWI 664
Cdd:cd13276    79 ADNEKEKEEWI 89
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
1137-1250 7.19e-14

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 68.81  E-value: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1137 ERLLLASQTSREIVAGRFPINKELALEMAALMAQVEYGDLEKPALPGpggtspakaqhlLQQVLDRFHPRRYRHGAPAEQ 1216
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKP------------KYLSLKRFLPKQLLKQRKPEE 68
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767981142 1217 LRhlaDMLTTKWATLQGCSPPECIRIYLTVARKW 1250
Cdd:cd14473    69 WE---KRIVELHKKLRGLSPAEAKLKYLKIARKL 99
PH_Sbf1_hMTMR5 cd01235
Set binding factor 1 (also called Human MTMR5) Pleckstrin Homology (PH) domain; Sbf1 is a ...
583-672 1.26e-13

Set binding factor 1 (also called Human MTMR5) Pleckstrin Homology (PH) domain; Sbf1 is a myotubularin-related pseudo-phosphatase. Both Sbf1 and myotubularin interact with the SET domains of Hrx and other epigenetic regulatory proteins, but Sbf1 lacks phosphatase activity due to several amino acid changes in its structurally preserved catalytic pocket. It contains pleckstrin (PH), GEF, and myotubularin homology domains that are thought to be responsible for signaling and growth control. Sbf1 functions as an inhibitor of cellular growth. The N-terminal GEF homology domain serves to inhibit the transforming effects of Sbf1. 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: 269941  Cd Length: 106  Bit Score: 68.13  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  583 GYLLKMGSQVKTWKRRWFVL--RQGQIMYYKSPSDviRKPQGQVDLN--SRCQIV--------RGEGSQTFQLISEKKTY 650
Cdd:cd01235     7 GYLYKRGALLKGWKQRWFVLdsTKHQLRYYESRED--TKCKGFIDLAevESVTPAtpiigapkRADEGAFFDLKTNKRVY 84
                          90       100
                  ....*....|....*....|..
gi 767981142  651 YLTADSPSLLEEWIRVLQSLLK 672
Cdd:cd01235    85 NFCAFDAESAQQWIEKIQSCLS 106
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
577-668 1.72e-13

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 68.42  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  577 ESLEKSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLnSRCQIVRGEGSQ--TFQLI---SEKKTYY 651
Cdd:cd13288     6 SPVDKEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKKGD--REPLGVIVL-EGCTVELAEDAEpyAFAIRfdgPGARSYV 82
                          90
                  ....*....|....*..
gi 767981142  652 LTADSPSLLEEWIRVLQ 668
Cdd:cd13288    83 LAAENQEDMESWMKALS 99
PH_TBC1D2A cd01265
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1 ...
582-669 2.00e-13

TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. 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: 269966  Cd Length: 102  Bit Score: 67.73  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKM---GSQVKTWKRRWFVL--RQGQIMYYKSPSDVirKPQGQVDLNSRC---QIVRGEGsqTFQLISEKKTYYLT 653
Cdd:cd01265     3 CGYLNKLetrGLGLKGWKRRWFVLdeSKCQLYYYRSPQDA--TPLGSIDLSGAAfsyDPEAEPG--QFEIHTPGRVHILK 78
                          90
                  ....*....|....*.
gi 767981142  654 ADSPSLLEEWIRVLQS 669
Cdd:cd01265    79 ASTRQAMLYWLQALQS 94
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
580-669 6.54e-12

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. 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: 269954  Cd Length: 119  Bit Score: 63.87  E-value: 6.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  580 EKSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLNS----RCQIVRGE------GSQTFQLISEKKT 649
Cdd:cd01252     4 DREGWLLKLGGRVKSWKRRWFILTDNCLYYFEYTTD--KEPRGIIPLENlsvrEVEDKKKPfcfelySPSNGQVIKACKT 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767981142  650 -------------YYLTADSPSLLEEWIRVLQS 669
Cdd:cd01252    82 dsdgkvvegnhtvYRISAASEEERDEWIKSIKA 114
PH2_TAPP1_2 cd13271
Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal ...
576-679 1.61e-11

Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal repeat; The binding of TAPP1 (also called PLEKHA1/pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1) and TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP1 and TAPP2 contain two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. 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: 270090  Cd Length: 114  Bit Score: 62.37  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  576 GESLEKSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLNSRCQIVRGEGSQT------FQLISEKKT 649
Cdd:cd13271     5 GRNVIKSGYCVKQGAVRKNWKRRFFILDDNTISYYKSETD--KEPLRTIPLREVLKVHECLVKSLlmrdnlFEIITTSRT 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 767981142  650 YYLTADSPSLLEEWIRVLQSLLKVQATGPP 679
Cdd:cd13271    83 FYIQADSPEEMHSWIKAISGAIVARRGPSR 112
PH_Gab-like cd13324
Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are ...
582-665 1.57e-10

Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. There are 3 families: Gab1, Gab2, and Gab3. 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: 270133  Cd Length: 112  Bit Score: 59.73  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKMGSQVK----TWKRRWFVLRQGQIM-------YYKspSDVIRKPQGQVDLNsRCQIV---------RGEGSQTF 641
Cdd:cd13324     4 EGWLTKSPPEKKiwraAWRRRWFVLRSGRLSggqdvleYYT--DDHCKKLKGIIDLD-QCEQVdagltfekkKFKNQFIF 80
                          90       100
                  ....*....|....*....|....
gi 767981142  642 QLISEKKTYYLTADSPSLLEEWIR 665
Cdd:cd13324    81 DIRTPKRTYYLVAETEEEMNKWVR 104
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
581-681 1.74e-10

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. 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: 270094  Cd Length: 104  Bit Score: 59.27  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRK-PQGQVDLNSrCQIV------RGEGsqtFQLIS-EKKTYYL 652
Cdd:cd13275     1 KKGWLMKQGSRQGEWSKHWFVLRGAALKYYRDPSAEEAGeLDGVIDLSS-CTEVtelpvsRNYG---FQVKTwDGKVYVL 76
                          90       100
                  ....*....|....*....|....*....
gi 767981142  653 TADSPSLLEEWIRVLQSllKVQATGPPAL 681
Cdd:cd13275    77 SAMTSGIRTNWIQALRK--AAGLPSPPAL 103
PH2_ADAP cd01251
ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 2; ADAP (also called ...
581-671 3.22e-10

ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 2; ADAP (also called centaurin alpha) is a phophatidlyinositide binding protein consisting of an N-terminal ArfGAP domain and two PH domains. In response to growth factor activation, PI3K phosphorylates phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 1 is recruited to the plasma membrane following growth factor stimulation by specific binding of its PH domain to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 2 is constitutively bound to the plasma membrane since it binds phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate with equal affinity. This cd contains the second PH domain 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: 241282  Cd Length: 105  Bit Score: 58.37  E-value: 3.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMG-SQVKTWKRRWFVLRQGQIMYYKSPSDVIrkPQGQVDLNSRCQ---IVRG-------EGSQTFQLISEKKT 649
Cdd:cd01251     4 KEGYLEKTGpKQTDGFRKRWFTLDDRRLMYFKDPLDAF--PKGEIFIGSKEEgysVREGlppgikgHWGFGFTLVTPDRT 81
                          90       100
                  ....*....|....*....|..
gi 767981142  650 YYLTADSPSLLEEWIRVLQSLL 671
Cdd:cd01251    82 FLLSAETEEERREWITAIQKVL 103
PH_RASA1 cd13260
RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...
578-668 4.17e-10

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. 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: 270080  Cd Length: 103  Bit Score: 58.12  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  578 SLEKSGYLLKMGSQVKTWKRRWFVLRQG--QIMYYKSPSDVirKPQGQVDLNSrCQIVRGEGS-----QTFQLI----SE 646
Cdd:cd13260     2 GIDKKGYLLKKGGKNKKWKNLYFVLEGKeqHLYFFDNEKRT--KPKGLIDLSY-CSLYPVHDSlfgrpNCFQIVvralNE 78
                          90       100
                  ....*....|....*....|..
gi 767981142  647 KKTYYLTADSPSLLEEWIRVLQ 668
Cdd:cd13260    79 STITYLCADTAELAQEWMRALR 100
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
565-679 5.22e-10

Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. 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: 270109  Cd Length: 126  Bit Score: 58.60  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  565 SSYSTDGlglGGESLEKSGYLLKMG--SQVKTW---KRRWFVLRQGQIMYYKSPSDVIRKpQGQVDLNSRCQIVRGE--- 636
Cdd:cd13297     2 PKGDLDE---GGQDVIERGWLYKEGgkGGARGNltkKKRWFVLTGNSLDYYKSSEKNSLK-LGTLVLNSLCSVVPPDekm 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767981142  637 ----GSQTFQLISEKKTYYLTAdspSLLEEWIRVLQSLLKVQATGPP 679
Cdd:cd13297    78 aketGYWTFTVHGRKHSFRLYT---KLQEEAMRWVNAIQDVIDSKPP 121
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
580-674 6.23e-10

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. 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: 270073  Cd Length: 94  Bit Score: 57.40  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  580 EKSGYLLKMGSQ--VKTWKRRWFVLRQGQIMYYKSPSDVIRKpqGQVDLnSRCQIVRGEGSQTFQLISEKKTYYLTADSP 657
Cdd:cd13253     1 IKSGYLDKQGGQgnNKGFQKRWVVFDGLSLRYFDSEKDAYSK--RIIPL-SAISTVRAVGDNKFELVTTNRTFVFRAESD 77
                          90
                  ....*....|....*..
gi 767981142  658 SLLEEWIRVLQSLLKVQ 674
Cdd:cd13253    78 DERNLWCSTLQAAISEY 94
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
581-665 1.24e-09

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain 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: 270113  Cd Length: 108  Bit Score: 57.00  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLNSrCQIVR-----GEGSQTFQLISEKKT-YYLTA 654
Cdd:cd13301     5 KEGYLVKKGHVVNNWKARWFVLKEDGLEYYKKKTD--SSPKGMIPLKG-CTITSpcleyGKRPLVFKLTTAKGQeHFFQA 81
                          90
                  ....*....|.
gi 767981142  655 DSPSLLEEWIR 665
Cdd:cd13301    82 CSREERDAWAK 92
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
581-667 5.03e-09

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: 55.49  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKT---WKRRWFVLRQGQIMYYKSPSDVirKPQGQVDLN--SRCQI--VRGEGSQTFQLI---SEKKTY 650
Cdd:cd13308    11 HSGTLTKKGGSQKTlqnWQLRYVIIHQGCVYYYKNDQSA--KPKGVFSLNgyNRRAAeeRTSKLKFVFKIIhlsPDHRTW 88
                          90
                  ....*....|....*..
gi 767981142  651 YLTADSPSLLEEWIRVL 667
Cdd:cd13308    89 YFAAKSEDEMSEWMEYI 105
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
580-673 5.75e-09

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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: 269964  Cd Length: 121  Bit Score: 55.36  E-value: 5.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  580 EKSGYL--LKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRK-PQGQVDL----NSRCQIVRGE---GSQTFQLI----- 644
Cdd:cd01263     3 EYRGFLtvFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKkPIGSIDLtkciTEKVEPAPRElcaRPNTFLLEtlrpa 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767981142  645 --------SEKKTYYLTADSPSLLEEWIRVLQSLLKV 673
Cdd:cd01263    83 edddrddtNEKIRVLLSADTKEERIEWLSALNQTLAD 119
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
20-171 5.99e-09

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 58.01  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   20 TLETQLFRFRlqasKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKnVDSEGSLHRKYQELLKAIKGK 99
Cdd:COG1579    14 ELDSELDRLE----HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEARIKKYEEQLGNVRNN 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767981142  100 DE---LISQLEAqLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG1579    89 KEyeaLQKEIES-LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
PH_OSBP_ORP4 cd13284
Human Oxysterol binding protein and OSBP-related protein 4 Pleckstrin homology (PH) domain; ...
581-675 7.57e-09

Human Oxysterol binding protein and OSBP-related protein 4 Pleckstrin homology (PH) domain; Human OSBP is proposed to function is sterol-dependent regulation of ERK dephosphorylation and sphingomyelin synthesis as well as modulation of insulin signaling and hepatic lipogenesis. It contains a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBPs and Osh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. ORP4 is proposed to function in Vimentin-dependent sterol transport and/or signaling. Human ORP4 has 2 forms, a long (ORP4L) and a short (ORP4S). ORP4L contains a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP4S is truncated and contains only an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 270101  Cd Length: 99  Bit Score: 54.31  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLNSRCqiVRGEGSQTFqLISE--KKTYYLTADSPS 658
Cdd:cd13284     1 MKGWLLKWTNYIKGYQRRWFVLSNGLLSYYRNQAEMAHTCRGTINLAGAE--IHTEDSCNF-VISNggTQTFHLKASSEV 77
                          90
                  ....*....|....*..
gi 767981142  659 LLEEWIRVLQsLLKVQA 675
Cdd:cd13284    78 ERQRWVTALE-LAKAKA 93
PH_Gab1_Gab2 cd01266
Grb2-associated binding proteins 1 and 2 pleckstrin homology (PH) domain; The Gab subfamily ...
575-665 1.00e-08

Grb2-associated binding proteins 1 and 2 pleckstrin homology (PH) domain; The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. The members in this cd include the Gab1 and Gab2 proteins. 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: 241297  Cd Length: 123  Bit Score: 54.95  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  575 GGESLeKSGYLLKMGSQVK----TWKRRWFVLRQGQIM-------YYKspSDVIRKPQGQVDLNSRCQIVRG-------- 635
Cdd:cd01266     1 GGEVV-CSGWLRKSPPEKKlrryAWKKRWFVLRSGRLSgdpdvleYYK--NDHAKKPIRVIDLNLCEQVDAGltfnkkel 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 767981142  636 EGSQTFQLISEKKTYYLTADSPSLLEEWIR 665
Cdd:cd01266    78 ENSYIFDIKTIDRIFYLVAETEEDMNKWVR 107
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
577-671 1.34e-08

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241529  Cd Length: 116  Bit Score: 54.18  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  577 ESLEKSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVirKPQGQVDLNSR----------------CQIVRGEGSQT 640
Cdd:cd13378     1 EGVLKAGWLKKQRSIMKNWQQRWFVLRGDQLFYYKDEEET--KPQGCISLQGSqvnelppnpeepgkhlFEILPGGAGDR 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767981142  641 FQLISEKKTYYLTADSPSLLEEWIRVLQSLL 671
Cdd:cd13378    79 EKVPMNHEAFLLMANSQSDMEDWVKAIRRVI 109
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
582-667 1.89e-08

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. 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: 270126  Cd Length: 97  Bit Score: 53.15  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKpqGQVDLNSRcQIVRGE------GSQTFQLI--SEKKTYYLT 653
Cdd:cd13316     3 SGWMKKRGERYGTWKTRYFVLKGTRLYYLKSENDDKEK--GLIDLTGH-RVVPDDsnspfrGSYGFKLVppAVPKVHYFA 79
                          90
                  ....*....|....
gi 767981142  654 ADSPSLLEEWIRVL 667
Cdd:cd13316    80 VDEKEELREWMKAL 93
PH_Gab2_2 cd13384
Grb2-associated binding protein family pleckstrin homology (PH) domain; The Gab subfamily ...
595-664 2.46e-08

Grb2-associated binding protein family pleckstrin homology (PH) domain; The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. Members here include insect, nematodes, and crustacean Gab2s. 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: 241535  Cd Length: 115  Bit Score: 53.60  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  595 WKRRWFVLRQGQI------MYYKspSDVIRKPQGQVDLNsRCQIV----------RGEGSQTFQLISEKKTYYLTADSPS 658
Cdd:cd13384    23 WRRRYFVLRQSEIpgqyflEYYT--DRTCRKLKGSIDLD-QCEQVdagltfetknKLKDQHIFDIRTPKRTYYLVADTED 99

                  ....*.
gi 767981142  659 LLEEWI 664
Cdd:cd13384   100 EMNKWV 105
PH_Osh1p_Osh2p_yeast cd13292
Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p ...
582-669 3.19e-08

Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p is proposed to function in postsynthetic sterol regulation, piecemeal microautophagy of the nucleus, and cell polarity establishment. Yeast Osh2p is proposed to function in sterol metabolism and cell polarity establishment. Both Osh1p and Osh2p contain 3 N-terminal ankyrin repeats, a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBP andOsh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 241446  Cd Length: 103  Bit Score: 52.70  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDL-NSRCQIVRGEGSQtFQLISEKKT---YYLTADSP 657
Cdd:cd13292     5 KGYLKKWTNYAKGYKTRWFVLEDGVLSYYRHQDDEGSACRGSINMkNARLVSDPSEKLR-FEVSSKTSGspkWYLKANHP 83
                          90
                  ....*....|..
gi 767981142  658 SLLEEWIRVLQS 669
Cdd:cd13292    84 VEAARWIQALQK 95
PH_RhoGap24 cd13379
Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ...
581-671 4.22e-08

Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241530  Cd Length: 114  Bit Score: 52.67  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVirKPQGQVDLNSRCQI---VRGEGSQTF-----------QLISE 646
Cdd:cd13379     5 KCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDET--KPLGTIFLPGNRVTehpCNEEEPGKFlfevvpggdreRMTAN 82
                          90       100
                  ....*....|....*....|....*
gi 767981142  647 KKTYYLTADSPSLLEEWIRVLQSLL 671
Cdd:cd13379    83 HETYLLMASTQNDMEDWVKSIRRVI 107
PH_ASAP cd13251
ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs ...
573-668 4.27e-08

ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs (ASAP1, ASAP2, and ASAP3) function as an Arf-specific GAPs, participates in rhodopsin trafficking, is associated with tumor cell metastasis, modulates phagocytosis, promotes cell proliferation, facilitates vesicle budding, Golgi exocytosis, and regulates vesicle coat assembly via a Bin/Amphiphysin/Rvs domain. ASAPs contain an NH2-terminal BAR domain, a tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 (SH3) 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: 270071  Cd Length: 108  Bit Score: 52.75  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  573 GLGGES---LEKSGYLLKM--GSQVKTWKRRWFVLRQGQIMYYKSPSDvirKPQGQVDLNSrCQI-VRGEGSQTFQLISE 646
Cdd:cd13251     1 QQQGNKshgTEKSGYLLKKseGKIRKVWQKRRCSIKDGFLTISHADEN---KPPAKLNLLT-CQVkLVPEDKKCFDLISH 76
                          90       100
                  ....*....|....*....|..
gi 767981142  647 KKTYYLTADSPSLLEEWIRVLQ 668
Cdd:cd13251    77 NRTYHFQAEDENDANAWMSVLK 98
PH2_Pleckstrin_2 cd13302
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 2; Pleckstrin is a protein found in ...
581-670 7.80e-08

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 2; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the second PH domain 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: 270114  Cd Length: 109  Bit Score: 51.74  E-value: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQ--GQIMYYKSPSDviRKPQGQVDL------------NSRCQIVRGegsQTFQLISE 646
Cdd:cd13302     9 KQGCLLKQGHRRKNWKVRKFVLRDdpAYLHYYDPAKG--EDPLGAIHLrgcvvtavednsNPRKGSVEG---NLFEIITA 83
                          90       100
                  ....*....|....*....|....*
gi 767981142  647 KKT-YYLTADSPSLLEEWIRVLQSL 670
Cdd:cd13302    84 DEVhYYLQAATPAERTEWIKAIQMA 108
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
581-668 8.37e-08

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 52.62  E-value: 8.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMgSQVK------TWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLNS-RC-QIVRGEGSQT----FQLISEKK 648
Cdd:cd01238     1 LEGLLVKR-SQGKkrfgpvNYKERWFVLTKSSLSYYEGDGEKRGKEKGSIDLSKvRCvEEVKDEAFFErkypFQVVYDDY 79
                          90       100
                  ....*....|....*....|
gi 767981142  649 TYYLTADSPSLLEEWIRVLQ 668
Cdd:cd01238    80 TLYVFAPSEEDRDEWIAALR 99
PH_evt cd13265
Evectin Pleckstrin homology (PH) domain; There are 2 members of the evectin family (also ...
581-668 3.08e-07

Evectin Pleckstrin homology (PH) domain; There are 2 members of the evectin family (also called pleckstrin homology domain containing, family B): evt-1 (also called PLEKHB1) and evt-2 (also called PLEKHB2). evt-1 is specific to the nervous system, where it is expressed in photoreceptors and myelinating glia. evt-2 is widely expressed in both neural and nonneural tissues. Evectins possess a single N-terminal PH domain and a C-terminal hydrophobic region. evt-1 is thought to function as a mediator of post-Golgi trafficking in cells that produce large membrane-rich organelles. It is a candidate gene for the inherited human retinopathy autosomal dominant familial exudative vitreoretinopathy and a susceptibility gene for multiple sclerosis. evt-2 is essential for retrograde endosomal membrane transport from the plasma membrane (PM) to the Golgi. Two membrane trafficking pathways pass through recycling endosomes: a recycling pathway and a retrograde pathway that links the PM to the Golgi/ER. Its PH domain that is unique in that it specifically recognizes phosphatidylserine (PS), but not polyphosphoinositides. PS is an anionic phospholipid class in eukaryotic biomembranes, is highly enriched in the PM, and plays key roles in various physiological processes such as the coagulation cascade, recruitment and activation of signaling molecules, and clearance of apoptotic cells. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270085  Cd Length: 108  Bit Score: 49.99  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQ-GQIMYYKSPSDviRKPQGQVDLNSRCQIVR------------GEGSQT-FQLIS- 645
Cdd:cd13265     5 KSGWLLRQSTILKRWKKNWFVLYGdGNLVYYEDETR--REVEGRINMPRECRNIRvglecrdvqppeGRSRDClLQIVLr 82
                          90       100
                  ....*....|....*....|...
gi 767981142  646 EKKTYYLTADSPSLLEEWIRVLQ 668
Cdd:cd13265    83 DGSTLFLCAESADDALAWKLALQ 105
PH_DGK_type2 cd13274
Type 2 Diacylglycerol kinase Pleckstrin homology (PH) domain; DGK (also called DAGK) catalyzes ...
581-669 3.21e-07

Type 2 Diacylglycerol kinase Pleckstrin homology (PH) domain; DGK (also called DAGK) catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low and DAG is used for glycerophospholipid biosynthesis. Upon receptor activation of the phosphoinositide pathway, DGK activity increases which drives the conversion of DAG to PA. DGK acts as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another. There are 9 mammalian DGK isoforms all with conserved catalytic domains and two cysteine rich domains. These are further classified into 5 groups according to the presence of additional functional domains and substrate specificity: Type 1 - DGK-alpha, DGK-beta, DGK-gamma - contain EF-hand motifs and a recoverin homology domain; Type 2 - DGK-delta, DGK-eta, and DGK-kappa- contain a pleckstrin homology domain, two cysteine-rich zinc finger-like structures, and a separated catalytic region; Type 3 - DGK-epsilon - has specificity for arachidonate-containing DAG; Type 4 - DGK-zeta, DGK-iota- contain a MARCKS homology domain, ankyrin repeats, a C-terminal nuclear localization signal, and a PDZ-binding motif; Type 5 - DGK-theta - contains a third cysteine-rich domain, a pleckstrin homology domain and a proline rich region. The type 2 DGKs are present as part of this Metazoan DGK hierarchy. They have a N-terminal PH domain, two cysteine rich domains, followed by bipartite catalytic domains, and a C-terminal SAM domain. Their catalytic domains and perhaps other DGK catalytic domains may function as two independent units in a coordinated fashion. They may also require other motifs for maximal activity because several DGK catalytic domains have very little DAG kinase activity when expressed as isolated subunits. 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: 270093  Cd Length: 97  Bit Score: 49.70  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRqGQIMYY-KSPSDVIRKpqgQVDLNsrcQIVRGEGS-----QTFQLISEKKTYYLTA 654
Cdd:cd13274     2 KEGPLLKQTSSFQRWKRRYFKLK-GRKLYYaKDSKSLIFE---EIDLS---DASVAECStknvnNSFTVITPFRKLILCA 74
                          90
                  ....*....|....*
gi 767981142  655 DSPSLLEEWIRVLQS 669
Cdd:cd13274    75 ESRKEMEEWISALKT 89
PH_FAPP1_FAPP2 cd01247
Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also ...
583-669 3.79e-07

Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also called PLEKHA3/Pleckstrin homology domain-containing, family A member 3) regulates secretory transport from the trans-Golgi network to the plasma membrane. It is recruited through binding of PH domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). These two binding sites have little overlap the FAPP1 PH domain to associate with both ligands simultaneously and independently. FAPP1 has a N-terminal PH domain followed by a short proline-rich region. FAPP1 is a member of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), and Goodpasture antigen binding protein (GPBP). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. FAPP2 (also called PLEKHA8/Pleckstrin homology domain-containing, family A member 8), a member of the Glycolipid lipid transfer protein(GLTP) family has an N-terminal PH domain that targets the TGN and C-terminal GLTP domain. FAPP2 functions to traffic glucosylceramide (GlcCer) which is made in the Golgi. It's interaction with vesicle-associated membrane protein-associated protein (VAP) could be a means of regulation. Some FAPP2s share the FFAT-like motifs found in GLTP. 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: 269951  Cd Length: 100  Bit Score: 49.71  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  583 GYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLnSRCQIVRGEGSQT-FQL-ISEKKTYYLTADSPSLL 660
Cdd:cd01247     3 GVLWKWTNYLSGWQPRWFVLDDGVLSYYKSQEEVNQGCKGSVKM-SVCEIIVHPTDPTrMDLiIPGEQHFYLKASSAAER 81

                  ....*....
gi 767981142  661 EEWIRVLQS 669
Cdd:cd01247    82 QRWLVALGS 90
PH_11 pfam15413
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
581-668 4.34e-07

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


Pssm-ID: 405988  Cd Length: 105  Bit Score: 49.51  E-value: 4.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   581 KSGYLLKMGSqvKTWKRRWF-VLRQGQIMYYKSPSDVIRKPQGQVDLNSRC--------------QIVRGEGSQTFQLI- 644
Cdd:pfam15413    1 IEGYLKKKGP--KTWKHRWFaVLRNGVLFYYKSEKMKVVKHVIVLSNYIVGklgtdiisgalfkiDNIRSETSDDLLLEi 78
                           90       100
                   ....*....|....*....|....*
gi 767981142   645 -SEKKTYYLTADSPSLLEEWIRVLQ 668
Cdd:pfam15413   79 sTETKIFFLYGDNNEETYEWVEALQ 103
PH_DOCK-D cd13267
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also ...
575-672 4.69e-07

Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. 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: 270087  Cd Length: 126  Bit Score: 50.02  E-value: 4.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  575 GGESLEKSGYLLK--MGSQ-------VKTWKRRWFVLRQ----GQIM-YYKSpsDVIRKPQGQVDLNSRCQIVRGE--GS 638
Cdd:cd13267     2 GESGITKEGYLYKgpENSSdsfislaMKSFKRRFFHLKQlvdgSYILeFYKD--EKKKEAKGTIFLDSCTGVVQNSkrRK 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767981142  639 QTFQL-ISEKKTYYLTADSPSLLEEWIRVLQSLLK 672
Cdd:cd13267    80 FCFELrMQDKKSYVLAAESEAEMDEWISKLNKILQ 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
19-171 6.27e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 6.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   19 LTLETQLFRFRLQASKIRELLAD------KMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLK---NVDSEGSLHRKY 89
Cdd:COG1196   218 LKEELKELEAELLLLKLRELEAEleeleaELEELEAELEELEAELAELEAELEELRLELEELELEleeAQAEEYELLAEL 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   90 QELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEW---VTLKLAKLEMENQHLKSHNQRLVEQVGSLQDA 166
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                  ....*
gi 767981142  167 LEAIQ 171
Cdd:COG1196   378 EEELE 382
PH_GPBP cd13283
Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called ...
581-669 7.38e-07

Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called Collagen type IV alpha-3-binding protein/hCERT; START domain-containing protein 11/StARD11; StAR-related lipid transfer protein 11) is a kinase that phosphorylates an N-terminal region of the alpha 3 chain of type IV collagen, which is commonly known as the goodpasture antigen. Its splice variant the ceramide transporter (CERT) mediates the cytosolic transport of ceramide. There have been additional splice variants identified, but all of them function as ceramide transport proteins. GPBP and CERT both contain an N-terminal PH domain, followed by a serine rich domain, and a C-terminal START domain. However, GPBP has an additional serine rich domain just upstream of its START domain. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 270100 [Multi-domain]  Cd Length: 100  Bit Score: 48.82  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVDLnsRCQIV--------RgegsqtFQLISEKKTYYL 652
Cdd:cd13283     1 LRGVLSKWTNYIHGWQDRYFVLKDGTLSYYKSESEKEYGCRGSISL--SKAVIkphefdecR------FDVSVNDSVWYL 72
                          90
                  ....*....|....*..
gi 767981142  653 TADSPSLLEEWIRVLQS 669
Cdd:cd13283    73 RAESPEERQRWIDALES 89
PH_ORP3_ORP6_ORP7 cd13287
Human Oxysterol binding protein related proteins 3, 6, and 7 Pleckstrin homology (PH) domain; ...
577-668 7.89e-07

Human Oxysterol binding protein related proteins 3, 6, and 7 Pleckstrin homology (PH) domain; Human ORP3 is proposed to function in regulating the cell-matrix and cell-cell adhesion. A proposed specific function for Human ORP6 was not found at present. Human ORP7is proposed to function in negatively regulating the Golgi soluble NSF attachment protein receptor (SNARE) of 28kDa (GS28) protein stability via sequestration of Golgi-associated ATPase enhancer of 16 kDa (GATE-16). ORP3 has 2 isoforms: the longer ORP3(1) and the shorter ORP3(2). ORP3(1), ORP6, and ORP7 all contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. The shorter ORP3(2) is missing the C-terminal portion of its OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 270104  Cd Length: 123  Bit Score: 49.25  E-value: 7.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  577 ESLEKSGYLLKMGSQ-VKTWKRRWFVLRQGQIMYYKSPSDVIR-KPQGQVDLNSRCQIVRGEgSQTFQLISEKKTYYLTA 654
Cdd:cd13287    20 EPGKQEGYLLKKRKWpLKGWHKRFFVLEKGILKYAKSPLDIAKgKLHGSIDVGLSVMSIKKK-ARRIDLDTEEFIYHLKV 98
                          90
                  ....*....|....
gi 767981142  655 DSPSLLEEWIRVLQ 668
Cdd:cd13287    99 KSQDLFDSWVAKLR 112
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-171 8.22e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   21 LETQLFRFRLQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLHRKYQELLKAIKGKD 100
Cdd:COG4372     4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981142  101 ELISQLEAQLEKQKQMRaEEAKTVQEKAAKIKEwvtlKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG4372    84 ELNEQLQAAQAELAQAQ-EELESLQEEAEELQE----ELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
15-179 1.36e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   15 QKRCLTLETQLFRFRLQASKIRELLA---DKMQELEQRLLEAEQRAENAETQVGVMEEKvklsnLKNVDSEgslhrkyqe 91
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEqarSELEQLEEELEELNEQLQAAQAELAQAQEE-----LESLQEE--------- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   92 llkaikgKDELISQLEaQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKlaklEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG4372   110 -------AEELQEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAER----EEELKELEEQLESLQEELAALEQELQALS 177

                  ....*...
gi 767981142  172 IAPSRKLL 179
Cdd:COG4372   178 EAEAEQAL 185
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
22-171 1.67e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 1.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    22 ETQLFRFRLQASKIRELLADKMQELEQrlleAEQRAENAETQVGvmEEKVKLSNLKNVDSEGsLHRKYQELLKAIKGK-- 99
Cdd:TIGR04523  252 QTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQLN--QLKSEISDLNNQKEQD-WNKELKSELKNQEKKle 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   100 ---------DELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTlKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAI 170
Cdd:TIGR04523  325 eiqnqisqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-EIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403

                   .
gi 767981142   171 Q 171
Cdd:TIGR04523  404 E 404
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1024-1127 1.86e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 47.63  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRkpSHSGFALF---TDDPS--GRDLEHclqgsvkICDAISKWE 1098
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLK--DTFGFSLYialFDKVSslGSGTDH-------VMDAISQCE 71
                          90       100
                  ....*....|....*....|....*....
gi 767981142 1099 QAMKElhPGKSEGGTrvvklmyKNRLYFR 1127
Cdd:cd17092    72 QYAKE--KGAQEREA-------PWRLYFR 91
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-194 2.21e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   32 ASKIrELLADKMQELEQRLLEAEQRAENAETQVGVMEE-KVKLSNLKNVDSE----GSLHRKYQEL---LKAI-KGKDEL 102
Cdd:COG4913   609 RAKL-AALEAELAELEEELAEAEERLEALEAELDALQErREALQRLAEYSWDeidvASAEREIAELeaeLERLdASSDDL 687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  103 iSQLEAQLEKQkqmRAEEAKTVQEKAAKIKEwvtlkLAKLEMENQHLkshnQRLVEQVGSLQDALEAIQIAPSRKLLVPP 182
Cdd:COG4913   688 -AALEEQLEEL---EAELEELEEELDELKGE-----IGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEER 754
                         170
                  ....*....|..
gi 767981142  183 YGAAEQDSVPSE 194
Cdd:COG4913   755 FAAALGDAVERE 766
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
1025-1106 2.39e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 46.81  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1025 FSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRkpSHSGFALFTDDPSgrDLEHCLQGSvkicDAISKWeqaMKEL 1104
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLL--EKDYFGLFYEDND--GQKHWLDLD----KKISKQ---LKRS 69

                  ..
gi 767981142 1105 HP 1106
Cdd:cd01765    70 GP 71
PH_IRS cd01257
Insulin receptor substrate (IRS) pleckstrin homology (PH) domain; Insulin receptor substrate ...
581-677 2.57e-06

Insulin receptor substrate (IRS) pleckstrin homology (PH) domain; Insulin receptor substrate (IRS) molecules are mediators in insulin signaling and play a role in maintaining basic cellular functions such as growth and metabolism. They act as docking proteins between the insulin receptor and a complex network of intracellular signaling molecules containing Src homology 2 (SH2) domains. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified that differ as to tissue distribution, subcellular localization, developmental expression, binding to the insulin receptor, and interaction with SH2 domain-containing proteins. IRS molecules have an N-terminal PH domain, followed by an IRS-like PTB domain which has a PH-like fold. 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.cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 269959  Cd Length: 106  Bit Score: 47.28  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKmgsqVKTWKRRWFVLR------QGQIMYYKSPSDVIRK--PQGQVDLNSRCQIVR---GEGSQTFQLISEKKT 649
Cdd:cd01257     5 KSGYLKK----LKTMRKRYFVLRaeshggPARLEYYENEKKFRRNaePKRVIPLSSCFNINKradAKHKHLIALYTKDEC 80
                          90       100
                  ....*....|....*....|....*...
gi 767981142  650 YYLTADSPSLLEEWirvLQSLLKVQATG 677
Cdd:cd01257    81 FGLVAESEEEQDEW---YQALLELQRPA 105
PH_Skap_family cd13266
Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain; Skap adaptor ...
581-673 2.68e-06

Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain; Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270086  Cd Length: 106  Bit Score: 47.52  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLK-------MGSQvktWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLNS----RCQIVRGEGSQ--TFQLIS-E 646
Cdd:cd13266     3 KAGYLEKrrkdhsfFGSE---WQKRWCAISKNVFYYYGSDKD--KQQKGEFAINGydvrMNPTLRKDGKKdcCFELVCpD 77
                          90       100
                  ....*....|....*....|....*..
gi 767981142  647 KKTYYLTADSPSLLEEWIRVLQSLLKV 673
Cdd:cd13266    78 KRTYQFTAASPEDAEDWVDQISFILQD 104
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-171 2.72e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   27 RFRLQASKIRELLA--DKMQELEQRLLEAEQRAENAETQVGVMEEKVKLsnLKNVDSEGSLHRKYQELLKAIKGKDELIS 104
Cdd:COG4717    72 ELKELEEELKEAEEkeEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLE 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  105 QLEAQLEKQKQMRAEEA---KTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG4717   150 ELEERLEELRELEEELEeleAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
581-671 2.73e-06

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). 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: 269939  Cd Length: 103  Bit Score: 47.20  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRkpQGQVDLnSRCQIVRGEGSQ-------TFQLISEKKTYYLT 653
Cdd:cd01233     8 KRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDE--RGVINL-STARVEYSPDQEallgrpnVFAVYTPTNSYLLQ 84
                          90
                  ....*....|....*...
gi 767981142  654 ADSPSLLEEWIRVLQSLL 671
Cdd:cd01233    85 ARSEKEMQDWLYAIDPLL 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
13-172 2.79e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    13 DWQKRCLTLETQLFRFRLQASKIRELLADKM---QELEQRLLEAEQRAENAETQVGVMEEKvklsnlknvdsegsLHrKY 89
Cdd:TIGR02169  713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEedlSSLEQEIENVKSELKELEARIEELEED--------------LH-KL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    90 QELLKAIKGK--DELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEwVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDAL 167
Cdd:TIGR02169  778 EEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                   ....*
gi 767981142   168 EAIQI 172
Cdd:TIGR02169  857 ENLNG 861
PH_PHLDB1_2 cd14673
Pleckstrin homology-like domain-containing family B member 2 pleckstrin homology (PH) domain; ...
583-667 3.03e-06

Pleckstrin homology-like domain-containing family B member 2 pleckstrin homology (PH) domain; PHLDB2 (also called LL5beta) and PHLDB1 (also called LL5alpha) are cytoskeleton- and membrane-associated proteins. PHLDB2 has been identified as a key component of the synaptic podosomes that play an important role in in postsynaptic maturation. Both are large proteins containing an N-terminal pleckstrin (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: 270192  Cd Length: 105  Bit Score: 47.18  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  583 GYLLKMGSQVKTWKRRWFV--LRQGQIMYYKSPSDviRKPQGQVDLNS---------RCQIVRGEGSQTFQLISEKKTYY 651
Cdd:cd14673     7 GFLTKMGGKIKTWKKRWFVfdRNKRTLSYYVDKHE--KKLKGVIYFQAieevyydhlRSAAKSPNPALTFCVKTHDRLYY 84
                          90
                  ....*....|....*.
gi 767981142  652 LTADSPSLLEEWIRVL 667
Cdd:cd14673    85 MVAPSPEAMRIWMDVI 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-173 3.22e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142     2 AELKVEAPASVDWQKRCLTLETQLFRFRLQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSN--LKNV 79
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqLETL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    80 DSEGSLHRKYQELLKA-IKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAakiKEWVTLKLAKLEMENQHLKSHNQRLVE 158
Cdd:TIGR02168  385 RSKVAQLELQIASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLEE 461
                          170
                   ....*....|....*
gi 767981142   159 QVGSLQDALEAIQIA 173
Cdd:TIGR02168  462 ALEELREELEEAEQA 476
PH2_FGD4_insect-like cd13238
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 4 pleckstrin homology (PH) ...
582-667 3.64e-06

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 4 pleckstrin homology (PH) domain, C-terminus, in insect and related arthropods; In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. This cd contains insects, crustaceans, and chelicerates. 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: 270058  Cd Length: 97  Bit Score: 46.87  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKMGSQVKTWKRRWFVLRQGQIMY-YKSPSDVIRK-----PQGQVDLNSRCQIVRG----EGSQTFQLISEKKTYY 651
Cdd:cd13238     2 SGYLKLKTNGRKTWSRRWFALQPDFVLYsYKSQEDKLPLtatpvPGFLVTLLEKGSAVDPlndpKRPRTFKMFHVKKSYY 81
                          90
                  ....*....|....*.
gi 767981142  652 LTADSPSLLEEWIRVL 667
Cdd:cd13238    82 FQANDGDEQKKWVLTL 97
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
20-266 5.32e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   20 TLETQLFRFRLQASKIREL---LADKMQELEQRLLEAEQRAENAETQVGVMEEKVK------------------------ 72
Cdd:COG3883    34 AAQAELDALQAELEELNEEyneLQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsggsvsyldvllgses 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   73 ----LSNLKNVDSegsLHRKYQELLKAIKGKDELISQLEAQLEKQKQmraeEAKTVQEKAAKIKEWVTLKLAKLEMENQH 148
Cdd:COG3883   114 fsdfLDRLSALSK---IADADADLLEELKADKAELEAKKAELEAKLA----ELEALKAELEAAKAELEAQQAEQEALLAQ 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  149 LKSHNQRLVEQVGSLQDALEAIQIAPSrkllvppygAAEQDSVPSEPGIQPMGQDSGSQAQGLKAAVLAPSPGALQSKDS 228
Cdd:COG3883   187 LSAEEAAAEAQLAELEAELAAAEAAAA---------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767981142  229 VSEAASPLEDSSSSTVHSGETVEAKPLQPHLGRESPPH 266
Cdd:COG3883   258 AAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGG 295
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
583-668 5.43e-06

Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 is proposed to function in regulation of Akt phosphorylation. ORP9 has 2 forms, a long (ORP9L) and a short (ORP9S). ORP9L contains an N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains a FFAT motif and an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 241444  Cd Length: 102  Bit Score: 46.28  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  583 GYLLKMGSQVKTWKRRWFVLRQ--GQIMYYKSPSDVIRKPQ-GQVDLNSRCQIVRGEGSQTFQLISEKKTYYLTADSPSL 659
Cdd:cd13290     3 GPLSKWTNVMKGWQYRWFVLDDnaGLLSYYTSKEKMMRGSRrGCVRLKGAVVGIDDEDDSTFTITVDQKTFHFQARDAEE 82

                  ....*....
gi 767981142  660 LEEWIRVLQ 668
Cdd:cd13290    83 RERWIRALE 91
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-173 5.76e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   33 SKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKV-KLSNLKNVDSEgsLHRKYQELLKAIKgKDELISQLEAQLE 111
Cdd:PRK03918  299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEeRLEELKKKLKE--LEKRLEELEERHE-LYEEAKAKKEELE 375
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767981142  112 KQKQMRA----EEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKShnqrlveQVGSLQDALEAIQIA 173
Cdd:PRK03918  376 RLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKK-------EIKELKKAIEELKKA 434
PH2_FGD5_FGD6 cd13237
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6 pleckstrin ...
582-667 5.88e-06

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6 pleckstrin homology (PH) domain, C-terminus; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH 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: 270057  Cd Length: 91  Bit Score: 45.87  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVirkpqgqVDLNSR-------CQIVRGEGSQT---FQLISEKKTYY 651
Cdd:cd13237     2 SGYLQRRKKSKKSWKRLWFVLKDKVLYTYKASEDV-------VALESVpllgftvVTIDESFEEDEslvFQLLHKGQLPI 74
                          90
                  ....*....|....*..
gi 767981142  652 -LTADSPSLLEEWIRVL 667
Cdd:cd13237    75 iFRADDAETAQRWIEAL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-171 6.23e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 6.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    21 LETQLFRFRLQASK----------IREL-----------LADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNv 79
Cdd:TIGR02168  198 LERQLKSLERQAEKaerykelkaeLRELelallvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV- 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    80 dseGSLHRKYQELLKAIKGKDELISQLE---------------------AQLEKQKQMR---AEEAKTVQEKAAKIKEWV 135
Cdd:TIGR02168  277 ---SELEEEIEELQKELYALANEISRLEqqkqilrerlanlerqleeleAQLEELESKLdelAEELAELEEKLEELKEEL 353
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 767981142   136 TL---KLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:TIGR02168  354 ESleaELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
37-133 6.29e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.94  E-value: 6.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    37 ELLADKMQELEQRL------LEAE----QRAENAETQvgvMEEKVKLSNLKNVDSEGSLHRKYQELLKAIKGKdelISQL 106
Cdd:pfam01576  906 ELLNDRLRKSTLQVeqltteLAAErstsQKSESARQQ---LERQNKELKAKLQEMEGTVKSKFKSSIAALEAK---IAQL 979
                           90       100
                   ....*....|....*....|....*..
gi 767981142   107 EAQLEKQKQMRAEEAKTVQEKAAKIKE 133
Cdd:pfam01576  980 EEQLEQESRERQAANKLVRRTEKKLKE 1006
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
581-669 6.88e-06

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. 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: 269947  Cd Length: 107  Bit Score: 46.09  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMGSQVKTWKRRWFVLRQ-GQIMYYKspsdviRKPQGQVD---LNS----RCQIVRGE--GSQTF-----QLIS 645
Cdd:cd01241     5 KEGWLLKRGEYIKNWRPRYFVLKSdGSFIGYK------EKPKPNQDpppLNNfsvaECQLMKTEkpKPNTFiirclQWTT 78
                          90       100
                  ....*....|....*....|....*
gi 767981142  646 E-KKTYYltADSPSLLEEWIRVLQS 669
Cdd:cd01241    79 ViERTFH--VESEEEREEWMKAIQG 101
PRK12704 PRK12704
phosphodiesterase; Provisional
41-143 1.53e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   41 DKMQELEQRLLEAEQRAENAETQVGVMEEKVKlsnlknvDSEGSLHRKYQELLKAIKGKDELISQLEAQLEKQKQMRAEE 120
Cdd:PRK12704   82 NELQKLEKRLLQKEENLDRKLELLEKREEELE-------KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767981142  121 AK----------TVQEKAAKIKEWVtlKLAKLE 143
Cdd:PRK12704  155 AKeillekveeeARHEAAVLIKEIE--EEAKEE 185
PH_ORP_plant cd13294
Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain; Plant ORPs ...
583-669 1.67e-05

Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain; Plant ORPs contain a N-terminal PH domain and a C-terminal OSBP-related domain. Not much is known about its specific function in plants to date. Members here include: Arabidopsis, spruce, and petunia. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 241448  Cd Length: 100  Bit Score: 44.79  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  583 GYLLKMGSQVKTWKRRWFVLRQGQIMYYK--SPSDVirKPQGQVDLnsRCQIVRGEGS--QTFQLISEKKTYYLTADSPS 658
Cdd:cd13294     3 GILYKWVNYGKGWRSRWFVLQDGVLSYYKvhGPDKV--KPSGEVHL--KVSSIRESRSddKKFYIFTGTKTLHLRAESRE 78
                          90
                  ....*....|.
gi 767981142  659 LLEEWIRVLQS 669
Cdd:cd13294    79 DRAAWLEALQA 89
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
577-671 1.91e-05

Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the second 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: 270111  Cd Length: 102  Bit Score: 44.93  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  577 ESLEKSGYLLKM-GSQVKTWKRRWFVLRQGQIMYYKSPSDVirKPQGQVDLNSRCQIVRGEG-SQT----FQLISEKKTY 650
Cdd:cd13299     4 ERVIEQGYLQVLkKKGVNQWKKYWLVLRNRSLSFYKDQSEY--SPVKIIPIDDIIDVVELDPlSKSkkwcLQIITPEKRI 81
                          90       100
                  ....*....|....*....|.
gi 767981142  651 YLTADSPSLLEEWIRVLQSLL 671
Cdd:cd13299    82 RFCADDEESLIKWLGALKSLL 102
PH_Skap-hom_Skap2 cd13381
Src kinase-associated phosphoprotein homolog and Skap 2 Pleckstrin homology (PH) domain; ...
581-672 2.00e-05

Src kinase-associated phosphoprotein homolog and Skap 2 Pleckstrin homology (PH) domain; Adaptor protein Skap-hom, a homolog of Skap55, which interacts with actin and with ADAP (adhesion and degranulation promoting adapter protein) undergoes tyrosine phosphorylation in response to plating of bone marrow-derived macrophages on fibronectin. Skap-hom has an N-terminal coiled-coil conformation that is involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap-hom PH domain regulates intracellular targeting; its interaction with the DM domain inhibits Skap-hom actin-based ruffles in macrophages and its binding to 3'-phosphoinositides reverses this autoinhibition. The Skap-hom PH domain binds PI[3,4]P2 and PI[3,4,5]P3, but not to PI[3]P, PI[5]P, or PI[4,5]P2. Skap2 is a downstream target of Heat shock transcription factor 4 (HSF4) and functions in the regulation of actin reorganization during lens differentiation. It is thought that SKAP2 anchors the complex of tyrosine kinase adaptor protein 2 (NCK20/focal adhesion to fibroblast growth factor receptors at the lamellipodium in lens epithelial cells. Skap2 has an N-terminal coiled-coil conformation which interacts with the SH2 domain of NCK2, a central PH domain and a C-terminal SH3 domain that associates with ADAP (adhesion and degranulation promoting adapter protein)/FYB (the Fyn binding protein). Skap2 PH domain binds to membrane lipids. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-hom have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. 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: 270181  Cd Length: 106  Bit Score: 44.95  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLK-------MGSQvktWKRRWFVLRQGQIMYYKSPSDVIRKPQGQVD-----LNSrcqIVRGEGSQ--TFQLIS- 645
Cdd:cd13381     3 KAGYLEKrrkdhsfFGFE---WQKRWCALSNSVFYYYGSDKDKQQKGEFAIDgydvkMNN---TLRKDAKKdcCFEICAp 76
                          90       100
                  ....*....|....*....|....*..
gi 767981142  646 EKKTYYLTADSPSLLEEWIRVLQSLLK 672
Cdd:cd13381    77 DKRVYQFTAASPKEAEEWVQQIKFILQ 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
36-223 2.39e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   36 RELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLHRKYQELLKAIKGKDELISQLE-------- 107
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaeea 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  108 -----AQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQIApsrkllvpp 182
Cdd:COG1196   412 llerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL--------- 482
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767981142  183 yGAAEQDSVPSEPGIQPMGQDSGSQAQGLKAAVLAPSPGAL 223
Cdd:COG1196   483 -LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
21-173 2.47e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   21 LETQLFRFRLQASKI---RELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLHRKYQElLKAIK 97
Cdd:COG1196   251 LEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE-LAELE 329
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767981142   98 GKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQIA 173
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
FERM_F1_Myo10_like cd17110
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional ...
1024-1126 2.48e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins; Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin.


Pssm-ID: 340630  Cd Length: 97  Bit Score: 44.30  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1024 PFSIPVHFTNGTYHVVGFDGSSTVDEFLQRLNQEIGMRKpSHSGFALFtdDPSGrDLEHCLQGSVKICDAISKWE-QAMK 1102
Cdd:cd17110     3 ELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLER-SRNGFALF--ETSG-DIERALEAKTRVVDVLSKWEkLAAT 78
                          90       100
                  ....*....|....*....|....
gi 767981142 1103 ELHPGKSEggtrvVKLMYKNRLYF 1126
Cdd:cd17110    79 GSSPGDDG-----WKLLFKLYLFL 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
15-171 2.53e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    15 QKRCLTLETQLFRFRLQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVK-----LSNLKNVDSE-----GS 84
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalreaLDELRAELTLlneeaAN 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    85 LHRKYQELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTV---QEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVG 161
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALALLRSELEELSE 901
                          170
                   ....*....|
gi 767981142   162 SLQDALEAIQ 171
Cdd:TIGR02168  902 ELRELESKRS 911
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
1254-1335 3.86e-05

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 43.52  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142 1254 GAKLFaaqPAQLSSKENALVWIAVNEDGVSILDHNTMQVHITYPYSSVTTFG-GCRDDFMLVIRsipdkssGKSHIEKLI 1332
Cdd:cd00836     1 GVEFF---PVKDKSKKGSPIILGVNPEGISVYDELTGQPLVLFPWPNIKKISfSGAKKFTIVVA-------DEDKQSKLL 70

                  ...
gi 767981142 1333 FRM 1335
Cdd:cd00836    71 FQT 73
PH_SKIP cd13309
SifA and kinesin-interacting protein Pleckstrin homology (PH) domain; SKIP (also called ...
581-677 4.53e-05

SifA and kinesin-interacting protein Pleckstrin homology (PH) domain; SKIP (also called PLEKHM2/Pleckstrin homology domain-containing family M member 2) is a soluble cytosolic protein that contains a RUN domain and a PH domain separated by a unstructured linker region. SKIP is a target of the Salmonella effector protein SifA and the SifA-SKIP complex regulates kinesin-1 on the bacterial vacuole. The PH domain of SKIP binds to the N-terminal region of SifA while the N-terminus of SKIP is proposed to bind the TPR domain of the kinesin light chain. The opposite side of the SKIP PH domain is proposed to bind phosphoinositides. TSifA, SKIP, SseJ, and RhoA family GTPases are also thought to promote host membrane tubulation. Recently, it was shown that the lysosomal GTPase Arl8 binds to the kinesin-1 linker SKIP and that both are required for the normal intracellular distribution of lysosomes. Interestingly, two kinesin light chain binding motifs (WD) in SKIP have now been identified to match a consensus sequence for a kinesin light chain binding site found in several proteins including calsyntenin-1/alcadein, caytaxin, and vaccinia virus A36. SKIP has also been shown to interact with Rab1A. 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: 270119  Cd Length: 103  Bit Score: 43.91  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLL-KMGSQ---VKTWKRRWFVLRQGQIMYYKSPSDVIrkPQGQVDL-NSRCQ----IVRGEGSQTFQLI-SEKKTY 650
Cdd:cd13309     2 KEGMLMyKTGTSylgGETWKPGYFLLKNGVLYQYPDRSDRL--PLLSISLgGEQCGgcrrINNTERPHTFELIlTDRSSL 79
                          90       100
                  ....*....|....*....|....*..
gi 767981142  651 YLTADSPSLLEEWirvLQSLLKVQATG 677
Cdd:cd13309    80 ELAAPDEYEASEW---LQSLCQSASGG 103
PH_Skap1 cd13380
Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain; Adaptor protein Skap1 ...
581-672 5.15e-05

Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain; Adaptor protein Skap1 (also called Skap55/Src kinase-associated phosphoprotein of 55 kDa) and its partner, ADAP (adhesion and degranulation promoting adapter protein) help reorganize the cytoskeleton and/or promote integrin-mediated adhesion upon immunoreceptor activation. Skap1 is also involved in T Cell Receptor (TCR)-induced RapL-Rap1 complex formation and LFA-1 activation. Skap1 has an N-terminal coiled-coil conformation which is proposed to be involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap1 PH domain plays a role in controlling integrin function via recruitment of ADAP-SKAP complexes to integrins as well as in controlling the ability of ADAP to interact with the CBM signalosome and regulate NF-kappaB. SKAP1 is necessary for RapL binding to membranes in a PH domain-dependent manner and the PI3K pathway. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Skap55/Skap1, Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. 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: 270180  Cd Length: 106  Bit Score: 43.69  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLK-------MGSQvktWKRRWFVLRQGQIMYYKSPSDviRKPQGQVDL-NSRCQIV-----RGEGSQTFQLISE- 646
Cdd:cd13380     3 KQGYLEKrskdhsfFGSE---WQKRWCVLTNRAFYYYASEKS--KQPKGGFLIkGYSAQMAphlrkDSRRDSCFELTTPg 77
                          90       100
                  ....*....|....*....|....*.
gi 767981142  647 KKTYYLTADSPSLLEEWIRVLQSLLK 672
Cdd:cd13380    78 RRTYQFTAASPSEARDWVDQIQFLLK 103
PH_ORP10_ORP11 cd13291
Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin ...
583-641 5.88e-05

Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin homology (PH) domain; Human ORP10 is involvedt in intracellular transport or organelle positioning and is proposed to function as a regulator of cellular lipid metabolism. Human ORP11 localizes at the Golgi-late endosome interface and is thought to form a dimer with ORP9 functioning as an intracellular lipid sensor or transporter. Both ORP10 and ORP11 contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 270106  Cd Length: 107  Bit Score: 43.44  E-value: 5.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981142  583 GYLLKMGSQVKTWKRRWFVL--RQGQIMYYKSPSDVIRKPQGQVDLNSRCQIVRGEGSQTF 641
Cdd:cd13291     3 GQLLKYTNVVKGWQNRWFVLdpDTGILEYFLSEESKNQKPRGSLSLAGAVISPSDEDSHTF 63
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-173 7.82e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   21 LETQLFRFRlQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEG-----SLHRK---YQEL 92
Cdd:COG4717    83 AEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELperleELEERleeLREL 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   93 LKAIKGKDELISQLEAQL-EKQKQMRAEEAKTVQEKAAKIKEWvTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG4717   162 EEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL-QQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240

                  ..
gi 767981142  172 IA 173
Cdd:COG4717   241 LE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
37-126 9.23e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   37 ELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKlsnlknvdsegslhrKYQELLKAIKGK-DELISQLEAQLEKQKQ 115
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELA---------------ELEAELEEKKAElDEELAELEAELEELEA 163
                          90
                  ....*....|.
gi 767981142  116 MRAEEAKTVQE 126
Cdd:COG1579   164 EREELAAKIPP 174
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
21-171 1.03e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   21 LETQLFRFRLQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVM----EEKVKLSNLKNVDSE--------GSLHRK 88
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVdlseEAKLLLQQLSELESQlaearaelAEAEAR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   89 YQELLKAIKGK---------DELISQLEAQLEKQKQMRAEEAKT-------VQEKAAKIKEWVTLKLAKLEMENQHLKSH 152
Cdd:COG3206   242 LAALRAQLGSGpdalpellqSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAE 321
                         170
                  ....*....|....*....
gi 767981142  153 NQRLVEQVGSLQDALEAIQ 171
Cdd:COG3206   322 LEALQAREASLQAQLAQLE 340
PH_Bem3 cd13277
Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces ...
581-671 1.06e-04

Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces cerevisiae involves cell cycle-regulated reorganizations of cortical cytoskeletal elements and requires the action of the Rho-type GTPase Cdc42. Bem3 contains a RhoGAP domain and a PH domain. Though Bem3 and Bem2 both contain a RhoGAP, but only Bem3 is able to stimulate the hydrolysis of GTP on Cdc42. Bem3 is thought to be the GAP for Cdc42. 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: 270096  Cd Length: 111  Bit Score: 43.04  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  581 KSGYLLKMG----SQVKTWKRRWFVLRQGQIMYYKSPSDVIrkpQGQVDLNSrCQIvrgeGSQT------------FQLI 644
Cdd:cd13277     5 KEGYLLKRRkktlGSTGGWKLRYGVLDGNILELYESRGGQL---LESIKLRN-AQI----ERQPnlpddkygtrhgFLIN 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767981142  645 SEKKT-------YYLTADSPSLLEEWIRVLQSLL 671
Cdd:cd13277    77 EHKKSglssttkYYLCAETDKERDEWVSALSEYI 110
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
21-171 1.12e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    21 LETQLFRFRLQASKIRELLADKMQEL---EQRLLEAEQRAENAETQVGVMEEKV--------KLSNLKN-VDSE-GSLHR 87
Cdd:TIGR04523  466 LETQLKVLSRSINKIKQNLEQKQKELkskEKELKKLNEEKKELEEKVKDLTKKIsslkekieKLESEKKeKESKiSDLED 545
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    88 ---------KYQELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWV------TLKLAKLEMENQHLKSH 152
Cdd:TIGR04523  546 elnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIkeieekEKKISSLEKELEKAKKE 625
                          170
                   ....*....|....*....
gi 767981142   153 NQRLVEQVGSLQDALEAIQ 171
Cdd:TIGR04523  626 NEKLSSIIKNIKSKKNKLK 644
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1-133 1.24e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    1 MAELKVEAPASVDWQKRCLTLETQLFRFRLQASKIREL---LADKMQELEQRLLEA-----EQRAENAETQvgvmEEKVK 72
Cdd:COG1340   145 LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKikeLAEEAQELHEEMIELykeadELRKEADELH----KEIVE 220
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981142   73 LSnlKNVDsegSLHRKYQELLKAIKGKDELISQLEAQLEKQKqmRAEEAKTVQEKAAKIKE 133
Cdd:COG1340   221 AQ--EKAD---ELHEEIIELQKELRELRKELKKLRKKQRALK--REKEKEELEEKAEEIFE 274
PH_Bud4 cd13278
Bud4 Pleckstrin homology (PH) domain; Bud4 is an anillin-like yeast protein involved in the ...
577-679 1.88e-04

Bud4 Pleckstrin homology (PH) domain; Bud4 is an anillin-like yeast protein involved in the formation and the disassembly of the double ring structure formed by the septins during cytokinesis. Bud4 acts with Bud3 and and in parallel with septin phosphorylation by the p21-activated kinase Cla4 and the septin-dependent kinase Gin4. Bud4 is regulated by the cyclin-dependent protein kinase Cdk1, the master regulator of cell cycle progression. Bud4 contains an anillin-like domain followed by a PH domain. In addition there are two consensus Cdk phosphorylation sites: one at the N-terminus and one right before the C-terminal PH domain. Anillins also have C-terminal PH domains. 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: 241432  Cd Length: 139  Bit Score: 42.96  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  577 ESLEKSGYLLKMGSQVKTWKRRWFVLRQGQIMYYkspSDVIRKPQGQVDLNSRCQIV-----RGEGSQT----------- 640
Cdd:cd13278    17 QKITKEGYLLQEGGDCEYWRRRFFKLQGTKLVAY---HEVTRKPRATINLLKVVDVVddddaRERTSSFkrnftdlvlfe 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767981142  641 --FQLISEKKTY-YLTADSPSLLEEWIRVLQSLLKVQATGPP 679
Cdd:cd13278    94 ecFRLVFANGEViDFYADSKEEKADWYSKLKEVVELNRFHQP 135
PH_Gab3 cd13385
Grb2-associated binding protein 3 pleckstrin homology (PH) domain; The Gab subfamily includes ...
595-665 2.13e-04

Grb2-associated binding protein 3 pleckstrin homology (PH) domain; The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. The members in this cd include the Gab1, Gab2, and Gab3 proteins. 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: 270184  Cd Length: 125  Bit Score: 42.65  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  595 WKRRWFVLRQGQIM-------YYKS-----PSDVIRKPQGQVDLNSRCQIVRGEGSQTFQLI--SEKKTYYLTADSPSLL 660
Cdd:cd13385    26 WRKRWFVLRRGRMSgnpdvleYYRNnhskkPIRVIDLSECEVLKHSGPNFIRKEFQNNFVFIvkTTYRTFYLVAKTEEEM 105

                  ....*
gi 767981142  661 EEWIR 665
Cdd:cd13385   106 QVWVH 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
39-171 2.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   39 LADKMQELEQRL--LEAEqrAENAE------TQVGVMEEKVKLSNLKNVDSE-GSLHRKYQELLKAIKGKDELISQLEAQ 109
Cdd:COG1196   191 LEDILGELERQLepLERQ--AEKAEryrelkEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767981142  110 LEKQKQMRAEEAKTVQEKAAKIKEwVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
21-177 2.53e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    21 LETQLFRFRLQASK--------IRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLHRKYQEL 92
Cdd:pfam02463  163 AGSRLKRKKKEALKklieetenLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    93 LKAIKGKDELISQLEAQLEKQKQMRAEEAKtVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQI 172
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321

                   ....*
gi 767981142   173 APSRK 177
Cdd:pfam02463  322 EKKKA 326
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
582-667 2.86e-04

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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: 270069  Cd Length: 111  Bit Score: 41.60  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYL--LKMGSQVKTWKRRWFVLRQGQIMYYKSPSDVIRK--PQGQVDLNSRCQIVRGEG-----SQTFQLIS----EKK 648
Cdd:cd13249     5 SGYLsqQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKvePLLTIPINKETRIRAVEKdskgrASSLSIINpysgEEV 84
                          90
                  ....*....|....*....
gi 767981142  649 TYYLTADSPSLLEEWIRVL 667
Cdd:cd13249    85 THVLSADSREELQKWMEAL 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
19-173 3.53e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   19 LTLETQLFRFRLQASKIRELLADKmQELEQRLLEAEQRAENAETQVGVMEEKvklsnlknvdsEGSLHRKYQELLKAIKG 98
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDI-ARLEERRRELEERLEELEEELAELEEE-----------LEELEEELEELEEELEE 348
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767981142   99 KDELISQLEAQLEKQKQMRAEEAktvQEKAAKIKEWVTLKLAKLEMENQH--LKSHNQRLVEQVGSLQDALEAIQIA 173
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAE---AELAEAEEELEELAEELLEALRAAaeLAAQLEELEEAEEALLERLERLEEE 422
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
29-170 3.64e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   29 RLQASKIRELLADK-MQELEQRLLEAEQRAENAETQVGVMEEKVKlsNLKNVDSEGSLHRKYQELLKAIKGKDELISQLE 107
Cdd:PRK03918  239 EIEELEKELESLEGsKRKLEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767981142  108 AQLEKQKQMRAEEAKTVQEKAAKIkEWVTLKLAKLEMENQHLKShNQRLVEQVGSLQDALEAI 170
Cdd:PRK03918  317 SRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERL 377
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
41-145 3.99e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 43.48  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    41 DKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLHRKYQELLKAIKGKDEL-----------------I 103
Cdd:pfam00261   15 ERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESergrkvlenralkdeekM 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767981142   104 SQLEAQLekqkqmraEEAKTVQEKAAKIKEWVTLKLAKLEME 145
Cdd:pfam00261   95 EILEAQL--------KEAKEIAEEADRKYEEVARKLVVVEGD 128
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
26-166 4.29e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   26 FRFRLQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEgsLHRKYQELLKAIKGKDELISQ 105
Cdd:COG4717   387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE--LEEELEELREELAELEAELEQ 464
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981142  106 LEAQLEKQkQMRAEEAKTVQEKAAKIKEWVTLKLAkLEMENQHLKSHNQRLVEQVgsLQDA 166
Cdd:COG4717   465 LEEDGELA-ELLQELEELKAELRELAEEWAALKLA-LELLEEAREEYREERLPPV--LERA 521
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
21-171 5.39e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   21 LETQLFRFRLQASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSnLKNVDSEGSLHRKYQELLKAIKGKD 100
Cdd:COG4942    81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADL 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767981142  101 ELISQLEAQLEKQkqmRAEEAKTVQEKAAKIKEWVTLK------LAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG4942   160 AELAALRAELEAE---RAELEALLAELEEERAALEALKaerqklLARLEKELAELAAELAELQQEAEELEALIARLE 233
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
39-164 6.44e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 41.01  E-value: 6.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    39 LADKMQELE--QRLLEaEQRAEnaetqvgvMEEKVKLSNLKnvdsEGSLHRKYQELLKAIKGKDELISQLEAQLEKQKQM 116
Cdd:pfam13863    1 LLEKKREMFlvQLALD-AKREE--------IERLEELLKQR----EEELEKKEQELKEDLIKFDKFLKENDAKRRRALKK 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767981142   117 RAEEAKTVQEKAAKIKewvtlklaKLEMENQHLKSHNQRLVEQVGSLQ 164
Cdd:pfam13863   68 AEEETKLKKEKEKEIK--------KLTAQIEELKSEISKLEEKLEEYK 107
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
41-149 7.26e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 42.71  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    41 DKMQELEQRLLEAEQRAENAETQVGVMEEKVKLsnlknvdSEGSLHR----------KYQELLKAIKGKDELISQLEAQL 110
Cdd:pfam00261   92 EKMEILEAQLKEAKEIAEEADRKYEEVARKLVV-------VEGDLERaeeraelaesKIVELEEELKVVGNNLKSLEASE 164
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767981142   111 EK--QKQMRAEEA-KTVQEkaaKIKEWVTL------KLAKLEMENQHL 149
Cdd:pfam00261  165 EKasEREDKYEEQiRFLTE---KLKEAETRaefaerSVQKLEKEVDRL 209
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
29-167 7.62e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   29 RLQASKIREL---LADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVdSEGSLHRKYQELLKAIKGKD----- 100
Cdd:COG1340    56 REEAQELREKrdeLNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGG-SIDKLRKEIERLEWRQQTEVlspee 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767981142  101 -----ELISQLEAQLEKQKQMRaEEAKTVQEKAAKIKEWvtlklaKLEMENQHLKSHNqrLVEQVGSLQDAL 167
Cdd:COG1340   135 ekelvEKIKELEKELEKAKKAL-EKNEKLKELRAELKEL------RKEAEEIHKKIKE--LAEEAQELHEEM 197
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
91-166 9.68e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.47  E-value: 9.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   91 ELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIK----EWVTL---------KLAKLEMENQHLKshnQRLV 157
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEilndELIALqiennlleeKLRKLQEENDELV---ERWM 77

                  ....*....
gi 767981142  158 EQVGslQDA 166
Cdd:cd22887    78 AKKQ--QEA 84
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
48-171 9.96e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.74  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   48 QRLLEAEQR-AENAETQVGVMEEKVK--LSNLKNVDSE-GSLHRKYQELLKAIKGKDEL--ISQLEAQLEKQKQMRAEEA 121
Cdd:cd22656   120 KALLDDLLKeAKKYQDKAAKVVDKLTdfENQTEKDQTAlETLEKALKDLLTDEGGAIARkeIKDLQKELEKLNEEYAAKL 199
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767981142  122 K-TVQEKAAKIKEWvTLKLAKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:cd22656   200 KaKIDELKALIADD-EAKLAAALRLIADLTAADTDLDNLLALIGPAIPALE 249
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
37-171 1.07e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.79  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   37 ELLADKMQELEQRLLEAEQRAE---NAETQvgvMEEKVKLSNlKNVDSEGSLHRKYQELlkaikgkDELISQLEAQLEKQ 113
Cdd:COG3096   508 QALAQRLQQLRAQLAELEQRLRqqqNAERL---LEEFCQRIG-QQLDAAEELEELLAEL-------EAQLEELEEQAAEA 576
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767981142  114 KQMRAEEAKTVQEKAAKIKEwvtlkLAKLEMENQHLKSHNQRLVEQVG----SLQDALEAIQ 171
Cdd:COG3096   577 VEQRSELRQQLEQLRARIKE-----LAARAPAWLAAQDALERLREQSGealaDSQEVTAAMQ 633
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1-156 1.15e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142     1 MAELKVEAPASVDWQKRCLTLETQLFRFRLQAsKIRELLADKMQELEQRLLEAEQRAENAEtQVGVMEEKVKLSNLKNVD 80
Cdd:pfam13868   49 MEEERERALEEEEEKEEERKEERKRYRQELEE-QIEEREQKRQEEYEEKLQEREQMDEIVE-RIQEEDQAEAEEKLEKQR 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    81 SEGSLHRKYQELLKAIKGKDELISQLE----AQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRL 156
Cdd:pfam13868  127 QLREEIDEFNEEQAEWKELEKEEEREEderiLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL 206
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
29-132 1.27e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   29 RLQASKirellADKMQELEQRLLEAEQRAENAETQVGVMEEKVKlsnlknvdsegslhRKYQELLKAIKGKDELISQleA 108
Cdd:PRK09510   66 RQQQQQ-----KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLK--------------QLEKERLAAQEQKKQAEEA--A 124
                          90       100
                  ....*....|....*....|....
gi 767981142  109 QLEKQKQMRAEEAKTVQEKAAKIK 132
Cdd:PRK09510  125 KQAALKQKQAEEAAAKAAAAAKAK 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-156 1.42e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    21 LETQLFRFRLQASKIR---ELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKlsnlknvdsegSLHRKYQELLKAIK 97
Cdd:TIGR02168  857 LAAEIEELEELIEELEselEALLNERASLEEALALLRSELEELSEELRELESKRS-----------ELRRELEELREKLA 925
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767981142    98 GKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEmenQHLKSHNQRL 156
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
29-148 1.54e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   29 RLQASKIRELLADKMQELEQRLLEAEQRAENAETQvgvmEEKVKLSNLKNVDSEGSLHRKYQELLKAIKGKDELISQLEA 108
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEE----LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767981142  109 QLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQH 148
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
PH_CpORP2-like cd13293
Cryptosporidium-like Oxysterol binding protein related protein 2 Pleckstrin homology (PH) ...
583-668 1.57e-03

Cryptosporidium-like Oxysterol binding protein related protein 2 Pleckstrin homology (PH) domain; There are 2 types of ORPs found in Cryptosporidium: CpORP1 and CpORP2. Cryptosporium differs from other apicomplexans like Plasmodium, Toxoplasma, and Eimeria which possess only a single long-type ORP consisting of an N-terminal PH domain followed by a C-terminal ligand binding (LB) domain. CpORP2 is like this, but CpORP1 differs and has a truncated N-terminus resulting in only having a LB domain present. The exact functions of these proteins are largely unknown though CpORP1 is thought to be involved in lipid transport across the parasitophorous vacuole membrane. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. 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: 241447  Cd Length: 88  Bit Score: 38.85  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  583 GYLLKMGSQVKTWKRRWFVLRQGQIMYYKSPSdviRKPQGQVDLNSrCQI-VRGEGSQTFQLISEKKTYYLTADSPSLLE 661
Cdd:cd13293     3 GYLKKWTNIFNSWKPRYFILYPGILCYSKQKG---GPKKGTIHLKI-CDIrLVPDDPLRIIINTGTNQLHLRASSVEEKL 78

                  ....*..
gi 767981142  662 EWIRVLQ 668
Cdd:cd13293    79 KWYNALK 85
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
42-133 1.72e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 41.20  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    42 KMQELEQRlleaeQRAENAETQVGVMEEKVKLSNLknvdsegslHRKYQELLKAIKGKDELISQLEAQLEKQKQM-RAEE 120
Cdd:pfam05010    5 DMDAALEK-----ARNEIEEKELEINELKAKYEEL---------RRENLEMRKIVAEFEKTIAQMIEEKQKQKELeHAEI 70
                           90
                   ....*....|...
gi 767981142   121 AKTVQEKAAKIKE 133
Cdd:pfam05010   71 QKVLEEKDQALAD 83
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
15-171 1.78e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   15 QKRCLTLETQLFRFRL-QASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVklsnlknvdsegslhRKYQELL 93
Cdd:COG4913   268 RERLAELEYLRAALRLwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL---------------DELEAQI 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   94 KAIKGKDelISQLEAQ---LEKQKQMRAEEAKTVQEKAAKI--------KEWVTLKL---AKLEMENQHLKSHNQRLVEQ 159
Cdd:COG4913   333 RGNGGDR--LEQLEREierLERELEERERRRARLEALLAALglplpasaEEFAALRAeaaALLEALEEELEALEEALAEA 410
                         170
                  ....*....|..
gi 767981142  160 VGSLQDALEAIQ 171
Cdd:COG4913   411 EAALRDLRRELR 422
PRK12704 PRK12704
phosphodiesterase; Provisional
37-131 1.82e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   37 ELLADKMQELEQR---LLEAEQRAENAETQVGVMEEKVKlsnlknvdsegSLHRKYQELLKAIKG------KDELISQLE 107
Cdd:PRK12704   96 ENLDRKLELLEKReeeLEKKEKELEQKQQELEKKEEELE-----------ELIEEQLQELERISGltaeeaKEILLEKVE 164
                          90       100
                  ....*....|....*....|....*....
gi 767981142  108 AQLEKQKQMRA----EEAK-TVQEKAAKI 131
Cdd:PRK12704  165 EEARHEAAVLIkeieEEAKeEADKKAKEI 193
PH2_FGD1-4 cd13236
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins pleckstrin homology (PH) ...
582-667 2.07e-03

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins pleckstrin homology (PH) domain, C-terminus; In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Not much is known about FGD2. FGD1 is the best characterized member of the group with mutations here leading to the X-linked disorder known as faciogenital dysplasia (FGDY). Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP). FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. 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: 270056  Cd Length: 105  Bit Score: 39.26  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  582 SGYLLKMGSQvKTWKRRWFVL--RQGQIMY-YKSPSDVirKPQGQV-----DLNSRCQIVRGEGSQTFQLISEKKTYYLT 653
Cdd:cd13236    11 CGFLQYSEKG-KTWQKVWCVIprTEPLVLYlYGAPQDV--RAQRTIplpgcEVTVPPPEERLDGRHVFKLSQSKQSHYFS 87
                          90
                  ....*....|....
gi 767981142  654 ADSPSLLEEWIRVL 667
Cdd:cd13236    88 AESEELQQRWLEAL 101
COG5022 COG5022
Myosin heavy chain [General function prediction only];
19-164 2.19e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   19 LTLETQLFRFRlqaSKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDS-EGSLHRKYQELLKAIK 97
Cdd:COG5022   902 LELESEIIELK---KSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEvESKLKETSEEYEDLLK 978
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767981142   98 GKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKlaKLEMENQHLKSHNQRLVEQVGSLQ 164
Cdd:COG5022   979 KSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK--ELPVEVAELQSASKIISSESTELS 1043
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
32-171 2.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   32 ASKIRELLADKMQELEQRLleaeQRAENAETQVGVMEEKV--KLSNLKNVDSE--------GSLHRKYQELlKAIKgkdE 101
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELeeVLREINEISSElpelreelEKLEKEVKEL-EELK---E 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  102 LISQLEAQLEK-QKQMRAEEAKTVQ------EKAAKIKE------------WVTLKLAKLEMENQHLKSHNQRLVEQVGS 162
Cdd:PRK03918  239 EIEELEKELESlEGSKRKLEEKIREleerieELKKEIEEleekvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSR 318

                  ....*....
gi 767981142  163 LQDALEAIQ 171
Cdd:PRK03918  319 LEEEINGIE 327
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
31-171 2.52e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   31 QASKIRELLADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLhrkyQELLKAIKGKDELISQLEAQL 110
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767981142  111 EKQKQMRAEEAKTVQekaaKIKEWVTLKL-------AKLEMENQHLKSHNQRLVEQVGSLQDALEAIQ 171
Cdd:COG4942   100 EAQKEELAELLRALY----RLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
595-675 2.72e-03

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. 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: 269962  Cd Length: 114  Bit Score: 38.93  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  595 WKRRWFVLRQGQIMYYKSPSDviRKPQGQVDLnSRCQIVRGEGSQ---TFQLISEK-KTYYLTADSPSLLEEWIRVLQSL 670
Cdd:cd01260    33 WKKYWFVLKGSSLYWYSNQQD--EKAEGFINL-PDFKIERASECKkkyAFKACHPKiKTFYFAAENLDDMNKWLSKLNMA 109

                  ....*
gi 767981142  671 LKVQA 675
Cdd:cd01260   110 INKYA 114
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
58-173 3.47e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   58 ENAETQVGvmEEKVKLSNL--KNVDSEGSLHRKYQELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIkewv 135
Cdd:PRK00409  505 EEAKKLIG--EDKEKLNELiaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQA---- 578
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767981142  136 tLKLAKLEMEnQHLKSHNQRLVEQVGS-----LQDALEAIQIA 173
Cdd:PRK00409  579 -IKEAKKEAD-EIIKELRQLQKGGYASvkaheLIEARKRLNKA 619
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
16-170 3.56e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   16 KRCLTLETQLFRFRLQASKIRELlADKMQELEQRLLEAEQRAENAETQVgvmeEKVKLSNLKNVDSE----GSLHRKYQE 91
Cdd:PRK03918  532 EKLIKLKGEIKSLKKELEKLEEL-KKKLAELEKKLDELEEELAELLKEL----EELGFESVEELEERlkelEPFYNEYLE 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   92 LLKA---IKGKDELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTL----KLAKLEMENQHLKSHNQRLVEQVGSLQ 164
Cdd:PRK03918  607 LKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELE 686

                  ....*.
gi 767981142  165 DALEAI 170
Cdd:PRK03918  687 KRREEI 692
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
591-668 4.58e-03

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. 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: 269942  Cd Length: 136  Bit Score: 38.96  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  591 QVKTWKRRWFVL-RQGQIMYY--KSPSDVirkPQGQVDLNSRCQIVRGEG--SQTFQL--ISEKKTYYLTADSPSLLEEW 663
Cdd:cd01236    50 RSKRWQRRWFVLyDDGELTYAldEMPDTL---PQGSIDMSQCTEVTDAEArtGHPHSLaiTTPERIHFVKADSKEEIRWW 126

                  ....*
gi 767981142  664 IRVLQ 668
Cdd:cd01236   127 LELLA 131
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-140 4.94e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    1 MAELKVEAPASVDWQKRClTLETQLFRFRLQASKIRELLADkMQELEQRLLEAEQRAENAETQvgvMEEKVKLSNLKNVD 80
Cdd:COG4717   118 LEKLEKLLQLLPLYQELE-ALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEE---LEELLEQLSLATEE 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767981142   81 SEGSLHRKYQELLKAIKGKDELISQLEAQLEKQKQ--MRAEEAKTVQEKAAKIKEWVTLKLA 140
Cdd:COG4717   193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEelEQLENELEAAALEERLKEARLLLLI 254
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-132 5.86e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   21 LETQLFRFRLQASKIRELLAD-------------KMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLKNVDSEGSLHR 87
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKEleekeerleelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767981142   88 KYQELLKAIKGKDELISQLEAQLEKQKQMRAEEAKTVQE-KAAKIK 132
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKGK 437
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
34-186 5.94e-03

FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.


Pssm-ID: 428323 [Multi-domain]  Cd Length: 140  Bit Score: 38.50  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    34 KIRELLADKMQELEQ--RLLEAEQRAenaetqvgvmeekvklsnLKNVDSEgslhrkyqELLKAIKGKDELISQLeAQLE 111
Cdd:pfam05130    2 ELIELLEEELELLEEllELLEEEQEA------------------LKAGDIE--------ALEELTEEKQELLQKL-AQLE 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   112 KQKQmRAEEAKTVQEKAAKIKEWVTL------------KLAKLEMENQHLKSHNQRLVEQV-GSLQDALEAIQIAPSRKL 178
Cdd:pfam05130   55 KERR-ELLAELGLSPEEATLSELLAKeeedpelrelwqELLELLERLKELNELNGELIEQSlEFNNRSLNILQGAANGSN 133

                   ....*...
gi 767981142   179 LvppYGAA 186
Cdd:pfam05130  134 T---YGAD 138
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
41-146 6.05e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   41 DKMQELEQRLLEAEQRAENAETQVGVMEEKV---------------KLSNLK---NVDSEG--SLHRKYQELLKAIKGKD 100
Cdd:COG0497   261 PSLAELAERLESALIELEEAASELRRYLDSLefdperleeveerlaLLRRLArkyGVTVEEllAYAEELRAELAELENSD 340
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767981142  101 ELISQLEAQLEKQKQMRAEEAKTV----QEKAAKIKEWVTLKLAKLEMEN 146
Cdd:COG0497   341 ERLEELEAELAEAEAELLEAAEKLsaarKKAAKKLEKAVTAELADLGMPN 390
RNase_Y_N pfam12072
RNase Y N-terminal region;
15-133 6.73e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    15 QKRCLTLETQ--LFRFRLQA---SKIREllaDKMQELEQRLLeaeQRAENAETQVGVMEEKvklsnlknvdsEGSLHRKY 89
Cdd:pfam12072   50 KKKEALLEAKeeIHKLRAEAereLKERR---NELQRQERRLL---QKEETLDRKDESLEKK-----------EESLEKKE 112
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981142    90 QELLKA---IKGK----DELISQLEAQLEKQKQMRAEEAK----------TVQEKAAKIKE 133
Cdd:pfam12072  113 KELEAQqqqLEEKeeelEELIEEQRQELERISGLTSEEAKeilldeveeeLRHEAAVMIKE 173
PH_PLEKHD1 cd13281
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH ...
580-673 8.47e-03

Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain; Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, , dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. 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: 270099  Cd Length: 139  Bit Score: 38.07  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  580 EKSGYLLK--MGSQVKTWKRRWFVLRQGQIMYYkspSDVIRK-----------PQGQVDLNSrCQIVRG-EGSQTFQLIS 645
Cdd:cd13281    13 QLHGILWKkpFGHQSAKWSKRFFIIKEGFLLYY---SESEKKdfektrhfnihPKGVIPLGG-CSIEAVeDPGKPYAISI 88
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767981142  646 EKKTY----YLTADSPSLLEEWIRVLQSLLKV 673
Cdd:cd13281    89 SHSDFkgniILAADSEFEQEKWLDMLRESGKI 120
mukB PRK04863
chromosome partition protein MukB;
33-179 8.91e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   33 SKIREL-----LADKMQELEQRLLEAEQRAENAETQVGVMEEKVKLSNLkNVDSEGSLHRKYQELLKAIKGKDELISQLE 107
Cdd:PRK04863  500 ELLRRLreqrhLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK-NLDDEDELEQLQEELEARLESLSESVSEAR 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142  108 AQLEKQKQMRAEEAKTVQEKAAKIKEWVTL--KLAKLE-------MENQHLKSHNQRLVEQVGSLQdaLEAIQIAPSRKL 178
Cdd:PRK04863  579 ERRMALRQQLEQLQARIQRLAARAPAWLAAqdALARLReqsgeefEDSQDVTEYMQQLLERERELT--VERDELAARKQA 656

                  .
gi 767981142  179 L 179
Cdd:PRK04863  657 L 657
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
31-167 9.18e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   31 QAS--KIRELLADKMQELEQRL--------------LEAEQRAE---NAETQVGVMEEKVKLSNLKNVDSEG-SLHRKYQ 90
Cdd:cd16269   112 EASskRCQALLQELSAPLEEKIsqgsysvpggyqlyLEDREKLVekyRQVPRKGVKAEEVLQEFLQSKEAEAeAILQADQ 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142   91 ELLKAIKGKDEL-----ISQLEAQLEKQKQMRAEEAKTVQEKAakIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQD 165
Cdd:cd16269   192 ALTEKEKEIEAErakaeAAEQERKLLEEQQRELEQKLEDQERS--YEEHLRQLKEKMEEERENLLKEQERALESKLKEQE 269

                  ..
gi 767981142  166 AL 167
Cdd:cd16269   270 AL 271
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
27-164 9.23e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.06  E-value: 9.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981142    27 RFRLQasKIRELLADKMQELEQRLLEAEQRAENAETQVgVMEEKVKLSNLKNVDSEGSL------HRKYQELLKAIkgkD 100
Cdd:TIGR02473    1 EFRLQ--KLLDLREKEEEQAKLELAKAQAEFERLETQL-QQLIKYREEYEQQALEKVGAgtsaleLSNYQRFIRQL---D 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767981142   101 ELISQLEAQLEKQKQMRAEEAKTVQEKAAKIKEWVTLKLAKLEMENQHLKSHNQRLVEQVGSLQ 164
Cdd:TIGR02473   75 QRIQQQQQELALLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
 
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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