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Conserved domains on  [gi|281182822|ref|NP_065911|]
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stromal interaction molecule 2 isoform 2 precursor [Homo sapiens]

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 ...
 346-445 8.49e-53

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: 177.83  E-value: 8.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  346 SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTT 425
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 281182822  426 CLRERLFRWQQIEKICGFQI 445
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 132-205 5.83e-50

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: 169.01  E-value: 5.83e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182822 132 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFG 205
Cdd:cd09574    1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
PRK00409 super family cl29770
recombination and DNA strand exchange inhibitor protein; Reviewed
 250-340 1.10e-05

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: 49.05  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 250 KDLESL-QTAEQSLMDLQERLEKAQEENRNvavEKQNLERKMMDEINYAKEEACR-LRELREGAECELSrrQYAEQELEQ 327
Cdd:PRK00409 537 EEAEALlKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYA--SVKAHELIE 611

                         90
                 ....*....|...
gi 281182822 328 VRMALKKAEKEFE 340
Cdd:PRK00409 612 ARKRLNKANEKKE 624
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 346-445 8.49e-53

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: 177.83  E-value: 8.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  346 SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTT 425
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 281182822  426 CLRERLFRWQQIEKICGFQI 445
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 132-205 5.83e-50

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: 169.01  E-value: 5.83e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182822 132 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFG 205
Cdd:cd09574    1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 351-442 4.47e-38

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: 136.61  E-value: 4.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 351 LQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRER 430
Cdd:cd11722    1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                         90
                 ....*....|..
gi 281182822 431 LFRWQQIEKICG 442
Cdd:cd11722   81 QHRWSQIESLCG 92
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
133-202 2.07e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 54.20  E-value: 2.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  133 VHNWTLEDTLQWLiEFVELPQYEKNFRDNNVKGTTLprIAVHEPSFMIsQLKISDRSHRQKLQLKALDVV 202
Cdd:pfam07647   1 VESWSLESVADWL-RSIGLEQYTDNFRDQGITGAEL--LLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 133-197 1.47e-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: 46.13  E-value: 1.47e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281182822   133 VHNWTLEDTLQWLIEFVeLPQYEKNFRDNNVKGTTLPRIAVHEpsfMISQLKISDRSHRQKLQLK 197
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLLTSEE---DLKELGITKLGHRKKILKA 61
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 250-340 1.10e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.05  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 250 KDLESL-QTAEQSLMDLQERLEKAQEENRNvavEKQNLERKMMDEINYAKEEACR-LRELREGAECELSrrQYAEQELEQ 327
Cdd:PRK00409 537 EEAEALlKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYA--SVKAHELIE 611

                         90
                 ....*....|...
gi 281182822 328 VRMALKKAEKEFE 340
Cdd:PRK00409 612 ARKRLNKANEKKE 624
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-392 2.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 250 KDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEINYAKEEACRlRELREGAEC--ELSRRqyaEQELEQ 327
Cdd:COG4717   85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERleELEER---LEELRE 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182822 328 VRMALKKAEKEF-ELRSSwsvPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRS 392
Cdd:COG4717  161 LEEELEELEAELaELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-454 2.50e-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: 44.67  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   240 TSKEHVAKMMKDLESLQTA----EQSLMDLQERLEKAQEENRNVAVEKQNLERKMM--------DEINYAKEEACRLREL 307
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEienvKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqAELSKLEEEVSRIEAR 813

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   308 REGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSwSVPDALqkwlqltHEVEVQYYNIKRQNAEMQLAIAKDEAE-- 385
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK-SIEKEI-------ENLNGKKEELEEELEELEAALRDLESRlg 885

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182822   386 KIKKKRSTVFGTLHVAHsSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSL 454
Cdd:TIGR02169  886 DLKKERDELEAQLRELE-RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-440 6.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 236 TQNKTSKEHVAKMMKDLES-LQTAEQSLMDLQERLEKAQE------ENRNVAVEKQNLER---KMMDEINYAKEEACRLR 305
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEkIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 306 ELREGAECELSRRQYAEQELEQVRMALKKAEKEFElrsswsvpdALQKWLQLTHEVEVQyynikrqnaemqlaiaKDEAE 385
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------ELEERHELYEEAKAK----------------KEELE 375

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 281182822 386 KIKKKRStvfgtlhvahSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKI 440
Cdd:PRK03918 376 RLKKRLT----------GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 257-342 4.00e-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: 37.98  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  257 TAEQSLMDLQERLEKAQEENR---NVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSR--RQYAEQELEQVRMA 331
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKkaqEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERleESAEMEAEEKEQLE 82

                          90
                  ....*....|.
gi 281182822  332 LKKAEKEFELR 342
Cdd:pfam20492  83 AELAEAQEEIA 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-385 7.19e-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: 40.04  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   250 KDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMD----------EINYAKEEACRLRELREGAECELS--- 316
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqletlrsKVAQLELQIASLNNEIERLEARLErle 413

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182822   317 -RRQYAEQELEQVRMALKKAEKEfELRSSWSVPDALQKWLQLTHE-VEVQYYNIKRQNAEMQLAIAKDEAE 385
Cdd:TIGR02168  414 dRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELErLEEALEELREELEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-439 7.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 243 EHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLErkmmdeinyAKEEACRLRELREGAECELSRRQYAE 322
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---------EELEELEEELEEAEEELEEAEAELAE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 323 QELEQVRMALKKAEKEFELRSSWSvpDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAH 402
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 281182822 403 SSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEK 439
Cdd:COG1196  441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 346-445 8.49e-53

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: 177.83  E-value: 8.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  346 SVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTT 425
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 281182822  426 CLRERLFRWQQIEKICGFQI 445
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 132-205 5.83e-50

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: 169.01  E-value: 5.83e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182822 132 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFG 205
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 ...
 132-205 1.30e-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: 142.86  E-value: 1.30e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182822 132 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFG 205
Cdd:cd09504    1 EVHNWTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDVVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 351-442 4.47e-38

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: 136.61  E-value: 4.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 351 LQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRER 430
Cdd:cd11722    1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                         90
                 ....*....|..
gi 281182822 431 LFRWQQIEKICG 442
Cdd:cd11722   81 QHRWSQIESLCG 92
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 132-205 4.70e-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: 107.44  E-value: 4.70e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182822 132 EVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFG 205
Cdd:cd09573    1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
133-202 2.07e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 54.20  E-value: 2.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  133 VHNWTLEDTLQWLiEFVELPQYEKNFRDNNVKGTTLprIAVHEPSFMIsQLKISDRSHRQKLQLKALDVV 202
Cdd:pfam07647   1 VESWSLESVADWL-RSIGLEQYTDNFRDQGITGAEL--LLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 133-197 1.47e-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: 46.13  E-value: 1.47e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281182822   133 VHNWTLEDTLQWLIEFVeLPQYEKNFRDNNVKGTTLPRIAVHEpsfMISQLKISDRSHRQKLQLK 197
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLLTSEE---DLKELGITKLGHRKKILKA 61
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 250-340 1.10e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.05  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 250 KDLESL-QTAEQSLMDLQERLEKAQEENRNvavEKQNLERKMMDEINYAKEEACR-LRELREGAECELSrrQYAEQELEQ 327
Cdd:PRK00409 537 EEAEALlKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYA--SVKAHELIE 611

                         90
                 ....*....|...
gi 281182822 328 VRMALKKAEKEFE 340
Cdd:PRK00409 612 ARKRLNKANEKKE 624
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 140-200 8.86e-05

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: 8.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182822 140 DTLQWLIEfVELPQYEKNFRDNNVKGTTLPRIAVHEpsfmISQLKISDRSHRQKLqLKALD 200
Cdd:cd09487    1 DVAEWLES-LGLEQYADLFRKNEIDGDALLLLTDED----LKELGITSPGHRKKI-LRAIQ 55
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 236-424 1.36e-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: 45.48  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  236 TQNKTSKEHVAKMMKDLES-LQTAEQSLMDLQERLEKAQEENRNVAVEKQN----LERKMMDEINYAKEEACRLRELREG 310
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTeLEKEKLKNIELTAHCDKLLLENKELTQEASDmtleLKKHQEDIINCKKQEERMLKQIENL 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  311 AECELSRRqyaeQELEQVRMALKKAEKEFELR------SSWSVPDALQKWLQLTHEVEVQYYNIKRQ--NAEMQLAIAKD 382
Cdd:pfam05483 540 EEKEMNLR----DELESVREEFIQKGDEVKCKldkseeNARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKNIEELHQ 615

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 281182822  383 EAEKIKKKRSTVFGTLHvAHSSSLDEVDHKILEAKKALSELT 424
Cdd:pfam05483 616 ENKALKKKGSAENKQLN-AYEIKVNKLELELASAKQKFEEII 656
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 133-194 1.79e-04

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: 40.38  E-value: 1.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182822 133 VHNWTLEDTLQWLIEfVELPQYEKNFRDNNVKGTTLPRIAvhePSFMISQLKISDRSHRQKL 194
Cdd:cd09505    2 LQDWSEEDVCTWLRS-IGLEQYVEVFRANNIDGKELLNLT---KESLSKDLKIESLGHRNKI 59
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-392 2.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 250 KDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEINYAKEEACRlRELREGAEC--ELSRRqyaEQELEQ 327
Cdd:COG4717   85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERleELEER---LEELRE 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182822 328 VRMALKKAEKEF-ELRSSwsvPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRS 392
Cdd:COG4717  161 LEEELEELEAELaELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-454 2.50e-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: 44.67  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   240 TSKEHVAKMMKDLESLQTA----EQSLMDLQERLEKAQEENRNVAVEKQNLERKMM--------DEINYAKEEACRLREL 307
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEienvKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqAELSKLEEEVSRIEAR 813

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   308 REGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSwSVPDALqkwlqltHEVEVQYYNIKRQNAEMQLAIAKDEAE-- 385
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK-SIEKEI-------ENLNGKKEELEEELEELEAALRDLESRlg 885

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182822   386 KIKKKRSTVFGTLHVAHsSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSL 454
Cdd:TIGR02169  886 DLKKERDELEAQLRELE-RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 134-196 2.98e-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: 39.56  E-value: 2.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281182822  134 HNWTLEDTLQWLiEFVELPQYEKNFRDNNVKGTTLPRIAVHEpsfmISQLKISDRSHRQKLQL 196
Cdd:pfam00536   1 DGWSVEDVGEWL-ESIGLGQYIDSFRAGYIDGDALLQLTEDD----LLKLGVTLLGHRKKILY 58
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 242-423 3.22e-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: 44.29  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   242 KEHVAKMMKDLESLQTA----EQSLMDLQERLEKAQEENRNVAVEKQNLER----------KMMDEINYAKEEacrLREL 307
Cdd:TIGR02169  293 KEKIGELEAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEReieeerkrrdKLTEEYAELKEE---LEDL 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   308 REGAECELSRRQYAEQELEQVRMALKKAEKEFE--LRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEM-------QLA 378
Cdd:TIGR02169  370 RAELEEVDKEFAETRDELKDYREKLEKLKREINelKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeeekedkALE 449

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 281182822   379 IAKDE--AEKIKKKRSTVFGTLHvAHSSSLDEVDHKILEAKKALSEL 423
Cdd:TIGR02169  450 IKKQEwkLEQLAADLSKYEQELY-DLKEEYDRVEKELSKLQRELAEA 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-439 5.29e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   237 QNKTSKEHVAKMMKDLES-LQTAEQSLMDL-------QERLEKAQEENRNVAVEKQNLERKMM----------DEINYAK 298
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAeLQELEEKLEELrlevselEEEIEELQKELYALANEISRLEQQKQilrerlanleRQLEELE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   299 EEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEF-----ELRSSWSVPDAL-----QKWLQLTHEVEVQyyNI 368
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleELESRLEELEEQletlrSKVAQLELQIASL--NN 400

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182822   369 KRQNAEMQLAIAKDEAEKIKKKRSTVfgtLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEK 439
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEEL---LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-440 6.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 236 TQNKTSKEHVAKMMKDLES-LQTAEQSLMDLQERLEKAQE------ENRNVAVEKQNLER---KMMDEINYAKEEACRLR 305
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEkIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 306 ELREGAECELSRRQYAEQELEQVRMALKKAEKEFElrsswsvpdALQKWLQLTHEVEVQyynikrqnaemqlaiaKDEAE 385
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------ELEERHELYEEAKAK----------------KEELE 375

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 281182822 386 KIKKKRStvfgtlhvahSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKI 440
Cdd:PRK03918 376 RLKKRLT----------GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 255-391 6.82e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 255 LQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERkmmdEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKK 334
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 281182822 335 AEKEFElrsswsvpDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKR 391
Cdd:COG1196  345 ELEEAE--------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 252-338 8.87e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 40.71  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 252 LESLQTAEQSLMDLQERLEKAQEenrNVAVEKQNLERKMMDeinyAKEEACRLRE------------LREGAECELSrrq 319
Cdd:PRK07352  56 LQALKEAEERLRQAAQALAEAQQ---KLAQAQQEAERIRAD----AKARAEAIRAeiekqaiedmarLKQTAAADLS--- 125

                         90       100
                 ....*....|....*....|....*.
gi 281182822 320 yAEQE--LEQVR-----MALKKAEKE 338
Cdd:PRK07352 126 -AEQErvIAQLRreaaeLAIAKAESQ 150
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 135-173 1.02e-03

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: 38.07  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 281182822 135 NWTLEDTLQWlIEFVELPQYEKNFRDNNVKG--------TTLPRIAV 173
Cdd:cd09530    2 SWDTEDVAEW-IEGLGFPQYRECFTTNFIDGrklilvdaSTLPRMGV 47
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
242-444 1.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 242 KEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDE-INYAKEEACRLRELRE---------GA 311
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPfyneylelkDA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 312 ECELSRRQ----YAEQELEQVRMALKKAEKEFELRSSwSVPDALQKWLQLTHEvevqyyNIKRQNAE--MQLAIAKDEAE 385
Cdd:PRK03918 611 EKELEREEkelkKLEEELDKAFEELAETEKRLEELRK-ELEELEKKYSEEEYE------ELREEYLElsRELAGLRAELE 683

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182822 386 KIKKKRSTVFGTLHVAhSSSLDEVDHKILEAK---KALSELTTcLRERLFRWQQIEKICGFQ 444
Cdd:PRK03918 684 ELEKRREEIKKTLEKL-KEELEEREKAKKELEkleKALERVEE-LREKVKKYKALLKERALS 743
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 235-441 1.95e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   235 YTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEE-NRNVAVEKQNLERKMMDEINYAKEEA-CRLRELREGAE 312
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRA 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   313 CELSRRQYA---EQELEQVRMALKKAEKEFELRSSW-----SVPDALQKWLQLTHEVEVQYYNIkrQNAEMQLAIAKDEA 384
Cdd:TIGR00618  325 KLLMKRAAHvkqQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQK--TTLTQKLQSLCKEL 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   385 EKIKKKRSTVFGTL--------HVAHSSSLDEVDHKILE---------------AKKALSELTTCLRERLFRWQQIEKIC 441
Cdd:TIGR00618  403 DILQREQATIDTRTsafrdlqgQLAHAKKQQELQQRYAElcaaaitctaqceklEKIHLQESAQSLKEREQQLQTKEQIH 482
PTZ00121 PTZ00121
MAEBL; Provisional
 246-439 2.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  246 AKMMKDLESLQTAEQSLMDLQERLEKAQ--EENRNVAVEKQNLERKMM--DEINYAKEEACRLRELREGAECELSRRQYA 321
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  322 EQELEQVRMA--LKKAEKEFELRSSwsvpdalqkwlQLTHEVEVQyyniKRQNAEMQlaiaKDEAEKIKKKRSTvfgTLH 399
Cdd:PTZ00121 1640 KKEAEEKKKAeeLKKAEEENKIKAA-----------EEAKKAEED----KKKAEEAK----KAEEDEKKAAEAL---KKE 1697

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 281182822  400 VAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEK 439
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-391 3.60e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 253 ESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERkmmdEINYAKEEACRLRELREGAECELSRRQ----YAEQELEQV 328
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEE----ELEQARSELEQLEEELEELNEQLQAAQaelaQAQEELESL 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281182822 329 RMALKKAEKEFElrsswsvpdalqkwlqlthEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKR 391
Cdd:COG4372  107 QEEAEELQEELE-------------------ELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 257-342 4.00e-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: 37.98  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  257 TAEQSLMDLQERLEKAQEENR---NVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSR--RQYAEQELEQVRMA 331
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKkaqEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERleESAEMEAEEKEQLE 82

                          90
                  ....*....|.
gi 281182822  332 LKKAEKEFELR 342
Cdd:pfam20492  83 AELAEAQEEIA 93
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 241-388 6.86e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  241 SKEHVAKMMKDLESLQTAEQsLMDLQ--ERLEKAQEENRNVAVEKQNLERKMMDEINYAKEE-ACRLRELREGAEC---E 314
Cdd:pfam05557  34 KKASALKRQLDRESDRNQEL-QKRIRllEKREAEAEEALREQAELNRLKKKYLEALNKKLNEkESQLADAREVISClknE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182822  315 LSRRQyaeQELEQVRMALKKAEKEFElrsswsvpdALQKWLQLTHEvEVQYYNIKRQNAEMQLAIAKDEAEKIK 388
Cdd:pfam05557 113 LSELR---RQIQRAELELQSTNSELE---------ELQERLDLLKA-KASEAEQLRQNLEKQQSSLAEAEQRIK 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-385 7.19e-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: 40.04  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822   250 KDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMD----------EINYAKEEACRLRELREGAECELS--- 316
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqletlrsKVAQLELQIASLNNEIERLEARLErle 413

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182822   317 -RRQYAEQELEQVRMALKKAEKEfELRSSWSVPDALQKWLQLTHE-VEVQYYNIKRQNAEMQLAIAKDEAE 385
Cdd:TIGR02168  414 dRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELErLEEALEELREELEEAEQALDAAERE 483
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 245-431 7.19e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  245 VAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEinyAKEEACRLRELREGAECELSRRQYAEQE 324
Cdd:pfam07888  75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQ---RAAHEARIRELEEDIKTLTQRVLERETE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  325 LEQVRMALKKAEKefELRSSWSVPDALQKWLQLThEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHss 404
Cdd:pfam07888 152 LERMKERAKKAGA--QRKEEEAERKQLQAKLQQT-EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH-- 226

                         170       180
                  ....*....|....*....|....*..
gi 281182822  405 sldevdHKILEAKKALSELTTcLRERL 431
Cdd:pfam07888 227 ------RKEAENEALLEELRS-LQERL 246
SAM_Ste50_fungal cd09536
SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal ...
 131-171 7.50e-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: 7.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 281182822 131 SEVHNWTLEDTLQWLIEFVELPQYEK---NFRDNNVKGTTLPRI 171
Cdd:cd09536    1 EEFNEWSTDEVVKWCISSLGLDDGDPlcdRLRENNITGSLLSEL 44
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 233-423 7.54e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 39.63  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  233 FAYTQNKTSKEhvakmmkdLESLQTAEQSLMDLQERLEKAQEENRNVaveKQNLErKMMDEINYAKEEACRLR-EL---- 307
Cdd:pfam05701 267 AAYMESKLKEE--------ADGEGNEKKTSTSIQAALASAKKELEEV---KANIE-KAKDEVNCLRVAAASLRsELekek 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822  308 --------REGA--------ECELSRRQyaeQELEQVRMALKKA-EKEFELrsswsvPDALQKWLQlthevEVQYYNIKR 370
Cdd:pfam05701 335 aelaslrqREGMasiavsslEAELNRTK---SEIALVQAKEKEArEKMVEL------PKQLQQAAQ-----EAEEAKSLA 400

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281182822  371 QNAEMQLAIAKDEAEKIKKKRSTVfgtlhvahSSSLDEVDHKIlEAKKALSEL 423
Cdd:pfam05701 401 QAAREELRKAKEEAEQAKAAASTV--------ESRLEAVLKEI-EAAKASEKL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-439 7.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 243 EHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLErkmmdeinyAKEEACRLRELREGAECELSRRQYAE 322
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---------EELEELEEELEEAEEELEEAEAELAE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182822 323 QELEQVRMALKKAEKEFELRSSWSvpDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAH 402
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 281182822 403 SSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEK 439
Cdd:COG1196  441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
 
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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