NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958643792|ref|XP_038961495|]
View 

A-kinase anchor protein 13 isoform X11 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PH_AKAP13 cd13392
A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...
2170-2272 8.26e-62

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity of AKAP13 (also called Brx-1, AKAP-Lbc, and proto-Lbc) mediates signaling downstream of G-protein coupled receptors and Toll-like receptor 2. It plays a role in cell growth, cell development and actin fiber formation. Protein kinase A (PKA) binds and phosphorylates AKAP13, regulating its Rho-GEF activity. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, Brx) containing a dbl oncogene homology (DH) domain and PH domain which are required for full transforming activity. The DH domain is associated with guanine nucleotide exchange activation while the PH domain has multiple functions including determine protein sub-cellular localisation via phosphoinositide interactions, while others bind protein partners. Other ligands include protein kinase C which is bound by the PH domain of AKAP13, serving to activate protein kinase D and mobilize a cardiac hypertrophy signaling pathway. 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: 275427  Cd Length: 103  Bit Score: 206.68  E-value: 8.26e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 2249
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80
                           90       100
                   ....*....|....*....|...
gi 1958643792 2250 EVHASSREERNSWIQIIQDTINS 2272
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1933-2127 1.66e-48

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: 171.71  E-value: 1.66e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1933 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSeknfl 2011
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2012 ikRIGDVLVsqfsgeNAERLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSvvRRLGIPECILLVTQRITKY 2091
Cdd:cd00160     76 --RIGDVFL------KLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958643792 2092 PVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
C1_AKAP13 cd20878
protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...
1729-1784 1.03e-29

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) and similar proteins; AKAP-13, also called AKAP-Lbc, breast cancer nuclear receptor-binding auxiliary protein (Brx-1), guanine nucleotide exchange factor Lbc, human thyroid-anchoring protein 31, lymphoid blast crisis oncogene (LBC oncogene), non-oncogenic Rho GTPase-specific GTP exchange factor, protein kinase A-anchoring protein 13 (PRKA13), or p47, is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors (GPCRs). It activates RhoA in response to GPCR signaling via its function as a 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. Its Rho-GEF activity is regulated by protein kinase A (PKA), through binding and phosphorylation. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, and Brx) that contain a C1 domain followed by a dbl oncogene homology (DH) domain and a PH domain which are required for full transforming activity. 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: 410428  Cd Length: 60  Bit Score: 113.21  E-value: 1.03e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958643792 1729 LNGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCAKVKMK 1784
Cdd:cd20878      5 LNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2263-2625 2.68e-06

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2263 IQIIQDTINSLNRDEDE---GIPSENEEEKRLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTplpedcspth 2339
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN---------- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2340 sprMLFRSNTEEALKGGPLMKSAISEVEILQGLVSGSLGGTLGQPISSPVEQEVMAGPISLPRRAETFGGfdcHQLNASK 2419
Cdd:COG4717    235 ---ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2420 GGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSIVHLHELLTMLQgvvLQQdsyIEDQKLVLTEKVLTR 2499
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEAGVE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2500 SASRPSSLIEQEKQRslEKQRQDLANLQKQQAQHLEEKRRREREWEarelelrdrEAKLAEREETVRRRQQDLERDREEL 2579
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958643792 2580 QQKKGtyqcdleRLRAAQKQLER---------EQEQLKRDAEQLSQRQMEQDLCQ 2625
Cdd:COG4717    452 REELA-------ELEAELEQLEEdgelaellqELEELKAELRELAEEWAALKLAL 499
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
545-837 5.16e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  545 PEEIPTGKPGMETQERGCEGGiTSDQSSQVLPAAAAATENKVLDGLELETLPACPCETASSLDLTVSGPRPDGMPKQNSE 624
Cdd:PHA03307    67 PPTGPPPGPGTEAPANESRST-PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPG 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  625 SSAQHAQSLNSQAPLCSIAGAGTPS----AESACPQSTETSSGGSVI-------EHGSGEASLPESTAAQPEPqglCTAP 693
Cdd:PHA03307   146 PPPAASPPAAGASPAAVASDAASSRqaalPLSSPEETARAPSSPPAEpppstppAAASPRPPRRSSPISASAS---SPAP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  694 CPEDPQAD--TVTSDTAAHNQKSV---GSCHLCALDAKNQEKDLRQ-DTPSVNTLEDVPHLPSVVPQSEEKLEPDQVSPR 767
Cdd:PHA03307   223 APGRSAADdaGASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRiWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792  768 GSSFSLASSP---ESESVTKDDVLSLVSSQKEK-----GTATPQLHRAPACSDGPDGRDLNDTDKVGDGAASPPTPSA 837
Cdd:PHA03307   303 PGSGPAPSSPrasSSSSSSRESSSSSTSSSSESsrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAA 380
 
Name Accession Description Interval E-value
PH_AKAP13 cd13392
A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...
2170-2272 8.26e-62

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity of AKAP13 (also called Brx-1, AKAP-Lbc, and proto-Lbc) mediates signaling downstream of G-protein coupled receptors and Toll-like receptor 2. It plays a role in cell growth, cell development and actin fiber formation. Protein kinase A (PKA) binds and phosphorylates AKAP13, regulating its Rho-GEF activity. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, Brx) containing a dbl oncogene homology (DH) domain and PH domain which are required for full transforming activity. The DH domain is associated with guanine nucleotide exchange activation while the PH domain has multiple functions including determine protein sub-cellular localisation via phosphoinositide interactions, while others bind protein partners. Other ligands include protein kinase C which is bound by the PH domain of AKAP13, serving to activate protein kinase D and mobilize a cardiac hypertrophy signaling pathway. 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: 275427  Cd Length: 103  Bit Score: 206.68  E-value: 8.26e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 2249
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80
                           90       100
                   ....*....|....*....|...
gi 1958643792 2250 EVHASSREERNSWIQIIQDTINS 2272
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103
PH_16 pfam17838
PH domain;
2154-2271 3.75e-51

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 177.21  E-value: 3.75e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2154 MKSGQMFAKEDLRRKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASL-------DHK--STVISLKKL 2224
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958643792 2225 IVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 2271
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1933-2127 1.66e-48

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: 171.71  E-value: 1.66e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1933 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSeknfl 2011
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2012 ikRIGDVLVsqfsgeNAERLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSvvRRLGIPECILLVTQRITKY 2091
Cdd:cd00160     76 --RIGDVFL------KLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958643792 2092 PVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1936-2127 8.88e-45

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


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 160.93  E-value: 8.88e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  1936 VIYELMQTELHHIRTLKIMSDVYSRGM-MTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKseknfliKR 2014
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV-------ER 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  2015 IGDVLVSQfsgenaERLKKTYGKFCGQHNQSVNYFKDLyTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVL 2094
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146
                           170       180       190
                    ....*....|....*....|....*....|...
gi 1958643792  2095 FQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1936-2127 1.42e-35

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 134.35  E-value: 1.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1936 VIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFqrilerkkesLVDKSEKNFLIKRI 2015
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL----------LEELLKEWISIQRI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2016 GDVLVSQFSGenaerlKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLF 2095
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958643792 2096 QRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
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) ...
1729-1784 1.03e-29

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) and similar proteins; AKAP-13, also called AKAP-Lbc, breast cancer nuclear receptor-binding auxiliary protein (Brx-1), guanine nucleotide exchange factor Lbc, human thyroid-anchoring protein 31, lymphoid blast crisis oncogene (LBC oncogene), non-oncogenic Rho GTPase-specific GTP exchange factor, protein kinase A-anchoring protein 13 (PRKA13), or p47, is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors (GPCRs). It activates RhoA in response to GPCR signaling via its function as a 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. Its Rho-GEF activity is regulated by protein kinase A (PKA), through binding and phosphorylation. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, and Brx) that contain a C1 domain followed by a dbl oncogene homology (DH) domain and a PH domain which are required for full transforming activity. 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: 410428  Cd Length: 60  Bit Score: 113.21  E-value: 1.03e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958643792 1729 LNGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCAKVKMK 1784
Cdd:cd20878      5 LNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2170-2271 2.14e-08

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


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 54.09  E-value: 2.14e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  2170 LVRDGSVFLKSATGRL--KEVQAVLLTDILVFLQEKDQKYVFasldHKSTVISLKKLIVREVAH----EEKGLFLISMGv 2243
Cdd:smart00233    1 VIKEGWLYKKSGGGKKswKKRYFVLFNSTLLYYKSKKDKKSY----KPKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75
                            90       100
                    ....*....|....*....|....*...
gi 1958643792  2244 kDPEMVEVHASSREERNSWIQIIQDTIN 2271
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1905-2205 2.53e-06

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 53.36  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1905 DSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLF----EQQMVEKLFPCL 1980
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHVFANI 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1981 DELISIHSQFfqrilerkKESLVDKSEKNFLIKRIGDV------LVSQFSGENAERLkktYGKFCGQHNQSVNYfkdlyt 2054
Cdd:COG5422    537 NEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP------ 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2055 kdkRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYE 2134
Cdd:COG5422    600 ---NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAE 676
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958643792 2135 KKVRLGEIYTKTDSKSiMRMKSGQMFAKEDLRRKKLVRDGSVFLKSATGRlKEVQAVLLTDILVFLQEKDQ 2205
Cdd:COG5422    677 NRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAKSKTDGSLR-GDIQFFLLDNMLLFCKAKAV 745
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2263-2625 2.68e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2263 IQIIQDTINSLNRDEDE---GIPSENEEEKRLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTplpedcspth 2339
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN---------- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2340 sprMLFRSNTEEALKGGPLMKSAISEVEILQGLVSGSLGGTLGQPISSPVEQEVMAGPISLPRRAETFGGfdcHQLNASK 2419
Cdd:COG4717    235 ---ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2420 GGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSIVHLHELLTMLQgvvLQQdsyIEDQKLVLTEKVLTR 2499
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEAGVE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2500 SASRPSSLIEQEKQRslEKQRQDLANLQKQQAQHLEEKRRREREWEarelelrdrEAKLAEREETVRRRQQDLERDREEL 2579
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958643792 2580 QQKKGtyqcdleRLRAAQKQLER---------EQEQLKRDAEQLSQRQMEQDLCQ 2625
Cdd:COG4717    452 REELA-------ELEAELEQLEEdgelaellqELEELKAELRELAEEWAALKLAL 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2467-2627 1.11e-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: 51.21  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2467 LHELLTMLQGVVLQQDSYIED---QKLVLTEKV--LTRSASRPSSLIEQEKQRsLEKQRQDLANLQKQQAQHLEEKRRRE 2541
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRleqQKQILRERLanLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2542 REWEARELELRDREAKLAEREETVRRrqqdLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433

                   ....*.
gi 1958643792 2622 DLCQVS 2627
Cdd:TIGR02168  434 ELKELQ 439
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2480-2623 1.56e-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: 50.51  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2480 QQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKla 2559
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-- 432
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2560 eREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQ-----KQLEREQEQLKR-DAEQLSQRQMEQDL 2623
Cdd:pfam17380  433 -RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRDRkRAEEQRRKILEKEL 501
PRK12704 PRK12704
phosphodiesterase; Provisional
2551-2621 1.17e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958643792 2551 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLER-EQEQLKRdAEQLSQRQMEQ 2621
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEElIEEQLQE-LERISGLTAEE 154
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1732-1778 2.11e-04

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: 41.30  E-value: 2.11e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958643792  1732 HTFSPIPIVGPINCSQCMKP--FTNKDAYTCASCGAFVHKGCRENLAS-C 1778
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
2558-2621 3.18e-04

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: 42.81  E-value: 3.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958643792 2558 LAEREETVRRRQQDLERDREELQQKKGTYQcdlERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:cd06503     28 LDEREEKIAESLEEAEKAKEEAEELLAEYE---EKLAEARAEAQEIIEEARKEAEKIKEEILAE 88
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2559-2623 1.57e-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: 41.03  E-value: 1.57e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958643792  2559 AEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQ-LEREQEQLKRDAEQLsQRQMEQDL 2623
Cdd:smart00935   21 KQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRK-QQKLQQDL 85
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
545-837 5.16e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  545 PEEIPTGKPGMETQERGCEGGiTSDQSSQVLPAAAAATENKVLDGLELETLPACPCETASSLDLTVSGPRPDGMPKQNSE 624
Cdd:PHA03307    67 PPTGPPPGPGTEAPANESRST-PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPG 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  625 SSAQHAQSLNSQAPLCSIAGAGTPS----AESACPQSTETSSGGSVI-------EHGSGEASLPESTAAQPEPqglCTAP 693
Cdd:PHA03307   146 PPPAASPPAAGASPAAVASDAASSRqaalPLSSPEETARAPSSPPAEpppstppAAASPRPPRRSSPISASAS---SPAP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  694 CPEDPQAD--TVTSDTAAHNQKSV---GSCHLCALDAKNQEKDLRQ-DTPSVNTLEDVPHLPSVVPQSEEKLEPDQVSPR 767
Cdd:PHA03307   223 APGRSAADdaGASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRiWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792  768 GSSFSLASSP---ESESVTKDDVLSLVSSQKEK-----GTATPQLHRAPACSDGPDGRDLNDTDKVGDGAASPPTPSA 837
Cdd:PHA03307   303 PGSGPAPSSPrasSSSSSSRESSSSSTSSSSESsrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAA 380
 
Name Accession Description Interval E-value
PH_AKAP13 cd13392
A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...
2170-2272 8.26e-62

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity of AKAP13 (also called Brx-1, AKAP-Lbc, and proto-Lbc) mediates signaling downstream of G-protein coupled receptors and Toll-like receptor 2. It plays a role in cell growth, cell development and actin fiber formation. Protein kinase A (PKA) binds and phosphorylates AKAP13, regulating its Rho-GEF activity. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, Brx) containing a dbl oncogene homology (DH) domain and PH domain which are required for full transforming activity. The DH domain is associated with guanine nucleotide exchange activation while the PH domain has multiple functions including determine protein sub-cellular localisation via phosphoinositide interactions, while others bind protein partners. Other ligands include protein kinase C which is bound by the PH domain of AKAP13, serving to activate protein kinase D and mobilize a cardiac hypertrophy signaling pathway. 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: 275427  Cd Length: 103  Bit Score: 206.68  E-value: 8.26e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 2249
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80
                           90       100
                   ....*....|....*....|...
gi 1958643792 2250 EVHASSREERNSWIQIIQDTINS 2272
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103
PH_16 pfam17838
PH domain;
2154-2271 3.75e-51

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 177.21  E-value: 3.75e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2154 MKSGQMFAKEDLRRKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASL-------DHK--STVISLKKL 2224
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958643792 2225 IVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 2271
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1933-2127 1.66e-48

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: 171.71  E-value: 1.66e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1933 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSeknfl 2011
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2012 ikRIGDVLVsqfsgeNAERLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSvvRRLGIPECILLVTQRITKY 2091
Cdd:cd00160     76 --RIGDVFL------KLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958643792 2092 PVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1936-2127 8.88e-45

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


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 160.93  E-value: 8.88e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  1936 VIYELMQTELHHIRTLKIMSDVYSRGM-MTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKseknfliKR 2014
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV-------ER 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  2015 IGDVLVSQfsgenaERLKKTYGKFCGQHNQSVNYFKDLyTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVL 2094
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146
                           170       180       190
                    ....*....|....*....|....*....|...
gi 1958643792  2095 FQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179
PH_ARHGEF18 cd15794
Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also ...
2167-2286 5.10e-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: 156.60  E-value: 5.10e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2167 RKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDP 2246
Cdd:cd15794      1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958643792 2247 EMVEVHASSREERNSWIQIIQDTINSLNrDEDEGIPSENE 2286
Cdd:cd15794     81 EMYEIHTNSKEDRNTWMAHIRRAVESCP-DEEEGLFSEPE 119
PH_p190RhoGEF cd14680
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called ...
2170-2270 2.73e-43

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: 153.62  E-value: 2.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 2249
Cdd:cd14680      1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMY 80
                           90       100
                   ....*....|....*....|.
gi 1958643792 2250 EVHASSREERNSWIQIIQDTI 2270
Cdd:cd14680     81 EIHTSSKEERNNWMRLIQEAV 101
PH_ARHGEF2 cd13393
Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called ...
2167-2278 3.72e-41

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: 148.11  E-value: 3.72e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2167 RKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDhKSTVISLKKLIVREVAHEEKGLFLISmgVKDP 2246
Cdd:cd13393      1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLIS--AAPP 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958643792 2247 EMVEVHASSREERNSWIQIIQDTINSLNRDED 2278
Cdd:cd13393     78 EMYEVHAASRDDRNTWMRLIQQTVKTCPSREE 109
PH_RhoGEF cd13329
Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...
2170-2270 7.19e-40

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: 143.94  E-value: 7.19e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYV--------FASLDHKSTVISLKKLIVREVAHEEKGLFLISM 2241
Cdd:cd13329      1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80
                           90       100
                   ....*....|....*....|....*....
gi 1958643792 2242 GVKDPEMVEVHASSREERNSWIQIIQDTI 2270
Cdd:cd13329     81 SKNGPQMYELVANSSSERKTWIKHISDAV 109
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1936-2127 1.42e-35

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 134.35  E-value: 1.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1936 VIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFqrilerkkesLVDKSEKNFLIKRI 2015
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL----------LEELLKEWISIQRI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2016 GDVLVSQFSGenaerlKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLF 2095
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958643792 2096 QRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2127
Cdd:pfam00621  145 KELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
PH_ARHGEF2_18_like cd15789
rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling ...
2170-2267 3.16e-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: 116.40  E-value: 3.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISmgVKDPEMV 2249
Cdd:cd15789      1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLIS--ASPDGMP 78
                           90       100
                   ....*....|....*....|.
gi 1958643792 2250 EVHASSRE---ERNSWIQIIQ 2267
Cdd:cd15789     79 EMYELKVQkpkDKNTWIQTIR 99
C1_AKAP13 cd20878
protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...
1729-1784 1.03e-29

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) and similar proteins; AKAP-13, also called AKAP-Lbc, breast cancer nuclear receptor-binding auxiliary protein (Brx-1), guanine nucleotide exchange factor Lbc, human thyroid-anchoring protein 31, lymphoid blast crisis oncogene (LBC oncogene), non-oncogenic Rho GTPase-specific GTP exchange factor, protein kinase A-anchoring protein 13 (PRKA13), or p47, is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors (GPCRs). It activates RhoA in response to GPCR signaling via its function as a 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. Its Rho-GEF activity is regulated by protein kinase A (PKA), through binding and phosphorylation. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, and Brx) that contain a C1 domain followed by a dbl oncogene homology (DH) domain and a PH domain which are required for full transforming activity. 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: 410428  Cd Length: 60  Bit Score: 113.21  E-value: 1.03e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958643792 1729 LNGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCAKVKMK 1784
Cdd:cd20878      5 LNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60
C1_p190RhoGEF-like cd20815
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...
1730-1781 2.01e-16

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: 75.15  E-value: 2.01e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958643792 1730 NGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHK-GCRENLASCAKV 1781
Cdd:cd20815      2 NTHQFVPVSFSNSTKCDVCSKPLTNKPALQCENCSVNVHDsSCKDQLADCTKF 54
PH_PRG cd13391
PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called ...
2160-2271 1.93e-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: 66.98  E-value: 1.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2160 FAKEDLRRKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHKST---VISLKKLIVRE 2228
Cdd:cd13391     18 FKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSDSKQTfspVLKLNSVLIRS 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958643792 2229 VAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 2271
Cdd:cd13391     98 VATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAVR 140
PH_p115RhoGEF cd14679
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...
2160-2273 5.55e-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: 5.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2160 FAKEDLRRKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHK---STVISLKKLIVRE 2228
Cdd:cd14679      1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLkchsrtttPTPDGKqmlSPIIKLNSAMTRE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958643792 2229 VAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTINSL 2273
Cdd:cd14679     81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125
PH_LARG cd13390
Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; ...
2164-2266 7.24e-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: 65.39  E-value: 7.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2164 DLRRKKLVRDGSVFLKSATGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHKST---VISLKKLIVREVAHE 2232
Cdd:cd13390     20 DLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKHTfspVIKLNTVLVRQVATD 99
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958643792 2233 EKGLFLISMGVKDPEMVEVHASSREERNSWIQII 2266
Cdd:cd13390    100 NKAFFVISMSENGAQIYELVAQTVSEKTVWQDLI 133
C1_p190RhoGEF cd20876
protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange ...
1729-1780 2.12e-11

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: 61.30  E-value: 2.12e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958643792 1729 LNGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCAK 1780
Cdd:cd20876      5 SNGHQFVTGSFSGPTLCVVCDKPVTGKELLQCSNCTVNVHKGCKESAPPCTK 56
C1_ARHGEF2 cd20877
protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange ...
1730-1787 4.46e-11

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: 60.36  E-value: 4.46e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792 1730 NGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCAKVKMKQPK 1787
Cdd:cd20877      4 NGHLFTTITVSGTTMCSACNKSITAKEALICPTCNVTIHNRCKDTLPNCTKVKQKQQK 61
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2170-2271 2.14e-08

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


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 54.09  E-value: 2.14e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  2170 LVRDGSVFLKSATGRL--KEVQAVLLTDILVFLQEKDQKYVFasldHKSTVISLKKLIVREVAH----EEKGLFLISMGv 2243
Cdd:smart00233    1 VIKEGWLYKKSGGGKKswKKRYFVLFNSTLLYYKSKKDKKSY----KPKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75
                            90       100
                    ....*....|....*....|....*...
gi 1958643792  2244 kDPEMVEVHASSREERNSWIQIIQDTIN 2271
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102
C1_ARHGEF18-like cd20879
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
1730-1779 3.24e-08

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: 52.12  E-value: 3.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1730 NGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCA 1779
Cdd:cd20879      2 NGHQLVPGTFSSCATCSLCSKPLQNRNGLQCLNCAVNVHKNCKTLLTECS 51
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1732-1777 1.77e-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: 47.13  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958643792 1732 HTFSPIPIVGPINCSQCMKPFTN--KDAYTCASCGAFVHKGCRENLAS 1777
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWGlfKQGLKCSDCGLVCHKKCLDKAPS 48
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1905-2205 2.53e-06

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 53.36  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1905 DSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLF----EQQMVEKLFPCL 1980
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHVFANI 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1981 DELISIHSQFfqrilerkKESLVDKSEKNFLIKRIGDV------LVSQFSGENAERLkktYGKFCGQHNQSVNYfkdlyt 2054
Cdd:COG5422    537 NEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP------ 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2055 kdkRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYE 2134
Cdd:COG5422    600 ---NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAE 676
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958643792 2135 KKVRLGEIYTKTDSKSiMRMKSGQMFAKEDLRRKKLVRDGSVFLKSATGRlKEVQAVLLTDILVFLQEKDQ 2205
Cdd:COG5422    677 NRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAKSKTDGSLR-GDIQFFLLDNMLLFCKAKAV 745
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2263-2625 2.68e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2263 IQIIQDTINSLNRDEDE---GIPSENEEEKRLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTplpedcspth 2339
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN---------- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2340 sprMLFRSNTEEALKGGPLMKSAISEVEILQGLVSGSLGGTLGQPISSPVEQEVMAGPISLPRRAETFGGfdcHQLNASK 2419
Cdd:COG4717    235 ---ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2420 GGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSIVHLHELLTMLQgvvLQQdsyIEDQKLVLTEKVLTR 2499
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEAGVE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2500 SASRPSSLIEQEKQRslEKQRQDLANLQKQQAQHLEEKRRREREWEarelelrdrEAKLAEREETVRRRQQDLERDREEL 2579
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958643792 2580 QQKKGtyqcdleRLRAAQKQLER---------EQEQLKRDAEQLSQRQMEQDLCQ 2625
Cdd:COG4717    452 REELA-------ELEAELEQLEEdgelaellqELEELKAELRELAEEWAALKLAL 499
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
1730-1780 7.77e-06

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: 45.41  E-value: 7.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958643792 1730 NGHTFSPIPIVGPINCSQCMKPFT---NKDAYTCASCGAFVHKGCRENLAS-CAK 1780
Cdd:cd20831      4 NDHTFVATHFKGGPSCAVCNKLIPgrfGKQGYQCRDCGLICHKRCHVKVEThCPS 58
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2464-2617 8.18e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 8.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2464 IVHLHELLTMLQGVVLQQDSYIEDQK-LVLTEKVLTRSASRPSSLieQEKQRSLEKQRQDLANLQKQQA--QHLEEKRRR 2540
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEeLEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEAleAELAELPER 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2541 EREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKK----GTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQ 2616
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                   .
gi 1958643792 2617 R 2617
Cdd:COG4717    228 E 228
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2170-2270 9.72e-06

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.79  E-value: 9.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2170 LVRDGSVFLKS--ATGRLKEVQAVLLTDILVFLQEKDQKYVFAsldhKSTVISLKKLIVREVAHEEKG----LFLISMGV 2243
Cdd:pfam00169    1 VVKEGWLLKKGggKKKSWKKRYFVLFDGSLLYYKDDKSGKSKE----PKGSISLSGCEVVEVVASDSPkrkfCFELRTGE 76
                           90       100
                   ....*....|....*....|....*...
gi 1958643792 2244 KDP-EMVEVHASSREERNSWIQIIQDTI 2270
Cdd:pfam00169   77 RTGkRTYLLQAESEEERKDWIKAIQSAI 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2467-2627 1.11e-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: 51.21  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2467 LHELLTMLQGVVLQQDSYIED---QKLVLTEKV--LTRSASRPSSLIEQEKQRsLEKQRQDLANLQKQQAQHLEEKRRRE 2541
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRleqQKQILRERLanLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2542 REWEARELELRDREAKLAEREETVRRrqqdLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433

                   ....*.
gi 1958643792 2622 DLCQVS 2627
Cdd:TIGR02168  434 ELKELQ 439
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2480-2623 1.56e-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: 50.51  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2480 QQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKla 2559
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-- 432
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2560 eREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQ-----KQLEREQEQLKR-DAEQLSQRQMEQDL 2623
Cdd:pfam17380  433 -RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRDRkRAEEQRRKILEKEL 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2453-2622 1.98e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2453 LKRNSEQVVQSIVHLHELLTMLQgvvlQQDSYIEDQKLVLTEKVLTRSASRPSsliEQEKQRSLEKQRQDLANLQKQQAQ 2532
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2533 HLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQkkgtyqcDLERLRAAQKQLEREQEQLKRDAE 2612
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-------RLERLEEELEELEEALAELEEEEE 438
                          170
                   ....*....|
gi 1958643792 2613 QLSQRQMEQD 2622
Cdd:COG1196    439 EEEEALEEAA 448
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2510-2622 3.46e-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: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 2589
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958643792 2590 LERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAE 350
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2510-2639 4.48e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 4.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQcD 2589
Cdd:COG4717     52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-L 130
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792 2590 LERLRAAQKQLEREQ---EQLKRDAEQLSQ-----RQMEQDLCQVSNKHGRLMRVPSF 2639
Cdd:COG4717    131 YQELEALEAELAELPerlEELEERLEELREleeelEELEAELAELQEELEELLEQLSL 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2453-2607 1.03e-04

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: 48.13  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2453 LKRNSEQVVQSIVHLHELLTMLQGVVLQQDSYIED--QKLVLTEKVLTRSASRPSSLIEQEK--QRSLEKQRQDLANLQK 2528
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIEslAAEIEELEELIEELES 873
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958643792 2529 QQAQHLEEKRRREREWEAreleLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAaqkQLEREQEQL 2607
Cdd:TIGR02168  874 ELEALLNERASLEEALAL----LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERL 945
PRK12704 PRK12704
phosphodiesterase; Provisional
2551-2621 1.17e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958643792 2551 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLER-EQEQLKRdAEQLSQRQMEQ 2621
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEElIEEQLQE-LERISGLTAEE 154
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2508-2635 1.59e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2508 IEQEKQRSLEKQRQDLANLQKQQAQHleekrrrereweareLELR--------DREAKLAEREETVRRRQQ--DLERDRE 2577
Cdd:pfam13868  178 IEEEKEREIARLRAQQEKAQDEKAER---------------DELRaklyqeeqERKERQKEREEAEKKARQrqELQQARE 242
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958643792 2578 E-LQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQDLcqvsnKHGRLMR 2635
Cdd:pfam13868  243 EqIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL-----EHRRELE 296
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2510-2622 1.76e-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: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQQAQhLEEKRrreREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQcd 2589
Cdd:COG1196    277 EELELELEEAQAEEYELLAELAR-LEQDI---ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-- 350
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958643792 2590 lERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG1196    351 -EELEEAEAELAEAEEALLEAEAELAEAEEELE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2427-2622 2.05e-04

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: 46.97  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2427 DDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSIVHLHELLTMLQGVVLQQDSYIE---DQKLVLTEKVLTRSASr 2503
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEeaeEELAEAEAEIEELEAQ- 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2504 psslIEQEKQRsLEKQRQDLANLQKQQAQhleekrrrereweareleLRDREAKLAEREETVRRRQQDLERDREELQQKK 2583
Cdd:TIGR02168  791 ----IEQLKEE-LKALREALDELRAELTL------------------LNEEAANLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958643792 2584 GTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2509-2622 2.05e-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: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANLQKQQAQHleekrrrEREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqc 2588
Cdd:COG1196    220 EELKELEAELLLLKLRELEAELEEL-------EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----- 287
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958643792 2589 dlERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG1196    288 --AEEYELLAELARLEQDIARLEERRRELEERLE 319
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1732-1778 2.11e-04

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: 41.30  E-value: 2.11e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958643792  1732 HTFSPIPIVGPINCSQCMKP--FTNKDAYTCASCGAFVHKGCRENLAS-C 1778
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2510-2622 2.36e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQQAQhleekrrrerewearelelrdREAKLAEREETVRRRQQDLERDREEL---QQKKGTY 2586
Cdd:COG4372     55 EQAREELEQLEEELEQARSELEQ---------------------LEEELEELNEQLQAAQAELAQAQEELeslQEEAEEL 113
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958643792 2587 QCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG4372    114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2509-2621 3.08e-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: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQC 2588
Cdd:COG1196    258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958643792 2589 DLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:COG1196    338 ELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
2558-2621 3.18e-04

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: 42.81  E-value: 3.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958643792 2558 LAEREETVRRRQQDLERDREELQQKKGTYQcdlERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:cd06503     28 LDEREEKIAESLEEAEKAKEEAEELLAEYE---EKLAEARAEAQEIIEEARKEAEKIKEEILAE 88
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2453-2618 4.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2453 LKRNSEQVVQSIVHLHELLTMLQGVVLQQDSYIEDQKLvltEKVLTRSASRPSSLIEQ-----EKQRSLEKQRQDLANLQ 2527
Cdd:COG4717    100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL---EAELAELPERLEELEERleelrELEEELEELEAELAELQ 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2528 KQQAQHLEEKRRRErewearelelRDREAKLAEREETVRRRQQDLERDREELQQKkgtyqcdLERLRAAQKQLEREQEQL 2607
Cdd:COG4717    177 EELEELLEQLSLAT----------EEELQDLAEELEELQQRLAELEEELEEAQEE-------LEELEEELEQLENELEAA 239
                          170
                   ....*....|.
gi 1958643792 2608 KrDAEQLSQRQ 2618
Cdd:COG4717    240 A-LEERLKEAR 249
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2509-2621 4.53e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQC 2588
Cdd:pfam13868  115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE 194
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958643792 2589 DLERLRAAQKQL--EREQEQLKRDAEQLSQRQMEQ 2621
Cdd:pfam13868  195 KAQDEKAERDELraKLYQEEQERKERQKEREEAEK 229
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
2508-2625 4.54e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 45.13  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2508 IEQEKQRSLEKQRQDL-ANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTY 2586
Cdd:pfam09787   58 LLREEIQKLRGQIQQLrTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL 137
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958643792 2587 QcdlERLRAAQKQLEREQEQLK-RDAEQLSQRQMEQDLCQ 2625
Cdd:pfam09787  138 Q---SRIKDREAEIEKLRNQLTsKSQSSSSQSELENRLHQ 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2453-2627 4.71e-04

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: 45.82  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2453 LKRNSEQVVQSIVHLHELLTMLQGVVLQQDsyiEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQ---DLANLQKQ 2529
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2530 QAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREEL--------------QQKKGTYQCDLERLRA 2595
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraeltllneeaANLRERLESLERRIAA 835
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958643792 2596 AQKQLEREQEQLKRDAEQLSQRQMEQDLCQVS 2627
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2510-2633 5.08e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQ--QAQHLEEKRRREREWEARELELRDREAKLAEREEtvrrRQQDLERDREELQQKkgtyq 2587
Cdd:COG4717     91 AELQEELEELEEELEELEAEleELREELEKLEKLLQLLPLYQELEALEAELAELPE----RLEELEERLEELREL----- 161
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958643792 2588 cdLERLRAAQKQLEREQEQLKRDAEQLSQrQMEQDLCQVSNKHGRL 2633
Cdd:COG4717    162 --EEELEELEAELAELQEELEELLEQLSL-ATEEELQDLAEELEEL 204
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2486-2634 6.88e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.94  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2486 EDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQdlanlQKQQAQHLEEKRRREREWEARELELRDREAKLAErEETV 2565
Cdd:pfam15709  318 EDPSKALLEKREQEKASRDRLRAERAEMRRLEVERK-----RREQEEQRRLQQEQLERAEKMREELELEQQRRFE-EIRL 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2566 RRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLE-----------REQEQLKRdAEQLSQRQMEQDLcQVSNKHGRLM 2634
Cdd:pfam15709  392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrklqelqrkKQQEEAER-AEAEKQRQKELEM-QLAEEQKRLM 469
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
1732-1775 7.17e-04

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: 39.70  E-value: 7.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958643792 1732 HTFSPIPIVGPINCSQCMKPFT-NKDAYTCASCGAFVHKGCRENL 1775
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIKfGKKALKCKDCRVVCHPDCKDKL 47
Zwint pfam15556
ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ...
2561-2633 7.58e-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: 43.81  E-value: 7.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958643792 2561 REETVRRRQQDLERDREELQQKKgtyQCDLERLRAAQKQLEREQE----QLKRDAEQLSQRQ--MEQDLCQVSNKHGRL 2633
Cdd:pfam15556   92 KMEEAQRKRAQLQEALEQLQAKK---QMAMEKLRTAQKQWQLQQEkhlqHLAEVSAEVRERQtgTQQELERLYQELGTL 167
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2510-2622 7.68e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 7.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANlQKQQAQHLEEKRRREREWEARELELRDREAKLA-------------EREETVRRRQQDLERDR 2576
Cdd:COG4913    630 EERLEALEAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELErldassddlaaleEQLEELEAELEELEEEL 708
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958643792 2577 EELQQKKGtyqcdleRLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG4913    709 DELKGEIG-------RLEKELEQAEEELDELQDRLEAAEDLARLEL 747
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2458-2618 8.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 8.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2458 EQVVQSIVHLHELLTMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQ-----RSLEKQR-----QDLANLQ 2527
Cdd:COG4913    265 AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlreelDELEAQIrgnggDRLEQLE 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2528 KQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQL 2607
Cdd:COG4913    345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
                          170
                   ....*....|.
gi 1958643792 2608 KRDAEQLSQRQ 2618
Cdd:COG4913    425 EAEIASLERRK 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2510-2647 9.26e-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: 44.37  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQrqdLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqcd 2589
Cdd:COG4942     19 ADAAAEAEAE---LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE------ 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792 2590 lERLRAAQKQLEREQEQLkrdAEQLSQRQMeqdlcqvSNKHGRLMrvpsFLPNSDEFS 2647
Cdd:COG4942     90 -KEIAELRAELEAQKEEL---AELLRALYR-------LGRQPPLA----LLLSPEDFL 132
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2559-2623 1.04e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.79  E-value: 1.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958643792 2559 AEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLsQRQMEQDL 2623
Cdd:pfam03938   22 AQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQL-QQKAQQEL 85
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
2558-2621 1.12e-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: 41.70  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958643792 2558 LAEREETVRRRQQDLERDREELQQKKGTYQcdlERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:COG0711     29 LDERQEKIADGLAEAERAKEEAEAALAEYE---EKLAEARAEAAEIIAEARKEAEAIAEEAKAE 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2458-2618 1.28e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2458 EQVVQSIVHLHELLTMLQGVVLQQDSYIEDQKLVLTEKvltRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQ----- 2532
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEEL---EAELEELESRLEELEEQLETLRSKVAQLELQIASlnnei 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2533 -----HLEEKRRREREWEARELELRdREAKLAEREEtVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQL 2607
Cdd:TIGR02168  403 erleaRLERLEDRRERLQQEIEELL-KKLEEAELKE-LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          170
                   ....*....|.
gi 1958643792 2608 KRDAEQLSQRQ 2618
Cdd:TIGR02168  481 ERELAQLQARL 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2509-2622 1.38e-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: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANLQKQQAQhleekrrrereweARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTyqc 2588
Cdd:COG1196    264 ELEAELEELRLELEELELELEEAQ-------------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE--- 327
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958643792 2589 DLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG1196    328 LEEELEELEEELEELEEELEEAEEELEEAEAELA 361
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2559-2623 1.57e-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: 41.03  E-value: 1.57e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958643792  2559 AEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQ-LEREQEQLKRDAEQLsQRQMEQDL 2623
Cdd:smart00935   21 KQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRK-QQKLQQDL 85
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2480-2620 1.76e-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: 43.96  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2480 QQDSY--IEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQ--------DLANLQKQQAQHLEEKRRREREWEAREL 2549
Cdd:pfam17380  289 QQEKFekMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQaaiyaeqeRMAMERERELERIRQEERKRELERIRQE 368
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958643792 2550 ELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLeREQEQLKRDAEQLSQRQME 2620
Cdd:pfam17380  369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK-VEMEQIRAEQEEARQREVR 438
mukB PRK04863
chromosome partition protein MukB;
2511-2617 1.82e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2511 EKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKG---TYQ 2587
Cdd:PRK04863   530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlAAQ 609
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792 2588 CDLERLRAA---------------QKQLERE-------------QEQLKRDAEQLSQR 2617
Cdd:PRK04863   610 DALARLREQsgeefedsqdvteymQQLLEREreltverdelaarKQALDEEIERLSQP 667
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
1732-1778 1.91e-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: 1.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958643792 1732 HTFSPipivgPINCSQCMK----PFtnKDAYTCASCGAFVHKGCRENLASC 1778
Cdd:cd20810      8 TTFKE-----PTTCSVCKKllkgLF--FQGYKCSVCGAAVHKECIAKVKRC 51
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2555-2623 2.03e-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: 40.29  E-value: 2.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958643792 2555 EAKLAEREETVRRRQQDLERDRE---ELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDA--EQLSQRQMEQDL 2623
Cdd:pfam20492   12 EERLKQYEEETKKAQEELEESEEtaeELEEERRQAEEEAERLEQKRQEAEEEKERLEESAemEAEEKEQLEAEL 85
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2510-2622 2.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQqaqhleekrrrereweareleLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 2589
Cdd:COG4372     34 RKALFELDKLQEELEQLREE---------------------LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958643792 2590 LERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG4372     93 QAELAQAQEELESLQEEAEELQEELEELQKERQ 125
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2508-2621 2.71e-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: 42.83  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2508 IEQEKQRSLEKQRQDLANLQKQQAQhleekrrrereweareleLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQ 2587
Cdd:COG4942    144 LAPARREQAEELRADLAELAALRAE------------------LEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958643792 2588 CDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:COG4942    206 KELAELAAELAELQQEAEELEALIARLEAEAAAA 239
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2555-2620 2.77e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 2.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958643792 2555 EAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQ-LSQRQME 2620
Cdd:pfam03938   25 EKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQeLQKKQQE 91
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2505-2621 3.59e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2505 SSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREET----------VRRRQQDLER 2574
Cdd:COG3206    226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRA 305
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958643792 2575 D-REELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:COG3206    306 QlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2487-2621 3.64e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 42.33  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2487 DQKLVltEKVLTRsasrpssliEQEKQRSLEKQRQdlANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVR 2566
Cdd:pfam15558    6 DRKIA--ALMLAR---------HKEEQRMRELQQQ--AALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKA 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958643792 2567 RRQQDLERDREelQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:pfam15558   73 RLGREERRRAD--RREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQ 125
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2551-2622 3.73e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 3.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958643792 2551 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:COG3883    145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
2498-2621 3.77e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.69  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2498 TRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDRE 2577
Cdd:pfam08614   41 KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREE 120
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958643792 2578 ELQQKKGTYQC---DLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:pfam08614  121 ELREKRKLNQDlqdELVALQLQLNMAEEKLRKLEKENRELVERWMKR 167
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1730-1778 4.40e-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: 4.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958643792 1730 NGHTFSPIPIVGPINCSQCMKPFTNKdAYTCASCGAFVHKGCREN-LASC 1778
Cdd:cd20822      1 RGHKFVQKQFYQIMRCAVCGEFLVNA-GYQCEDCKYTCHKKCYEKvVTKC 49
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2509-2621 4.51e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANLQKQQAQHleekrrrereweaRELELRDREAKLAERE---ETVRRRQQDLERDREELQQKKGT 2585
Cdd:pfam13868   61 EEKEEERKEERKRYRQELEEQIEER-------------EQKRQEEYEEKLQEREqmdEIVERIQEEDQAEAEEKLEKQRQ 127
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958643792 2586 YQCDLE---RLRAAQKQLEREQEQL--KRDAEQLSQRQMEQ 2621
Cdd:pfam13868  128 LREEIDefnEEQAEWKELEKEEEREedERILEYLKEKAERE 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2510-2623 5.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQK---QQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTY 2586
Cdd:COG4372     62 EQLEEELEQARSELEQLEEeleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958643792 2587 QCD-------LERLRAAQKQLEREQEQLKRDAEQLSQRQMEQDL 2623
Cdd:COG4372    142 QSEiaereeeLKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
545-837 5.16e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  545 PEEIPTGKPGMETQERGCEGGiTSDQSSQVLPAAAAATENKVLDGLELETLPACPCETASSLDLTVSGPRPDGMPKQNSE 624
Cdd:PHA03307    67 PPTGPPPGPGTEAPANESRST-PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPG 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  625 SSAQHAQSLNSQAPLCSIAGAGTPS----AESACPQSTETSSGGSVI-------EHGSGEASLPESTAAQPEPqglCTAP 693
Cdd:PHA03307   146 PPPAASPPAAGASPAAVASDAASSRqaalPLSSPEETARAPSSPPAEpppstppAAASPRPPRRSSPISASAS---SPAP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792  694 CPEDPQAD--TVTSDTAAHNQKSV---GSCHLCALDAKNQEKDLRQ-DTPSVNTLEDVPHLPSVVPQSEEKLEPDQVSPR 767
Cdd:PHA03307   223 APGRSAADdaGASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRiWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792  768 GSSFSLASSP---ESESVTKDDVLSLVSSQKEK-----GTATPQLHRAPACSDGPDGRDLNDTDKVGDGAASPPTPSA 837
Cdd:PHA03307   303 PGSGPAPSSPrasSSSSSSRESSSSSTSSSSESsrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAA 380
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1730-1782 6.22e-03

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: 37.45  E-value: 6.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792 1730 NGHTFSPIPIVGPINCSQCmKPFT----NKDAYTCASCGAFVHKGCRENLAS-CAKVK 1782
Cdd:cd20835      8 NGHKFMATYLRQPTYCSHC-KDFIwgviGKQGYQCQVCTCVVHKRCHQLVVTkCPGNK 64
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2510-2617 6.48e-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: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2510 QEKQRSLEKQRQDLANLQKQQAQHLeekrrrereweareLELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 2589
Cdd:COG4942    149 REQAEELRADLAELAALRAELEAER--------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
                           90       100
                   ....*....|....*....|....*...
gi 1958643792 2590 LERLRAAQKQLEREQEQLKRDAEQLSQR 2617
Cdd:COG4942    215 LAELQQEAEELEALIARLEAEAAAAAER 242
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
2555-2623 6.61e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 6.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2555 EAKLAEREETVRRRQQDLERDREELQQKKGTyqcdlerLRAAQKQ-LEREQEQLKRDAEQLsQRQMEQDL 2623
Cdd:COG2825     49 EKEFKKRQAELQKLEKELQALQEKLQKEAAT-------LSEEERQkKERELQKKQQELQRK-QQEAQQDL 110
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2509-2621 7.53e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANLQKQQAQHleekrrrerewearELELRDREAKLAERE-ETVRRRQQDLER----DREELQQKK 2583
Cdd:pfam13868  223 EREEAEKKARQRQELQQAREEQIEL--------------KERRLAEEAEREEEEfERMLRKQAEDEEieqeEAEKRRMKR 288
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958643792 2584 GTYQCDLERL---RAAQKQLEREQEQLKRDAEQLSQRQMEQ 2621
Cdd:pfam13868  289 LEHRRELEKQieeREEQRAAEREEELEEGERLREEEAERRE 329
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2567-2622 7.61e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 7.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958643792 2567 RRQQDLERDREELQQKKGTYQcdlERLRAAQKQLEREQEQLKRDAEQLSQRQMEQD 2622
Cdd:PRK09510    80 QRKKKEQQQAEELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQK 132
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2509-2629 7.86e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 7.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643792 2509 EQEKQRSLEKQRQDLANL-----QKQQAQhleekrrRErewearelelrdrEAKLAEREETVRRRQQDLERDREELQQKK 2583
Cdd:pfam13868  138 EQAEWKELEKEEEREEDErileyLKEKAE-------RE-------------EEREAEREEIEEEKEREIARLRAQQEKAQ 197
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958643792 2584 GtYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQDLCQVSNK 2629
Cdd:pfam13868  198 D-EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQARE 242
DUF1090 pfam06476
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ...
2551-2608 8.27e-03

Protein of unknown function (DUF1090); This family consists of several bacterial proteins of unknown function and is known as YqjC in E. coli.


Pssm-ID: 428965 [Multi-domain]  Cd Length: 109  Bit Score: 38.37  E-value: 8.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958643792 2551 LRDREAKLAEREETVRRRQQDLerdrEELQQKKgtyqcDLERLRAAQKQLEREQEQLK 2608
Cdd:pfam06476   60 RAERQQKVAEKREEVAEREAEL----AEAQAKG-----DADKIAKRQRKLAEARQELK 108
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
2551-2620 8.83e-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: 39.30  E-value: 8.83e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958643792 2551 LRDREAKLAEREETVRRRqqdLERDREELQQKkgtyqcdLERLRAAQKQLER-------EQEQLKRDAEQLSQRQME 2620
Cdd:pfam07321   78 LRENEADLEKQVAEARQQ---LEAEREALRQA-------RQALAEARRAVEKfaelvrlVQAEELRQQERQEEQELE 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH