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Conserved domains on  [gi|1958674987|ref|XP_038947489|]
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stromal interaction molecule 2 isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 317-424 1.13e-49

STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are calcium sensors in the endoplasmic reticulum. As the store of calcium is depleted the calcium sensor in the ER activates Orai1, a Ca2+-release-activated Ca2+ (CRAC) channel, in the plasma membrane. The SOAR region, which runs from residues 340-443 on UniProtKB:Q13586, forms a dimer, and is essential for oligomerization of the whole of STIM1.


:

Pssm-ID: 465164 [Multi-domain]  Cd Length: 100  Bit Score: 168.97  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 317 SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEvaasylmqAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAK 396
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEA--------CEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAK 72

                          90       100
                  ....*....|....*....|....*...
gi 1958674987 397 KALSELTTCLRERLFRWQQIEKICGFQI 424
Cdd:pfam16533  73 NALEEVTKDLQERQHRWQQIEKLCGFPI 100
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 103-176 1.61e-48

SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal interaction molecule) subfamily 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 STIM2 protein is an inhibitor of store operated channels in plasma membrane.


:

Pssm-ID: 188973  Cd Length: 74  Bit Score: 164.77  E-value: 1.61e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674987 103 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFG 176
Cdd:cd09574     1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
PRK00409 super family cl29770
recombination and DNA strand exchange inhibitor protein; Reviewed
 221-401 6.81e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


The actual alignment was detected with superfamily member PRK00409:

Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.44  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 221 KDLESL-QTAEQSLMDLQERLEKAQEENRTvavEKQNLERKMMDEINYAKEEACR-LRELREGAECELSrrQYAEQELEQ 298
Cdd:PRK00409  537 EEAEALlKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYA--SVKAHELIE 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 299 VRMALKKAEKEFElrSSWSVPDALQKWLQLTHEVEVQYYNIK--------RQNAEMQLAIAKDEVAASYL--MQAEKIKK 368
Cdd:PRK00409  612 ARKRLNKANEKKE--KKKKKQKEKQEELKVGDEVKYLSLGQKgevlsipdDKEAIVQAGIMKMKVPLSDLekIQKPKKKK 689

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958674987 369 KRSTVFGTLHVAHSS-SLD----EVDHKILEAKKALSE 401
Cdd:PRK00409  690 KKKPKTVKPKPRTVSlELDlrgmRYEEALERLDKYLDD 727
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 317-424 1.13e-49

STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are calcium sensors in the endoplasmic reticulum. As the store of calcium is depleted the calcium sensor in the ER activates Orai1, a Ca2+-release-activated Ca2+ (CRAC) channel, in the plasma membrane. The SOAR region, which runs from residues 340-443 on UniProtKB:Q13586, forms a dimer, and is essential for oligomerization of the whole of STIM1.


Pssm-ID: 465164 [Multi-domain]  Cd Length: 100  Bit Score: 168.97  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 317 SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEvaasylmqAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAK 396
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEA--------CEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAK 72

                          90       100
                  ....*....|....*....|....*...
gi 1958674987 397 KALSELTTCLRERLFRWQQIEKICGFQI 424
Cdd:pfam16533  73 NALEEVTKDLQERQHRWQQIEKLCGFPI 100
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 103-176 1.61e-48

SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal interaction molecule) subfamily 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 STIM2 protein is an inhibitor of store operated channels in plasma membrane.


Pssm-ID: 188973  Cd Length: 74  Bit Score: 164.77  E-value: 1.61e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674987 103 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFG 176
Cdd:cd09574     1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 322-421 3.08e-35

STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan transmembrane protein located in the endoplasmic reticulum (ER) membrane, which functions as a sensor for ER calcium ion levels and activates store-operated Ca2+ influx channels (SOCs), such as the Orai1 Ca2+ channel located in the plasma membrane. STIM1 has an N-terminal Ca-binding EF-hand domain, which is located in the ER lumen. Responding to the release of Ca2+ from the ER, STIM1 was found to aggregate near the plasma membrane and contact Orai1. This model describes a region near the C-terminus of STIM1, which has been shown to mediate the interaction with Orai1 and has been labeled SOAR (STIM1 Orai1-activating region). STIM1 has also been linked to sensing oxidative and temperature-variation stress and may play a rather general role in mediating calcium signaling in response to stress. Dimerization of STIM1 via the SOAR domain appears required for the activation of the Orai1 calcium channel. A model for STIM1 activation has been proposed, in which an inhibitory helix N-terminal to the SOAR domain prevents STIM1 clustering or aggregation, and in which conformational changes triggered by depletion of the calcium stores allow the clustering and activation of Orai1.


Pssm-ID: 212596 [Multi-domain]  Cd Length: 92  Bit Score: 128.52  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 322 LQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDevaasylmQAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSE 401
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKE--------ACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEE 72

                          90       100
                  ....*....|....*....|
gi 1958674987 402 LTTCLRERLFRWQQIEKICG 421
Cdd:cd11722    73 VTRELQERQHRWSQIESLCG 92
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
104-173 4.73e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.04  E-value: 4.73e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 104 VHNWTLEDTLQWLiEFVELPQYEKNFRDNNVKGTTLprIAVHETSFMIsQLKISDRSHRQKLQLKALDVV 173
Cdd:pfam07647   1 VESWSLESVADWL-RSIGLEQYTDNFRDQGITGAEL--LLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 104-168 1.85e-06

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: 45.75  E-value: 1.85e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958674987  104 VHNWTLEDTLQWLIEFVeLPQYEKNFRDNNVKGTTLPRIAVHEtsfMISQLKISDRSHRQKLQLK 168
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLLTSEE---DLKELGITKLGHRKKILKA 61
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 221-401 6.81e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.44  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 221 KDLESL-QTAEQSLMDLQERLEKAQEENRTvavEKQNLERKMMDEINYAKEEACR-LRELREGAECELSrrQYAEQELEQ 298
Cdd:PRK00409  537 EEAEALlKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYA--SVKAHELIE 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 299 VRMALKKAEKEFElrSSWSVPDALQKWLQLTHEVEVQYYNIK--------RQNAEMQLAIAKDEVAASYL--MQAEKIKK 368
Cdd:PRK00409  612 ARKRLNKANEKKE--KKKKKQKEKQEELKVGDEVKYLSLGQKgevlsipdDKEAIVQAGIMKMKVPLSDLekIQKPKKKK 689

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958674987 369 KRSTVFGTLHVAHSS-SLD----EVDHKILEAKKALSE 401
Cdd:PRK00409  690 KKKPKTVKPKPRTVSlELDlrgmRYEEALERLDKYLDD 727
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 207-403 4.45e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 207 TQNKTSKEHVAKMMKDLES-LQTAEQSLMDLQERLEKAQEENRTVAVEKQN----LERKMMDEINYAKEEACRLRELREG 281
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTeLEKEKLKNIELTAHCDKLLLENKELTQEASDmtleLKKHQEDIINCKKQEERMLKQIENL 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 282 AECELSRRqyaeQELEQVRMALKKAEKEFELRSSWSVPDALQ-KWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEVAAsyL 360
Cdd:pfam05483 540 EEKEMNLR----DELESVREEFIQKGDEVKCKLDKSEENARSiEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE--L 613

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958674987 361 MQAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELT 403
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 211-433 9.26e-04

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: 42.75  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  211 TSKEHVAKMMKDLESLQTA----EQSLMDLQERLEKAQEENRTVAVEKQNLERKMM--------DEINYAKEEACRLREL 278
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEienvKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqAELSKLEEEVSRIEAR 813

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  279 REGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSwsvpdalqkwlqlthEVEVQYYNIKRQNAEMQLAIAKDEVA-A 357
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---------------SIEKEIENLNGKKEELEEELEELEAAlR 878

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958674987  358 SYLMQAEKIKKKRSTVFGTLHVAHsSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSL 433
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELE-RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 226-402 9.27e-04

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: 9.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 226 LQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKK 305
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 306 AEKEFELRSSwSVPDALQKWLQLT---HEVEVQYYNIKRQNAEMQLAIAKDEVAASYLMQAEKIKKKRSTVFGTLHVAHS 382
Cdd:COG1196   349 AEEELEEAEA-ELAEAEEALLEAEaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         170       180
                  ....*....|....*....|
gi 1958674987 383 SSLDEVDHKILEAKKALSEL 402
Cdd:COG1196   428 EALAELEEEEEEEEEALEEA 447
PTZ00121 PTZ00121
MAEBL; Provisional
 217-418 1.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  217 AKMMKDLESLQTAEQSLMDLQERLEKAQ--EENRTVAVEKQNLERKMM--DEINYAKEEACRLRELREGAECELSRRQYA 292
Cdd:PTZ00121  1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  293 EQELEQVRMA--LKKAEKEFELRSSwsvpdalqkwlQLTHEVEVQyyniKRQNAEMQLAIAKDEVAASYLMQAEKIKKKr 370
Cdd:PTZ00121  1640 KKEAEEKKKAeeLKKAEEENKIKAA-----------EEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKK- 1703

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958674987  371 stvfgtlhvahsssLDEVDHKILEAKKALSELTTCLRERLFRWQQIEK 418
Cdd:PTZ00121  1704 --------------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 317-424 1.13e-49

STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are calcium sensors in the endoplasmic reticulum. As the store of calcium is depleted the calcium sensor in the ER activates Orai1, a Ca2+-release-activated Ca2+ (CRAC) channel, in the plasma membrane. The SOAR region, which runs from residues 340-443 on UniProtKB:Q13586, forms a dimer, and is essential for oligomerization of the whole of STIM1.


Pssm-ID: 465164 [Multi-domain]  Cd Length: 100  Bit Score: 168.97  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 317 SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEvaasylmqAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAK 396
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEA--------CEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAK 72

                          90       100
                  ....*....|....*....|....*...
gi 1958674987 397 KALSELTTCLRERLFRWQQIEKICGFQI 424
Cdd:pfam16533  73 NALEEVTKDLQERQHRWQQIEKLCGFPI 100
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 103-176 1.61e-48

SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal interaction molecule) subfamily 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 STIM2 protein is an inhibitor of store operated channels in plasma membrane.


Pssm-ID: 188973  Cd Length: 74  Bit Score: 164.77  E-value: 1.61e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674987 103 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFG 176
Cdd:cd09574     1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 103-176 3.04e-40

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: 141.70  E-value: 3.04e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674987 103 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFG 176
Cdd:cd09504     1 EVHNWTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDVVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 322-421 3.08e-35

STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan transmembrane protein located in the endoplasmic reticulum (ER) membrane, which functions as a sensor for ER calcium ion levels and activates store-operated Ca2+ influx channels (SOCs), such as the Orai1 Ca2+ channel located in the plasma membrane. STIM1 has an N-terminal Ca-binding EF-hand domain, which is located in the ER lumen. Responding to the release of Ca2+ from the ER, STIM1 was found to aggregate near the plasma membrane and contact Orai1. This model describes a region near the C-terminus of STIM1, which has been shown to mediate the interaction with Orai1 and has been labeled SOAR (STIM1 Orai1-activating region). STIM1 has also been linked to sensing oxidative and temperature-variation stress and may play a rather general role in mediating calcium signaling in response to stress. Dimerization of STIM1 via the SOAR domain appears required for the activation of the Orai1 calcium channel. A model for STIM1 activation has been proposed, in which an inhibitory helix N-terminal to the SOAR domain prevents STIM1 clustering or aggregation, and in which conformational changes triggered by depletion of the calcium stores allow the clustering and activation of Orai1.


Pssm-ID: 212596 [Multi-domain]  Cd Length: 92  Bit Score: 128.52  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 322 LQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDevaasylmQAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSE 401
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKE--------ACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEE 72

                          90       100
                  ....*....|....*....|
gi 1958674987 402 LTTCLRERLFRWQQIEKICG 421
Cdd:cd11722    73 VTRELQERQHRWSQIESLCG 92
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 103-176 1.29e-28

SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal interaction molecule) subfamily 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 protein is an activator of store operated channels in plasma membrane.


Pssm-ID: 188972  Cd Length: 74  Bit Score: 108.98  E-value: 1.29e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674987 103 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFG 176
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
104-173 4.73e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.04  E-value: 4.73e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 104 VHNWTLEDTLQWLiEFVELPQYEKNFRDNNVKGTTLprIAVHETSFMIsQLKISDRSHRQKLQLKALDVV 173
Cdd:pfam07647   1 VESWSLESVADWL-RSIGLEQYTDNFRDQGITGAEL--LLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 104-168 1.85e-06

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: 45.75  E-value: 1.85e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958674987  104 VHNWTLEDTLQWLIEFVeLPQYEKNFRDNNVKGTTLPRIAVHEtsfMISQLKISDRSHRQKLQLK 168
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLLTSEE---DLKELGITKLGHRKKILKA 61
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 221-401 6.81e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.44  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 221 KDLESL-QTAEQSLMDLQERLEKAQEENRTvavEKQNLERKMMDEINYAKEEACR-LRELREGAECELSrrQYAEQELEQ 298
Cdd:PRK00409  537 EEAEALlKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYA--SVKAHELIE 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 299 VRMALKKAEKEFElrSSWSVPDALQKWLQLTHEVEVQYYNIK--------RQNAEMQLAIAKDEVAASYL--MQAEKIKK 368
Cdd:PRK00409  612 ARKRLNKANEKKE--KKKKKQKEKQEELKVGDEVKYLSLGQKgevlsipdDKEAIVQAGIMKMKVPLSDLekIQKPKKKK 689

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958674987 369 KRSTVFGTLHVAHSS-SLD----EVDHKILEAKKALSE 401
Cdd:PRK00409  690 KKKPKTVKPKPRTVSlELDlrgmRYEEALERLDKYLDD 727
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 104-165 5.77e-05

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 41.53  E-value: 5.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958674987 104 VHNWTLEDTLQWLIEfVELPQYEKNFRDNNVKGTTLPRIAvheTSFMISQLKISDRSHRQKL 165
Cdd:cd09505     2 LQDWSEEDVCTWLRS-IGLEQYVEVFRANNIDGKELLNLT---KESLSKDLKIESLGHRNKI 59
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 111-171 1.03e-04

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: 40.69  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958674987 111 DTLQWLIEfVELPQYEKNFRDNNVKGTTLPRIAVHEtsfmISQLKISDRSHRQKLqLKALD 171
Cdd:cd09487     1 DVAEWLES-LGLEQYADLFRKNEIDGDALLLLTDED----LKELGITSPGHRKKI-LRAIQ 55
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 105-167 1.16e-04

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: 40.72  E-value: 1.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958674987 105 HNWTLEDTLQWLiEFVELPQYEKNFRDNNVKGTTLPRIavheTSFMISQLKISDRSHRQKLQL 167
Cdd:pfam00536   1 DGWSVEDVGEWL-ESIGLGQYIDSFRAGYIDGDALLQL----TEDDLLKLGVTLLGHRKKILY 58
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 207-403 4.45e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 207 TQNKTSKEHVAKMMKDLES-LQTAEQSLMDLQERLEKAQEENRTVAVEKQN----LERKMMDEINYAKEEACRLRELREG 281
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTeLEKEKLKNIELTAHCDKLLLENKELTQEASDmtleLKKHQEDIINCKKQEERMLKQIENL 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 282 AECELSRRqyaeQELEQVRMALKKAEKEFELRSSWSVPDALQ-KWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEVAAsyL 360
Cdd:pfam05483 540 EEKEMNLR----DELESVREEFIQKGDEVKCKLDKSEENARSiEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE--L 613

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958674987 361 MQAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELT 403
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 106-167 6.04e-04

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: 38.84  E-value: 6.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 106 NWTLEDTLQWlIEFVELPQYEKNFRDNNVKG--------TTLPRIAVheTSFmiSQLKISDRSHRQKLQL 167
Cdd:cd09530     2 SWDTEDVAEW-IEGLGFPQYRECFTTNFIDGrklilvdaSTLPRMGV--TDF--EHIKAIARKIRELLGI 66
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 223-309 8.00e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 41.09  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 223 LESLQTAEQSLMDLQERLEKAQEE--------NRTVAVEKQNLERKMMDEINYAKEEACRlreLREGAECELSrrqyAEQ 294
Cdd:PRK07352   56 LQALKEAEERLRQAAQALAEAQQKlaqaqqeaERIRADAKARAEAIRAEIEKQAIEDMAR---LKQTAAADLS----AEQ 128

                          90       100
                  ....*....|....*....|..
gi 1958674987 295 E--LEQVR-----MALKKAEKE 309
Cdd:PRK07352  129 ErvIAQLRreaaeLAIAKAESQ 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 211-433 9.26e-04

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: 42.75  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  211 TSKEHVAKMMKDLESLQTA----EQSLMDLQERLEKAQEENRTVAVEKQNLERKMM--------DEINYAKEEACRLREL 278
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEienvKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqAELSKLEEEVSRIEAR 813

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  279 REGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSwsvpdalqkwlqlthEVEVQYYNIKRQNAEMQLAIAKDEVA-A 357
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---------------SIEKEIENLNGKKEELEEELEELEAAlR 878

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958674987  358 SYLMQAEKIKKKRSTVFGTLHVAHsSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSL 433
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELE-RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 226-402 9.27e-04

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: 9.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 226 LQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKK 305
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 306 AEKEFELRSSwSVPDALQKWLQLT---HEVEVQYYNIKRQNAEMQLAIAKDEVAASYLMQAEKIKKKRSTVFGTLHVAHS 382
Cdd:COG1196   349 AEEELEEAEA-ELAEAEEALLEAEaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         170       180
                  ....*....|....*....|
gi 1958674987 383 SSLDEVDHKILEAKKALSEL 402
Cdd:COG1196   428 EALAELEEEEEEEEEALEEA 447
PTZ00121 PTZ00121
MAEBL; Provisional
 217-418 1.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  217 AKMMKDLESLQTAEQSLMDLQERLEKAQ--EENRTVAVEKQNLERKMM--DEINYAKEEACRLRELREGAECELSRRQYA 292
Cdd:PTZ00121  1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  293 EQELEQVRMA--LKKAEKEFELRSSwsvpdalqkwlQLTHEVEVQyyniKRQNAEMQLAIAKDEVAASYLMQAEKIKKKr 370
Cdd:PTZ00121  1640 KKEAEEKKKAeeLKKAEEENKIKAA-----------EEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKK- 1703

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958674987  371 stvfgtlhvahsssLDEVDHKILEAKKALSELTTCLRERLFRWQQIEK 418
Cdd:PTZ00121  1704 --------------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 213-402 1.64e-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: 41.98  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  213 KEHVAKMMKDLESLQTA----EQSLMDLQERLEKAQEENRTVAVEKQNLER----------KMMDEINYAKEEacrLREL 278
Cdd:TIGR02169  293 KEKIGELEAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEReieeerkrrdKLTEEYAELKEE---LEDL 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  279 REGAECELSRRQYAEQELEQVRMALKKAEKEFElrSSWSVPDALQKWLQLTHEvevqyyniKRQNAEMQLAIAKD---EV 355
Cdd:TIGR02169  370 RAELEEVDKEFAETRDELKDYREKLEKLKREIN--ELKRELDRLQEELQRLSE--------ELADLNAAIAGIEAkinEL 439

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958674987  356 AASYLMQAEKIKK---KRSTVFGTL------HVAHSSSLDEVDHKILEAKKALSEL 402
Cdd:TIGR02169  440 EEEKEDKALEIKKqewKLEQLAADLskyeqeLYDLKEEYDRVEKELSKLQRELAEA 495
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 206-420 2.84e-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: 41.11  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  206 YTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEE-NRTVAVEKQNLERKMMDEINYAKEEA-CRLRELREGAE 283
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRA 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  284 CELSRRQYA---EQELEQVRMALKKAEKEFELRSSW-----SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEV 355
Cdd:TIGR00618  325 KLLMKRAAHvkqQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI 404

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958674987  356 AASYLMQAEKIKKKRSTVFGTLHVAHSS-SLDEVDHKILE------------AKKALSELTTCLRERLFRWQQIEKIC 420
Cdd:TIGR00618  405 LQREQATIDTRTSAFRDLQGQLAHAKKQqELQQRYAELCAaaitctaqceklEKIHLQESAQSLKEREQQLQTKEQIH 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 213-408 3.80e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  213 KEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKmmdeINYAKEEACRLRELREGAECELSRRQYA 292
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ----ISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987  293 EQELEQVRMAL-KKAEKEFELRSswsvpDALQKWLQLthEVEVQYYNIKRQNAEMQLAIAKDEVAA---SYLMQAEKIK- 367
Cdd:TIGR02168  756 LTELEAEIEELeERLEEAEEELA-----EAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLlneEAANLRERLEs 828

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958674987  368 -KKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRE 408
Cdd:TIGR02168  829 lERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
221-357 3.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 221 KDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRlRELREGAEC--ELSRRqyaEQELEQ 298
Cdd:COG4717    85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERleELEER---LEELRE 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 299 VRMALKKAEKEF-ELRSSwsvPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEVAA 357
Cdd:COG4717   161 LEEELEELEAELaELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 228-313 5.72e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.21  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 228 TAEQSLMDLQERLEKAQEENRTVaveKQNLER------KMMDEINYAKEEACRLRELREGAECELSR--RQYAEQELEQV 299
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKKA---QEELEEseetaeELEEERRQAEEEAERLEQKRQEAEEEKERleESAEMEAEEKE 79

                          90
                  ....*....|....
gi 1958674987 300 RMALKKAEKEFELR 313
Cdd:pfam20492  80 QLEAELAEAQEEIA 93
SAM_Ste50_fungal cd09536
SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal ...
 102-142 6.77e-03

SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and Ras-associated UBQ superfamily domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response, and contribute to cell wall integrity in vegetative cells. Ste50 of S.cerevisiae acts as an adaptor protein between G protein and MAP triple kinase Ste11. Ste50 proteins are able to form homooligomers, binding each other via their SAM domains, as well as heterodimers and heterogeneous complexes with SAM domain or SAM homodimers of MAPKKK Ste11 protein kinase.


Pssm-ID: 188935  Cd Length: 74  Bit Score: 35.87  E-value: 6.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958674987 102 SEVHNWTLEDTLQWLIEFVELPQYEK---NFRDNNVKGTTLPRI 142
Cdd:cd09536     1 EEFNEWSTDEVVKWCISSLGLDDGDPlcdRLRENNITGSLLSEL 44
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
207-419 7.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 207 TQNKTSKEHVAKMMKDLES-LQTAEQSLMDLQERLEKAQE------ENRTVAVEKQNLER---KMMDEINYAKEEACRLR 276
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEkIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 277 ELREGAECELSRRQYAEQELEQVRMALKKAEKEFElrsswsvpdALQKWLQLthevevqYYNIKRQNAEMqlaiakdeva 356
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------ELEERHEL-------YEEAKAKKEEL---------- 374

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958674987 357 asylmqaEKIKKKRStvfgtlhvahSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKI 419
Cdd:PRK03918  375 -------ERLKKRLT----------GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
224-311 8.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674987 224 ESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERkmmdEINYAKEEACRLRELREGAECELSRRQ----YAEQELEQV 299
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEE----ELEQARSELEQLEEELEELNEQLQAAQaelaQAQEELESL 106

                          90
                  ....*....|..
gi 1958674987 300 RMALKKAEKEFE 311
Cdd:COG4372   107 QEEAEELQEELE 118
 
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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