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Conserved domains on  [gi|1911189734|ref|XP_036211735|]
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A-kinase anchor protein 13 isoform X3 [Myotis myotis]

Protein Classification

Graphical summary

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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 ...
2235-2337 1.09e-66

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: 220.55  E-value: 1.09e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMKDPEMV 2314
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80
                           90       100
                   ....*....|....*....|...
gi 1911189734 2315 EVHASSKEERNSWIQIIQDTINT 2337
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1998-2192 1.18e-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: 172.10  E-value: 1.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1998 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTELL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSernfl 2076
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2077 irRMGDVLVNQFSgenaerLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSAvvRRLGIPECILLVTQRITKY 2156
Cdd:cd00160     76 --RIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1911189734 2157 PVLFQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
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) ...
1794-1849 8.40e-31

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: 116.67  E-value: 8.40e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1911189734 1794 LNGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHKGCRESLASCAKVKMK 1849
Cdd:cd20878      5 LNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2616-2857 1.34e-10

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 66.01  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDACQVRGRL 2695
Cdd:COG3883    138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2696 SGTGQVRGRLSGTGPPVRYGAACQVRGRLSGTGPPVRYGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGS 2775
Cdd:COG3883    218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2776 GMGPPVRYGSGLGPPDRYGSGPGPPVRYGSGPGPPVRYGSGLGPPVRYGSGLGPPVRYGSGTGPPVRYGGRLSGTGPPVG 2855
Cdd:COG3883    298 AASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVG 377

                   ..
gi 1911189734 2856 SG 2857
Cdd:COG3883    378 GA 379
PHA03247 super family cl33720
large tegument protein UL36; Provisional
673-1338 5.13e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.73  E-value: 5.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  673 GALAAEHRDDTDTPPAGSATGPPHAQPPPTAVCPEGP--QAEAVTPD-PVGDTQEDVGFC---PLEVL--DTAGQtrrvn 744
Cdd:PHA03247  2476 GAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPsrLAPAILPDePVGEPVHPRMLTwirGLEELasDDAGD----- 2550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  745 sqtpltnalevelhPHAVFPKADREPVPDQAVTSGRtfsPAGSPGSESVTkddalslvpSQNEKGTATPQPltaTDGRDG 824
Cdd:PHA03247  2551 --------------PPPPLPPAAPPAAPDRSVPPPR---PAPRPSEPAVT---------SRARRPDAPPQS---ARPRAP 2601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  825 GDWSDPDKQPledgAAGLPTPPAALDPQPSMGNASPGGFggEQEDPCLPAAPEvrnmeggtdssRLHVAEAPLASDSSLT 904
Cdd:PHA03247  2602 VDDRGDPRGP----APPSPLPPDTHAPDPPPPSPSPAAN--EPDPHPPPTVPP-----------PERPRDDPAPGRVSRP 2664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  905 EEGKSPVVPESSAAQGQGDRLKAvicsstkedtLPPGALREEQGTDPPRQESPGDQGEPGAAACSRDKALEHSGSRGTPS 984
Cdd:PHA03247  2665 RRARRLGRAAQASSPPQRPRRRA----------ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA 2734
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  985 ACLNAetkhneevAPPASllteggaAQSPVPPGAGLATDAGQEAVGAEQSSSPRLPGLSPdASRAPNCNGPSAVDGVTDA 1064
Cdd:PHA03247  2735 LPAAP--------APPAV-------PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP-PRRLTRPAVASLSESRESL 2798
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1065 QAQGETAACEASGNMALDVAVGNALQGTAEARGTALSHSAQDLPVPEVLLRQENGIQVLPGALPDKGGTNLQGAAAPETV 1144
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP 2878
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1145 --PPVWEKGKPegahrSCSRDASEGAQMNDTRSVPLQPTAKELPAEaglsTSDDKAPSRDRGAPPDPHAVSAEAGHLPES 1222
Cdd:PHA03247  2879 arPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQP----QPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1223 AdSIEEAASRIVDAVIEHVRASGALLTEGDISHLPPSSPA---ETGPGAGQPES-----ASAGKVH--------ALLSGE 1286
Cdd:PHA03247  2950 A-GAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREApasSTPPLTGHSLSrvsswASSLALHeetdpppvSLKQTL 3028
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 1287 TPP-------AGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPDTKADDEVDF 1338
Cdd:PHA03247  3029 WPPddtedsdADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQF 3087
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2328-2682 5.29e-09

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


:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.71  E-value: 5.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2328 IQIIQDTINTLNRDEDE---GIPSENEEEKKMLDTKARELKEQLQQKDQQILLLLEEKEGIFRDMMECSTPLPEEysptv 2404
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----- 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2405 sprilfrsNTEEALKGGPLMKSAINEVEILQGLVSGSLGGPLGQAVSSPVGQEGTVGPVSLPRRAETFGGfdsHQMNASK 2484
Cdd:COG4717    240 --------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2485 GGDKEEGDDGQDLRRTESDSGLKKGGNANLAFMLKRNNEQVIQSIVHLHELLSTLQgvvlQQDSYIEDQRLLlsERALAR 2564
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----LEELEQEIAALL--AEAGVE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2565 SSSRPSSLVEQEKQRslERQRQDLADLQRQQAQHLEERRRREREWEareralqerEARLAQREEEVQRGQQDLERDREAL 2644
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1911189734 2645 LQKRGAYQYDLERLRAAQK--QLEREQEQLKRDAERLGQR 2682
Cdd:COG4717    452 REELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
484-718 5.15e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.08  E-value: 5.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  484 PETAEGAERGLRNPdATTQKKVLAAGERTKERLENSHVGAAGASHVKDTRQPVDKAMVP-NCVSATSSLDGETPA---ES 559
Cdd:PRK07003   360 PAVTGGGAPGGGVP-ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAaAATRAEAPPAAPAPPataDR 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  560 VLVLSHGGAPIEKTAETETSrcydASADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPFPRPQKDALPKEKAETNSPH 639
Cdd:PRK07003   439 GDDAADGDAPVPAKANARAS----ADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA 514
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  640 LQSQNDQPPICSPPGDDQPQAASASGQSTVTSSGALA-------AEHRDDTDTPPAGSATGPPHAQPPPTAVcPEGPQAE 712
Cdd:PRK07003   515 AASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAaldvlrnAGMRVSSDRGARAAAAAKPAAAPAAAPK-PAAPRVA 593

                   ....*.
gi 1911189734  713 AVTPDP 718
Cdd:PRK07003   594 VQVPTP 599
 
Name Accession Description Interval E-value
PH_AKAP13 cd13392
A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...
2235-2337 1.09e-66

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: 220.55  E-value: 1.09e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMKDPEMV 2314
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80
                           90       100
                   ....*....|....*....|...
gi 1911189734 2315 EVHASSKEERNSWIQIIQDTINT 2337
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103
PH_16 pfam17838
PH domain;
2219-2336 1.20e-54

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 187.22  E-value: 1.20e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2219 MKSGQMFAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASL-------DQK--STVISLKKL 2289
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1911189734 2290 IVREVAHEEKGLFLISMGMKDPEMVEVHASSKEERNSWIQIIQDTIN 2336
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1998-2192 1.18e-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: 172.10  E-value: 1.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1998 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTELL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSernfl 2076
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2077 irRMGDVLVNQFSgenaerLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSAvvRRLGIPECILLVTQRITKY 2156
Cdd:cd00160     76 --RIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1911189734 2157 PVLFQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
2001-2192 1.46e-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: 163.24  E-value: 1.46e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  2001 VIYELMQTELHHIRTLKIMSDVYSRGM-MTELLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSernflirR 2079
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVE-------R 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  2080 MGDVLVNQfsgenaERLKKTYGKFCGQHNQSVNYFKDLyTKDKRFQAFVKKKMSSAVVRRLGIPECILLVTQRITKYPVL 2159
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146
                           170       180       190
                    ....*....|....*....|....*....|...
gi 1911189734  2160 FQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
2001-2192 9.07e-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: 132.04  E-value: 9.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2001 VIYELMQTELHHIRTLKIMSDVYSRGMMTELLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESlvdksernflIRRM 2080
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLLLEELLKEWIS----------IQRI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2081 GDVLVNQFSGenaerlKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSAVVRRLGIPECILLVTQRITKYPVLF 2160
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1911189734 2161 QRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
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) ...
1794-1849 8.40e-31

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: 116.67  E-value: 8.40e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1911189734 1794 LNGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHKGCRESLASCAKVKMK 1849
Cdd:cd20878      5 LNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2616-2857 1.34e-10

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 66.01  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDACQVRGRL 2695
Cdd:COG3883    138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2696 SGTGQVRGRLSGTGPPVRYGAACQVRGRLSGTGPPVRYGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGS 2775
Cdd:COG3883    218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2776 GMGPPVRYGSGLGPPDRYGSGPGPPVRYGSGPGPPVRYGSGLGPPVRYGSGLGPPVRYGSGTGPPVRYGGRLSGTGPPVG 2855
Cdd:COG3883    298 AASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVG 377

                   ..
gi 1911189734 2856 SG 2857
Cdd:COG3883    378 GA 379
PHA03247 PHA03247
large tegument protein UL36; Provisional
673-1338 5.13e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.73  E-value: 5.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  673 GALAAEHRDDTDTPPAGSATGPPHAQPPPTAVCPEGP--QAEAVTPD-PVGDTQEDVGFC---PLEVL--DTAGQtrrvn 744
Cdd:PHA03247  2476 GAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPsrLAPAILPDePVGEPVHPRMLTwirGLEELasDDAGD----- 2550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  745 sqtpltnalevelhPHAVFPKADREPVPDQAVTSGRtfsPAGSPGSESVTkddalslvpSQNEKGTATPQPltaTDGRDG 824
Cdd:PHA03247  2551 --------------PPPPLPPAAPPAAPDRSVPPPR---PAPRPSEPAVT---------SRARRPDAPPQS---ARPRAP 2601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  825 GDWSDPDKQPledgAAGLPTPPAALDPQPSMGNASPGGFggEQEDPCLPAAPEvrnmeggtdssRLHVAEAPLASDSSLT 904
Cdd:PHA03247  2602 VDDRGDPRGP----APPSPLPPDTHAPDPPPPSPSPAAN--EPDPHPPPTVPP-----------PERPRDDPAPGRVSRP 2664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  905 EEGKSPVVPESSAAQGQGDRLKAvicsstkedtLPPGALREEQGTDPPRQESPGDQGEPGAAACSRDKALEHSGSRGTPS 984
Cdd:PHA03247  2665 RRARRLGRAAQASSPPQRPRRRA----------ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA 2734
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  985 ACLNAetkhneevAPPASllteggaAQSPVPPGAGLATDAGQEAVGAEQSSSPRLPGLSPdASRAPNCNGPSAVDGVTDA 1064
Cdd:PHA03247  2735 LPAAP--------APPAV-------PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP-PRRLTRPAVASLSESRESL 2798
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1065 QAQGETAACEASGNMALDVAVGNALQGTAEARGTALSHSAQDLPVPEVLLRQENGIQVLPGALPDKGGTNLQGAAAPETV 1144
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP 2878
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1145 --PPVWEKGKPegahrSCSRDASEGAQMNDTRSVPLQPTAKELPAEaglsTSDDKAPSRDRGAPPDPHAVSAEAGHLPES 1222
Cdd:PHA03247  2879 arPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQP----QPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1223 AdSIEEAASRIVDAVIEHVRASGALLTEGDISHLPPSSPA---ETGPGAGQPES-----ASAGKVH--------ALLSGE 1286
Cdd:PHA03247  2950 A-GAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREApasSTPPLTGHSLSrvsswASSLALHeetdpppvSLKQTL 3028
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 1287 TPP-------AGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPDTKADDEVDF 1338
Cdd:PHA03247  3029 WPPddtedsdADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQF 3087
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2328-2682 5.29e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.71  E-value: 5.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2328 IQIIQDTINTLNRDEDE---GIPSENEEEKKMLDTKARELKEQLQQKDQQILLLLEEKEGIFRDMMECSTPLPEEysptv 2404
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----- 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2405 sprilfrsNTEEALKGGPLMKSAINEVEILQGLVSGSLGGPLGQAVSSPVGQEGTVGPVSLPRRAETFGGfdsHQMNASK 2484
Cdd:COG4717    240 --------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2485 GGDKEEGDDGQDLRRTESDSGLKKGGNANLAFMLKRNNEQVIQSIVHLHELLSTLQgvvlQQDSYIEDQRLLlsERALAR 2564
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----LEELEQEIAALL--AEAGVE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2565 SSSRPSSLVEQEKQRslERQRQDLADLQRQQAQHLEERRRREREWEareralqerEARLAQREEEVQRGQQDLERDREAL 2644
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1911189734 2645 LQKRGAYQYDLERLRAAQK--QLEREQEQLKRDAERLGQR 2682
Cdd:COG4717    452 REELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2235-2336 7.57e-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: 52.55  E-value: 7.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  2235 LVRDGSVFLK--NAAGRLKEVQAVLLTDILVFLQEKDQKYVFAsldqKSTVISLKKLIVREVAH----EEKGLFLISMGm 2308
Cdd:smart00233    1 VIKEGWLYKKsgGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK----PKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75
                            90       100
                    ....*....|....*....|....*...
gi 1911189734  2309 kDPEMVEVHASSKEERNSWIQIIQDTIN 2336
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2532-2700 8.08e-08

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: 58.53  E-value: 8.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2532 LHELLSTLQGVVLQQDSYIED--QRLLLSERALARSSSRPSSLVEQ--EKQRSLERQRQDLADLQRQQAQHLEERRRRER 2607
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRleQQKQILRERLANLERQLEELEAQleELESKLDELAEELAELEEKLEELKEELESLEA 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2608 EWEARERALQEREARLAQREEEVQRgqqdLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERD 2687
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
                          170
                   ....*....|...
gi 1911189734 2688 ACQVRGRLSGTGQ 2700
Cdd:TIGR02168  435 LKELQAELEELEE 447
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1966-2270 8.99e-07

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 8.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1966 DFESESKQLEAESWSRVVDSKFLKQQkkdaVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTELLF----EQQMVEKL 2041
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQE----IKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHV 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2042 FPCLDELISIHSQFfqrilerkKESLVDKSERNFLIRRMGDV------LVNQFSGENAERLkktYGKFCGQHNQSVNYfk 2115
Cdd:COG5422    533 FANINEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP-- 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2116 dlytkdkRFQAFVKKKMSSAVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVDNKV 2195
Cdd:COG5422    600 -------NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFES 672
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2196 ASYEKKVRLNEIYTKTDSKSiMRMKSGQMFAKEDLKRKKLVRDGSVfLKNAAGRLKEVQAVLLTDILVFLQEKDQ 2270
Cdd:COG5422    673 GKAENRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAK-SKTDGSLRGDIQFFLLDNMLLFCKAKAV 745
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2545-2687 1.01e-06

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: 54.36  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2545 QQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREArla 2624
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE--- 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 2625 QREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQ-----KQLEREQEQLKR-DAERLGQRQLERD 2687
Cdd:pfam17380  432 ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRDRkRAEEQRRKILEKE 500
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
484-718 5.15e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.08  E-value: 5.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  484 PETAEGAERGLRNPdATTQKKVLAAGERTKERLENSHVGAAGASHVKDTRQPVDKAMVP-NCVSATSSLDGETPA---ES 559
Cdd:PRK07003   360 PAVTGGGAPGGGVP-ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAaAATRAEAPPAAPAPPataDR 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  560 VLVLSHGGAPIEKTAETETSrcydASADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPFPRPQKDALPKEKAETNSPH 639
Cdd:PRK07003   439 GDDAADGDAPVPAKANARAS----ADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA 514
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  640 LQSQNDQPPICSPPGDDQPQAASASGQSTVTSSGALA-------AEHRDDTDTPPAGSATGPPHAQPPPTAVcPEGPQAE 712
Cdd:PRK07003   515 AASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAaldvlrnAGMRVSSDRGARAAAAAKPAAAPAAAPK-PAAPRVA 593

                   ....*.
gi 1911189734  713 AVTPDP 718
Cdd:PRK07003   594 VQVPTP 599
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2518-2686 7.39e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 7.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2518 LKRNNEQVIQSIVHLHEL----------LSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQD 2587
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELekalaelrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2588 LADLQRQQAQHLeerrrrerewEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQydleRLRAAQKQLER 2667
Cdd:TIGR02168  759 LEAEIEELEERL----------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRE 824
                          170
                   ....*....|....*....
gi 1911189734 2668 EQEQLKRDAERLgQRQLER 2686
Cdd:TIGR02168  825 RLESLERRIAAT-ERRLED 842
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2545-2686 1.12e-04

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: 47.81  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2545 QQDSYIEDQRLLLS-ERALARsssrpssLVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREreweareralQEREARL 2623
Cdd:pfam17380  332 QAAIYAEQERMAMErERELER-------IRQEERKRELERIRQEEIAMEISRMRELERLQMER----------QQKNERV 394
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2624 AQrEEEVQRGQ--QDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLER 2686
Cdd:pfam17380  395 RQ-ELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER 458
PRK12704 PRK12704
phosphodiesterase; Provisional
2616-2674 2.05e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 2.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLER-EQEQLKR 2674
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEElIEEQLQE 143
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2552-2686 2.05e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2552 DQRLLLSERALArsssrpsslVEQEKQRSLERQRQDLADLQRQQAQHleerrrrereweareraLQEREARLaqrEEEVQ 2631
Cdd:cd16269    190 DQALTEKEKEIE---------AERAKAEAAEQERKLLEEQQRELEQK-----------------LEDQERSY---EEHLR 240
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2632 RGQQDLERDREALlqkrgayqydLERLRAAQKQLEREQEQLKRDAERLGQRQLER 2686
Cdd:cd16269    241 QLKEKMEEERENL----------LKEQERALESKLKEQEALLEEGFKEQAELLQE 285
 
Name Accession Description Interval E-value
PH_AKAP13 cd13392
A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...
2235-2337 1.09e-66

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: 220.55  E-value: 1.09e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMKDPEMV 2314
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80
                           90       100
                   ....*....|....*....|...
gi 1911189734 2315 EVHASSKEERNSWIQIIQDTINT 2337
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103
PH_16 pfam17838
PH domain;
2219-2336 1.20e-54

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 187.22  E-value: 1.20e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2219 MKSGQMFAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASL-------DQK--STVISLKKL 2289
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1911189734 2290 IVREVAHEEKGLFLISMGMKDPEMVEVHASSKEERNSWIQIIQDTIN 2336
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1998-2192 1.18e-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: 172.10  E-value: 1.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1998 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTELL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSernfl 2076
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2077 irRMGDVLVNQFSgenaerLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSAvvRRLGIPECILLVTQRITKY 2156
Cdd:cd00160     76 --RIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1911189734 2157 PVLFQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
PH_ARHGEF18 cd15794
Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also ...
2232-2351 1.39e-45

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: 160.84  E-value: 1.39e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2232 RKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMKDP 2311
Cdd:cd15794      1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1911189734 2312 EMVEVHASSKEERNSWIQIIQDTINTLNrDEDEGIPSENE 2351
Cdd:cd15794     81 EMYEIHTNSKEDRNTWMAHIRRAVESCP-DEEEGLFSEPE 119
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
2001-2192 1.46e-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: 163.24  E-value: 1.46e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  2001 VIYELMQTELHHIRTLKIMSDVYSRGM-MTELLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSernflirR 2079
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVE-------R 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  2080 MGDVLVNQfsgenaERLKKTYGKFCGQHNQSVNYFKDLyTKDKRFQAFVKKKMSSAVVRRLGIPECILLVTQRITKYPVL 2159
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146
                           170       180       190
                    ....*....|....*....|....*....|...
gi 1911189734  2160 FQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179
PH_p190RhoGEF cd14680
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called ...
2235-2335 1.73e-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: 154.39  E-value: 1.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMKDPEMV 2314
Cdd:cd14680      1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMY 80
                           90       100
                   ....*....|....*....|.
gi 1911189734 2315 EVHASSKEERNSWIQIIQDTI 2335
Cdd:cd14680     81 EIHTSSKEERNNWMRLIQEAV 101
PH_ARHGEF2 cd13393
Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called ...
2232-2343 1.40e-42

Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called GEF-H1, acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275428  Cd Length: 116  Bit Score: 152.34  E-value: 1.40e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2232 RKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDqKSTVISLKKLIVREVAHEEKGLFLISmgMKDP 2311
Cdd:cd13393      1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLIS--AAPP 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1911189734 2312 EMVEVHASSKEERNSWIQIIQDTINTLNRDED 2343
Cdd:cd13393     78 EMYEVHAASRDDRNTWMRLIQQTVKTCPSREE 109
PH_RhoGEF cd13329
Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...
2235-2335 1.34e-41

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275411  Cd Length: 109  Bit Score: 148.95  E-value: 1.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYV--------FASLDQKSTVISLKKLIVREVAHEEKGLFLISM 2306
Cdd:cd13329      1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80
                           90       100
                   ....*....|....*....|....*....
gi 1911189734 2307 GMKDPEMVEVHASSKEERNSWIQIIQDTI 2335
Cdd:cd13329     81 SKNGPQMYELVANSSSERKTWIKHISDAV 109
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
2001-2192 9.07e-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: 132.04  E-value: 9.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2001 VIYELMQTELHHIRTLKIMSDVYSRGMMTELLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESlvdksernflIRRM 2080
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLLLEELLKEWIS----------IQRI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2081 GDVLVNQFSGenaerlKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSAVVRRLGIPECILLVTQRITKYPVLF 2160
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1911189734 2161 QRILQCTKDNEVEQQDLAQSLSLVKEVIGAVD 2192
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) ...
1794-1849 8.40e-31

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: 116.67  E-value: 8.40e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1911189734 1794 LNGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHKGCRESLASCAKVKMK 1849
Cdd:cd20878      5 LNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60
PH_ARHGEF2_18_like cd15789
rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling ...
2235-2332 3.98e-29

rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275432  Cd Length: 102  Bit Score: 113.32  E-value: 3.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMKD-PEM 2313
Cdd:cd15789      1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLISASPDGmPEM 80
                           90
                   ....*....|....*....
gi 1911189734 2314 VEVHASSKEERNSWIQIIQ 2332
Cdd:cd15789     81 YELKVQKPKDKNTWIQTIR 99
C1_p190RhoGEF-like cd20815
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...
1795-1846 1.00e-15

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: 73.22  E-value: 1.00e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1911189734 1795 NGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHK-GCRESLASCAKV 1846
Cdd:cd20815      2 NTHQFVPVSFSNSTKCDVCSKPLTNKPALQCENCSVNVHDsSCKDQLADCTKF 54
C1_p190RhoGEF cd20876
protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange ...
1793-1852 5.10e-14

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


Pssm-ID: 410426  Cd Length: 61  Bit Score: 68.62  E-value: 5.10e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1793 LLNGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHKGCRESLASCakVKMKQPK 1852
Cdd:cd20876      4 QSNGHQFVTGSFSGPTLCVVCDKPVTGKELLQCSNCTVNVHKGCKESAPPC--TKKLQDK 61
C1_ARHGEF2 cd20877
protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange ...
1795-1852 1.80e-13

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: 67.30  E-value: 1.80e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1911189734 1795 NGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHKGCRESLASCAKVKMKQPK 1852
Cdd:cd20877      4 NGHLFTTITVSGTTMCSACNKSITAKEALICPTCNVTIHNRCKDTLPNCTKVKQKQQK 61
PH_PRG cd13391
PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called ...
2225-2336 1.10e-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: 67.75  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2225 FAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDQKST---VISLKKLIVRE 2293
Cdd:cd13391     18 FKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSDSKQTfspVLKLNSVLIRS 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1911189734 2294 VAHEEKGLFLISMGMKDPEMVEVHASSKEERNSWIQIIQDTIN 2336
Cdd:cd13391     98 VATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAVR 140
PH_LARG cd13390
Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; ...
2229-2331 3.27e-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: 66.16  E-value: 3.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2229 DLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDQKST---VISLKKLIVREVAHE 2297
Cdd:cd13390     20 DLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKHTfspVIKLNTVLVRQVATD 99
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1911189734 2298 EKGLFLISMGMKDPEMVEVHASSKEERNSWIQII 2331
Cdd:cd13390    100 NKAFFVISMSENGAQIYELVAQTVSEKTVWQDLI 133
PH_p115RhoGEF cd14679
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...
2225-2338 6.73e-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: 64.86  E-value: 6.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2225 FAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDQK---STVISLKKLIVRE 2293
Cdd:cd14679      1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLkchsrtttPTPDGKqmlSPIIKLNSAMTRE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1911189734 2294 VAHEEKGLFLISMGMKDPEMVEVHASSKEERNSWIQIIQDTINTL 2338
Cdd:cd14679     81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2616-2857 1.34e-10

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 66.01  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDACQVRGRL 2695
Cdd:COG3883    138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2696 SGTGQVRGRLSGTGPPVRYGAACQVRGRLSGTGPPVRYGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGS 2775
Cdd:COG3883    218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2776 GMGPPVRYGSGLGPPDRYGSGPGPPVRYGSGPGPPVRYGSGLGPPVRYGSGLGPPVRYGSGTGPPVRYGGRLSGTGPPVG 2855
Cdd:COG3883    298 AASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVG 377

                   ..
gi 1911189734 2856 SG 2857
Cdd:COG3883    378 GA 379
PHA03247 PHA03247
large tegument protein UL36; Provisional
673-1338 5.13e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.73  E-value: 5.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  673 GALAAEHRDDTDTPPAGSATGPPHAQPPPTAVCPEGP--QAEAVTPD-PVGDTQEDVGFC---PLEVL--DTAGQtrrvn 744
Cdd:PHA03247  2476 GAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPsrLAPAILPDePVGEPVHPRMLTwirGLEELasDDAGD----- 2550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  745 sqtpltnalevelhPHAVFPKADREPVPDQAVTSGRtfsPAGSPGSESVTkddalslvpSQNEKGTATPQPltaTDGRDG 824
Cdd:PHA03247  2551 --------------PPPPLPPAAPPAAPDRSVPPPR---PAPRPSEPAVT---------SRARRPDAPPQS---ARPRAP 2601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  825 GDWSDPDKQPledgAAGLPTPPAALDPQPSMGNASPGGFggEQEDPCLPAAPEvrnmeggtdssRLHVAEAPLASDSSLT 904
Cdd:PHA03247  2602 VDDRGDPRGP----APPSPLPPDTHAPDPPPPSPSPAAN--EPDPHPPPTVPP-----------PERPRDDPAPGRVSRP 2664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  905 EEGKSPVVPESSAAQGQGDRLKAvicsstkedtLPPGALREEQGTDPPRQESPGDQGEPGAAACSRDKALEHSGSRGTPS 984
Cdd:PHA03247  2665 RRARRLGRAAQASSPPQRPRRRA----------ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA 2734
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  985 ACLNAetkhneevAPPASllteggaAQSPVPPGAGLATDAGQEAVGAEQSSSPRLPGLSPdASRAPNCNGPSAVDGVTDA 1064
Cdd:PHA03247  2735 LPAAP--------APPAV-------PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP-PRRLTRPAVASLSESRESL 2798
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1065 QAQGETAACEASGNMALDVAVGNALQGTAEARGTALSHSAQDLPVPEVLLRQENGIQVLPGALPDKGGTNLQGAAAPETV 1144
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP 2878
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1145 --PPVWEKGKPegahrSCSRDASEGAQMNDTRSVPLQPTAKELPAEaglsTSDDKAPSRDRGAPPDPHAVSAEAGHLPES 1222
Cdd:PHA03247  2879 arPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQP----QPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1223 AdSIEEAASRIVDAVIEHVRASGALLTEGDISHLPPSSPA---ETGPGAGQPES-----ASAGKVH--------ALLSGE 1286
Cdd:PHA03247  2950 A-GAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREApasSTPPLTGHSLSrvsswASSLALHeetdpppvSLKQTL 3028
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 1287 TPP-------AGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPDTKADDEVDF 1338
Cdd:PHA03247  3029 WPPddtedsdADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQF 3087
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2328-2682 5.29e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.71  E-value: 5.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2328 IQIIQDTINTLNRDEDE---GIPSENEEEKKMLDTKARELKEQLQQKDQQILLLLEEKEGIFRDMMECSTPLPEEysptv 2404
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----- 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2405 sprilfrsNTEEALKGGPLMKSAINEVEILQGLVSGSLGGPLGQAVSSPVGQEGTVGPVSLPRRAETFGGfdsHQMNASK 2484
Cdd:COG4717    240 --------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2485 GGDKEEGDDGQDLRRTESDSGLKKGGNANLAFMLKRNNEQVIQSIVHLHELLSTLQgvvlQQDSYIEDQRLLlsERALAR 2564
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----LEELEQEIAALL--AEAGVE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2565 SSSRPSSLVEQEKQRslERQRQDLADLQRQQAQHLEERRRREREWEareralqerEARLAQREEEVQRGQQDLERDREAL 2644
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1911189734 2645 LQKRGAYQYDLERLRAAQK--QLEREQEQLKRDAERLGQR 2682
Cdd:COG4717    452 REELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2494-2728 7.97e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 7.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2494 GQDLRRTESDSGLKKGGNANLAFMLKRNNEQVIQSIVHLHELLSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLV 2573
Cdd:COG1196    294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEAreraLQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQY 2653
Cdd:COG1196    374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911189734 2654 DLERLRAAQKQLEREQEQLKRDAERLGQ--RQLERDACQVRGRLSGTGQVRGRLSGTGPPVRYGAACQVRGRLSGTG 2728
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2544-2688 2.95e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2544 LQQDSYIEDQRLLLSERALARsssrpsslvEQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREARL 2623
Cdd:COG1196    286 AQAEEYELLAELARLEQDIAR---------LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2624 AQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDA 2688
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
939-1360 5.38e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 5.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  939 PPGALREEQGTDPPRQESPGDQGEPGAAAcsrdkALEHSGSRGTPSACLNAETKHNEEVAPPASLLTEGGAAQSPVPPGA 1018
Cdd:PRK07764   387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAA-----APAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1019 GLATDAGQEAVGAEQSSSPRLPGLSPDASRAPncngpsavdgvtDAQAQGETAACEASGNMALDVA---VGNALQGTAEA 1095
Cdd:PRK07764   462 PSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAA------------PAAPAAPAAPAGADDAATLRERwpeILAAVPKRSRK 529
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1096 RGTALSHSAQDLPV--PEVLLRQENGiqVLPGALPDKGGT-NLQGAAAPE---TVPPVWEKGKPEGAHRSCSRDASEGAQ 1169
Cdd:PRK07764   530 TWAILLPEATVLGVrgDTLVLGFSTG--GLARRFASPGNAeVLVTALAEElggDWQVEAVVGPAPGAAGGEGPPAPASSG 607
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1170 MNDTRSVPLQPTAKELPAEAglstSDDKAPSRDRGAPPDPHAVSAEAGHLPESADsiEEAASRIVDAVIEHVRASGALLT 1249
Cdd:PRK07764   608 PPEEAARPAAPAAPAAPAAP----APAGAAAAPAEASAAPAPGVAAPEHHPKHVA--VPDASDGGDGWPAKAGGAAPAAP 681
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1250 EGDISHLPPSSPAETGPGAGQPESASAGKVHALLSGETPPAGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPD 1329
Cdd:PRK07764   682 PPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPP 761
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1911189734 1330 TKADDEVDFLRNPRQSSVSEEAAGGDTAAPS 1360
Cdd:PRK07764   762 PAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2517-2683 6.98e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 6.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2517 MLKRNNEQVIQSIVHLHELLSTLQGVVLQQDSYIEDQ-RLLLSERALARSSSRPSSLveQEKQRSLERQRQDLADLQRQQ 2595
Cdd:COG4717     58 LFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQeELEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELE 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2596 A--QHLEERRRREREWEARERALQEREARLAQREEEVQRGQQDLER------------------DREALLQKRGAYQYDL 2655
Cdd:COG4717    136 AleAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleqlslateeelqdlaeELEELQQRLAELEEEL 215
                          170       180
                   ....*....|....*....|....*...
gi 1911189734 2656 ERLRAAQKQLEREQEQLKRDAERLGQRQ 2683
Cdd:COG4717    216 EEAQEELEELEEELEQLENELEAAALEE 243
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2235-2336 7.57e-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: 52.55  E-value: 7.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  2235 LVRDGSVFLK--NAAGRLKEVQAVLLTDILVFLQEKDQKYVFAsldqKSTVISLKKLIVREVAH----EEKGLFLISMGm 2308
Cdd:smart00233    1 VIKEGWLYKKsgGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK----PKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75
                            90       100
                    ....*....|....*....|....*...
gi 1911189734  2309 kDPEMVEVHASSKEERNSWIQIIQDTIN 2336
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2532-2700 8.08e-08

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: 58.53  E-value: 8.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2532 LHELLSTLQGVVLQQDSYIED--QRLLLSERALARSSSRPSSLVEQ--EKQRSLERQRQDLADLQRQQAQHLEERRRRER 2607
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRleQQKQILRERLANLERQLEELEAQleELESKLDELAEELAELEEKLEELKEELESLEA 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2608 EWEARERALQEREARLAQREEEVQRgqqdLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERD 2687
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
                          170
                   ....*....|...
gi 1911189734 2688 ACQVRGRLSGTGQ 2700
Cdd:TIGR02168  435 LKELQAELEELEE 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2531-2692 1.94e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2531 HLHELLSTLQGVVLQQDSYIEDQRLLLSERALARSSsrpsslVEQEKQRsLERQRQDLADLQRQQAQHLEERRRREREWE 2610
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAE------LEELRLE-LEELELELEEAQAEEYELLAELARLEQDIA 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2611 ARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDACQ 2690
Cdd:COG1196    306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                   ..
gi 1911189734 2691 VR 2692
Cdd:COG1196    386 EE 387
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2518-2742 2.39e-07

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: 55.93  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2518 LKRNNEQVIQSIVHLHELLSTlQGVVLQQDSYIEDQRLLLSERALARSSSRPSSL--VEQEKQRSLERQRQDLADLQRQQ 2595
Cdd:COG4942     88 LEKEIAELRAELEAQKEELAE-LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALR 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2596 AQhleerrrrereweareraLQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRD 2675
Cdd:COG4942    167 AE------------------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911189734 2676 AERLGQRQLERDAcqvRGRLSGTGQVRGRLSgtgPPV------RYGAACQVRGRLSGtgppVRYGSGPGPPVR 2742
Cdd:COG4942    229 IARLEAEAAAAAE---RTPAAGFAALKGKLP---WPVsgrvvrRFGERDGGGGRNKG----IDIAAPPGAPVR 291
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
584-1029 4.47e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 55.76  E-value: 4.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  584 ASADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPFPRPQKDALPkekaetnsphlQSQNDQPPICSPPGDDQPQAASA 663
Cdd:PRK07764   390 GAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAP-----------APAPAPPSPAGNAPAGGAPSPPP 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  664 SGQSTVTSSGALAAehrddTDTPPAGSATGPPHAQPPPTAvcPEGPQAEAVTPDPVGDTQEDvGFCPlEVLDTAGQTRRV 743
Cdd:PRK07764   459 AAAPSAQPAPAPAA-----APEPTAAPAPAPPAAPAPAAA--PAAPAAPAAPAGADDAATLR-ERWP-EILAAVPKRSRK 529
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  744 NSQTPLTNALEVELHPHAV------------FPKADREPVPDQAVTS--GRTF------SPAGSPGSESVTKDDALSLVP 803
Cdd:PRK07764   530 TWAILLPEATVLGVRGDTLvlgfstgglarrFASPGNAEVLVTALAEelGGDWqveavvGPAPGAAGGEGPPAPASSGPP 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  804 SQNEKGTATPQPLTATDGRDGGDWSDPDKQPlEDGAAGLPTPPAALDPQPSMGNASPGGFGGEQEDPCLPAAPEVRNMEG 883
Cdd:PRK07764   610 EEAARPAAPAAPAAPAAPAPAGAAAAPAEAS-AAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPA 688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  884 GTDSSRlhVAEAPLASDSSLTEEGKSPVVPESSAAQGQGDRLKAVICSSTKEDTLPPGALREEQGTDPPRQESPGDQGEP 963
Cdd:PRK07764   689 APAAPA--GAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911189734  964 GAAacsrdkalehsgsrgtPSACLNAETKHNEEVAPPAsllteggAAQSPVPPGAGLATDAGQEAV 1029
Cdd:PRK07764   767 AAA----------------PAAAPPPSPPSEEEEMAED-------DAPSMDDEDRRDAEEVAMELL 809
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
1795-1845 4.73e-07

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


Pssm-ID: 410381  Cd Length: 58  Bit Score: 48.88  E-value: 4.73e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 1795 NGHAFSAIPIVGPISCSQCAKSFTS---KDAYACANCSAFVHKGCRESLAS-CAK 1845
Cdd:cd20831      4 NDHTFVATHFKGGPSCAVCNKLIPGrfgKQGYQCRDCGLICHKRCHVKVEThCPS 58
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2575-2688 5.45e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.52  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2575 QEKQRSLERQRQDLADLQRQqaqhleerrrrereweareraLQEREARLAQREEEVQRGQQDLERDREALLQKRGAY--- 2651
Cdd:COG4372     55 EQAREELEQLEEELEQARSE---------------------LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAeel 113
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1911189734 2652 QYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDA 2688
Cdd:COG4372    114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
C1_ARHGEF18-like cd20879
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
1795-1844 7.80e-07

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: 48.27  E-value: 7.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1795 NGHAFSAIPIVGPISCSQCAKSFTSKDAYACANCSAFVHKGCRESLASCA 1844
Cdd:cd20879      2 NGHQLVPGTFSSCATCSLCSKPLQNRNGLQCLNCAVNVHKNCKTLLTECS 51
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1966-2270 8.99e-07

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 8.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1966 DFESESKQLEAESWSRVVDSKFLKQQkkdaVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTELLF----EQQMVEKL 2041
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQE----IKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHV 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2042 FPCLDELISIHSQFfqrilerkKESLVDKSERNFLIRRMGDV------LVNQFSGENAERLkktYGKFCGQHNQSVNYfk 2115
Cdd:COG5422    533 FANINEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP-- 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2116 dlytkdkRFQAFVKKKMSSAVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQQDLAQSLSLVKEVIGAVDNKV 2195
Cdd:COG5422    600 -------NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFES 672
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2196 ASYEKKVRLNEIYTKTDSKSiMRMKSGQMFAKEDLKRKKLVRDGSVfLKNAAGRLKEVQAVLLTDILVFLQEKDQ 2270
Cdd:COG5422    673 GKAENRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAK-SKTDGSLRGDIQFFLLDNMLLFCKAKAV 745
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2545-2687 1.01e-06

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: 54.36  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2545 QQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREArla 2624
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE--- 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 2625 QREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQ-----KQLEREQEQLKR-DAERLGQRQLERD 2687
Cdd:pfam17380  432 ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRDRkRAEEQRRKILEKE 500
PHA03247 PHA03247
large tegument protein UL36; Provisional
591-1051 1.03e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  591 PASVPAAADGKMD----APLAHTGGAVSSADLPFPRPQKDALPKEKAETNSPHLQSQNDQPPICSPPGDDQPQAASASGq 666
Cdd:PHA03247  2557 PAAPPAAPDRSVPpprpAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAA- 2635
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  667 STVTSSGALAAEHRDDTDTPPAGS----------------ATGPPHAQPPPTAVCPEGPQAEAVTPDPVGDTQEDV--GF 728
Cdd:PHA03247  2636 NEPDPHPPPTVPPPERPRDDPAPGrvsrprrarrlgraaqASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAphAL 2715
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  729 CPLEVLDTAGQTRRVNSQTPLTNALEVELHPHAVFPKADRePVPDQAVTSG--RTFSPAGSPGS--ESVTKDDALSLVPS 804
Cdd:PHA03247  2716 VSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA-RPARPPTTAGppAPAPPAAPAAGppRRLTRPAVASLSES 2794
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  805 QNekgtATPQPLTATDGRDGGDWSDPDKQPLEDGAAGLPTPPAALDPQPSMgnasPGGFGGEQEDPCLPAAPevrnmegG 884
Cdd:PHA03247  2795 RE----SLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP----PPGPPPPSLPLGGSVAP-------G 2859
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  885 TDSSRLHVAEAPLASDSSlteegkSPVVPESSAAQGQGDRlkavicsSTKEDTLPPgaLREEQGTDPPRQESPGDQGEPG 964
Cdd:PHA03247  2860 GDVRRRPPSRSPAAKPAA------PARPPVRRLARPAVSR-------STESFALPP--DQPERPPQPQAPPPPQPQPQPP 2924
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  965 AAAcSRDKALEHSGSRGTPsaclnaetkhneevAPPASLLTEGGAAQSPVPPGAGLATDAGQEAVGAEQSSSPRLPGLSP 1044
Cdd:PHA03247  2925 PPP-QPQPPPPPPPRPQPP--------------LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP 2989

                   ....*..
gi 1911189734 1045 DASRAPN 1051
Cdd:PHA03247  2990 ASSTPPL 2996
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2235-2335 2.17e-06

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 48.71  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2235 LVRDGSVFLK--NAAGRLKEVQAVLLTDILVFLQEKDQKyvfaSLDQKSTVISLKKLIVREVAHEEKG----LFLISMGM 2308
Cdd:pfam00169    1 VVKEGWLLKKggGKKKSWKKRYFVLFDGSLLYYKDDKSG----KSKEPKGSISLSGCEVVEVVASDSPkrkfCFELRTGE 76
                           90       100
                   ....*....|....*....|....*...
gi 1911189734 2309 KDP-EMVEVHASSKEERNSWIQIIQDTI 2335
Cdd:pfam00169   77 RTGkRTYLLQAESEEERKDWIKAIQSAI 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2514-2695 3.13e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2514 LAFMLKRNNEQVIQSIVHLHELLSTLQGVVLQQDSYIEDQrlllsERALARSSSRPSSLVEQ--EKQRSLERQRQDLADL 2591
Cdd:COG4372     25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-----EEELEQARSELEQLEEEleELNEQLQAAQAELAQA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2592 QRQQAQhleerrrrereweareraLQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQ 2671
Cdd:COG4372    100 QEELES------------------LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
                          170       180
                   ....*....|....*....|....
gi 1911189734 2672 LKRDAERLGQRQLERDACQVRGRL 2695
Cdd:COG4372    162 LQEELAALEQELQALSEAEAEQAL 185
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2572-2690 4.23e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2572 LVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREARLAQREEEVQRGQQDLERDREALL------ 2645
Cdd:COG1196    218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellael 297
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1911189734 2646 -QKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDACQ 2690
Cdd:COG1196    298 aRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2552-2686 5.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 5.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2552 DQRLLLSERALARSSSRPSSLVEQEKQR--SLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREARLAQREEE 2629
Cdd:COG1196    643 AGRLREVTLEGEGGSAGGSLTGGSRRELlaALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1911189734 2630 VQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLgQRQLER 2686
Cdd:COG1196    723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL-EREIEA 778
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
2697-2883 6.07e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.57  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2697 GTGQVRGRLSGTGPPVRYGAacqvrgrlsgTGPPVRYGSGPGPPvryGSGPGPPVRYGSGPGPPVRYGSGPGPPVRYGSG 2776
Cdd:COG5164     97 GGTTPAGDGGATGPPDDGGA----------TGPPDDGGSTTPPS---GGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2777 MGPPVRYGSGLGPPDRYGSGpGPPVRYGSGPGPPVrygSGLGPPvrygsglGPPVrygsgtgpPVRYGGRLSGTGPPVGS 2856
Cdd:COG5164    164 STTPPGPGGSTTPPDDGGST-TPPNKGETGTDIPT---GGTPRQ-------GPDG--------PVKKDDKNGKGNPPDDR 224
                          170       180
                   ....*....|....*....|....*..
gi 1911189734 2857 GAACRVRGRLSGTGPSVRYGGPRQKGP 2883
Cdd:COG5164    225 GGKTGPKDQRPKTNPIERRGPERPEAA 251
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2511-2677 6.47e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 6.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2511 NANLAFMLKRNNEQVIQSIVHLHELLSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRsLERQRQDLAD 2590
Cdd:COG3206    203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQ-LAELEAELAE 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2591 LQRQ-QAQHleerrrrereweARERALQEREARL-AQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQL--- 2665
Cdd:COG3206    282 LSARyTPNH------------PDVIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpel 349
                          170
                   ....*....|..
gi 1911189734 2666 EREQEQLKRDAE 2677
Cdd:COG3206    350 EAELRRLEREVE 361
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
583-1359 7.27e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 7.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  583 DASADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPfprpqKDALPKEKAETNSPHLQSQNDQPPICSPPGDDQPQAAS 662
Cdd:PHA03307    13 AAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAE-----LAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRST 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  663 ASGQSTVTSSGALAAEHRDDTDTPPAGSATGP--PHAQPPPTAVCPEGPQAEAVTPDPVGDTQEDVgFCPLEVLDTAGQT 740
Cdd:PHA03307    88 PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPtpPPASPPPSPAPDLSEMLRPVGSPGPPPAASPP-AAGASPAAVASDA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  741 RRVNSQTPLTNALEVELHP-----HAVFPKADREPVPDQAVTSGRTFSPAGSPGSESVTKDDALSLVPSqNEKGTATPQP 815
Cdd:PHA03307   167 ASSRQAALPLSSPEETARApssppAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGAS-SSDSSSSESS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  816 LTATDGRD--GGDWSDPDKQPLEDGAAGLPTPPAAlDPQPSMGNASPGGFGGEQED------PCLPAAPEVRNMEGGTDS 887
Cdd:PHA03307   246 GCGWGPENecPLPRPAPITLPTRIWEASGWNGPSS-RPGPASSSSSPRERSPSPSPsspgsgPAPSSPRASSSSSSSRES 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  888 SrlhvAEAPLASDSSLTEEGKSPVVPESSAAQGQGDRlKAVICSSTKEDTlPPGALREEQGTDPPRQESPGDQGEPGAAA 967
Cdd:PHA03307   325 S----SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPP-PPADPSSPRKRP-RPSRAPSSPAASAGRPTRRRARAAVAGRA 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  968 CSRDKALEHSGSRGTPSACLNAETkhNEEVAPPASLLTEGG--------------------------------------- 1008
Cdd:PHA03307   399 RRRDATGRFPAGRPRPSPLDAGAA--SGAFYARYPLLTPSGepwpgspppppgrvrygglgdsrpglwdapevreaaary 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1009 -AAQSPVPPGAGLATDAGQ--------------EAVGAEQSssPRLPGlsPDA---------SRAPNCNGpSAVDG---- 1060
Cdd:PHA03307   477 eASPGPVPVYVPEMGDSAKqyaalvrllytpdrEAMGWLQN--PKLTG--PDQaldqfcqkkFQAPRGSG-SFITGsvar 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1061 ----VTDAQAQGE-------TAACEASGN-----------MALDVAVGNALQ-GTAEARGTALSHSAQDLPVP------- 1110
Cdd:PHA03307   552 pvphIGDAMAAGNalwalphAAAAVAMSRrydraqkgfllQSLRRAYAPMAYpENAADTGAGAAAPAPAAPRPdaaaagg 631
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1111 ---------------------EVLLRQENGiqvlPGALPDKGgtnlqgAAAPETVPPVWEK--GKPEGAHRSCS--RDAS 1165
Cdd:PHA03307   632 asarplreladacvlacravlEALLEGPDG----LSAVPGLA------FPRPACPPRALEAcpARLESWLRELRdlRDAV 701
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1166 EGAQMNDTRSVPLQPTAKELPAEAGLSTSDDKAPSrdrgAPPDPHAVSAEAGHLpESADSIEEAASRIVDAVIEHVRASG 1245
Cdd:PHA03307   702 YLARLRGDLPVAGGREERVAAVRAVSLVARTVAPL----VRYSPRRARARASAW-DITDALFSNPSLVPAKLAEALALLE 776
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1246 ALLTEGDISHLPPSSPAETGPGAGQPESASAGKVHAllSGETPPAGSSREETPGSPAGCSAGREEPEKIIPPVP------ 1319
Cdd:PHA03307   777 PAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAA--SRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPArssess 854
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|
gi 1911189734 1320 GPEPATEMPDTKADDEVDFLRNPRQSSVSEEAAGGDTAAP 1359
Cdd:PHA03307   855 KSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAA 894
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1093-1437 9.12e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 9.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1093 AEARGTALSHSAQDLPVPEVLLRQENGiqVLPGALPDKGGTNLQGAAAPETVPPVWEKGKPEGAHRSCSRDAsegaqmND 1172
Cdd:PHA03307    15 AEGGEFFPRPPATPGDAADDLLSGSQG--QLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANES------RS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1173 TRSVPLQPTAKELPAEAGLSTsddkAPSRDRGAPPDPHAVSAEAghlPESADSIEEAASRIVDAVIEHVRASGAlltegd 1252
Cdd:PHA03307    87 TPTWSLSTLAPASPAREGSPT----PPGPSSPDPPPPTPPPASP---PPSPAPDLSEMLRPVGSPGPPPAASPP------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1253 ISHLPPSSPAETGPGAGQPESASAgkvhaLLSGETPPAGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPDTKA 1332
Cdd:PHA03307   154 AAGASPAAVASDAASSRQAALPLS-----SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1333 DDEVDFLRNPRQSSVSEEAA-GGDTAAPSGTRQGLKTQTINRESWCTIEPCADAASllAPPQSPVSFSECENFLGVGLGR 1411
Cdd:PHA03307   229 ADDAGASSSDSSSSESSGCGwGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGP--ASSSSSPRERSPSPSPSSPGSG 306
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1911189734 1412 ECAPT-----EGELKRESGSDSDLFHSPSED 1437
Cdd:PHA03307   307 PAPSSprassSSSSSRESSSSSTSSSSESSR 337
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2527-2695 1.01e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2527 QSIVHLHELLSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQ------------RSLERQR-----QDLA 2589
Cdd:COG4913    262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERlearldalreelDELEAQIrgnggDRLE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2590 DLQRQQAQHLEERRRREREWEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQ 2669
Cdd:COG4913    342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
                          170       180
                   ....*....|....*....|....*...
gi 1911189734 2670 EQLKRDAERLGQRQ--LERDACQVRGRL 2695
Cdd:COG4913    422 RELEAEIASLERRKsnIPARLLALRDAL 449
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2537-2687 1.32e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2537 STLQGVVLqqdsYIEDQRLLLSERALARSSSRPSSLVEQEkqrsLERQRQDLADLQRQQAQHleerrrrereweareRAL 2616
Cdd:COG4717     37 STLLAFIR----AMLLERLEKEADELFKPQGRKPELNLKE----LKELEEELKEAEEKEEEY---------------AEL 93
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911189734 2617 QEREARLAQREEEVQRGQQDLERDREALLQKRGAYQyDLERLRAAQKQLEREQEQLKRDAERLGQ-RQLERD 2687
Cdd:COG4717     94 QEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEELEERLEElRELEEE 164
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
731-1078 1.34e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  731 LEVLDTAGQTRRVNSQTPLTNALEVELHPHAVFPKADRE---PVPDQAVTSGRTFSPAGSPGSESVTKDDA--LSLVPSQ 805
Cdd:PHA03307    11 IEAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAElaaVTVVAGAAACDRFEPPTGPPPGPGTEAPAneSRSTPTW 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  806 NEKGTATPQPLTATDGRDGGDWSDPDKQPLEDGAAGLPTPPAALDPQPSMGNASPGGFGGEQEDPCLPAAPEvrnmEGGT 885
Cdd:PHA03307    91 SLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV----ASDA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  886 DSSRlhvaeaPLASDSSLTEEGKSPVVPESSAAQGQGDRLKAvicsstkedtlppgalreeQGTDPPRQESPGDQGEPGA 965
Cdd:PHA03307   167 ASSR------QAALPLSSPEETARAPSSPPAEPPPSTPPAAA-------------------SPRPPRRSSPISASASSPA 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  966 AACSRDKALEHSGSRGTPSACLNAETKHNEEVAPPASLLTEGGAAQSPVPPGAGLATDAGQEAVGAEQSSSPRLPGLSPD 1045
Cdd:PHA03307   222 PAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS 301
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1911189734 1046 ASRAPNCNGPSAVDGVTDAQAQGETAACEASGN 1078
Cdd:PHA03307   302 SPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE 334
PHA03247 PHA03247
large tegument protein UL36; Provisional
1124-1398 1.40e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1124 PGALPDKGGTNLQGAAAPETVPPVWEKGKPEGAHRSCSRDASEGAQMNDTRSVPLQPTAKELPAEAGLSTSDDKAPSRDR 1203
Cdd:PHA03247  2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP 2706
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1204 GAPPDPHAVSAeAGHLPESADSIEEAASRIVDAVIEHVRASGALLTEGD-------ISHLPPSSPAETGPGAGQPESASA 1276
Cdd:PHA03247  2707 TPEPAPHALVS-ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGParparppTTAGPPAPAPPAAPAAGPPRRLTR 2785
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1277 GKVhALLSGETPPAGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPDTKADDEvdflrNPRQSSVSEE---AAG 1353
Cdd:PHA03247  2786 PAV-ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-----GPPPPSLPLGgsvAPG 2859
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1911189734 1354 GDTAAPSGTRQGLKTQTINReswctiEPCADAASLLAPPQSPVSF 1398
Cdd:PHA03247  2860 GDVRRRPPSRSPAAKPAAPA------RPPVRRLARPAVSRSTESF 2898
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2617-2686 1.92e-05

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: 46.45  E-value: 1.92e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2617 QEREARLAQREEEVQRGQQDLERDREA---LLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLG--QRQLER 2686
Cdd:pfam20492    9 QELEERLKQYEEETKKAQEELEESEETaeeLEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAeeKEQLEA 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2552-2688 2.73e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2552 DQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREARLAQREEEVQ 2631
Cdd:COG1196    226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1911189734 2632 RGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDA 2688
Cdd:COG1196    306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2561-2702 2.83e-05

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: 49.26  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2561 ALARSSSRPSslvEQEKQRSLERQRQdLADLQRQQAQHleerrrrereweareralQEREARLAQREEEVQRGQQDLERD 2640
Cdd:pfam15558   31 ALAWEELRRR---DQKRQETLERERR-LLLQQSQEQWQ------------------AEKEQRKARLGREERRRADRREKQ 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2641 -------REALLQKRGAY-QYDLERLRAAQKQLEREQEQLKRDAERLGQRQLERDACQVRGRLSGTGQVR 2702
Cdd:pfam15558   89 viekesrWREQAEDQENQrQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKR 158
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
584-866 2.85e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.85  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  584 ASADDQSPASVPAAADGKMDAPLAHTGGAVSS--ADLPFPRPQKDALPKEKAETNSPHLQSQNDQPPICS-----PPGDD 656
Cdd:PRK07003   405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATAdrGDDAADGDAPVPAKANARASADSRCDERDAQPPADSgsasaPASDA 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  657 QPQAASASGQSTVTSSGALAAEHRDDTDTPPAGSATGPPHAQPPPTAVCPEGPQAEAVTPDPVGDTqedvgfCPLEVLDT 736
Cdd:PRK07003   485 PPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAA------AALDVLRN 558
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  737 AGQtrRVNSQTPLTNALEVElhPHAVFPKADREPVPDQAVtsgRTFSPAGSPGSESVTKDDALSLVPSQNEKGTATP--- 813
Cdd:PRK07003   559 AGM--RVSSDRGARAAAAAK--PAAAPAAAPKPAAPRVAV---QVPTPRARAATGDAPPNGAARAEQAAESRGAPPPwed 631
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911189734  814 ------QPLTATDGRDGGDW-------SDPDKQPLEDGAAGLPTPPAALDPQPSMGNASPGGFGGE 866
Cdd:PRK07003   632 ippddyVPLSADEGFGGPDDgfvpvfdSGPDDVRVAPKPADAPAPPVDTRPLPPAIPLDAIGFDGE 697
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2574-2686 4.99e-05

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: 48.38  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQY 2653
Cdd:pfam13868  115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE 194
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1911189734 2654 DLERLRAAQKQL--EREQEQLKRDAERLGQRQLER 2686
Cdd:pfam13868  195 KAQDEKAERDELraKLYQEEQERKERQKEREEAEK 229
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
484-718 5.15e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.08  E-value: 5.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  484 PETAEGAERGLRNPdATTQKKVLAAGERTKERLENSHVGAAGASHVKDTRQPVDKAMVP-NCVSATSSLDGETPA---ES 559
Cdd:PRK07003   360 PAVTGGGAPGGGVP-ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAaAATRAEAPPAAPAPPataDR 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  560 VLVLSHGGAPIEKTAETETSrcydASADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPFPRPQKDALPKEKAETNSPH 639
Cdd:PRK07003   439 GDDAADGDAPVPAKANARAS----ADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA 514
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  640 LQSQNDQPPICSPPGDDQPQAASASGQSTVTSSGALA-------AEHRDDTDTPPAGSATGPPHAQPPPTAVcPEGPQAE 712
Cdd:PRK07003   515 AASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAaldvlrnAGMRVSSDRGARAAAAAKPAAAPAAAPK-PAAPRVA 593

                   ....*.
gi 1911189734  713 AVTPDP 718
Cdd:PRK07003   594 VQVPTP 599
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
528-862 6.48e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.01  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  528 HVKDTRQPVDKAMVPNCVSATSSLDGETPAESVLVLSHGGAPIEKTAETETSRCYDASADDQSPAsvpAAADGKMDAPla 607
Cdd:PHA03307    43 LVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPT---PPGPSSPDPP-- 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  608 htgGAVSSADLPFPRPQKDALPKEKAETNSPHlqsqndqPPICSPPGDDQPQAASASGQSTVTSSGALAAEHRDDTDTPP 687
Cdd:PHA03307   118 ---PPTPPPASPPPSPAPDLSEMLRPVGSPGP-------PPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  688 AGSATGPPHAQPPPTAVCPEGP----QAEAVTPDPVGDTQEDVGfcPLEVLDTAGQTRRVNSQTPLTNALEVELHPHAVF 763
Cdd:PHA03307   188 SPPAEPPPSTPPAAASPRPPRRsspiSASASSPAPAPGRSAADD--AGASSSDSSSSESSGCGWGPENECPLPRPAPITL 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  764 PKADREPVPdqAVTSGRTFSPAGSPGSESVTKDDALSLVPSQNEKGTATPQPLTATDGRDGGDWSDPDKQPLEDGAAGLP 843
Cdd:PHA03307   266 PTRIWEASG--WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSP 343
                          330
                   ....*....|....*....
gi 1911189734  844 TPPAALDPQPSMGNASPGG 862
Cdd:PHA03307   344 GPSPSRSPSPSRPPPPADP 362
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2538-2686 6.49e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2538 TLQGVVLQQDSYIEDQRLLLSERALaRSSSRPsslveQEKQRSLERQRQDLADLQRQQAQhleerrrrereweareraLQ 2617
Cdd:COG4913    253 LLEPIRELAERYAAARERLAELEYL-RAALRL-----WFAQRRLELLEAELEELRAELAR------------------LE 308
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 2618 EREARLAQREEEVQrgqqdlERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLgQRQLER 2686
Cdd:COG4913    309 AELERLEARLDALR------EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARL-EALLAA 370
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
1797-1840 6.75e-05

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: 42.78  E-value: 6.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1911189734 1797 HAFSAIPIVGPISCSQCAKSFT-SKDAYACANCSAFVHKGCRESL 1840
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIKfGKKALKCKDCRVVCHPDCKDKL 47
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2518-2686 7.39e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 7.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2518 LKRNNEQVIQSIVHLHEL----------LSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQD 2587
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELekalaelrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2588 LADLQRQQAQHLeerrrrerewEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQydleRLRAAQKQLER 2667
Cdd:TIGR02168  759 LEAEIEELEERL----------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRE 824
                          170
                   ....*....|....*....
gi 1911189734 2668 EQEQLKRDAERLgQRQLER 2686
Cdd:TIGR02168  825 RLESLERRIAAT-ERRLED 842
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1797-1843 9.16e-05

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: 42.12  E-value: 9.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1797 HAFSAIPIVGPISCSQCAKSFTS--KDAYACANCSAFVHKGCRESLAS-C 1843
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWGlfKQGLKCSDCGLVCHKKCLDKAPSpC 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2523-2712 1.04e-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: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2523 EQVIQSIVHLHELLSTLQGVVLQQDSYIEDQRLLLSERALARSSSRpSSLVEQEKQrsLERQRQDLADLQRQQAQH---- 2598
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE-SRLEELEEQ--LETLRSKVAQLELQIASLnnei 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2599 LEERRRREREWEARERALQEREARLAQREE----EVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKR 2674
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1911189734 2675 DAERLGQRQ--LERDACQVRGRLSGTGQV---RGRLSGTGPPV 2712
Cdd:TIGR02168  483 ELAQLQARLdsLERLQENLEGFSEGVKALlknQSGLSGILGVL 525
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2545-2686 1.12e-04

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: 47.81  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2545 QQDSYIEDQRLLLS-ERALARsssrpssLVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREreweareralQEREARL 2623
Cdd:pfam17380  332 QAAIYAEQERMAMErERELER-------IRQEERKRELERIRQEEIAMEISRMRELERLQMER----------QQKNERV 394
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2624 AQrEEEVQRGQ--QDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQRQLER 2686
Cdd:pfam17380  395 RQ-ELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER 458
RNase_Y_N pfam12072
RNase Y N-terminal region;
2616-2686 1.19e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 45.65  E-value: 1.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRgayqydlERLRAAQKQLEREQEQLkrdaERLGQRQLER 2686
Cdd:pfam12072   80 LQRQERRLLQKEETLDRKDESLEKKEESLEKKE-------KELEAQQQQLEEKEEEL----EELIEEQRQE 139
PHA03247 PHA03247
large tegument protein UL36; Provisional
853-1448 1.35e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  853 PSMGNASPGGFGGEQEDPCLPAAPevrnmeggtdsSRLhvaeAPlasdSSLTEEGKSPVVPESSAAQGQGDRLKAVICSS 932
Cdd:PHA03247  2489 PFAAGAAPDPGGGGPPDPDAPPAP-----------SRL----AP----AILPDEPVGEPVHPRMLTWIRGLEELASDDAG 2549
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  933 TKEDTLPPGALreEQGTD---PPRQESPGDQGEPGAAACSRDKALEHSGSRGTPSAclnaETKHNEEVAPPASLLTEGGA 1009
Cdd:PHA03247  2550 DPPPPLPPAAP--PAAPDrsvPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVD----DRGDPRGPAPPSPLPPDTHA 2623
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1010 AQSPVPPGAGLATDAGQ-EAVGAEQSSSPRLPGLSPDASRAPNCNGPSAVDGVTdAQAQGET--AACEASGNMAlDVAVG 1086
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPhPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS-SPPQRPRrrAARPTVGSLT-SLADP 2701
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1087 NALQGTAEARGTALSHSAQDLPVPEVLLRQENGIQVLPGALPDKGGTNLQGAAAPETVPPVwekgkPEGAHRSCS-RDAS 1165
Cdd:PHA03247  2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPT-----TAGPPAPAPpAAPA 2776
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1166 EGAQmndtRSVPLQPTAKELPAEAGLSTSDDKAPSRDRGAPPDP--HAVSAEAGHLPESADSIEEAASRIVDAVIEHVRA 1243
Cdd:PHA03247  2777 AGPP----RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAalPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1244 SGALLTEGDISHLPPSSPAETGPGA---------GQPESASAGKVHAL--LSGETPPAGSSREETPGSPAGCSAGREEPE 1312
Cdd:PHA03247  2853 GGSVAPGGDVRRRPPSRSPAAKPAAparppvrrlARPAVSRSTESFALppDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1313 KIIPPVPGPEPATEMPDTKADDEVDFLRNPRQSSVseeaAGGDTAAPsgtRQGLKTQTINRESwctiePCADAASLLAPP 1392
Cdd:PHA03247  2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL----VPGRVAVP---RFRVPQPAPSREA-----PASSTPPLTGHS 3000
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1911189734 1393 QSPVSFSECEnflgVGLGRECAPTEGELKRESGSDSDLFHSpseDVDSIVFSKPEE 1448
Cdd:PHA03247  3001 LSRVSSWASS----LALHEETDPPPVSLKQTLWPPDDTEDS---DADSLFDSDSER 3049
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
452-671 1.61e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 46.90  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  452 AALPGVTLMESGPAPHFPAGEQEGRSTGDAGVPETAEGAErglrnpdattqkkvlAAGertkerlenshvGAAGASHVKD 531
Cdd:PRK13108   283 GALRGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGE---------------PNQ------------PDDVAEAVKA 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  532 TRQPVDKAMVPNCVSATSSLDGETPAESVlvlSHGGAPIEKTAETETSRcyDASADDQSPASVPAAADGkmdaplahtgg 611
Cdd:PRK13108   336 EVAEVTDEVAAESVVQVADRDGESTPAVE---ETSEADIEREQPGDLAG--QAPAAHQVDAEAASAAPE----------- 399
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  612 avSSADLPfpRPQKDALPKEKAETNSPHLQSQNDQPPICSPPGDDQPQAASASGQSTVTS 671
Cdd:PRK13108   400 --EPAALA--SEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSS 455
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2572-2687 1.71e-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: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2572 LVEQEKQRSLERQRQDLADLQ----RQQAqhleerrrrereweareraLQEREARLAQREEEVQRGQQDL-----ERDRE 2642
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLDEMmeeeRERA-------------------LEEEEEKEEERKEERKRYRQELeeqieEREQK 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1911189734 2643 ALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERlgQRQLERD 2687
Cdd:pfam13868   89 RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK--QRQLREE 131
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2574-2687 1.74e-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: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRSLERQRQDLADL-----QRQQAQHLEERRrrereweareralQEREARLAQREEEVQRGQQDLER------DRE 2642
Cdd:pfam13868  138 EQAEWKELEKEEEREEDErileyLKEKAEREEERE-------------AEREEIEEEKEREIARLRAQQEKaqdekaERD 204
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1911189734 2643 ALLQKRgaYQYDLER------LRAAQKQLEREQE------QLKRDAERLGQRQLERD 2687
Cdd:pfam13868  205 ELRAKL--YQEEQERkerqkeREEAEKKARQRQElqqareEQIELKERRLAEEAERE 259
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2575-2700 1.82e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2575 QEKQRSLERQRQDLADLQRQQAQHleerrRREREWEARERALQEREARLAQREEEVQRGQQDLERDRE-----ALLQKRg 2649
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDAL-----QERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlAALEEQ- 693
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1911189734 2650 ayqydLERLRAAQKQLEREQEQLKRDAERLGQR--QLERDACQVRGRLSGTGQ 2700
Cdd:COG4913    694 -----LEELEAELEELEEELDELKGEIGRLEKEleQAEEELDELQDRLEAAED 741
PRK12704 PRK12704
phosphodiesterase; Provisional
2616-2674 2.05e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 2.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLER-EQEQLKR 2674
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEElIEEQLQE 143
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
2576-2687 2.22e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.25  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2576 EKQRSLER---QRQDLADLQRQQAqhleerrrrerewearerALQEREARLAQREEEVQRGQQDLERDREA------LLQ 2646
Cdd:COG3096    279 ERRELSERaleLRRELFGARRQLA------------------EEQYRLVEMARELEELSARESDLEQDYQAasdhlnLVQ 340
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1911189734 2647 -------KRGAYQYDLE----RLRAAQKQLEREQEQLKRDAERLGQRQLERD 2687
Cdd:COG3096    341 talrqqeKIERYQEDLEelteRLEEQEEVVEEAAEQLAEAEARLEAAEEEVD 392
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1137-1360 2.38e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.77  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1137 GAAAPETVPPVWEKGKPEGAHRSCSRDASEGAQMNDTRSVPLQPTAKELPAEAGLSTSDDKAPSRDRGAPPDPHAVSAEA 1216
Cdd:PRK07003   365 GGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAAD 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1217 GHLPESADSIEEAASRIVDAVIEHVRASGALLTEGDISHLPPSSPAETGPGAGQPESASAGKVhallSGETPPAGSSREE 1296
Cdd:PRK07003   445 GDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAV----PDARAPAAASRED 520
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 1297 TPGSPAgcsagreEPEkiiPPVPGPEPATEMPDTK---ADDEVDFLRNP--RQSSVSEEAAGGdTAAPS 1360
Cdd:PRK07003   521 APAAAA-------PPA---PEARPPTPAAAAPAARaggAAAALDVLRNAgmRVSSDRGARAAA-AAKPA 578
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1073-1400 2.45e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1073 CEASGNMALDVAVGNALQGtaeaRGTALSHSAQDLpvpEVLLRQENGIQVLPGALPDKGG-----TNLQGAAAPETVPPV 1147
Cdd:PRK12323   260 ALAAEDGAALLAIADEMAG----RSLSFAGALQDL---ASLLQKIALAQVVPAAVQDDWPeaddiRRLAGRFDAQEVQLF 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1148 WE---KGKPEgahRSCSRDASEGAQMNDTRSVPLQPTakelpaeaglSTSDDKAPSRDRGAP--PDPHAVSAEAGHLPES 1222
Cdd:PRK12323   333 YQianLGRSE---LALAPDEYAGFTMTLLRMLAFRPG----------QSGGGAGPATAAAAPvaQPAPAAAAPAAAAPAP 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1223 ADSIEEAASRIVDAVIEHVRASGALLTEGDISHLPPSSPAETGPGAGQPESASAgKVHALLSGETPPAGSSREetPGSPA 1302
Cdd:PRK12323   400 AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRP--VAAAA 476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1303 GCSAGREEPEKIIPPVP-GPEPATEMPDTKADDEVDFLRNPRQSSVSEEAAGGDTAAPSGTRQGLKTQTINRESwctieP 1381
Cdd:PRK12323   477 AAAPARAAPAAAPAPADdDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPA-----P 551
                          330
                   ....*....|....*....
gi 1911189734 1382 CADAASLLAPPQSPVSFSE 1400
Cdd:PRK12323   552 RAAAATEPVVAPRPPRASA 570
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2542-2686 3.91e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.43  E-value: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2542 VVLQQdsYIEDQRLLLSE--RALARSSSRpsslveqekQRSLERQrqdLADLQRQQAQHleerrrrereweareralqER 2619
Cdd:COG1842     26 KMLDQ--AIRDMEEDLVEarQALAQVIAN---------QKRLERQ---LEELEAEAEKW-------------------EE 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911189734 2620 EARLAqreeeVQRGQQDLERdrEALLQKRgAYQYDLERLRAAQKQLEREQEQLKRDAERLgQRQLER 2686
Cdd:COG1842     73 KARLA-----LEKGREDLAR--EALERKA-ELEAQAEALEAQLAQLEEQVEKLKEALRQL-ESKLEE 130
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
2557-2695 4.09e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 45.66  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2557 LSERA-LARSSSRPSSLVEQEKQR------SLERQRQDL--------ADLQRQQAQHLEERRRREREWEARERALQEREA 2621
Cdd:pfam07888   40 LQERAeLLQAQEAANRQREKEKERykrdreQWERQRRELesrvaelkEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2622 RLAQREEEVQRgQQDLERDREALLQKRGAYQYDLERLRAAQKQL---------EREQEQLKRDAERLGQRQLERDACQVR 2692
Cdd:pfam07888  120 LLAQRAAHEAR-IRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaERKQLQAKLQQTEEELRSLSKEFQELR 198

                   ...
gi 1911189734 2693 GRL 2695
Cdd:pfam07888  199 NSL 201
Zwint pfam15556
ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ...
2626-2706 4.09e-04

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


Pssm-ID: 464766 [Multi-domain]  Cd Length: 252  Bit Score: 44.97  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2626 REEEVQRGQQDLerdREALLQKRGAYQYDLERLRAAQKQLEREQEQlkrdaeRLgqRQLERDACQVRGRLSGTGQVRGRL 2705
Cdd:pfam15556   92 KMEEAQRKRAQL---QEALEQLQAKKQMAMEKLRTAQKQWQLQQEK------HL--QHLAEVSAEVRERQTGTQQELERL 160

                   .
gi 1911189734 2706 S 2706
Cdd:pfam15556  161 Y 161
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2574-2695 4.17e-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: 4.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRsleRQRQDLADLQRQQAQHLeerrrrereweareralQEREARLAQREEE-----VQRGQQDLERDR---EALL 2645
Cdd:pfam13868  226 EAEKKA---RQRQELQQAREEQIELK-----------------ERRLAEEAEREEEefermLRKQAEDEEIEQeeaEKRR 285
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2646 QKRGAYQYDLERL---RAAQKQLEREQEQlkRDAERLGQRQLERDAC--QVRGRL 2695
Cdd:pfam13868  286 MKRLEHRRELEKQieeREEQRAAEREEEL--EEGERLREEEAERRERieEERQKK 338
FliJ pfam02050
Flagellar FliJ protein;
2575-2675 4.79e-04

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 42.27  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2575 QEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQER-----EARLAQREEEVQRGQQDLERDREALL---Q 2646
Cdd:pfam02050    8 AEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAELRNYQAfisqlDEAIAQQQQELAQAEAQVEKAREEWQearQ 87
                           90       100
                   ....*....|....*....|....*....
gi 1911189734 2647 KRGAYQYDLERLRAAQKQLEREQEQLKRD 2675
Cdd:pfam02050   88 ERKSLEKLREREKKEERKEQNRREQKQLD 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2349-2680 6.66e-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: 45.43  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2349 ENEEEKKMLDTKARELKEQLQQKDQQILLLLEEKEGIFRDMMECSTPLPEEYSptvspRILFRSNTEEALkggpLMKSAI 2428
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-----DLARLEAEVEQL----EERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2429 NEVEILQGLVS-GSLGGPLGQAvsSPVGQEGTVGPVSLPRRAETFggfdSHQMNASKGGDKEEGDDGQDLRRTESDSGLK 2507
Cdd:TIGR02168  752 LSKELTELEAEiEELEERLEEA--EEELAEAEAEIEELEAQIEQL----KEELKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2508 KGGNANLAFMLKRNNEQVIQSIVHLHELLSTLQGVVLQQDSYIEDQRLLLsERALARSSSRPSSLVEQEKQRSLERQRQD 2587
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2588 LADLQRQQAQHLeerrrrereweareraLQEREARLAQREEEVQRGQQDLERDREALlqkRGAYQYDLE-------RLRA 2660
Cdd:TIGR02168  905 ELESKRSELRRE----------------LEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEeaealenKIED 965
                          330       340
                   ....*....|....*....|
gi 1911189734 2661 AQKQLEREQEQLKRDAERLG 2680
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKELG 985
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2550-2686 6.67e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2550 IEDQRLLLSERALARSSSRPSSLveQEKQRSLERQRQDLADLQRQ--QAQHLEERRRREREWEARERALQEREARLAQRE 2627
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEY--AELQEELEELEEELEELEAEleELREELEKLEKLLQLLPLYQELEALEAELAELP 145
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 2628 EEVQRGQQDLERDREALLQKRGAyqydLERLRAAQKQLEREQEQLKRDAERLGQRQLER 2686
Cdd:COG4717    146 ERLEELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEE 200
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
652-966 7.08e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.23  E-value: 7.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  652 PPGDDQPQAASASGQSTVTSSGALAAehrddTDTPPAGSATGPPHAQPPPTAVCPEGPqAEAVTPdPVGDTQedvgfcpl 731
Cdd:PRK07003   368 PGGGVPARVAGAVPAPGARAAAAVGA-----SAVPAVTAVTGAAGAALAPKAAAAAAA-TRAEAP-PAAPAP-------- 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  732 eVLDTAGQTRRVNSQTPLTNALEVELHPHAVFPKADREPVPDQAVTSGRTFSPAGSPGSESVTKDDAlslVPSQNEKGTA 811
Cdd:PRK07003   433 -PATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAA---PSAATPAAVP 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  812 TPQPLTATDGRDggdwsdpdkqpledgAAGLPTPPAALDPQPSMGNASPGGFGGEQEdpclpAAPEV-RN--MEGGTDSS 888
Cdd:PRK07003   509 DARAPAAASRED---------------APAAAAPPAPEARPPTPAAAAPAARAGGAA-----AALDVlRNagMRVSSDRG 568
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  889 RLHVAEAPLASDSSLTEEGKSP----VVPESSAAQGQGDRLKAVICSStkedtlPPGAlrEEQGTDPPRQESPGDQGEPG 964
Cdd:PRK07003   569 ARAAAAAKPAAAPAAAPKPAAPrvavQVPTPRARAATGDAPPNGAARA------EQAA--ESRGAPPPWEDIPPDDYVPL 640

                   ..
gi 1911189734  965 AA 966
Cdd:PRK07003   641 SA 642
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1795-1847 8.41e-04

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 39.76  E-value: 8.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1911189734 1795 NGHAFSAIPIVGPISCSQCaKSFT----SKDAYACANCSAFVHKGCRESLAS-CAKVK 1847
Cdd:cd20835      8 NGHKFMATYLRQPTYCSHC-KDFIwgviGKQGYQCQVCTCVVHKRCHQLVVTkCPGNK 64
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
522-721 8.52e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 8.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  522 GAAGASHVKDTR-QPVDKAMVPNCVSATSSLDGETPAESVLVLSHGGAPIEKTAETETSRCYDASADDQS---------P 591
Cdd:PRK12323   371 GAGPATAAAAPVaQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASargpggapaP 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  592 ASVPAAADGKMDAPLAHTGGAVSSADLPFPRPQKDALPKEKAETNSPHLQsqnDQPPICSPPGDDQPQAASASGQSTVTS 671
Cdd:PRK12323   451 APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWE---ELPPEFASPAPAQPDAAPAGWVAESIP 527
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1911189734  672 SGALAAEHRD-DTDTPPAGSATGPPHAQPPPTAVCPEGPQAEAVTPDPVGD 721
Cdd:PRK12323   528 DPATADPDDAfETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFD 578
cyano_w_EgtBD TIGR04375
hercynine metabolism protein; Hercynine is the betaine (trimethylated amino group) form of ...
2552-2687 9.59e-04

hercynine metabolism protein; Hercynine is the betaine (trimethylated amino group) form of histidine. This protein occurs in a conserved four-gene cyanobacterial cassette along with a EgtD, the methyltransferase that converts histidine to hercynine as in ergothioneine biosynthesis, an EgtB homolog that is likely to attach some thiol (e.g. gamma-glutamyl-cysteine) through its sulfur to the hercynine imidazole ring, and a small protein of unknown function (TIGR04374). Members are distantly related to phage shock protein A (PspA).


Pssm-ID: 275168 [Multi-domain]  Cd Length: 154  Bit Score: 42.38  E-value: 9.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2552 DQRLLLSERALarsssrpsslveQEKQRSLERQRQDL---ADLQRQQAQHLeerrrrerewEARERALQER--EARLAQR 2626
Cdd:TIGR04375   23 DQDQLLREQHL------------QDRQQDLQRQRQQLqseAEELRRQLLTL----------AEEVRAWRERsqRARAAGA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911189734 2627 EEEVQRGQQDLerdrEALL-QKRGAYQyDLERLRAAQKQLEREQEQLKRDAERLGQRQLERD 2687
Cdd:TIGR04375   81 SDLAGRAEQHL----QSLMeQGRQLWQ-ELEALGRRFKEVEQQLAALKQQQKQPSGSSLDED 137
dnaA PRK14086
chromosomal replication initiator protein DnaA;
687-860 9.74e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 44.82  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  687 PAGSATGPPhAQPPPTAVCPEGPQAEAVTPDPVG------DTQEDVGFCPLEVLDTA-------GQTRRVNSQTPLTNAL 753
Cdd:PRK14086    87 TVDPSAGEP-APPPPHARRTSEPELPRPGRRPYEgyggprADDRPPGLPRQDQLPTArpaypayQQRPEPGAWPRAADDY 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  754 EVELHPHAVFPKADREPVPDQAVTSGRTFSPAG------SPGSESVTKDDALSLVPSQNEKGTATPQPLTATDGRDGGDW 827
Cdd:PRK14086   166 GWQQQRLGFPPRAPYASPASYAPEQERDREPYDagrpeyDQRRRDYDHPRPDWDRPRRDRTDRPEPPPGAGHVHRGGPGP 245
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1911189734  828 SDPDKQPLEDGAAGLPTPPAAlDPQPSMGNASP 860
Cdd:PRK14086   246 PERDDAPVVPIRPSAPGPLAA-QPAPAPGPGEP 277
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2551-2687 1.09e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.95  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2551 EDQRLLLSERALARSSSrpsslvEQEKQRSLERQ---RQDLADLQRQQAQhleerrrrerewearerALQEREARLAQRE 2627
Cdd:pfam05672   11 EAARILAEKRRQAREQR------EREEQERLEKEeeeRLRKEELRRRAEE-----------------ERARREEEARRLE 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2628 EEvqRGQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERlgQRQlERD 2687
Cdd:pfam05672   68 EE--RRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAER--QRQ-ERE 122
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2575-2688 1.09e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2575 QEKQRSLERQRQDLADLQRQQAQhleerrrrereweaRERALQEREARLAQRE---EEVQRGQQDLERDREALLQKR-GA 2650
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEK--------------LTEEISELEKRLEEIEqllEELNKKIKDLGEEEQLRVKEKiGE 298
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1911189734 2651 YQYDLERLRAAQKQLEREQEQLkrdAERLGQRQLERDA 2688
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDA---EERLAKLEAEIDK 333
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
701-876 1.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 44.70  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  701 PTAVCPEGPQAeAVTPDPVGDTqeDVGFCPLEVLDTAGQTRRVNSQTPLTNALEVELHPHAVFPKADREPVPDQAVTSG- 779
Cdd:PRK08691   380 PSAQTAEKETA-AKKPQPRPEA--ETAQTPVQTASAAAMPSEGKTAGPVSNQENNDVPPWEDAPDEAQTAAGTAQTSAKs 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  780 -RTFSPAGSPGSESVTKDDA--------LSLVPSQNE-KGTATPQPL-TATDGRDGGDWSDP------DKQPLEDGAAGL 842
Cdd:PRK08691   457 iQTASEAETPPENQVSKNKAadnetdapLSEVPSENPiQATPNDEAVeTETFAHEAPAEPFYgygfpdNDCPPEDGAEIP 536
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1911189734  843 PTPPAALDPQPSMG-----NASPGGFGGeqedPCLPAAP 876
Cdd:PRK08691   537 PPDWEHAAPADTAGggadeEAEAGGIGG----NNTPSAP 571
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2573-2685 1.27e-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: 43.75  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2573 VEQEKQRSLERQRQDLADLQRQQAQH--LEERRRREReweareralQEREARLAQREEEVQRgqqdlERDREALLQKRGA 2650
Cdd:pfam13868  178 IEEEKEREIARLRAQQEKAQDEKAERdeLRAKLYQEE---------QERKERQKEREEAEKK-----ARQRQELQQAREE 243
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1911189734 2651 YQYDLERLRAAQKQLERE------------QEQLKRDAERLGQRQLE 2685
Cdd:pfam13868  244 QIELKERRLAEEAEREEEefermlrkqaedEEIEQEEAEKRRMKRLE 290
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2534-2672 1.35e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2534 ELLSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARE 2613
Cdd:COG1196    637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911189734 2614 RALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQ----YDLERLRAAQKQLEREQEQL 2672
Cdd:COG1196    717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpepPDLEELERELERLEREIEAL 779
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
2522-2686 1.66e-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: 41.84  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2522 NEQVIQSIVHLHELLSTLQGVVLQQDSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSleRQRQDLADLQRQQAQHLEE 2601
Cdd:pfam08614    2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLA--QLREELAELYRSRGELAQR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2602 RRRREREWEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAY---QYDLERLRAAQKQLEREQEQLKRDAER 2678
Cdd:pfam08614   80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNqdlQDELVALQLQLNMAEEKLRKLEKENRE 159

                   ....*...
gi 1911189734 2679 LGQRQLER 2686
Cdd:pfam08614  160 LVERWMKR 167
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2531-2686 1.78e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2531 HLHELLSTLQGVVLQQDSYieDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQDL----ADLQRQQAQhLEERRRRE 2606
Cdd:COG4913    625 ELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAELEAELERLdassDDLAALEEQ-LEELEAEL 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2607 REWEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDL--ERLRAA---------QKQLEREQEQLKRD 2675
Cdd:COG4913    702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleERFAAAlgdaverelRENLEERIDALRAR 781
                          170
                   ....*....|.
gi 1911189734 2676 AERLgQRQLER 2686
Cdd:COG4913    782 LNRA-EEELER 791
mukB PRK04863
chromosome partition protein MukB;
2546-2699 1.86e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2546 QDSYIEDQRLLLSERALA-RSSSRPSSLVEQE----KQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQERE 2620
Cdd:PRK04863   495 WDVARELLRRLREQRHLAeQLQQLRMRLSELEqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2621 ARLAQREEEVQRGQQDLERDREALLQKRG---AYQYDLERLRAA---------------QKQLEREQE-QLKRDAERLGQ 2681
Cdd:PRK04863   575 SEARERRMALRQQLEQLQARIQRLAARAPawlAAQDALARLREQsgeefedsqdvteymQQLLERERElTVERDELAARK 654
                          170
                   ....*....|....*...
gi 1911189734 2682 RQLERdacQVRgRLSGTG 2699
Cdd:PRK04863   655 QALDE---EIE-RLSQPG 668
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2552-2686 2.05e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2552 DQRLLLSERALArsssrpsslVEQEKQRSLERQRQDLADLQRQQAQHleerrrrereweareraLQEREARLaqrEEEVQ 2631
Cdd:cd16269    190 DQALTEKEKEIE---------AERAKAEAAEQERKLLEEQQRELEQK-----------------LEDQERSY---EEHLR 240
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1911189734 2632 RGQQDLERDREALlqkrgayqydLERLRAAQKQLEREQEQLKRDAERLGQRQLER 2686
Cdd:cd16269    241 QLKEKMEEERENL----------LKEQERALESKLKEQEALLEEGFKEQAELLQE 285
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
883-1154 2.29e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  883 GGTDSSRLHVAEAPLASDSSLTEEGKSPVVPESSAAQGQGDRLKAVICSSTKEDTLPPgalreeQGTDPPRQESPGDQGE 962
Cdd:PRK07003   370 GGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP------AAPAPPATADRGDDAA 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  963 PGAAACSRDKALEHSGSRGTPSACLNAETKHNEEVAPPASllTEGGAAQSPVPPGAGLATDAGQEAVGAEQ-SSSPRLPG 1041
Cdd:PRK07003   444 DGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASD--APPDAAFEPAPRAAAPSAATPAAVPDARApAAASREDA 521
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1042 LSPDASRAPNCNGPSAVDGVTDAQAQGETAACEASGNMALDVAVGNALQGTAEARGTALSHSAQDLPVPEVllrqenGIQ 1121
Cdd:PRK07003   522 PAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRV------AVQ 595
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1911189734 1122 V-LPGALPDKGGTNLQGAA-APETV-----PPVWEKGKPE 1154
Cdd:PRK07003   596 VpTPRARAATGDAPPNGAArAEQAAesrgaPPPWEDIPPD 635
PHA03247 PHA03247
large tegument protein UL36; Provisional
584-911 2.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  584 ASADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPFPRPQKDALPKEKAETNSPHLQSQNDQPPICSPPGDDQPQAASA 663
Cdd:PHA03247  2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  664 SGQSTVTSSGALAAEHRDDTDTPPAGSATGPPHAQPPPTAVCPegPQAEAVTPDPVgdtqedvgfcPLEVLDTAGQTRRV 743
Cdd:PHA03247  2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP--PAASPAGPLPP----------PTSAQPTAPPPPPG 2844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  744 NSQTPLTNAlevelhpHAVFPKAD--REPVPDQAVTS---------GRTFSPAGSPGSESvtkddaLSLVPSQNEKgtaT 812
Cdd:PHA03247  2845 PPPPSLPLG-------GSVAPGGDvrRRPPSRSPAAKpaaparppvRRLARPAVSRSTES------FALPPDQPER---P 2908
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  813 PQPLTATDGRDGGDWSDPDKQPLEDGAAGLPTPPAALDPQPSMGNASPGGFGGEQEDPCLPAAPEV-RNMEGGTDSSRlh 891
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVpRFRVPQPAPSR-- 2986
                          330       340
                   ....*....|....*....|
gi 1911189734  892 vaEAPLASDSSLTEEGKSPV 911
Cdd:PHA03247  2987 --EAPASSTPPLTGHSLSRV 3004
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1016-1334 2.52e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1016 PGAGLATDAGQEAVGAEQSSSPR-LPGLSPDASRAPNCNGPSAVDGVTDA-QAQGETAACEASGNMALDVAVGNALQGTA 1093
Cdd:PRK07003   362 VTGGGAPGGGVPARVAGAVPAPGaRAAAAVGASAVPAVTAVTGAAGAALApKAAAAAAATRAEAPPAAPAPPATADRGDD 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1094 EARGTALSHSAQDLPVPEVLLRQENGIQVLPGALPdkggtnlQGAAAPETVPPVwekgkpegahrscsrdASEGAQMNDT 1173
Cdd:PRK07003   442 AADGDAPVPAKANARASADSRCDERDAQPPADSGS-------ASAPASDAPPDA----------------AFEPAPRAAA 498
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1174 RSVPLQPTAKELPAEAGLSTSDDKAPSrdrgAPPDPHAVSAEAGHLPESADSIEEAASRIVdaviehVRASGaLLTEGDI 1253
Cdd:PRK07003   499 PSAATPAAVPDARAPAAASREDAPAAA----APPAPEARPPTPAAAAPAARAGGAAAALDV------LRNAG-MRVSSDR 567
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 1254 SHLPPSSPAetgPGAGQPESASAGKVHALLSGETPPAGSSREETPGSPAGCSAGREEPEKIIPPVPGPEPATEMPDTkAD 1333
Cdd:PRK07003   568 GARAAAAAK---PAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPPPWEDIPPDDYVPLS-AD 643

                   .
gi 1911189734 1334 D 1334
Cdd:PRK07003   644 E 644
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2555-2682 2.59e-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: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2555 LLLSERALARSSSRpsslveQEKQRSLERQRQDLADLQRQQAQhleerrrREREWEARERALQEREARLAQREEEVQRGQ 2634
Cdd:COG4942      9 LLLALAAAAQADAA------AEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALE 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2635 QDLE--RDREALLQKRgayqydLERLRAAQKQLEREQEQLKRDAERLGQR 2682
Cdd:COG4942     76 QELAalEAELAELEKE------IAELRAELEAQKEELAELLRALYRLGRQ 119
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2558-2688 3.05e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2558 SERALARSSSRPSslvEQEKQRSLERQRQDLADLQRQQAQHleerrrrerewEARERALQEREARLAQREEEVQrgqqDL 2637
Cdd:TIGR02169  301 AEIASLERSIAEK---ERELEDAEERLAKLEAEIDKLLAEI-----------EELEREIEEERKRRDKLTEEYA----EL 362
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1911189734 2638 ERDREALLQKRGAYQYDLERLRAAQKQLE-------REQEQLKRDAERLGQRQLERDA 2688
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEFAETRDELKDYRekleklkREINELKRELDRLQEELQRLSE 420
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2566-2697 3.75e-03

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: 42.63  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2566 SSRPSSLVEQEKQRSLE--RQRQDLADLQRQQAQHLEERRRREREWEARERALQErEARL-AQREEEVQRGQQDLERDRE 2642
Cdd:pfam15709  333 ASRDRLRAERAEMRRLEveRKRREQEEQRRLQQEQLERAEKMREELELEQQRRFE-EIRLrKQRLEEERQRQEEEERKQR 411
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1911189734 2643 ALLQ---KRGAYQYDLERLRAAQKQLEREQEQLKR-DAERLGQRQLERDACQVRGRLSG 2697
Cdd:pfam15709  412 LQLQaaqERARQQQEEFRRKLQELQRKKQQEEAERaEAEKQRQKELEMQLAEEQKRLME 470
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2578-2686 4.27e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2578 QRSLERQRQDLADLQRQQAQhleerrrrereweareraLQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQYDLER 2657
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAE------------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
                           90       100
                   ....*....|....*....|....*....
gi 1911189734 2658 LRAAQKQLEREQEQLKRDAERLgQRQLER 2686
Cdd:COG4942     81 LEAELAELEKEIAELRAELEAQ-KEELAE 108
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
388-718 4.54e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  388 TKEEEAEPTVDSETRSNPQScLQSMSDCGEKGKEGLPPCEIGNEETQAKSATLATAQGS--LSSGGAALPGVTLMESGPA 465
Cdd:PHA03307    64 RFEPPTGPPPGPGTEAPANE-SRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPppASPPPSPAPDLSEMLRPVG 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  466 PHFPAGEQEGRSTGDAGVPETAEGAE-RGLRNPDATTQKKVLAAGERTKERlenshVGAAGASHVKDTRQPVDKAMVPNC 544
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASsRQAALPLSSPEETARAPSSPPAEP-----PPSTPPAAASPRPPRRSSPISASA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  545 VSATSSlDGETPAESVLVLSHGGAPIE--KTAETETSRCYDAS-ADDQSPASVPAAADGKMDAPLAHTGGAVSSADLPFP 621
Cdd:PHA03307   218 SSPAPA-PGRSAADDAGASSSDSSSSEssGCGWGPENECPLPRpAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  622 RPQKDALPKEKAETNSPHLQSQNDQPPicspPGDDQPQAASASGQSTVTSSGAlaAEHRDDTDTPPAGSATGPPHAQPPP 701
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSSSSSSRE----SSSSSTSSSSESSRGAAVSPGP--SPSRSPSPSRPPPPADPSSPRKRPR 370
                          330
                   ....*....|....*..
gi 1911189734  702 TAVCPEGPQAEAVTPDP 718
Cdd:PHA03307   371 PSRAPSSPAASAGRPTR 387
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
584-721 4.65e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  584 ASADDQSPASVPAAADGKMDAPLAHTGGAvssadlPFPRPqkdalPKEKAETNSPHLQSQndqPPICSPPGDDQPQAASA 663
Cdd:PRK14951   374 APAEKKTPARPEAAAPAAAPVAQAAAAPA------PAAAP-----AAAASAPAAPPAAAP---PAPVAAPAAAAPAAAPA 439
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1911189734  664 SGQSTVTSSGALAAEHRDDTDTPPAGSATGPPHAQPPPTAvcPEGPQAEAVTPDPVGD 721
Cdd:PRK14951   440 AAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAP--AAAPAAARLTPTEEGD 495
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
2574-2671 4.86e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 39.89  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRSLERQRQDLADLQRQQAQhleerrrrereWEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQ- 2652
Cdd:COG2882     35 AEEQLEQLEQYREEYEQRLQQKLQ-----------QGLSAAQLRNYQQFIARLDEAIEQQQQQVAQAEQQVEQARQAWLe 103
                           90       100
                   ....*....|....*....|....*...
gi 1911189734 2653 -------YD--LERLRAAQKQLEREQEQ 2671
Cdd:COG2882    104 arqerkaLEklKERRREEERQEENRREQ 131
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2572-2687 5.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2572 LVEQEKQ-RSLERQRQDLADLQRQQAQhleerrrrereweareraLQEREARLA--------QREEEVQRGQQDLERDRE 2642
Cdd:COG1196    195 LGELERQlEPLERQAEKAERYRELKEE------------------LKELEAELLllklreleAELEELEAELEELEAELE 256
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1911189734 2643 ALLQKRGAYQYDLERLRAAQKQLEREQEQLKRDAERLGQR--QLERD 2687
Cdd:COG1196    257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElaRLEQD 303
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2574-2686 6.59e-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: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRSLERQRQDLAD------LQRQQAQhleerrrrerewearERALQEREarlaQREEEVQRGQQDLERDREALLQK 2647
Cdd:pfam13868   64 EEERKEERKRYRQELEEqieereQKRQEEY---------------EEKLQERE----QMDEIVERIQEEDQAEAEEKLEK 124
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1911189734 2648 RGAYQYDLE---RLRAAQKQLEREQEQ---------LKRDAERLGQRQLER 2686
Cdd:pfam13868  125 QRQLREEIDefnEEQAEWKELEKEEEReederileyLKEKAEREEEREAER 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2616-2708 6.99e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 6.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2616 LQEREARLAQREEEVQRGQQDLERDREALLQKRGAYQ------YDLERLRAAQKQLEREQEQLKR------DAERLgQRQ 2683
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeysWDEIDVASAEREIAELEAELERldassdDLAAL-EEQ 693
                           90       100
                   ....*....|....*....|....*
gi 1911189734 2684 LErdacQVRGRLSGTGQVRGRLSGT 2708
Cdd:COG4913    694 LE----ELEAELEELEEELDELKGE 714
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2574-2687 7.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2574 EQEKQRSLERQRQDLADLQRQQAQHLEERRRREREWEARERALQEREARLAQREEEVQRGQQDLERDREALLQKRgayqy 2653
Cdd:COG4372    110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA----- 184
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1911189734 2654 dLERLRAAQKQLEREQEQLKRDAERLGQRQLERD 2687
Cdd:COG4372    185 -LDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
PHA03378 PHA03378
EBNA-3B; Provisional
582-905 8.19e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  582 YDASADDQSPASVPAAADGKMDAPLAhtggavssADLPFPRPQKDALPKEKaetnsPHLQSQNDQPPICSPPGDDQPQAA 661
Cdd:PHA03378   674 YQPSPTGANTMLPIQWAPGTMQPPPR--------APTPMRPPAAPPGRAQR-----PAAATGRARPPAAAPGRARPPAAA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  662 SASGQSTVTSSGALAAEHRDDTDTPPAGSATGPPHAQPPPTAvcPEGPQAE---AVTPDPvgdtQEDVGFCPLEVLDTAG 738
Cdd:PHA03378   741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQA--PPAPQQRprgAPTPQP----PPQAGPTSMQLMPRAA 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  739 QTRRVNSQTPLTNALEVEL---HPHAVFPKADREPVPdqavtSGRTFSPAGSPGSESVTKDDAL--SLVPSQNEKGTATP 813
Cdd:PHA03378   815 PGQQGPTKQILRQLLTGGVkrgRPSLKKPAALERQAA-----AGPTPSPGSGTSDKIVQAPVFYppVLQPIQVMRQLGSV 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734  814 QPLTATDGRDGgdwsdPDKQPLEDGAAGlPTPP------------AALDPQPSMGNASPG--------GFGGEQEDPCLP 873
Cdd:PHA03378   890 RAAAASTVTQA-----PTEYTGERRGVG-PMHPtdippskraktdAYVESQPPHGGQSHSfsviwenvSQGQQQTLECGG 963
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1911189734  874 AAPEVRNMEGGTDSSrlhvAEAPLASDSSLTE 905
Cdd:PHA03378   964 TTKQERAMLGTGDIA----VSSPSSSETSNDE 991
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2518-2683 8.77e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 8.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2518 LKRNNEQVIQSIVHLHELLSTLQG--VVLQQ--DSYIEDQRLLLSERALARSSSRPSSLVEQEKQRSLERQRQDLADLQR 2593
Cdd:TIGR00618  713 IEEYDREFNEIENASSSLGSDLAAreDALNQslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2594 QqaqhleerrrrereweareraLQEREARLAQREEEVQR----GQQDLERDREALLQKRGAYQYDLERLRAAQKQLEREQ 2669
Cdd:TIGR00618  793 L---------------------REEDTHLLKTLEAEIGQeipsDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
                          170
                   ....*....|....
gi 1911189734 2670 EQlkrDAERLGQRQ 2683
Cdd:TIGR00618  852 LK---YEECSKQLA 862
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
2237-2331 9.13e-03

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 37.91  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2237 RDGSVFLKNAAGRL--KEVQAVLLTDILVFLQEKDQKYVfasldQKSTVISLKKLIVREVAHEEKGLFLISMGMKDPEMV 2314
Cdd:cd00821      1 KEGYLLKRGGGGLKswKKRWFVLFEGVLLYYKSKKDSSY-----KPKGSIPLSGILEVEEVSPKERPHCFELVTPDGRTY 75
                           90
                   ....*....|....*..
gi 1911189734 2315 EVHASSKEERNSWIQII 2331
Cdd:cd00821     76 YLQADSEEERQEWLKAL 92
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2570-2683 9.87e-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: 40.90  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911189734 2570 SSLVEQEKQRSLERQrqdLADLQRQQAQHLEERRRREREWEARERALQEREARLAQREEEVQRGQQDLerdreALLQKRg 2649
Cdd:COG4942     14 AAAAQADAAAEAEAE---LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-----AALEAE- 84
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1911189734 2650 ayqydLERLRAAQKQLEREQEQLKRD-AERLGQRQ 2683
Cdd:COG4942     85 -----LAELEKEIAELRAELEAQKEElAELLRALY 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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