NCBI Conserved Domain Search

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

2325-2678

2.13e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2325 IQIIQDTINTLNRDEDE---GIPSENEEEKKMLDTRARELKEQLHQKDQKILLLLEEKEMIFRDMAECSTPLpedcspth 2401
Cdd:COG4717   165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-------- 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2402 sprvlFRSNTEEALKGGPLMKSAINEVEILQGLVSGNLGGTLGPTvssPIEQDVVGPVSL----PRRAETFGGfdsHQMN 2477
Cdd:COG4717   237 -----EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA---GVLFLVLGLLALlfllLAREKASLG---KEAE 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2478 ASKGGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSVVHLYELLSALQgvvLQQdsyIEDQKLVLSERA 2557
Cdd:COG4717   306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEA 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2558 LTRSLSRPSSLIEQEKQRslEKQRQDLANLQKQQAQYLEEKRRREREWEARERElrereallaQREEEVQQGQQDLEKER 2637
Cdd:COG4717   380 GVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALDEEELE---------EELEELEEELEELEEEL 448

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 134048676 2638 EELQQKKGTYQYDLERLRAAQK--QLEREQEQLRREAERLSQR 2678
Cdd:COG4717   449 EELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491

DUF5401

pfam17380

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

2541-2684

2.77e-05

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: 49.74 E-value: 2.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2541 QQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRSLEKQRQDLANLQKQQAQyleEKRRREREWEARERELREREALLA 2620
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEE 431

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQ-----KQLEREQEQL-RREAERLSQRQTERDL 2684
Cdd:pfam17380  432 ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRdRKRAEEQRRKILEKEL 501

SMC_prok_B

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

2515-2680

5.58e-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: 5.58e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2515 KRNSEQVVQSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERA--LTRSLSRPSSLIEqEKQRSLEKQRQDLANLQKQQA 2592
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeeLQKELYALANEIS-RLEQQKQILRERLANLERQLE 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2593 QYLEEKRRREREWEARERELREREALLAQREEEVQQGQQDLEKEREELQ---QKKGTYQYDLERLRAAQKQLEREQEQLR 2669
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLN 399

                          170
                   ....*....|.
gi 134048676  2670 REAERLSQRQT 2680
Cdd:TIGR02168  400 NEIERLEARLE 410

PRK12704

phosphodiesterase; Provisional

2621-2681

9.75e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 9.75e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTE 2681
Cdd:PRK12704   93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153

ATP-synt_Fo_b

cd06503

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...

2621-2682

1.03e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.

Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.65 E-value: 1.03e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRA--------AQKQLEREQEQLRREAERLSQRQTER 2682
Cdd:cd06503    30 EREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAeaqeiieeARKEAEKIKEEILAEAKEEAERILEQ 99

smart00109

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

1792-1838

2.29e-03

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: 38.22 E-value: 2.29e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 134048676   1792 HTFSSIPVVGPISCSQCMKP--FTNKDAYTCANCSAFVHKGCRESLAS-C 1838
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

2621-2684

3.71e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.26 E-value: 3.71e-03

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134048676   2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQ-LEREQEQLRREAERLsQRQTERDL 2684
Cdd:smart00935   22 QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRK-QQKLQQDL 85

Name

Accession

Description

Interval

E-value

PH_AKAP13

cd13392

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

2232-2334

8.96e-64

Pssm-ID: 275427 Cd Length: 103 Bit Score: 212.46 E-value: 8.96e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2232 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMTDPEMV 2311
Cdd:cd13392     1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80

                          90       100
                  ....*....|....*....|...
gi 134048676 2312 EVHASSKEERNSWIQIIQDTINT 2334
Cdd:cd13392    81 EVHASSKEERNSWMQIIQDTINT 103

PH_16

pfam17838

PH domain;

2216-2333

1.08e-52

PH domain;

Pssm-ID: 436083 Cd Length: 127 Bit Score: 181.45 E-value: 1.08e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2216 MKSGQMFAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASL-------DQK--STVISLKKL 2286
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 134048676  2287 IVREVAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTIN 2333
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127

RhoGEF

cd00160

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

1995-2189

3.22e-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: 3.22e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 1995 RQEVIYELMQTEFHHVRTLKIMSGVYSQGMMADLL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSeknfl 2073
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2074 ikRIGDVLVNQFSgenaerLKKTYGKFCGQHNQSVNYFKDLYAKDKRFQAFVKKKMSSSvvRRLGIPECILLVTQRITKY 2153
Cdd:cd00160    76 --RIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 134048676 2154 PVLFQRILQCTKDNEVEQEDLAQSLSLVKDVIGAVD 2189
Cdd:cd00160   146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181

RhoGEF

smart00325

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

1998-2189

1.03e-45

Pssm-ID: 214619 [Multi-domain] Cd Length: 180 Bit Score: 163.63 E-value: 1.03e-45

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676   1998 VIYELMQTEFHHVRTLKIMSGVYSQGMMADL-LFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKseknfliKR 2076
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELkLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV-------ER 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676   2077 IGDVLVNQfsgenaERLKKTYGKFCGQHNQSVNYFKDLyAKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVL 2156
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146

                           170       180       190
                    ....*....|....*....|....*....|...
gi 134048676   2157 FQRILQCTKDNEVEQEDLAQSLSLVKDVIGAVD 2189
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179

PH_p190RhoGEF

cd14680

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

2232-2332

5.63e-44

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: 155.54 E-value: 5.63e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2232 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMTDPEMV 2311
Cdd:cd14680     1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMY 80

                          90       100
                  ....*....|....*....|.
gi 134048676 2312 EVHASSKEERNSWIQIIQDTI 2332
Cdd:cd14680    81 EIHTSSKEERNNWMRLIQEAV 101

PH_ARHGEF18

cd15794

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

2229-2348

8.47e-44

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: 155.83 E-value: 8.47e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2229 RKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMTDP 2308
Cdd:cd15794     1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 134048676 2309 EMVEVHASSKEERNSWIQIIQDTINTLNrDEDEGIPSENE 2348
Cdd:cd15794    81 EMYEIHTNSKEDRNTWMAHIRRAVESCP-DEEEGLFSEPE 119

PH_ARHGEF2

cd13393

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

2229-2340

9.69e-42

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: 149.65 E-value: 9.69e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2229 RKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDqKSTVISLKKLIVREVAHEEKGLFLISmgMTDP 2308
Cdd:cd13393     1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLIS--AAPP 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 134048676 2309 EMVEVHASSKEERNSWIQIIQDTINTLNRDED 2340
Cdd:cd13393    78 EMYEVHAASRDDRNTWMRLIQQTVKTCPSREE 109

PH_RhoGEF

cd13329

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

2232-2332

4.77e-41

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: 147.41 E-value: 4.77e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2232 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYI--------FASLDQKSTVISLKKLIVREVAHEEKGLFLISM 2303
Cdd:cd13329     1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80

                          90       100
                  ....*....|....*....|....*....
gi 134048676 2304 GMTDPEMVEVHASSKEERNSWIQIIQDTI 2332
Cdd:cd13329    81 SKNGPQMYELVANSSSERKTWIKHISDAV 109

RhoGEF

pfam00621

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

1998-2189

1.22e-35

Pssm-ID: 459876 [Multi-domain] Cd Length: 176 Bit Score: 134.73 E-value: 1.22e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  1998 VIYELMQTEFHHVRTLKIMSGVYSQGMMADLLFEQQMVEKLFPCLDELISIHSQFFqrilerkkesLVDKSEKNFLIKRI 2077
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL----------LEELLKEWISIQRI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2078 GDVLVNQFSGenaerlKKTYGKFCGQHNQSVNYFKDLYAKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLF 2157
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144

                          170       180       190
                   ....*....|....*....|....*....|..
gi 134048676  2158 QRILQCTKDNEVEQEDLAQSLSLVKDVIGAVD 2189
Cdd:pfam00621  145 KELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176

C1_AKAP13

cd20878

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

1788-1844

3.13e-32

Pssm-ID: 410428 Cd Length: 60 Bit Score: 120.52 E-value: 3.13e-32

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 134048676 1788 TVNGHTFSSIPVVGPISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCAKVKMK 1844
Cdd:cd20878     4 TLNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60

PH_ARHGEF2_18_like

cd15789

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

2232-2329

5.85e-29

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: 112.94 E-value: 5.85e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2232 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISmgMTDPEMV 2311
Cdd:cd15789     1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLIS--ASPDGMP 78

                          90       100
                  ....*....|....*....|.
gi 134048676 2312 EVHASSKE---ERNSWIQIIQ 2329
Cdd:cd15789    79 EMYELKVQkpkDKNTWIQTIR 99

C1_p190RhoGEF-like

cd20815

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

1790-1841

2.84e-18

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: 80.54 E-value: 2.84e-18

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 134048676 1790 NGHTFSSIPVVGPISCSQCMKPFTNKDAYTCANCSAFVHK-GCRESLASCAKV 1841
Cdd:cd20815     2 NTHQFVPVSFSNSTKCDVCSKPLTNKPALQCENCSVNVHDsSCKDQLADCTKF 54

C1_p190RhoGEF

cd20876

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

1789-1847

9.87e-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: 67.85 E-value: 9.87e-14

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 134048676 1789 VNGHTFSSIPVVGPISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCakVKMKQPK 1847
Cdd:cd20876     5 SNGHQFVTGSFSGPTLCVVCDKPVTGKELLQCSNCTVNVHKGCKESAPPC--TKKLQDK 61

C1_ARHGEF2

cd20877

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

1790-1847

1.57e-12

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: 64.60 E-value: 1.57e-12

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 134048676 1790 NGHTFSSIPVVGPISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCAKVKMKQPK 1847
Cdd:cd20877     4 NGHLFTTITVSGTTMCSACNKSITAKEALICPTCNVTIHNRCKDTLPNCTKVKQKQQK 61

PH_PRG

cd13391

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

2222-2333

2.99e-12

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: 66.59 E-value: 2.99e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2222 FAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIF--------ASLDQKST---VISLKKLIVRE 2290
Cdd:cd13391    18 FKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSDSKQTfspVLKLNSVLIRS 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 134048676 2291 VAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTIN 2333
Cdd:cd13391    98 VATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAVR 140

PH_LARG

cd13390

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

2226-2328

4.19e-12

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: 65.78 E-value: 4.19e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2226 DLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIF--------ASLDQKST---VISLKKLIVREVAHE 2294
Cdd:cd13390    20 DLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKHTfspVIKLNTVLVRQVATD 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 134048676 2295 EKGLFLISMGMTDPEMVEVHASSKEERNSWIQII 2328
Cdd:cd13390   100 NKAFFVISMSENGAQIYELVAQTVSEKTVWQDLI 133

PH_p115RhoGEF

cd14679

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

2222-2335

2.43e-11

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: 63.32 E-value: 2.43e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2222 FAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKY--------IFASLDQK---STVISLKKLIVRE 2290
Cdd:cd14679     1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLvlkchsrtTTPTPDGKqmlSPIIKLNSAMTRE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 134048676 2291 VAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTINTL 2335
Cdd:cd14679    81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125

C1_ARHGEF18-like

cd20879

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

1789-1839

8.49e-09

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: 53.66 E-value: 8.49e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 134048676 1789 VNGH-----TFSSIpvvgpISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCA 1839
Cdd:cd20879     1 VNGHqlvpgTFSSC-----ATCSLCSKPLQNRNGLQCLNCAVNVHKNCKTLLTECS 51

smart00233

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

2232-2333

4.41e-08

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 53.32 E-value: 4.41e-08

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676   2232 LVRDGSVFLK--NAAGRLKEVQAVLLTDILVFLQEKDQKYIFAsldqKSTVISLKKLIVREVAH----EEKGLFLISMGm 2305
Cdd:smart00233    1 VIKEGWLYKKsgGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK----PKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75

                            90       100
                    ....*....|....*....|....*...
gi 134048676   2306 tDPEMVEVHASSKEERNSWIQIIQDTIN 2333
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102

C1_dGM13116p-like

cd20831

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

1789-1840

3.91e-07

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: 49.26 E-value: 3.91e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 134048676 1789 VNGHTFSSIPVVGPISCSQCMKPFT---NKDAYTCANCSAFVHKGCRESLAS-CAK 1840
Cdd:cd20831     3 YNDHTFVATHFKGGPSCAVCNKLIPgrfGKQGYQCRDCGLICHKRCHVKVEThCPS 58

pfam00169

PH domain; PH stands for pleckstrin homology.

2232-2332

2.43e-06

PH domain; PH stands for pleckstrin homology.

Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 48.33 E-value: 2.43e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2232 LVRDGSVFLK--NAAGRLKEVQAVLLTDILVFLQEKDQKyifaSLDQKSTVISLKKLIVREVAHEEKG----LFLISMGM 2305
Cdd:pfam00169    1 VVKEGWLLKKggGKKKSWKKRYFVLFDGSLLYYKDDKSG----KSKEPKGSISLSGCEVVEVVASDSPkrkfCFELRTGE 76

                           90       100
                   ....*....|....*....|....*...
gi 134048676  2306 TDP-EMVEVHASSKEERNSWIQIIQDTI 2332
Cdd:pfam00169   77 RTGkRTYLLQAESEEERKDWIKAIQSAI 104

C1_MgcRacGAP

cd20821

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

1792-1835

3.71e-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: 46.24 E-value: 3.71e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 134048676 1792 HTFSSIPVVGPISCSQCMKPFT-NKDAYTCANCSAFVHKGCRESL 1835
Cdd:cd20821     3 HRFVSKTVIKPETCVVCGKRIKfGKKALKCKDCRVVCHPDCKDKL 47

cd00029

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

1792-1838

4.89e-06

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: 45.59 E-value: 4.89e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 134048676 1792 HTFSSIPVVGPISCSQCMKPFTN--KDAYTCANCSAFVHKGCRESLAS-C 1838
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGlfKQGLKCSDCGLVCHKKCLDKAPSpC 50

ROM1

COG5422

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

1963-2267

1.74e-05

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

Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 50.66 E-value: 1.74e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 1963 DFEIESKQLEAESWSRIIDSKFLKQQkkdvVKRQEVIYELMQTEFHHVRTLKIMSGVYSQGMMADLLF----EQQMVEKL 2038
Cdd:COG5422   457 DKFDEEKNLWTLSVPKEVWESLPKQE----IKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHV 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2039 FPCLDELISIHSQFfqrilerkKESLVDKSEKNFLIKRIGDV------LVNQFSGENAERLkktYGKFCGQHNQSVNYfk 2112
Cdd:COG5422   533 FANINEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP-- 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2113 dlyakdkRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLAQSLSLVKDVIGAVDSKV 2192
Cdd:COG5422   600 -------NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFES 672

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134048676 2193 ASYEKKVRLNEIYTKTDSKSiMRMKSGQMFAKEDLKRKKLVRDGSVfLKNAAGRLKEVQAVLLTDILVFLQEKDQ 2267
Cdd:COG5422   673 GKAENRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAK-SKTDGSLRGDIQFFLLDNMLLFCKAKAV 745

YhaN

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

2325-2678

2.13e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2325 IQIIQDTINTLNRDEDE---GIPSENEEEKKMLDTRARELKEQLHQKDQKILLLLEEKEMIFRDMAECSTPLpedcspth 2401
Cdd:COG4717   165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-------- 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2402 sprvlFRSNTEEALKGGPLMKSAINEVEILQGLVSGNLGGTLGPTvssPIEQDVVGPVSL----PRRAETFGGfdsHQMN 2477
Cdd:COG4717   237 -----EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA---GVLFLVLGLLALlfllLAREKASLG---KEAE 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2478 ASKGGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSVVHLYELLSALQgvvLQQdsyIEDQKLVLSERA 2557
Cdd:COG4717   306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEA 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2558 LTRSLSRPSSLIEQEKQRslEKQRQDLANLQKQQAQYLEEKRRREREWEARERElrereallaQREEEVQQGQQDLEKER 2637
Cdd:COG4717   380 GVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALDEEELE---------EELEELEEELEELEEEL 448

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 134048676 2638 EELQQKKGTYQYDLERLRAAQK--QLEREQEQLRREAERLSQR 2678
Cdd:COG4717   449 EELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491

DUF5401

pfam17380

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

2541-2684

2.77e-05

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: 49.74 E-value: 2.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2541 QQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRSLEKQRQDLANLQKQQAQyleEKRRREREWEARERELREREALLA 2620
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEE 431

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQ-----KQLEREQEQL-RREAERLSQRQTERDL 2684
Cdd:pfam17380  432 ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRdRKRAEEQRRKILEKEL 501

SMC_prok_B

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

2515-2680

5.58e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 5.58e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2515 KRNSEQVVQSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERA--LTRSLSRPSSLIEqEKQRSLEKQRQDLANLQKQQA 2592
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeeLQKELYALANEIS-RLEQQKQILRERLANLERQLE 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2593 QYLEEKRRREREWEARERELREREALLAQREEEVQQGQQDLEKEREELQ---QKKGTYQYDLERLRAAQKQLEREQEQLR 2669
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLN 399

                          170
                   ....*....|.
gi 134048676  2670 REAERLSQRQT 2680
Cdd:TIGR02168  400 NEIERLEARLE 410

SMC_prok_B

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

2530-2688

8.29e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 8.29e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2530 ELLSALQGVVLQQDSYIED---QKLVLSER--ALTRSLSRPSSLIEQEKQRsLEKQRQDLANLQKQQAQyleeKRRRERE 2604
Cdd:TIGR02168  281 EEIEELQKELYALANEISRleqQKQILRERlaNLERQLEELEAQLEELESK-LDELAEELAELEEKLEE----LKEELES 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2605 WEARERELREREALLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERDL 2684
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435


                   ....
gi 134048676  2685 CQVS 2688
Cdd:TIGR02168  436 KELQ 439

ZapB

COG3074

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...

2621-2681

9.12e-05

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 43.04 E-value: 9.12e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134048676 2621 QREEEVQQGQ---QDLEKEREELQQKKgtyqydlERLRAAQKQLEREQEQLRREAERLSQRQTE 2681
Cdd:COG3074     8 ELEAKVQQAVdtiELLQMEVEELKEKN-------EELEQENEELQSENEELQSENEQLKTENAE 64

OmpH

pfam03938

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

2621-2681

1.47e-04

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 44.10 E-value: 1.47e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134048676  2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTE 2681
Cdd:pfam03938   23 QLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQ 83

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

2571-2683

1.91e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2571 QEKQRSLEKQRQDLANLQKQQAQyleekrrrerewearerelreREALLAQREEEVQQGQQDLEKEREEL---QQKKGTY 2647
Cdd:COG4372    55 EQAREELEQLEEELEQARSELEQ---------------------LEEELEELNEQLQAAQAELAQAQEELeslQEEAEEL 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 134048676 2648 QYDLERLRAAQKQLEREQEQLRREAERLSQRQTERD 2683
Cdd:COG4372   114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149

Smc

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

2540-2683

2.71e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 2.71e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2540 LQQDSYIEDQKL--VLSERALTRSLSRPSSLIEQEKQRSLEKQRQDLANLQKQQAQyleeKRRREREWEARERELREREA 2617
Cdd:COG1196   286 AQAEEYELLAELarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE----LEEELEEAEEELEEAEAELA 361

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134048676 2618 LLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERD 2683
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

Zwint

pfam15556

ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ...

2622-2688

4.06e-04

ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are typically between 127 and 281 amino acids in length.

Pssm-ID: 464766 [Multi-domain] Cd Length: 252 Bit Score: 44.58 E-value: 4.06e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134048676  2622 REEEVQQGQQDLEKEREELQQKKgtyQYDLERLRAAQKQLEREQEQ-LRREAE-----RLSQRQTERDLCQVS 2688
Cdd:pfam15556   92 KMEEAQRKRAQLQEALEQLQAKK---QMAMEKLRTAQKQWQLQQEKhLQHLAEvsaevRERQTGTQQELERLY 161

EnvC

COG4942

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

2528-2677

4.55e-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: 45.14 E-value: 4.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2528 LYELLSALQgvVLQQDSYIedqKLVLSERALTRSLSRPSSL--IEQEKQRSLEKQRQDLANLQKQQAQyleekrrrerew 2605
Cdd:COG4942   106 LAELLRALY--RLGRQPPL---ALLLSPEDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALRAE------------ 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134048676 2606 earerelrerealLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQ 2677
Cdd:COG4942   169 -------------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

Smc

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

2547-2682

4.89e-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: 4.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2547 EDQKLVLSERALTRSLSRPSSLI--EQEKQRSLEKQRQDLANLQKQQAQYLEEKRRREREWEARERELREREALLAQREE 2624
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 134048676 2625 EVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTER 2682
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

C1_nPKC_epsilon-like_rpt1

cd20835

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...

1789-1842

7.09e-04

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first 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: 410385 Cd Length: 64 Bit Score: 40.14 E-value: 7.09e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 134048676 1789 VNGHTFSSIPVVGPISCSQCmKPFT----NKDAYTCANCSAFVHKGCRESLAS-CAKVK 1842
Cdd:cd20835     7 VNGHKFMATYLRQPTYCSHC-KDFIwgviGKQGYQCQVCTCVVHKRCHQLVVTkCPGNK 64

YhaN

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

2560-2683

8.38e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 8.38e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2560 RSLSRPSSLIEQEKQRSLEKQRQDLANLQKQQAQYLEEKRRREREWEARERELREREALLAQREE-EVQQGQQDLEKERE 2638
Cdd:COG4717    56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELE 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 134048676 2639 ELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERD 2683
Cdd:COG4717   136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180

Smc

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

2621-2683

9.68e-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: 9.68e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKgtyQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERD 2683
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDI---ARLEERRRELEERLEELEEELAELEEELEELEEELE 340

PRK12704

phosphodiesterase; Provisional

2621-2681

9.75e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 9.75e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTE 2681
Cdd:PRK12704   93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153

Smc

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

2528-2683

1.01e-03

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: 1.01e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2528 LYELLSALQGvvLQQDSYIEDQKLVLSERALTRSLSRpssliEQEKQRSLEKQRQDLANLQKQQAQYLEEKRRREREWEA 2607
Cdd:COG1196   290 EYELLAELAR--LEQDIARLEERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134048676 2608 RERELREREALLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERD 2683
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438

ATP-synt_Fo_b

cd06503

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...

2621-2682

1.03e-03

Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.65 E-value: 1.03e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRA--------AQKQLEREQEQLRREAERLSQRQTER 2682
Cdd:cd06503    30 EREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAeaqeiieeARKEAEKIKEEILAEAKEEAERILEQ 99

YhaN

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

2530-2678

1.28e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2530 ELLSALQGVVLQQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRsLEKQRQDLANLQKQQA--QYLEEKRRREREWEA 2607
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEAleAELAELPERLEELEE 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134048676 2608 RERELREREALLAQREEEVQQGQQDLEKEREELQQKK----GTYQYDLERLRAAQKQLEREQEQLRREAERLSQR 2678
Cdd:COG4717   154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

GumC

COG3206

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

2507-2681

1.59e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.59e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2507 NANLVFMLKRNSEQVVQSVVHLYELLSALQGVVLQQDSYIE--DQKLVLSERALTRSLSRP------SSLIEQEKQRSLE 2578
Cdd:COG3206   203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPviqqlrAQLAELEAELAEL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2579 KQR-----QDLANLQKQQAQYLEekrrrerewearerelrereallaQREEEVQQGQQDLEKEREELQQKKGTYQYDLER 2653
Cdd:COG3206   283 SARytpnhPDVIALRAQIAALRA------------------------QLQQEAQRILASLEAELEALQAREASLQAQLAQ 338

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 134048676 2654 LRAAQKQL---EREQEQLRREAER-------LSQRQTE 2681
Cdd:COG3206   339 LEARLAELpelEAELRRLEREVEVarelyesLLQRLEE 376

FliJ

pfam02050

Flagellar FliJ protein;

2571-2680

1.61e-03

Flagellar FliJ protein;

Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 40.73 E-value: 1.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676  2571 QEKQRSLEKQRQDLANLQKQQAQYLEEKRRREREWEAREREL-----REREALLAQREEEVQQGQQDLEKEREELQQKKg 2645
Cdd:pfam02050    8 AEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAELRNyqafiSQLDEAIAQQQQELAQAEAQVEKAREEWQEAR- 86

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 134048676  2646 tyqydlERLRAAQKQLEREQEQLRREAERLSQRQT 2680
Cdd:pfam02050   87 ------QERKSLEKLREREKKEERKEQNRREQKQL 115

Smc

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

2528-2683

1.72e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.72e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2528 LYELLSALQGVVLQQDSYIED-QKLVLSERALTRSLSRPSSLIEQEKQRsLEKQRQDLANLQKQQAQYLEEKRRREREWE 2606
Cdd:COG1196   227 AELLLLKLRELEAELEELEAElEELEAELEELEAELAELEAELEELRLE-LEELELELEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134048676 2607 ARERELREREALLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERD 2683
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

C1_VAV

cd20810

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

1792-1838

1.88e-03

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: 38.39 E-value: 1.88e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 134048676 1792 HTFSSipvvgPISCSQCMK----PFtnKDAYTCANCSAFVHKGCRESLASC 1838
Cdd:cd20810     8 TTFKE-----PTTCSVCKKllkgLF--FQGYKCSVCGAAVHKECIAKVKRC 51

mukB

PRK04863

chromosome partition protein MukB;

2572-2681

2.24e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 2.24e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2572 EKQRSLEKQRQDLAnlQKQQAQYleekrrrerewearerelrereallaQREEEVQQGQQDLEKEREELQQKKgtyqydl 2651
Cdd:PRK04863  530 RQQQRAERLLAEFC--KRLGKNL--------------------------DDEDELEQLQEELEARLESLSESV------- 574

                          90       100       110
                  ....*....|....*....|....*....|
gi 134048676 2652 ERLRAAQKQLEREQEQLRREAERLSQRQTE 2681
Cdd:PRK04863  575 SEARERRMALRQQLEQLQARIQRLAARAPA 604

smart00109

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

1792-1838

2.29e-03

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: 38.22 E-value: 2.29e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 134048676   1792 HTFSSIPVVGPISCSQCMKP--FTNKDAYTCANCSAFVHKGCRESLAS-C 1838
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50

YqiK

COG2268

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];

2621-2682

2.34e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];

Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 2.34e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKgtyqyDLERLRAAQKQ--LEREQEQLRREAERlSQRQTER 2682
Cdd:COG2268   209 ERETEIAIAQANREAEEAELEQER-----EIETARIAEAEaeLAKKKAEERREAET-ARAEAEA 266

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

2621-2686

2.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.46e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKgtyqydlERLRAAQKQLEREQEQLRREAERLSQRQTERDLCQ 2686
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQLE-------EELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

ADIP

pfam11559

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...

2626-2696

2.47e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.

Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.76 E-value: 2.47e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134048676  2626 VQQGQQDLEkEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAErlSQRQTERDL-CQVSHPHTKLMR 2696
Cdd:pfam11559   44 LQQRDRDLE-FRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELA--LLQAKERQLeKKLKTLEQKLKN 112

OmpH

pfam03938

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

2621-2681

2.65e-03

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 2.65e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134048676  2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAER-LSQRQTE 2681
Cdd:pfam03938   30 KRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQeLQKKQQE 91

YhaN

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

2631-2686

2.92e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 2.92e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 134048676 2631 QDLEKEREELQQKKGTY---QYDLERLRAAQKQLEREQEQLRREAERLSQRQTERDLCQ 2686
Cdd:COG4717    74 KELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132

COG4913

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

2621-2681

3.13e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.13e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKGtyqydleRLRAAQKQLEREQEQLRREAERLSQRQTE 2681
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLEAAEDLARL 745

COG4913

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

2523-2681

3.27e-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: 3.27e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2523 QSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERALTRSLSRPSSLIEQ--EKQRSLEKQRQDLANLQKQQAQyleekrr 2600
Cdd:COG4913   262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEleRLEARLDALREELDELEAQIRG------- 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2601 rerewearerelrereaLLAQREEEVQQGQQDLEKEREELQQKKGTYQ-----------YDLERLRAAQKQLEREQEQLR 2669
Cdd:COG4913   335 -----------------NGGDRLEQLEREIERLERELEERERRRARLEallaalglplpASAEEFAALRAEAAALLEALE 397

                         170
                  ....*....|..
gi 134048676 2670 REAERLSQRQTE 2681
Cdd:COG4913   398 EELEALEEALAE 409

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

2621-2684

3.71e-03

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.26 E-value: 3.71e-03

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134048676   2621 QREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQ-LEREQEQLRREAERLsQRQTERDL 2684
Cdd:smart00935   22 QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRK-QQKLQQDL 85

AtpF

COG0711

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...

2621-2682

4.92e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase

Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.16 E-value: 4.92e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134048676 2621 QREEEVQQGQQDLEKEREELQQKKGTYQydlERLRAAQKQLEREQEQLRREAERLSQRQTER 2682
Cdd:COG0711    31 ERQEKIADGLAEAERAKEEAEAALAEYE---EKLAEARAEAAEIIAEARKEAEAIAEEAKAE 89

YscO

pfam07321

Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...

2621-2684

5.51e-03

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.

Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 39.69 E-value: 5.51e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134048676  2621 QREEEVQQGQQDLEKEREELQQKkgtyqydLERLRAAQKQLER---EQEQLRREAERLSQRQTERDL 2684
Cdd:pfam07321   84 DLEKQVAEARQQLEAEREALRQA-------RQALAEARRAVEKfaeLVRLVQAEELRQQERQEEQEL 143

EnvC

COG4942

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

2571-2678

5.73e-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: 41.67 E-value: 5.73e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2571 QEKQRSLEKQRQDLANLQKQQAQyleekrrrerewearerelrereallaqREEEVQQGQQDLEKEREELQQKKGTYQYD 2650
Cdd:COG4942   163 AALRAELEAERAELEALLAELEE----------------------------ERAALEALKAERQKLLARLEKELAELAAE 214

                          90       100
                  ....*....|....*....|....*...
gi 134048676 2651 LERLRAAQKQLEREQEQLRREAERLSQR 2678
Cdd:COG4942   215 LAELQQEAEELEALIARLEAEAAAAAER 242

Smc

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

2514-2682

5.79e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 5.79e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2514 LKRNSEQVVQSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRSLEKQRQDLANLQKQQAQ 2593
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134048676 2594 yleekrrrerewearereLREREALLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAE 2673
Cdd:COG1196   398 ------------------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459


                  ....*....
gi 134048676 2674 RLSQRQTER 2682
Cdd:COG1196   460 ALLELLAEL 468

C1_ScPKC1-like_rpt1

cd20822

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...

1790-1838

5.99e-03

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first 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: 410372 Cd Length: 52 Bit Score: 37.27 E-value: 5.99e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 134048676 1790 NGHTFSSIPVVGPISCSQCMKPFTNKdAYTCANCSAFVHKGCRE-SLASC 1838
Cdd:cd20822     1 RGHKFVQKQFYQIMRCAVCGEFLVNA-GYQCEDCKYTCHKKCYEkVVTKC 49

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

2634-2681

6.60e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 6.60e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 134048676  2634 EKEREELQQKKGTYQYDLER----LRAAQ---KQLEREQEQLRREAERLSQRQTE 2681
Cdd:pfam20492    5 EREKQELEERLKQYEEETKKaqeeLEESEetaEELEEERRQAEEEAERLEQKRQE 59

SMC_prok_B