NCBI Conserved Domain Search

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

2327-2448

2.85e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.85e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG1196    422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

2231-2444

7.78e-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: 48.51 E-value: 7.78e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2231 EKEEGEDSL-DLRRTESDSVLKKGGNNNLLLLLKRNSEQVLHSVTYLHDLLNTLQAVVVQQDTFIEDQRHALAERPASRH 2309
Cdd:TIGR02168  706 ELEELEEELeQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2310 SSTSSLSSSSSRPNSLIEQ--EKQRSLEKQRQEVANLQRQQAAH---ADERRRREREWEVRESGLSDREAQVKEQDEETL 2384
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREAldELRAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065137183 2385 RRRGQLEEERQELQKRKEEYQRDLERLRDAQRKLDRDRDTLRREA-EMVEQMKKAEAEQAH 2444
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRsELRRELEELREKLAQ 926

C1_1

pfam00130

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...

1532-1578

9.37e-04

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.

Pssm-ID: 395079 Cd Length: 53 Bit Score: 39.35 E-value: 9.37e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2065137183 1532 HLFSSVNPAPSTTCHQCNKPINTKE--AFLCTNCNAQVHKGCRDSLPVC 1578
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGkqGLKCSWCKLNVHKRCHEKVPPE 49

DUF5401

Family of unknown function (DUF5401); This is a family of unknown function found in ...

2326-2445

1.03e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2326 IEQEKQRSLEKQRQEVANLQRQQAAHaderrrrerewevresglSDREAQVKEQDEETLRRRGQLEEERQ-ELQKRKEEY 2404
Cdd:pfam17380  383 LQMERQQKNERVRQELEAARKVKILE------------------EERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEER 444

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2405 QRDLERLR----DAQRKLDRDR----DTLRREAEM-VEQMKKAEAEQAHR 2445
Cdd:pfam17380  445 AREMERVRleeqERQQQVERLRqqeeERKRKKLELeKEKRDRKRAEEQRR 494

Name

Accession

Description

Interval

E-value

PH_AKAP13

cd13392

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...

1976-2078

7.17e-57

Pssm-ID: 275427 Cd Length: 103 Bit Score: 192.43 E-value: 7.17e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1976 LLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASLDQRSTVISLQKLIVREVANEERGLFLITAGIEKPEMV 2055
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80

                           90       100
                   ....*....|....*....|...
gi 2065137183 2056 EVLASTKEERNTWMQLIQDAMHS 2078
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103

RhoGEF

cd00160

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...

1737-1932

2.96e-49

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.

Pssm-ID: 238091 [Multi-domain] Cd Length: 181 Bit Score: 173.64 E-value: 2.96e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1737 RQDVIYELVQTEMHHVRTLRIMSEVYSKGLQKEVQ-LDTQVVERVFPMLDELLELHTHFFAHLLELKRKSSIEGRDdgsf 1815
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPR---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1816 lirkIGDVLVSQFSgpnadrMKKVYGKFCSRHNEAVNFYKELHTKDKRFQAFIKKKMSStiVRRLGIPECILLVTQRITK 1895
Cdd:cd00160     77 ----IGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--CGRLKLESLLLKPVQRLTK 144

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2065137183 1896 YPVLLQRILQHTKENEEDHDDITQALRLVKEILNAVD 1932
Cdd:cd00160    145 YPLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181

PH_16

pfam17838

PH domain;

1959-2076

7.02e-47

PH domain;

Pssm-ID: 436083 Cd Length: 127 Bit Score: 164.88 E-value: 7.02e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1959 MKSGQMFAREDLVRgRRLLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASL-------DQR--STVISLQK 2029
Cdd:pfam17838    1 HPLGEEFKKLDLTT-RKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2065137183 2030 LIVREVANEERGLFLITAGIEKPEMVEVLASTKEERNTWMQLIQDAM 2076
Cdd:pfam17838   80 LIVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAI 126

PH_p190RhoGEF

cd14680

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called ...

1976-2076

3.64e-45

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called RIP2 or ARHGEF28) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275430 Cd Length: 101 Bit Score: 159.01 E-value: 3.64e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1976 LLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASLDQRSTVISLQKLIVREVANEERGLFLITAGIEKPEMV 2055
Cdd:cd14680      1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMY 80

                           90       100
                   ....*....|....*....|.
gi 2065137183 2056 EVLASTKEERNTWMQLIQDAM 2076
Cdd:cd14680     81 EIHTSSKEERNNWMRLIQEAV 101

RhoGEF

smart00325

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...

1740-1932

3.67e-45

Pssm-ID: 214619 [Multi-domain] Cd Length: 180 Bit Score: 162.08 E-value: 3.67e-45

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183  1740 VIYELVQTEMHHVRTLRIMSEVYSKGLQKEVQ-LDTQVVERVFPMLDELLELHTHFFAHLLELKRKSSIegrddgsfLIR 1818
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKlLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDD--------SVE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183  1819 KIGDVLVSQfsgpnaDRMKKVYGKFCSRHNEAVNFYKELhTKDKRFQAFIKKKMSSTIVRRLGIPECILLVTQRITKYPV 1898
Cdd:smart00325   73 RIGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPL 145

                           170       180       190
                    ....*....|....*....|....*....|....
gi 2065137183  1899 LLQRILQHTKENEEDHDDITQALRLVKEILNAVD 1932
Cdd:smart00325  146 LLKELLKHTPEDHEDREDLKKALKAIKELANQVN 179

PH_ARHGEF18

cd15794

Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also ...

1974-2092

5.12e-43

Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also called p114RhoGEF, is a key regulator of RhoA-Rock2 signaling that is crucial for maintenance of polarity in the vertebrate retinal epithelium, and consequently is essential for cellular differentiation, morphology and eventually organ function. ARHGEF18 contains Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275437 Cd Length: 119 Bit Score: 153.52 E-value: 5.12e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1974 RRLLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASLDQRSTVISLQKLIVREVANEERGLFLITAGIEKPE 2053
Cdd:cd15794      2 RQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGPE 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2065137183 2054 MVEVLASTKEERNTWMQLIQDAMHSIeKDDDEGIPSETE 2092
Cdd:cd15794     82 MYEIHTNSKEDRNTWMAHIRRAVESC-PDEEEGLFSEPE 119

PH_ARHGEF2

cd13393

Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called ...

1974-2084

7.37e-40

Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called GEF-H1, acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275428 Cd Length: 116 Bit Score: 144.25 E-value: 7.37e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1974 RRLLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASLDqRSTVISLQKLIVREVANEERGLFLITAgiEKPE 2053
Cdd:cd13393      2 RKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLISA--APPE 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2065137183 2054 MVEVLASTKEERNTWMQLIQDAMHSIEKDDD 2084
Cdd:cd13393     79 MYEVHAASRDDRNTWMRLIQQTVKTCPSREE 109

PH_RhoGEF

cd13329

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...

1976-2076

3.85e-39

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. 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: 275411 Cd Length: 109 Bit Score: 142.02 E-value: 3.85e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1976 LLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYV--------FASLDQRSTVISLQKLIVREVANEERGLFLITA 2047
Cdd:cd13329      1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80

                           90       100
                   ....*....|....*....|....*....
gi 2065137183 2048 GIEKPEMVEVLASTKEERNTWMQLIQDAM 2076
Cdd:cd13329     81 SKNGPQMYELVANSSSERKTWIKHISDAV 109

RhoGEF

pfam00621

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...

1740-1932

1.45e-38

Pssm-ID: 459876 [Multi-domain] Cd Length: 176 Bit Score: 142.82 E-value: 1.45e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1740 VIYELVQTEMHHVRTLRIMSEVYSKGLQKEVQLDTQVVERVFPMLDELLELHTHFFahlLELKRKSSIEgrddgsflIRK 1819
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL---LEELLKEWIS--------IQR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1820 IGDVLVSQFSGpnadrmKKVYGKFCSRHNEAVNFYKELHTKDKRFQAFIKKKMSSTIVRRLGIPECILLVTQRITKYPVL 1899
Cdd:pfam00621   70 IGDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLL 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2065137183 1900 LQRILQHTKENEEDHDDITQALRLVKEILNAVD 1932
Cdd:pfam00621  144 LKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176

C1_AKAP13

cd20878

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...

1525-1584

1.38e-35

Pssm-ID: 410428 Cd Length: 60 Bit Score: 130.15 E-value: 1.38e-35

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1525 EKKTLNGHLFSSVNPAPSTTCHQCNKPINTKEAFLCTNCNAQVHKGCRDSLPVCVQVKMK 1584
Cdd:cd20878      1 DKKTLNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60

PH_ARHGEF2_18_like

cd15789

rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling ...

1976-2075

1.89e-30

rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. 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: 275432 Cd Length: 102 Bit Score: 116.79 E-value: 1.89e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1976 LLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASLDQRSTVISLQKLIVREVANEERGLFLITAGIEK-PEM 2054
Cdd:cd15789      1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLISASPDGmPEM 80

                           90       100
                   ....*....|....*....|.
gi 2065137183 2055 VEVLASTKEERNTWMQLIQDA 2075
Cdd:cd15789     81 YELKVQKPKDKNTWIQTIRQA 101

PH_PRG

cd13391

PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called ...

1950-2076

3.66e-19

PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called RhoGEF11) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. PRG contains an N-terminal PDZ domain, a regulators of G-protein signaling-like (RGSL) domain, a linker region, and a C-terminal Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. As is the case in p115-RhoGEF, it is thought that the PRG activated by relieving autoinhibition caused by the linker 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: 275426 Cd Length: 142 Bit Score: 86.24 E-value: 3.66e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1950 RTDSKSIQRMKS--GQMFAREDLvRGRRLLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVF--------ASLD 2019
Cdd:cd13391      1 RLDATALERASNplAAEFKNLDL-TTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2020 QRST---VISLQKLIVREVANEERGLFLITAGIEKPEMVEVLASTKEERNTWMQLIQDAM 2076
Cdd:cd13391     80 SKQTfspVLKLNSVLIRSVATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAV 139

C1_ARHGEF2

cd20877

protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange ...

1530-1588

2.42e-15

protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange factor 2 (ARHGEF2) and similar proteins; ARHGEF2, also called guanine nucleotide exchange factor H1 (GEF-H1), microtubule-regulated Rho-GEF, or proliferating cell nucleolar antigen p40, acts as guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 may be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. It contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410427 Cd Length: 61 Bit Score: 72.31 E-value: 2.42e-15

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2065137183 1530 NGHLFSSVNPAPSTTCHQCNKPINTKEAFLCTNCNAQVHKGCRDSLPVCvqVKMKQKQQ 1588
Cdd:cd20877      4 NGHLFTTITVSGTTMCSACNKSITAKEALICPTCNVTIHNRCKDTLPNC--TKVKQKQQ 60

C1_p190RhoGEF

cd20876

protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange ...

1524-1578

2.54e-14

protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange factor (p190RhoGEF) and similar proteins; p190RhoGEF, also called Rho guanine nucleotide exchange factor (RGNEF), Rho guanine nucleotide exchange factor 28 (ARHGEF28), or RIP2, is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410426 Cd Length: 61 Bit Score: 69.39 E-value: 2.54e-14

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065137183 1524 KEKKtLNGHLFSSVNPAPSTTCHQCNKPINTKEAFLCTNCNAQVHKGCRDSLPVC 1578
Cdd:cd20876      1 KEKQ-SNGHQFVTGSFSGPTLCVVCDKPVTGKELLQCSNCTVNVHKGCKESAPPC 54

C1_p190RhoGEF-like

cd20815

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...

1530-1578

8.76e-14

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410365 Cd Length: 54 Bit Score: 67.83 E-value: 8.76e-14

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1530 NGHLFSSVNPAPSTTCHQCNKPINTKEAFLCTNCNAQVHK-GCRDSLPVC 1578
Cdd:cd20815      2 NTHQFVPVSFSNSTKCDVCSKPLTNKPALQCENCSVNVHDsSCKDQLADC 51

PH_LARG

cd13390

Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; ...

1969-2072

3.53e-13

Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; LARG (also called RhoGEF12) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. LARG contains a N-terminal extension, followed by Dbl homology (DH)-PH domains which bind and catalyze the exchange of GDP for GTP on RhoA in addition to a RGS domain. The active site of RhoA adopts two distinct GDP-excluding conformations among the four unique complexes in the asymmetric unit. The LARG PH domain also contains a potential protein-docking site. LARG forms a homotetramer via its DH 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: 275425 Cd Length: 138 Bit Score: 68.86 E-value: 3.53e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1969 DLVRgRRLLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVF--------ASLDQRST---VISLQKLIVREVAN 2037
Cdd:cd13390     20 DLTK-RKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKHTfspVIKLNTVLVRQVAT 98

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2065137183 2038 EERGLFLITAGIEKPEMVEVLASTKEERNTWMQLI 2072
Cdd:cd13390     99 DNKAFFVISMSENGAQIYELVAQTVSEKTVWQDLI 133

PH_p115RhoGEF

cd14679

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...

1974-2075

4.52e-12

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, GEF1 or LBCL2) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p115RhoGEF contains an N-terminal RGS (Regulator of G-protein signalling) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275429 Cd Length: 125 Bit Score: 65.25 E-value: 4.52e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1974 RRLLHDGPLQLKNSAGRLKDVQAMLLSDVFVFLQEKDQKYVFASlDQRST------------VISLQKLIVREVANEERG 2041
Cdd:cd14679      9 KKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLKC-HSRTTtptpdgkqmlspIIKLNSAMTREVATDRKA 87

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2065137183 2042 LFLITAGIEKPEMVEVLASTKEERNTWMQLIQDA 2075
Cdd:cd14679     88 FYVIFTWEQGAQIYELVAQTVSERKNWCALISET 121

ROM1

COG5422

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...

1712-2011

6.17e-10

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];

Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 65.30 E-value: 6.17e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1712 DLEADSWTFTVDKKYVKGLKKEVVKRQDVIYELVQTEMHHVRTLRIMSEVYSKGLqkevqLDTQVVERvfpmlDELLELH 1791
Cdd:COG5422    460 DEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPL-----EESNIIPE-----NARRNFI 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1792 THFFAHLLEL-----KRKSSIEGRDDGSFLIRKIGDVLVSQFsgPNADRMKKV-----YGKFCSRHNEAVNFYkelhtkd 1861
Cdd:COG5422    530 KHVFANINEIyavnsKLLKALTNRQCLSPIVNGIADIFLDYV--PKFEPFIKYgasqpYAKYEFEREKSVNPN------- 600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1862 krFQAFIKKKMSSTIVRRLGIPECILLVTQRITKYPVLLQRILQHTKENEEDHDDITQALRLVKEILnavdskvnehdkK 1941
Cdd:COG5422    601 --FARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFL------------S 666

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065137183 1942 KRLKEVYSRTDSKSIQRMKSGQMFAREDLVRG-----RRLLHDGPLQLK----NSAGRLKDVQAMLLSDVFVFLQEKDQ 2011
Cdd:COG5422    667 RLNFESGKAENRGDLFHLNQQLLFKPEYVNLGlndeyRKIIFKGVLKRKakskTDGSLRGDIQFFLLDNMLLFCKAKAV 745

cd00029

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...

1532-1576

2.98e-07

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.

Pssm-ID: 410341 Cd Length: 50 Bit Score: 49.05 E-value: 2.98e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2065137183 1532 HLFSSVNPAPSTTCHQCNKPIN--TKEAFLCTNCNAQVHKGCRDSLP 1576
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWglFKQGLKCSDCGLVCHKKCLDKAP 47

smart00109

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...

1532-1576

1.17e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.

Pssm-ID: 197519 Cd Length: 50 Bit Score: 47.46 E-value: 1.17e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2065137183  1532 HLFSSVNPAPSTTCHQCNKPINT--KEAFLCTNCNAQVHKGCRDSLP 1576
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGsfKQGLRCSECKVKCHKKCADKVP 47

C1_ARHGEF18-like

cd20879

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...

1530-1578

1.32e-06

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor 18 (ARHGEF18)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate ARHGEF18, which is also called 114 kDa Rho-specific guanine nucleotide exchange factor (p114-Rho-GEF), p114RhoGEF, or septin-associated RhoGEF (SA-RhoGEF). ARHGEF18 acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. ARHGEF18 also acts as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Members of this family contain C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains, as well as a DUF5401 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410429 Cd Length: 53 Bit Score: 47.50 E-value: 1.32e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2065137183 1530 NGHLFSSVNPAPSTTCHQCNKPINTKEAFLCTNCNAQVHKGCRDSLPVC 1578
Cdd:cd20879      2 NGHQLVPGTFSSCATCSLCSKPLQNRNGLQCLNCAVNVHKNCKTLLTEC 50

C1_MgcRacGAP

cd20821

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...

1532-1581

8.12e-06

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410371 Cd Length: 55 Bit Score: 45.09 E-value: 8.12e-06

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2065137183 1532 HLFSSVNPAPSTTCHQCNKPIN-TKEAFLCTNCNAQVHKGCRDSLPV-CVQV 1581
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIKfGKKALKCKDCRVVCHPDCKDKLPLpCVPT 54

smart00233

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...

1976-2077

1.11e-05

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 46.39 E-value: 1.11e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183  1976 LLHDGPLQLKNSAGRL--KDVQAMLLSDVFVFLQEKDQKYVFASldqrSTVISLQKLIVREVAN----EERGLFLITagI 2049
Cdd:smart00233    1 VIKEGWLYKKSGGGKKswKKRYFVLFNSTLLYYKSKKDKKSYKP----KGSIDLSGCTVREAPDpdssKKPHCFEIK--T 74

                            90       100
                    ....*....|....*....|....*...
gi 2065137183  2050 EKPEMVEVLASTKEERNTWMQLIQDAMH 2077
Cdd:smart00233   75 SDRKTLLLQAESEEEREKWVEALRKAIA 102

PTZ00121

MAEBL; Provisional

2327-2469

2.34e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.34e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:PTZ00121  1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065137183 2407 DLERLRDAQRKLDRDRDtlrrEAEMVEQMKKAEAEQAHRTQRTPSSTSEESMKFQSSTSLDKE 2469
Cdd:PTZ00121  1683 AEEDEKKAAEALKKEAE----EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741

Smc

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

2327-2448

2.85e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.85e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG1196    422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

Smc

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

2328-2448

3.21e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 3.21e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2328 QEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQRD 2407
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2065137183 2408 LERLRDAQRKLDRDRDTLR-REAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG1196    318 LEELEEELAELEEELEELEeELEELEEELEEAEEELEEAEAE 359

C1_VAV

cd20810

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...

1530-1578

6.80e-05

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410360 Cd Length: 52 Bit Score: 42.63 E-value: 6.80e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065137183 1530 NGHLFSSVNPAPSTTCHQCNKpintkeaFL---------CTNCNAQVHKGCRDSLPVC 1578
Cdd:cd20810      1 TGHSFELTTFKEPTTCSVCKK-------LLkglffqgykCSVCGAAVHKECIAKVKRC 51

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

2231-2444

7.78e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 7.78e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2231 EKEEGEDSL-DLRRTESDSVLKKGGNNNLLLLLKRNSEQVLHSVTYLHDLLNTLQAVVVQQDTFIEDQRHALAERPASRH 2309
Cdd:TIGR02168  706 ELEELEEELeQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2310 SSTSSLSSSSSRPNSLIEQ--EKQRSLEKQRQEVANLQRQQAAH---ADERRRREREWEVRESGLSDREAQVKEQDEETL 2384
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREAldELRAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065137183 2385 RRRGQLEEERQELQKRKEEYQRDLERLRDAQRKLDRDRDTLRREA-EMVEQMKKAEAEQAH 2444
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRsELRRELEELREKLAQ 926

C1_Stac

cd20817

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...

1543-1578

8.66e-05

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410367 Cd Length: 51 Bit Score: 42.31 E-value: 8.66e-05

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2065137183 1543 TTCHQCNKPI--NTKEAFLCTNCNAQVHKGCRDSLPVC 1578
Cdd:cd20817     12 TFCDVCKELLvgLSKQGLRCKNCKMNVHHKCQEGVPDC 49

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

2276-2456

8.83e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 8.83e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2276 LHDLLNTLQAVVVQQDTfIEDQRHALAERPASRHSSTSSLSSSSSRPNSLIEQEKQRsLEKQRQEVANLQRQQAAHADER 2355
Cdd:TIGR02168  693 IAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2356 RRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQRDLERLRDAQRKLDRDRDTLRREAEMVEQM 2435
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                          170       180
                   ....*....|....*....|...
gi 2065137183 2436 KK--AEAEQAHRTQRTPSSTSEE 2456
Cdd:TIGR02168  851 SEdiESLAAEIEELEELIEELES 873

Smc

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

2327-2449

9.71e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 9.71e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:COG1196    258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQRT 2449
Cdd:COG1196    338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

2328-2448

1.43e-04

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: 1.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2328 QEKQRSLEKQRQEVANLQRQQAAH----ADERRRREREWEVRESGLSDREAQVKEQDEETL-RRRGQLEEERQELQKRKE 2402
Cdd:COG1579     41 AALEARLEAAKTELEDLEKEIKRLeleiEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLkRRISDLEDEILELMERIE 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2065137183 2403 EYQRDLERLRDAQRKLDRDRDTLRREAEmvEQMKKAEAEQAHRTQR 2448
Cdd:COG1579    121 ELEEELAELEAELAELEAELEEKKAELD--EELAELEAELEELEAE 164

Smc

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

2325-2448

1.81e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.81e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2325 LIEQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRgQLEEERQELQKRKEEY 2404
Cdd:COG1196    250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAEL 328

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2065137183 2405 QRDLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

pfam00169

PH domain; PH stands for pleckstrin homology.

1976-2077

2.22e-04

PH domain; PH stands for pleckstrin homology.

Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 42.55 E-value: 2.22e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1976 LLHDGPLQLKNS--AGRLKDVQAMLLSDVFVFLQEKDQKyvfaSLDQRSTVISLQKLIVREVANEERG----LF-LITAG 2048
Cdd:pfam00169    1 VVKEGWLLKKGGgkKKSWKKRYFVLFDGSLLYYKDDKSG----KSKEPKGSISLSGCEVVEVVASDSPkrkfCFeLRTGE 76

                           90       100
                   ....*....|....*....|....*....
gi 2065137183 2049 IEKPEMVEVLASTKEERNTWMQLIQDAMH 2077
Cdd:pfam00169   77 RTGKRTYLLQAESEEERKDWIKAIQSAIR 105

C1_dGM13116p-like

cd20831

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...

1530-1571

2.52e-04

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410381 Cd Length: 58 Bit Score: 41.17 E-value: 2.52e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2065137183 1530 NGHLFSSVNPAPSTTCHQCNKPINT---KEAFLCTNCNAQVHKGC 1571
Cdd:cd20831      4 NDHTFVATHFKGGPSCAVCNKLIPGrfgKQGYQCRDCGLICHKRC 48

PTZ00121

MAEBL; Provisional

2326-2499

2.86e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.86e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2326 IEQEKQRSLEKQRQEVANLQRQQAAH---ADERRRREREWEVRESGLSDREAQVKEQDEEtLRRRGQLEEERQELQKRKE 2402
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDEKKAAEALKKEA 1698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2403 EYQRDLERLRDAQRKLDRDRDTLRREAEM----VEQMKKAEAEQAHRTQRTPSSTSEES----MKFQSSTSLDKEPGGGE 2474
Cdd:PTZ00121  1699 EEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKkiahLKKEEEKKAEEIRKEKE 1778

                          170       180
                   ....*....|....*....|....*
gi 2065137183 2475 AELSSSPATKEPFLRMGSKRKGKNL 2499
Cdd:PTZ00121  1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803

Smc

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

2325-2448

2.91e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 2.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2325 LIEQEKQRSLEKQRQEVANLQRQQAAHAderrrrEREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEY 2404
Cdd:COG1196    297 LARLEQDIARLEERRRELEERLEELEEE------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2065137183 2405 QRDL-ERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG1196    371 EAELaEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

2369-2452

2.92e-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: 45.91 E-value: 2.92e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2369 LSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQRDLERLRDAQRKLDRDRDTLRREA-EMVEQMKKAEAEQAHRTQ 2447
Cdd:COG4942    162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAeELEALIARLEAEAAAAAE 241


                   ....*
gi 2065137183 2448 RTPSS 2452
Cdd:COG4942    242 RTPAA 246

C1_PIK3R-like_rpt2

cd20830

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...

1532-1578

4.48e-04

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410380 Cd Length: 52 Bit Score: 40.31 E-value: 4.48e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1532 HLFSSVNPAPSTTCHQCNKPIN--TKEAFLCTNCNAQVHKGC-RDSLPVC 1578
Cdd:cd20830      1 HRFVEQSFSTLQWCDKCGKFLFglVHQGLQCQDCGLVCHRTCaATGLPKC 50

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

2327-2457

5.74e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 5.74e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVresgLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE----LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQRTPSSTSEES 2457
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847

Smc

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

2327-2447

7.30e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 7.30e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQ---KRKEE 2403
Cdd:COG1196    220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELAR 299

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2065137183 2404 YQRDLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQ 2447
Cdd:COG1196    300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343

YhaN

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

2328-2448

7.48e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 7.48e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2328 QEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVREsgLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQRD 2407
Cdd:COG4717     91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELPERLEELEERLEELRELEEELEEL 168

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2065137183 2408 LERLRDAQRKLDRDRD-----TLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG4717    169 EAELAELQEELEELLEqlslaTEEELQDLAEELEELQQRLAELEEE 214

C1_1

pfam00130

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...

1532-1578

9.37e-04

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.

Pssm-ID: 395079 Cd Length: 53 Bit Score: 39.35 E-value: 9.37e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2065137183 1532 HLFSSVNPAPSTTCHQCNKPINTKE--AFLCTNCNAQVHKGCRDSLPVC 1578
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGkqGLKCSWCKLNVHKRCHEKVPPE 49

YhaN

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

2327-2443

9.81e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 9.81e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRRERewevresglsDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:COG4717    144 LPERLEELEERLEELRELEEELEELEAELAELQE----------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQA 2443
Cdd:COG4717    214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250

DUF5401

Family of unknown function (DUF5401); This is a family of unknown function found in ...

2326-2445

1.03e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2326 IEQEKQRSLEKQRQEVANLQRQQAAHaderrrrerewevresglSDREAQVKEQDEETLRRRGQLEEERQ-ELQKRKEEY 2404
Cdd:pfam17380  383 LQMERQQKNERVRQELEAARKVKILE------------------EERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEER 444

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2405 QRDLERLR----DAQRKLDRDR----DTLRREAEM-VEQMKKAEAEQAHR 2445
Cdd:pfam17380  445 AREMERVRleeqERQQQVERLRqqeeERKRKKLELeKEKRDRKRAEEQRR 494

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

2329-2456

1.99e-03

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: 43.90 E-value: 1.99e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2329 EKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRR---GQLEEERQELQKRKEEYQ 2405
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYE 468

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2065137183 2406 RDLERLRDAQRKLDRDRDTLRREAEMVEqmkkAEAEQAHRTQRTPSSTSEE 2456
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAE----AQARASEERVRGGRAVEEV 515

mukB

PRK04863

chromosome partition protein MukB;

2329-2445

2.03e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 2.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2329 EKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEE---YQ 2405
Cdd:PRK04863   530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQ 609

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065137183 2406 RDLERLRDA---------------QRKLDRDRdTLRREAEMVEQMKKAEAEQAHR 2445
Cdd:PRK04863   610 DALARLREQsgeefedsqdvteymQQLLERER-ELTVERDELAARKQALDEEIER 663

DUF5401

Family of unknown function (DUF5401); This is a family of unknown function found in ...

2325-2448

2.12e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 2.12e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2325 LIEQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLR------RRGQLEEERQELQ 2398
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRqqeeerKRKKLELEKEKRD 485

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065137183 2399 KRKEEYQR------DLERLRDAQRKLDRDRDTLRREAE-----MVEQMKKAEAEQAHRTQR 2448
Cdd:pfam17380  486 RKRAEEQRrkilekELEERKQAMIEEERKRKLLEKEMEerqkaIYEEERRREAEEERRKQQ 546

DUF5401

Family of unknown function (DUF5401); This is a family of unknown function found in ...

2326-2453

2.36e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.36e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2326 IEQEKQRSLEKQRQEVANLQ------RQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETlRRRGQLEEER----- 2394
Cdd:pfam17380  440 LEEERAREMERVRLEEQERQqqverlRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERkrkll 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2395 ------------QELQKRKEEYQRDLE-------RLRDAQRKLDRDR---DTLRREAEMVEQMKKAEAEQAHRTQRTPSS 2452
Cdd:pfam17380  519 ekemeerqkaiyEEERRREAEEERRKQqemeerrRIQEQMRKATEERsrlEAMEREREMMRQIVESEKARAEYEATTPIT 598


                   .
gi 2065137183 2453 T 2453
Cdd:pfam17380  599 T 599

Smc

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

2327-2434

2.55e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 2.55e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQR 2406
Cdd:COG1196    667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746

                           90       100
                   ....*....|....*....|....*...
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQ 2434
Cdd:COG1196    747 LLEEEALEELPEPPDLEELERELERLER 774

YhaN

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

2378-2448

2.61e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 2.61e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065137183 2378 EQDEETLRRRGQLEEERQELQKRKEEYQRDLERLRDAQRKLDRDRDTLRRE---AEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqlLPLYQELEALEAELAELPER 147

ARGLU

pfam15346

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...

2372-2437

2.85e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.

Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 40.80 E-value: 2.85e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065137183 2372 REAQVKEQ---DEETLRRRGQLEEERQELQKRKEEYQRDL--ERLRDAQRKLDRDRDTLRREAEMVEQMKK 2437
Cdd:pfam15346   62 REAELEEErrkEEEERKKREELERILEENNRKIEEAQRKEaeERLAMLEEQRRMKEERQRREKEEEEREKR 132

RNase_Y_N

pfam12072

RNase Y N-terminal region;

2326-2441

3.34e-03

RNase Y N-terminal region;

Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 3.34e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2326 IEQE-KQRSLEKQRQEVANLQRQQAahaderrrrereWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEY 2404
Cdd:pfam12072   69 AERElKERRNELQRQERRLLQKEET------------LDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQ 136

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2065137183 2405 QRDLERL-----RDA-QRKLDRDRDTLRRE-AEMV---EQMKKAEAE 2441
Cdd:pfam12072  137 RQELERIsgltsEEAkEILLDEVEEELRHEaAVMIkeiEEEAKEEAD 183

COG4913

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

2328-2448

3.60e-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: 3.60e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2328 QEKQRSLEKQRQEVANLQRQQAAHADerrrrerewevresglsdREAQVKEQDEETLRRRGQLEEERQELQ-KRKEEYQR 2406
Cdd:COG4913    284 WFAQRRLELLEAELEELRAELARLEA------------------ELERLEARLDALREELDELEAQIRGNGgDRLEQLER 345

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2065137183 2407 DLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG4913    346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

2328-2463

3.89e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 3.89e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2328 QEKQRSLEKQRQEVANLQRQQAAhaderrrrerewevresgLSDREAQVKEQDEETLRRRGQLEEERQELQKRKE----- 2402
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEE------------------LEAQLEELESKLDELAEELAELEEKLEELKEELEsleae 359

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065137183 2403 --EYQRDLERLRDAQRKLDRDRDTLRRE-AEMVEQMKKAEAEQ----------AHRTQRTPSSTSEESMKFQSS 2463
Cdd:TIGR02168  360 leELEAELEELESRLEELEEQLETLRSKvAQLELQIASLNNEIerlearlerlEDRRERLQQEIEELLKKLEEA 433

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

2369-2486

3.89e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.89e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2369 LSDREAQVKEQDEETLRRRGQLEEERQELQKRKEEYQRDLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG3883    145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065137183 2449 TPSSTSEESMKFQSSTSLDKEPGGGEAELSSSPATKEP 2486
Cdd:COG3883    225 AAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262

C1_Myosin-IXb

cd20884

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...

1530-1571

4.00e-03

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410434 Cd Length: 58 Bit Score: 37.53 E-value: 4.00e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2065137183 1530 NGHLFSSVNPAPSTTCHQCNKPINTKE-AFLCTNCNAQVHKGC 1571
Cdd:cd20884      4 NGHVFTSYQVNIMQSCEQCSSYIWAMEkALLCSVCKMTCHKKC 46

Smc

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

2327-2443

4.23e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 4.23e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQRSLEKQRQEVANLQRQQAAHA--DERRRR-EREWEVRESGLSDREAQVKEQDEETLRRRGQLEEERQELQKRKEE 2403
Cdd:COG1196    388 LLEALRAAAELAAQLEELEEAEEALLerLERLEEeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2065137183 2404 YQRDLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQA 2443
Cdd:COG1196    468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507

Smc

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

2327-2448

4.26e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 4.26e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2327 EQEKQ-RSLEKQ----------RQEVANLQRQQAAHADERRRREREWEVREsgLSDREAQVKEQDEETLRRRGQLEEERQ 2395
Cdd:COG1196    197 ELERQlEPLERQaekaeryrelKEELKELEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEELRL 274

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065137183 2396 ELQKRKEEYQRDLERLRDAQRKLDRDRDTLRREAEMVEQMKKAEAEQAHRTQR 2448
Cdd:COG1196    275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

YhaN

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

2329-2445

4.38e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 4.38e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2329 EKQRSLEKQRQEVANLQRQQAAHADerrrrerewevresglsDREAQVKEQDEETLRRR-GQLEEERQELQKRKEEYQRD 2407
Cdd:COG4717    392 EQAEEYQELKEELEELEEQLEELLG-----------------ELEELLEALDEEELEEElEELEEELEELEEELEELREE 454

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065137183 2408 LERLRDAQRKLDRDRDTLRREAEmvEQMKKAEAEQAHR 2445
Cdd:COG4717    455 LAELEAELEQLEEDGELAELLQE--LEELKAELRELAE 490

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

2328-2449

4.46e-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: 4.46e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 2328 QEKQRSLEKQRQEVANLQRQQAAHADERRRREREWEVRESGLSDREAQVK--EQDEETLRRR-GQLEEERQELQKRKEEY 2404
Cdd:COG4942     23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAElAELEKEIAELRAELEAQ 102

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2065137183 2405 QRDL-ERLRDAQRKLDRDR-----------DTLRReAEMVEQMKKAEAEQAHRTQRT 2449
Cdd:COG4942    103 KEELaELLRALYRLGRQPPlalllspedflDAVRR-LQYLKYLAPARREQAEELRAD 158

PH_alsin

cd13269

Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...

1974-2075

4.91e-03

Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual specificity for Rac1 and Rab5 GTPases. Alsin mutations in the form of truncated proteins are responsible for motor function disorders including juvenile-onset amyotrophic lateral sclerosis, familial juvenile primary lateral sclerosis, and infantile-onset ascending hereditary spastic paralysis. The alsin protein is widely expressed in the developing CNS including neurons of the cerebral cortex, brain stem, spinal cord, and cerebellum. Alsin contains a regulator of chromosome condensation 1 (RCC1) domain, a Rho guanine nucleotide exchanging factor (RhoGEF) domain, a PH domain, a Membrane Occupation and Recognition Nexus (MORN), a vacuolar protein sorting 9 (Vps9) domain, and a Dbl homology (DH) domain. Alsin interacts with Rab5 through its Vps9 domain and through this interaction modulates early endosome fusion and trafficking. The GEF activity of alsin towards Rab5 is regulated by Rac1 function. The GEF activity of alsin for Rac1 occurs via its DH domain and this interaction plays a role in promoting spinal motor neuron survival via multiple Rac-dependent signaling pathways. 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: 241423 Cd Length: 106 Bit Score: 38.91 E-value: 4.91e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065137183 1974 RRLLHDG---PLQLKNsAGRLKDVQAMLLSDVFVFLQekdqkyvFASldqrSTVISLQKLIVREVANEERGLFLITAGIE 2050
Cdd:cd13269      8 RRLIRESstrPLTLQN-AGRFSSHWFILFNDALVHAQ-------FST----HHIFPLATLWVEPIPDEDSGQNALKITTP 75

                           90       100
                   ....*....|....*....|....*
gi 2065137183 2051 KPEMVeVLASTKEERNTWMQLIQDA 2075
Cdd:cd13269     76 EESFT-LVASTPQEKAEWLRAINQA 99

SMC_prok_B