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Conserved domains on  [gi|1331917220|gb|PNJ65142|]
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SAMD15 isoform 1 [Pongo abelii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 544-610 6.10e-39

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


:

Pssm-ID: 188929  Cd Length: 67  Bit Score: 137.84  E-value: 6.10e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331917220 544 LNWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTRELLEIE 610
Cdd:cd09530     1 LSWDTEDVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIRELLGIE 67
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 215-413 2.25e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.46  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 215 DFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEP-PEETQPEVPEEMQ 293
Cdd:NF033839  269 DAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPqPEKPKPEVKPQLE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 294 RKATEEKGT-ELPE-QTKPDFPDHKPRKSTDENVPEPLEEIKLEFPEEESRKPNEETILE---QSEMMKPESPEEIKKSN 368
Cdd:NF033839  349 TPKPEVKPQpEKPKpEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPEKPK 428

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1331917220 369 EEKNPQPPEETGLVLPQEINPQVEEKTQIKPTEEKILELPDETKP 413
Cdd:NF033839  429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP 473
 
Name Accession Description Interval E-value
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 544-610 6.10e-39

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 137.84  E-value: 6.10e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331917220 544 LNWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTRELLEIE 610
Cdd:cd09530     1 LSWDTEDVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIRELLGIE 67
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 545-608 1.87e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 54.22  E-value: 1.87e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331917220  545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSN-LPQMGITNFEDMKAISRHTRELLE 608
Cdd:smart00454   3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 545-606 2.94e-09

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 53.43  E-value: 2.94e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331917220 545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTREL 606
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 215-413 2.25e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.46  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 215 DFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEP-PEETQPEVPEEMQ 293
Cdd:NF033839  269 DAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPqPEKPKPEVKPQLE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 294 RKATEEKGT-ELPE-QTKPDFPDHKPRKSTDENVPEPLEEIKLEFPEEESRKPNEETILE---QSEMMKPESPEEIKKSN 368
Cdd:NF033839  349 TPKPEVKPQpEKPKpEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPEKPK 428

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1331917220 369 EEKNPQPPEETGLVLPQEINPQVEEKTQIKPTEEKILELPDETKP 413
Cdd:NF033839  429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP 473
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 208-426 5.42e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.61  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 208 APEQTKPDFLSEKPGESLEETDLQPPKMTK-------------PEIPEETQRESTEKKRTEPPEQARPE---FPEKEPRK 271
Cdd:PTZ00449  548 KPGETKEGEVGKKPGPAKEHKPSKIPTLSKkpefpkdpkhpkdPEEPKKPKRPRSAQRPTRPKSPKLPElldIPKSPKRP 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 272 SSEEASLEPPEETQPEVPEEMQRKATeEKGTELPEQTKPDF-PDHKPR---------KSTDENVPEPLEEIKLEFPEEES 341
Cdd:PTZ00449  628 ESPKSPKRPPPPQRPSSPERPEGPKI-IKSPKPPKSPKPPFdPKFKEKfyddyldaaAKSKETKTTVVLDESFESILKET 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 342 RKPNEETILEQSEMMKPESPeeikkSNEEKNPQPPEETGLVLPQEI---NPQVEEKTQIKPTEEKILE---LPDETKPRE 415
Cdd:PTZ00449  707 LPETPGTPFTTPRPLPPKLP-----RDEEFPFEPIGDPDAEQPDDIeffTPPEEERTFFHETPADTPLpdiLAEEFKEED 781

                         250
                  ....*....|.
gi 1331917220 416 THVEFSKEDRP 426
Cdd:PTZ00449  782 IHAETGEPDEA 792
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 198-419 5.19e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.45  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  198 RVQHEETGLEAPEQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEAS 277
Cdd:TIGR00927  635 VAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEE 714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  278 LEPPEETQPEVPEEMQRKATEEKGTELPEQTKPDFP-DHKPRKSTDENVPEPLEEIKLEFPEEESRKpneETILEQSEMM 356
Cdd:TIGR00927  715 VEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEgKHEVETEGDRKETEHEGETEAEGKEDEDEG---EIQAGEDGEM 791

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331917220  357 KPESPEEIKKSNEEKNPQPPEETGLVLPQEINPQVEEKTQIKpTEEKILELPDETKPRETHVE 419
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG-EQELNAENQGEAKQDEKGVD 853
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 210-451 6.79e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 210 EQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEP-PEETQPEV 288
Cdd:NF033839  286 EPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPqPEKPKPEV 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 289 PEEMQRKATE---EKGTELPEqTKPDFPDHKPRKSTDENVPEPLEEIKLEFPEEE---SRKPNEETILEQSEMMKPESPE 362
Cdd:NF033839  366 KPQPEKPKPEvkpQPETPKPE-VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPEKPKPEVKP 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 363 EIKKSNEEKNPQPPEETGLVLPQEINPQVEEKTQI-KPTEEKILELPDETKPRETHvEFSKEDRPEPIKSKYSVGNDELE 441
Cdd:NF033839  445 QPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPeKPKPDNSKPQADDKKPSTPN-NLSKDKQPSNQASTNEKATNKPK 523

                         250
                  ....*....|
gi 1331917220 442 HHEPKRGKLS 451
Cdd:NF033839  524 KSLPSTGSIS 533
 
Name Accession Description Interval E-value
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 544-610 6.10e-39

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 137.84  E-value: 6.10e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331917220 544 LNWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTRELLEIE 610
Cdd:cd09530     1 LSWDTEDVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIRELLGIE 67
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 550-602 4.57e-11

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.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 58.40  E-value: 4.57e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1331917220 550 EVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRH 602
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRA 53
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 545-608 1.87e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 54.22  E-value: 1.87e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331917220  545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSN-LPQMGITNFEDMKAISRHTRELLE 608
Cdd:smart00454   3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 545-606 2.94e-09

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 53.43  E-value: 2.94e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331917220 545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTREL 606
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
545-607 3.32e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.43  E-value: 3.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331917220 545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLI-HVNCSNLPQMGITNFEDMKAISRHTRELL 607
Cdd:pfam07647   3 SWSLESVADWLRSIGLEQYTDNFRDQGITGAELLlRLTLEDLKRLGITSVGHRRKILKKIQELK 66
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 545-606 1.25e-08

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.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 51.64  E-value: 1.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331917220 545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTREL 606
Cdd:cd09507     4 NWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 543-606 1.29e-07

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-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-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 48.79  E-value: 1.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331917220 543 HLnWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTREL 606
Cdd:cd09575     3 HL-WGTEEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 550-591 1.51e-07

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.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 48.47  E-value: 1.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1331917220 550 EVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGIT 591
Cdd:cd09533     1 DVADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGIT 42
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
 546-606 5.17e-07

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.


Pssm-ID: 188975  Cd Length: 65  Bit Score: 47.27  E-value: 5.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331917220 546 WDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTREL 606
Cdd:cd09576     5 WGTDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 546-595 2.44e-06

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.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 45.28  E-value: 2.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331917220 546 WDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFED 595
Cdd:cd09534     1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGD 50
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 546-607 2.19e-05

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 42.69  E-value: 2.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331917220 546 WDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTRELL 607
Cdd:cd09506     5 WTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKLL 66
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 215-413 2.25e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.46  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 215 DFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEP-PEETQPEVPEEMQ 293
Cdd:NF033839  269 DAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPqPEKPKPEVKPQLE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 294 RKATEEKGT-ELPE-QTKPDFPDHKPRKSTDENVPEPLEEIKLEFPEEESRKPNEETILE---QSEMMKPESPEEIKKSN 368
Cdd:NF033839  349 TPKPEVKPQpEKPKpEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPEKPK 428

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1331917220 369 EEKNPQPPEETGLVLPQEINPQVEEKTQIKPTEEKILELPDETKP 413
Cdd:NF033839  429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP 473
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 546-592 2.46e-05

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 42.30  E-value: 2.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1331917220 546 WDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITN 592
Cdd:cd09566     2 LDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTS 48
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 208-426 5.42e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.61  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 208 APEQTKPDFLSEKPGESLEETDLQPPKMTK-------------PEIPEETQRESTEKKRTEPPEQARPE---FPEKEPRK 271
Cdd:PTZ00449  548 KPGETKEGEVGKKPGPAKEHKPSKIPTLSKkpefpkdpkhpkdPEEPKKPKRPRSAQRPTRPKSPKLPElldIPKSPKRP 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 272 SSEEASLEPPEETQPEVPEEMQRKATeEKGTELPEQTKPDF-PDHKPR---------KSTDENVPEPLEEIKLEFPEEES 341
Cdd:PTZ00449  628 ESPKSPKRPPPPQRPSSPERPEGPKI-IKSPKPPKSPKPPFdPKFKEKfyddyldaaAKSKETKTTVVLDESFESILKET 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 342 RKPNEETILEQSEMMKPESPeeikkSNEEKNPQPPEETGLVLPQEI---NPQVEEKTQIKPTEEKILE---LPDETKPRE 415
Cdd:PTZ00449  707 LPETPGTPFTTPRPLPPKLP-----RDEEFPFEPIGDPDAEQPDDIeffTPPEEERTFFHETPADTPLpdiLAEEFKEED 781

                         250
                  ....*....|.
gi 1331917220 416 THVEFSKEDRP 426
Cdd:PTZ00449  782 IHAETGEPDEA 792
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 546-606 8.32e-05

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 41.10  E-value: 8.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331917220 546 WDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRHTREL 606
Cdd:cd09512     7 WSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSDRSLLKKKLKEL 67
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 90-377 1.82e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  90 KSKRDIPSETQPGIPQKVKWETSREMGEFFKDLEAPMDETHEE----SDLEPPVEAKPNVTEDVFLESAMETDPDPVPPT 165
Cdd:PTZ00449  631 KSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEkfydDYLDAAAKSKETKTTVVLDESFESILKETLPET 710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 166 ETMSEVLGATVREINLELLEEETEPgvPEESLRVQHEETGLEAPEQTKPDFLSEKPGESlEETDLQPPKMTKPEIPEETQ 245
Cdd:PTZ00449  711 PGTPFTTPRPLPPKLPRDEEFPFEP--IGDPDAEQPDDIEFFTPPEEERTFFHETPADT-PLPDILAEEFKEEDIHAETG 787

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 246 RESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEPPEETQPEVPEEMQRKATEEKGTELPEQTKPDFPDHKPRKSTDENV 325
Cdd:PTZ00449  788 EPDEAMKRPDSPSEHEDKPPGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDASGKIVKLKRSKSFDDLTTVEEAEEMG 867

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331917220 326 PEP----LEEIKLEFPEEESRKPNEETILEQSEMMKPESPEEIKKSNEEKNPQPPE 377
Cdd:PTZ00449  868 AEArkivVDDDGTEADDEDTHPPEEKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPD 923
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 238-422 4.10e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.62  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  238 PEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEPPEETQPEVPEEMQRKATEEKGTELPEQTKPDFpDHKP 317
Cdd:PTZ00341   948 EEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEY-DEEN 1026

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  318 RKSTDENVPEPLEEIKLEFPE--EESRKPNEETILEQSEMMKPESPEEIKKSNEEKN-PQPPEETGLVLPQEINPQVEEK 394
Cdd:PTZ00341  1027 VEEVEENVEEYDEENVEEIEEnaEENVEENIEENIEEYDEENVEEIEENIEENIEENvEENVEENVEEIEENVEENVEEN 1106

                          170       180       190
                   ....*....|....*....|....*....|
gi 1331917220  395 TQIKPTE--EKILELPDETKPRETHVEFSK 422
Cdd:PTZ00341  1107 AEENAEEnaEENAEEYDDENPEEHNEEYDE 1136
PTZ00121 PTZ00121
MAEBL; Provisional
 194-466 5.07e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  194 EESLRVQHEETGLEAPEQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPE---FPEKEPR 270
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeaKKAEEDK 1674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  271 KSSEEASLEPPEETQPEvpEEMQRKATEEKGTE-LPEQTKPDFPDHKPRKSTDENVPEPLEEIKLEfpEEESRKPNEETI 349
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAA--EALKKEAEEAKKAEeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKE--AEEDKKKAEEAK 1750

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  350 LEQSEMMKpesPEEIKKSNEEKNPQPPEETGLVLPQEINPqvEEKTQIKPTEEKILELPDETkprETHVEFSKEDRPEPI 429
Cdd:PTZ00121  1751 KDEEEKKK---IAHLKKEEEKKAEEIRKEKEAVIEEELDE--EDEKRRMEVDKKIKDIFDNF---ANIIEGGKEGNLVIN 1822

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1331917220  430 KSKYSVGNDELEHHEPKRGKLSLSDEFRKEYYALGSI 466
Cdd:PTZ00121  1823 DSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNE 1859
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 198-419 5.19e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.45  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  198 RVQHEETGLEAPEQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEAS 277
Cdd:TIGR00927  635 VAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEE 714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  278 LEPPEETQPEVPEEMQRKATEEKGTELPEQTKPDFP-DHKPRKSTDENVPEPLEEIKLEFPEEESRKpneETILEQSEMM 356
Cdd:TIGR00927  715 VEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEgKHEVETEGDRKETEHEGETEAEGKEDEDEG---EIQAGEDGEM 791

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331917220  357 KPESPEEIKKSNEEKNPQPPEETGLVLPQEINPQVEEKTQIKpTEEKILELPDETKPRETHVE 419
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG-EQELNAENQGEAKQDEKGVD 853
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 243-444 5.62e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.24  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  243 ETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEPPEETQPEVPEEMQRKATEEKGTELPEQTKPDFPDHKPRKSTD 322
Cdd:PTZ00341   929 KNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVE 1008

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  323 ENVPEPLEEiKLEFPEEESRKPNEETILEQSEMMKPESPEEIKKSNEEKNPQPPEETGLVLPQEINPQVEEKTQiKPTEE 402
Cdd:PTZ00341  1009 ENVEENIEE-NVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIE-ENVEE 1086

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1331917220  403 KILELPDETKPR-----ETHVEFSKEDRPEPIKSKYSVGNDElEHHE 444
Cdd:PTZ00341  1087 NVEENVEEIEENveenvEENAEENAEENAEENAEEYDDENPE-EHNE 1132
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 210-451 6.79e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 210 EQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEP-PEETQPEV 288
Cdd:NF033839  286 EPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPqPEKPKPEV 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 289 PEEMQRKATE---EKGTELPEqTKPDFPDHKPRKSTDENVPEPLEEIKLEFPEEE---SRKPNEETILEQSEMMKPESPE 362
Cdd:NF033839  366 KPQPEKPKPEvkpQPETPKPE-VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPEKPKPEVKP 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 363 EIKKSNEEKNPQPPEETGLVLPQEINPQVEEKTQI-KPTEEKILELPDETKPRETHvEFSKEDRPEPIKSKYSVGNDELE 441
Cdd:NF033839  445 QPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPeKPKPDNSKPQADDKKPSTPN-NLSKDKQPSNQASTNEKATNKPK 523

                         250
                  ....*....|
gi 1331917220 442 HHEPKRGKLS 451
Cdd:NF033839  524 KSLPSTGSIS 533
PTZ00121 PTZ00121
MAEBL; Provisional
 202-427 7.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  202 EETGLEAPEQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARP-----EFPEKEPRKSSEEA 276
Cdd:PTZ00121  1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakkadEAKKAEEAKKADEA 1539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  277 SLEPPEETQPEVPE-EMQRKATEEKGTELPEQTKPDFPDHKPRKSTDENVPEPLEEIKLEFPEEESRKPNEETILEQSEM 355
Cdd:PTZ00121  1540 KKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331917220  356 MKPES---PEEIKKSNEEKNPQPPEEtglVLPQEINPQVEEKTQIKPTEEKILELPDETKPRETHVEFSKEDRPE 427
Cdd:PTZ00121  1620 IKAEElkkAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 545-626 8.83e-04

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 38.47  E-value: 8.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 545 NWDPEEVAEW-ISQLGFPQYKECFITNFISGrklihvncSNLPQMGITNFEDMKAIsrhtrelLEIEEPLFKRSISLPYR 623
Cdd:cd09504     4 NWTVEDTVEWlVNSVELPQYVEAFKENGVDG--------SALPRLAVNNPSFLTSV-------LGIKDPIHRQKLSLKAM 68


                  ...
gi 1331917220 624 DII 626
Cdd:cd09504    69 DVV 71
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 545-609 9.42e-04

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 38.05  E-value: 9.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331917220 545 NWDPEEVAEWISQLGFPQYKECFITNFISGRKLIHVNCSNLPQ-MGITNFEDMKaisRHTRELLEI 609
Cdd:cd09501     3 LWSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQdLGMSSGLLRK---RFLRELVEL 65
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 232-403 9.52e-04

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 41.60  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 232 PPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASLEPPEETQPEVPEEMQRKAT----EEKGTELPEQ 307
Cdd:TIGR02223  70 ETAADLPPKPEERWSYIEELEAREVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQADMRAAEKVlataPSEQTVAVEA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 308 TKPDFPDHKPRKSTDENVPEPLEEIKlefpeeesrkpneetileqsemmKPESPEEIKKSNEEKNPQPPEETGLVLPQEI 387
Cdd:TIGR02223 150 RKQTAEKKPQKARTAEAQKTPVETEK-----------------------IASKVKEAKQKQKALPKQTAETQSNSKPIET 206

                         170
                  ....*....|....*.
gi 1331917220 388 NPQVEEKTQIKPTEEK 403
Cdd:TIGR02223 207 APKADKADKTKPKPKE 222
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 194-393 9.95e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 42.47  E-value: 9.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  194 EESLRVQHEETGLEAPEQTKPDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPPEQARPEFPEkEPRKSS 273
Cdd:PTZ00341   952 EENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDE-ENVEEV 1030

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220  274 EEASLEPPEETQPEVPEEMQRKATEEKGTELPEQtkpdfpDHKPRKSTDENVPEPLEEiklefPEEESRKPNEETILEQS 353
Cdd:PTZ00341  1031 EENVEEYDEENVEEIEENAEENVEENIEENIEEY------DEENVEEIEENIEENIEE-----NVEENVEENVEEIEENV 1099

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1331917220  354 EMMKPESPEEIKKSNEEKNPQPPEETGlvlPQEINPQVEE 393
Cdd:PTZ00341  1100 EENVEENAEENAEENAEENAEEYDDEN---PEEHNEEYDE 1136
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 545-593 1.34e-03

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 37.53  E-value: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331917220 545 NWDPEEVAEWISQLGFPQY-KECFITNFISGRKLIHVNCSNLPQMGITNF 593
Cdd:cd09535     2 SWSPEQVAEWLLSAGFDDSvCEKFRENEITGDILLELDLEDLKELDIGSF 51
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
207-349 1.46e-03

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 41.27  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 207 EAPEQTKPDFLSEKPGESLEETDLqppkmTKPEIPEETQRESTEKKRTEPPEQARPEFPEKEPRKSSEEASlEPPEETQP 286
Cdd:PRK13335   31 EKIQSTKVDKVPTLKAERLAMINI-----TAGANSATTQAANTRQERTPKLEKAPNTNEEKTSASKIEKIS-QPKQEEQK 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331917220 287 EVPEEMQRKATEEKGTELPEQTKPdfpdhKPRKST--DENVPEPLEEIKLEFPEEESRKPNEETI 349
Cdd:PRK13335  105 SLNISATPAPKQEQSQTTTESTTP-----KTKVTTppSTNTPQPMQSTKSDTPQSPTIKQAQTDM 164
SAM_aveugle-like cd09510
SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like ...
 546-602 4.19e-03

SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.


Pssm-ID: 188909  Cd Length: 75  Bit Score: 36.51  E-value: 4.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 546 WDPEEVAEWISQ---LGFPQYKECFITNFISGRKLIHVNCSNLPQMGITNFEDMKAISRH 602
Cdd:cd09510     6 WSVQDVCKWLKRhcpDYYLLYAELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILRE 65
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 553-580 9.65e-03

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 35.14  E-value: 9.65e-03
                          10        20
                  ....*....|....*....|....*...
gi 1331917220 553 EWISQLGFPQYKECFITNFISGRKLIHV 580
Cdd:cd09565     9 EWLPSLGLPQYRSYFMECLVDARMLDHL 36
PTZ00465 PTZ00465
rhoptry-associated protein 1 (RAP-1); Provisional
 207-336 9.78e-03

rhoptry-associated protein 1 (RAP-1); Provisional


Pssm-ID: 185644 [Multi-domain]  Cd Length: 565  Bit Score: 38.97  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331917220 207 EAPEQTKpDFLSEKPGESLEETDLQPPKMTKPEIPEETQRESTEKKRTEPpeQARPEFPEKEPRKSSEEASLEPPEETQP 286
Cdd:PTZ00465  370 EAPQVTK-HFFDENIGQPTKEFFREAPQATKHFLDENIGQPTKEFFREAP--QVTKHFLDENIAQPTKEFFRDVPQVTKK 446

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331917220 287 EVPEEMQrKATEEKGTELPeqtkpdfpdHKPRKSTDENVPEPLEEIKLEF 336
Cdd:PTZ00465  447 VITENIA-QPTKEFLKEVP---------HTTMKVLNENIAQPAKEIIHEF 486
 
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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