transcriptional regulator ICP4; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   164 RRSPERFVDTSRGRSPPRNAGSfigIPREPSPPRNGRRMIGSARDRSPPRSDGRIIGSPRDISP-PRDA-GRRFGPPRDQ 241
Cdd:PHA03307  196 STPPAAASPRPPRRSSPISASA---SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlPRPApITLPTRIWEA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   242 SPPRNAGRVTGSPRDRSPPRNAGRRMGPPRDQSPPRSTRSFSSNSRALSPARNMGSYMSSSQGFSPPRNPRSYMGSSRGS 321
Cdd:PHA03307  273 SGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPS 352

                  ....
gi 22330538   322 PPRS 325
Cdd:PHA03307  353 PSRP 356

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 22330538 402 SVDGFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDL-IIPMGPRKKILQAI 454
Cdd:cd09487   1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELgITSPGHRKKILRAI 54

transcriptional regulator ICP4; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   164 RRSPERFVDTSRGRSPPRNAGSfigIPREPSPPRNGRRMIGSARDRSPPRSDGRIIGSPRDISP-PRDA-GRRFGPPRDQ 241
Cdd:PHA03307  196 STPPAAASPRPPRRSSPISASA---SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlPRPApITLPTRIWEA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   242 SPPRNAGRVTGSPRDRSPPRNAGRRMGPPRDQSPPRSTRSFSSNSRALSPARNMGSYMSSSQGFSPPRNPRSYMGSSRGS 321
Cdd:PHA03307  273 SGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPS 352

                  ....
gi 22330538   322 PPRS 325
Cdd:PHA03307  353 PSRP 356

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 22330538 402 SVDGFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDL-IIPMGPRKKILQAI 454
Cdd:cd09487   1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELgITSPGHRKKILRAI 54

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22330538 407 LNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDL-IIPMGPRKKILQAIASLPTR 460
Cdd:cd09520  11 LAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELgITAFGARRKMLLAISELNKR 65

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 22330538 406 FLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDLIIPMGPRKKILQAIA 455
Cdd:cd09517   8 FLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIA 57

SAM domain (Sterile alpha motif);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22330538   402 SVDGFLNSIGLGKYSLAFKREEVD-MTTIKQMKESDLKDL-IIPMGPRKKILQAIASL 457
Cdd:pfam07647   8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLgITSVGHRRKILKKIQEL 65

SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 22330538 407 LNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDLIIPMGPRKKI 450
Cdd:cd09584  16 LEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKI 59

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22330538 400 PLSVdgFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDLIIPMGPRKKILQAI 454
Cdd:cd09586   4 PLEV--FLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDAC 56

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22330538 401 LSVDGFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDL-IIPMGPRKKILQAIASL 457
Cdd:cd09524   6 FSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIgINAYGHRHKLIKGVERL 63

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22330538 403 VDGFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDLIIP-MGPRKKILQAIASL 457
Cdd:cd09507  10 VGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITkVGHVKRILQAIKDL 65

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   117 PPRSLDTRPRMAEPrDRPLSSSRTA-RGSSQMISSSSSHPAWALEDLRRRSPERFVDTSRGRSPPRNAGSFIGIPREPSP 195
Cdd:PHA03247 2551 PPPPLPPAAPPAAP-DRSVPPPRPApRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP 2629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   196 PRNGR--RMIGSARDRSPPRSDGRIIGSPRDISPPRDAGRRFGPPRDQSPPRNAGRvtGSPRDRSPPRNAGRRMGPPRDQ 273
Cdd:PHA03247 2630 SPSPAanEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSLADPPPPPPT 2707

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 22330538   274 SPPRSTRSFSSNSRALSPARNMGSYMSSSQGFSPPRNP 311
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVP 2745

transcriptional regulator ICP4; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   112 SRSEQPPRSLDTRPRMAEPRDRPLSSSRTAR-GSSQMISSSSSHPAWALEDLRRRSPERFVDTSRGRSPPRNAGSFIGIP 190
Cdd:PHA03307  216 SASSPAPAPGRSAADDAGASSSDSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330538   191 REPSPPRNGRRMIGSARDRSPPRSDGRIIGSP---RDISPPRDAGRRFGPPRDQSPPRNAGRvtgSPRDRSPPRNAGRRM 267
Cdd:PHA03307  296 PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSstsSSSESSRGAAVSPGPSPSRSPSPSRPP---PPADPSSPRKRPRPS 372

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 22330538   268 GPPRDQSPPRSTRSFSSNSRALSPARNMGSYMSSSQGFSPPRNPRSYMGSSRGSPPR 324
Cdd:PHA03307  373 RAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330538 398 DEPLSVDGFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDLIIPM-GPRKKILQAIASL 457
Cdd:cd09534   1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKvGDRIRLLRAIKSL 61

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 22330538 403 VDGFLNSIGLGKYSLAFKREEVDMTTIKQMKESDLKDL-IIPMGPRKKILQAI 454
Cdd:cd09533   2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMgITSVGHRLTILKAV 54

SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22330538 403 VDGFLNSIGLG-KYSLAFKREEVDMTTIKQMKESDLKDLIIPMGPrkkILQAIASL 457
Cdd:cd09528   8 VKQWLIEDLIDkKYAEILYEEEVTGAVLKELTEEDLVDMGLPHGP---ALLIIHSF 60