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Conserved domains on  [gi|1841838619|ref|NP_001369497|]
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stromal interaction molecule 1 isoform 6 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 ...
 342-448 3.01e-51

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: 172.83  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 342 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAnslssvfRQ 421
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAA-------KN 73

                          90       100
                  ....*....|....*....|....*..
gi 1841838619 422 ALSEVTAALRERLHRWQQIEILCGFQI 448
Cdd:pfam16533  74 ALEEVTKDLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 128-201 3.07e-49

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: 166.37  E-value: 3.07e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-337 2.18e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1841838619 331 AEKELES 337
Cdd:COG1196   349 AEEELEE 355
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 342-448 3.01e-51

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: 172.83  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 342 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAnslssvfRQ 421
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAA-------KN 73

                          90       100
                  ....*....|....*....|....*..
gi 1841838619 422 ALSEVTAALRERLHRWQQIEILCGFQI 448
Cdd:pfam16533  74 ALEEVTKDLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 128-201 3.07e-49

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: 166.37  E-value: 3.07e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 347-445 2.97e-39

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: 139.69  E-value: 2.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 347 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAnslssvfRQALSEV 426
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSA-------KQALEEV 73

                          90
                  ....*....|....*....
gi 1841838619 427 TAALRERLHRWQQIEILCG 445
Cdd:cd11722    74 TRELQERQHRWSQIESLCG 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-337 2.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1841838619 331 AEKELES 337
Cdd:COG1196   349 AEEELEE 355
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
249-464 6.62e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 249 EGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREAL 328
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 329 RKAEKELESHSSwyAPEALQKWL-QLTHEVEVQYYNIKKQNAEKQLLvakegAEKIKKKRNTLFGTFHVAHSSSLDDVDH 407
Cdd:COG4372   111 EELQEELEELQK--ERQDLEQQRkQLEAQIAELQSEIAEREEELKEL-----EEQLESLQEELAALEQELQALSEAEAEQ 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1841838619 408 KIltANSLSSVFRQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNID 464
Cdd:COG4372   184 AL--DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 129-193 7.40e-07

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: 46.91  E-value: 7.40e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841838619  129 VYNWTVDEVVQWLITYVeLPQYEETFRKLQLSGHAMPRLavtNTTMTGTVLKMTDRSHRQKLQLK 193
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLL---TSEEDLKELGITKLGHRKKILKA 61
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 238-334 2.18e-05

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.14  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 313
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 1841838619 314 QKYAEEELEQVREALRKAEKE 334
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 214-386 2.25e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 214 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 280
Cdd:PRK12704    8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 281 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 352
Cdd:PRK12704   87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1841838619 353 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 386
Cdd:PRK12704  166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 239-442 2.89e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  239 EHMKKMMKDLE-GLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK---KLRDEINLAKQE----AQRLKELREGTENE 310
Cdd:TIGR02168  708 EELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERleeaEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  311 RSRQKYAEEELEQVREALRKAEKELESHSSWYA--PEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK----------- 377
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAAnlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeleel 867

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619  378 -----EGAEKIKKKRNTLFGTFHvAHSSSLDDVDHKILTANSLSSVFRQALSEvtaaLRERLH----RWQQIEI 442
Cdd:TIGR02168  868 ieeleSELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEE----LREKLAqlelRLEGLEV 936
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 238-390 1.45e-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: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  238 KEHMKKMMKDLEG--------LHRAEQSLHDL-----QERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRLK 301
Cdd:TIGR02169  753 IENVKSELKELEArieeleedLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLE 832

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  302 ELREGTENER----SRQKYAEEELEQVREALRKAEKELESHsswyapealQKWLQlthEVEVQYYNIKKQ--NAEKQLLV 375
Cdd:TIGR02169  833 KEIQELQEQRidlkEQIKSIEKEIENLNGKKEELEEELEEL---------EAALR---DLESRLGDLKKErdELEAQLRE 900

                          170
                   ....*....|....*
gi 1841838619  376 AKEGAEKIKKKRNTL 390
Cdd:TIGR02169  901 LERKIEELEAQIEKK 915
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 241-336 2.32e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 241 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 306
Cdd:cd06503    24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1841838619 307 TENERSRqkyAEEELEQ--VREALRKAEKELE 336
Cdd:cd06503   104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
131-196 6.77e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 6.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841838619 131 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPrLAVTNTTMTGtvLKMTDRSHRQKLQLKALD 196
Cdd:pfam07647   3 SWSLESVADWLRS-IGLEQYTDNFRDQGITGAELL-LRLTLEDLKR--LGITSVGHRRKILKKIQE 64
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 342-448 3.01e-51

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: 172.83  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 342 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAnslssvfRQ 421
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAA-------KN 73

                          90       100
                  ....*....|....*....|....*..
gi 1841838619 422 ALSEVTAALRERLHRWQQIEILCGFQI 448
Cdd:pfam16533  74 ALEEVTKDLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 128-201 3.07e-49

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: 166.37  E-value: 3.07e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 347-445 2.97e-39

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: 139.69  E-value: 2.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 347 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAnslssvfRQALSEV 426
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSA-------KQALEEV 73

                          90
                  ....*....|....*....
gi 1841838619 427 TAALRERLHRWQQIEILCG 445
Cdd:cd11722    74 TRELQERQHRWSQIESLCG 92
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 128-201 1.88e-38

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: 136.69  E-value: 1.88e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09504     1 EVHNWTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDVVLFG 74
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 128-201 5.08e-28

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: 107.38  E-value: 5.08e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09574     1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-337 2.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1841838619 331 AEKELES 337
Cdd:COG1196   349 AEEELEE 355
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
249-464 6.62e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 249 EGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREAL 328
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 329 RKAEKELESHSSwyAPEALQKWL-QLTHEVEVQYYNIKKQNAEKQLLvakegAEKIKKKRNTLFGTFHVAHSSSLDDVDH 407
Cdd:COG4372   111 EELQEELEELQK--ERQDLEQQRkQLEAQIAELQSEIAEREEELKEL-----EEQLESLQEELAALEQELQALSEAEAEQ 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1841838619 408 KIltANSLSSVFRQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNID 464
Cdd:COG4372   184 AL--DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 129-193 7.40e-07

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: 46.91  E-value: 7.40e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841838619  129 VYNWTVDEVVQWLITYVeLPQYEETFRKLQLSGHAMPRLavtNTTMTGTVLKMTDRSHRQKLQLK 193
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLL---TSEEDLKELGITKLGHRKKILKA 61
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 244-386 3.23e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 244 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 322
Cdd:COG1579     2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619 323 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:COG1579    70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-390 3.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELR-------EGTENERSRQKYAEEELEQ 323
Cdd:COG1196   276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeeleeleEELEELEEELEEAEEELEE 355

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841838619 324 VREALRKAEKELESHSswyapEALQKWLQLTHEVEVQYYNIKKQ--NAEKQLLVAKEGAEKIKKKRNTL 390
Cdd:COG1196   356 AEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAaaELAAQLEELEEAEEALLERLERL 419
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-382 8.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1841838619 331 AEKELEshsswyapEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEK 382
Cdd:COG1196   447 AAEEEA--------ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
237-352 1.39e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 237 SKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvEKVHLEKKLRDEINLAKQE------------AQRLKELR 304
Cdd:COG4717   120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEEleelleqlslatEEELQDLA 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1841838619 305 EGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ 352
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
239-390 1.45e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 239 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR---------DEINLAKQEAQRLKELREGTEN 309
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 310 ERSRQKY---AEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYniKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:COG4717   151 LEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEE 228


                  ....
gi 1841838619 387 RNTL 390
Cdd:COG4717   229 LEQL 232
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-441 1.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKK---LRDEINLAKQE----AQRLKELREGTENERSRQKYAEEELEQ 323
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 324 VREALRKAEKELESHSswyapEALQKWLQlthevevqyyniKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHvAHSSSLD 403
Cdd:COG1196   321 LEEELAELEEELEELE-----EELEELEE------------ELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELE 382

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1841838619 404 DVDHKILTANSLSSVFRQALSEVTAALRERLHRWQQIE 441
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 238-334 2.18e-05

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.14  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 313
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 1841838619 314 QKYAEEELEQVREALRKAEKE 334
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 214-386 2.25e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 214 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 280
Cdd:PRK12704    8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 281 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 352
Cdd:PRK12704   87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1841838619 353 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 386
Cdd:PRK12704  166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 239-442 2.89e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  239 EHMKKMMKDLE-GLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK---KLRDEINLAKQE----AQRLKELREGTENE 310
Cdd:TIGR02168  708 EELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERleeaEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  311 RSRQKYAEEELEQVREALRKAEKELESHSSWYA--PEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK----------- 377
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAAnlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeleel 867

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619  378 -----EGAEKIKKKRNTLFGTFHvAHSSSLDDVDHKILTANSLSSVFRQALSEvtaaLRERLH----RWQQIEI 442
Cdd:TIGR02168  868 ieeleSELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEE----LREKLAqlelRLEGLEV 936
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 131-171 4.49e-05

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: 41.92  E-value: 4.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1841838619 131 NWTVDEVVQWlITYVELPQYEETFRKLQLSGH--------AMPRLAVTN 171
Cdd:cd09530     2 SWDTEDVAEW-IEGLGFPQYRECFTTNFIDGRklilvdasTLPRMGVTD 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-467 6.88e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 316
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  317 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTF 394
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  395 HvahsssldDVDHKILTANSLSSVFRQALSEVTAALRERLHRWQQIEILCGFQ------------IVNN----PGIHSLV 458
Cdd:TIGR02168  454 E--------ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfsegvkaLLKNqsglSGILGVL 525

                          250
                   ....*....|
gi 1841838619  459 AAL-NIDPSW 467
Cdd:TIGR02168  526 SELiSVDEGY 535
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-439 8.51e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 8.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  253 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 325
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  326 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLfgtfhvahSSSLDDV 405
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL--------RSKVAQL 391

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1841838619  406 DHKIltaNSLSSVFRQALSEVTaALRERLHRWQQ 439
Cdd:TIGR02168  392 ELQI---ASLNNEIERLEARLE-RLEDRRERLQQ 421
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 233-365 1.21e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 233 QNRYSKEHMK--KMMKDLEGLHR-AEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQR---------- 299
Cdd:PRK00409  508 KKLIGEDKEKlnELIASLEELEReLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeakkead 587

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841838619 300 --LKELREGTENERSRQKyaEEELEQVREALRKAEKELESHSswYAPEALQKWLQLTHEVEVQYYNIK 365
Cdd:PRK00409  588 eiIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKK--KKQKEKQEELKVGDEVKYLSLGQK 651
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 136-197 1.47e-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: 39.92  E-value: 1.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841838619 136 EVVQWLITyVELPQYEETFRKLQLSGHAMPRLavTNTTMTGtvLKMTDRSHRQKLqLKALDT 197
Cdd:cd09487     1 DVAEWLES-LGLEQYADLFRKNEIDGDALLLL--TDEDLKE--LGITSPGHRKKI-LRAIQR 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 238-432 1.74e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYA 317
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  318 EEELEQVREALRKAEKELESH-----SSWYAPEALQKWLQL------THEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALlneraSLEEALALLRSELEElseelrELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1841838619  387 RNTLFGTFHVAHSSSLDDVDHKILTANSLSSVFRQALSEVTAALRE 432
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 239-381 2.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 239 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAE 318
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841838619 319 EELEQVREALRKAEKELEShsswyapEALQKWLQLTHEVEVQYYN---IKKQNAEKQLLVAKEGAE 381
Cdd:COG1196   470 EEAALLEAALAELLEELAE-------AAARLLLLLEAEADYEGFLegvKAALLLAGLRGLAGAVAV 528
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
238-387 2.46e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR-------DEINL-----------------A 293
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEErlkelepfyneylelkdA 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 294 KQEAQRLKELREGTENERSRqkyAEEELEQVREALRKAEKELESHSSWYAPE----ALQKWLQLTHEV-----EVQYYNI 364
Cdd:PRK03918  611 EKELEREEKELKKLEEELDK---AFEELAETEKRLEELRKELEELEKKYSEEeyeeLREEYLELSRELaglraELEELEK 687

                         170       180
                  ....*....|....*....|...
gi 1841838619 365 KKQNAEKQLLVAKEGAEKIKKKR 387
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKAK 710
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
239-439 3.18e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  239 EHMKKMMKDLEGLHR----AEQSLHDLqERLHKAQEEHRTVEVEKVHLEKkLRDEINL--AKQEAQRLKELREGTENERS 312
Cdd:COG4913    228 DALVEHFDDLERAHEaledAREQIELL-EPIRELAERYAAARERLAELEY-LRAALRLwfAQRRLELLEAELEELRAELA 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  313 RQKYAEEELEQVREALRKAEKELeshsswyapealqkwlqlthevEVQYYNI---KKQNAEKQLLVAKEGAEKIKKKRNT 389
Cdd:COG4913    306 RLEAELERLEARLDALREELDEL----------------------EAQIRGNggdRLEQLEREIERLERELEERERRRAR 363

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1841838619  390 LFGTFHVAHSSSLDDVDhkILTANSLSSV-FRQALSEVTAALRERLHRWQQ 439
Cdd:COG4913    364 LEALLAALGLPLPASAE--EFAALRAEAAaLLEALEEELEALEEALAEAEA 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
251-330 3.85e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKlrDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG4717   434 LEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
233-390 5.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 233 QNRYSKEHMKKMMKDLEGLHRAEQSLHDLQ---ERLHKAQEEHRTVEVEKVHLE---KKLRDEINLAKQEAQRLKELREG 306
Cdd:COG4717    55 ADELFKPQGRKPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEaelEELREELEKLEKLLQLLPLYQEL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 307 TENERSRQKYAE---------EELEQVREALRKAEKELESHSSwyAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK 377
Cdd:COG4717   135 EALEAELAELPErleeleerlEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212

                         170
                  ....*....|...
gi 1841838619 378 EGAEKIKKKRNTL 390
Cdd:COG4717   213 EELEEAQEELEEL 225
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
247-437 5.98e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 5.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  247 DLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVRE 326
Cdd:COG4913    662 DVASAEREIAELEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQ---AEEELDELQD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  327 ALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQyynikkQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVD 406
Cdd:COG4913    735 RLEAAEDLARLELRALLEERFAAALGDAVERELR------ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLD 808

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1841838619  407 HKILTANSLSSVFRQ----ALSEVTAALRERLHRW 437
Cdd:COG4913    809 ADLESLPEYLALLDRleedGLPEYEERFKELLNEN 843
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
251-360 6.46e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 251 LHRAEQSLHDLQERLhkaQEEHRTVevekvhleKKLRDEINLAKQE-AQRLKELREGTENERSRQKYAEEELEQVREALR 329
Cdd:COG3206   272 LAELEAELAELSARY---TPNHPDV--------IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLE 340

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1841838619 330 KAEKELeshsswyaPEALQKWLQLTHEVEVQ 360
Cdd:COG3206   341 ARLAEL--------PELEAELRRLEREVEVA 363
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-337 6.79e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVREALRK 330
Cdd:COG4913    347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRE 423


                   ....*..
gi 1841838619  331 AEKELES 337
Cdd:COG4913    424 LEAEIAS 430
PTZ00121 PTZ00121
MAEBL; Provisional
 246-386 8.58e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 8.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  246 KDLEGLHRAEQSLHDlQERLHKAQEEHRTVEV---EKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELE 322
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKD-AEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841838619  323 QVREALRKAEKELESHSSWYAPEALQKwlqlthevEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:PTZ00121  1303 KADEAKKKAEEAKKADEAKKKAEEAKK--------KADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 131-190 9.43e-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: 38.07  E-value: 9.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 131 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPRLavTNTTMTgTVLKMTDRSHRQKL 190
Cdd:cd09505     4 DWSEEDVCTWLRS-IGLEQYVEVFRANNIDGKELLNL--TKESLS-KDLKIESLGHRNKI 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-337 1.18e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 249 EGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL---RDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVR 325
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90
                  ....*....|..
gi 1841838619 326 EALRKAEKELES 337
Cdd:COG1196   382 EELAEELLEALR 393
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 238-328 1.34e-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: 39.13  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 238 KEHMKKMMKDLEglhRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK-----------------KLRDEINLAKQEAQRL 300
Cdd:pfam20492  19 EEETKKAQEELE---ESEETAEELEEERRQAEEEAERLEQKRQEAEEekerleesaemeaeekeQLEAELAEAQEEIARL 95

                          90       100
                  ....*....|....*....|....*...
gi 1841838619 301 KELREGTENERSRqkyAEEELEQVREAL 328
Cdd:pfam20492  96 EEEVERKEEEARR---LQEELEEAREEE 120
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 238-390 1.45e-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: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  238 KEHMKKMMKDLEG--------LHRAEQSLHDL-----QERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRLK 301
Cdd:TIGR02169  753 IENVKSELKELEArieeleedLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLE 832

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  302 ELREGTENER----SRQKYAEEELEQVREALRKAEKELESHsswyapealQKWLQlthEVEVQYYNIKKQ--NAEKQLLV 375
Cdd:TIGR02169  833 KEIQELQEQRidlkEQIKSIEKEIENLNGKKEELEEELEEL---------EAALR---DLESRLGDLKKErdELEAQLRE 900

                          170
                   ....*....|....*
gi 1841838619  376 AKEGAEKIKKKRNTL 390
Cdd:TIGR02169  901 LERKIEELEAQIEKK 915
PTZ00121 PTZ00121
MAEBL; Provisional
 230-385 1.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  230 AYIQNRYSKEHMKKMMK--DLEGLHRAEQSLHDLQER-----LHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQ---R 299
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  300 LKELREGTENERSRQ---KYAEEELEQVREALRKAEKELESHSSWYAPEA--LQKWLQLTHEVEVQyyNIKKQNAEKQLL 374
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAeeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeeKKKAEELKKAEEEN--KIKAEEAKKEAE 1740

                          170
                   ....*....|.
gi 1841838619  375 VAKEGAEKIKK 385
Cdd:PTZ00121  1741 EDKKKAEEAKK 1751
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
246-344 1.64e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 246 KDLEG-LHRAEQSLHDLQERLHKAQEEHRTvevekvhlEKKLRDEINLAKQEAQRL-KELREgtenERSRQKYAEEELEQ 323
Cdd:COG2433   430 EELEAeLEEKDERIERLERELSEARSEERR--------EIRKDREISRLDREIERLeRELEE----ERERIEELKRKLER 497

                          90       100
                  ....*....|....*....|.
gi 1841838619 324 VREALRKaekeleSHSSWYAP 344
Cdd:COG2433   498 LKELWKL------EHSGELVP 512
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 253-382 2.24e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 253 RAEQSLHDLqERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQ---------------------EAQRLKELREGTENER 311
Cdd:pfam15709 342 RAEMRRLEV-ERKRREQEEQRRLQQEQLERAEKMREELELEQQrrfeeirlrkqrleeerqrqeEEERKQRLQLQAAQER 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 312 SRQKYAE-----EELEQVR--EALRKAE------KELESHSSwyapEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKE 378
Cdd:pfam15709 421 ARQQQEEfrrklQELQRKKqqEEAERAEaekqrqKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE 496


                  ....
gi 1841838619 379 GAEK 382
Cdd:pfam15709 497 RRQK 500
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 241-336 2.32e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 241 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 306
Cdd:cd06503    24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1841838619 307 TENERSRqkyAEEELEQ--VREALRKAEKELE 336
Cdd:cd06503   104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
PTZ00121 PTZ00121
MAEBL; Provisional
 238-385 2.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvekvhlEKKLRDEINLAKQEAQRlKELREGTENERSRQKYA 317
Cdd:PTZ00121  1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAEAAA-DEAEAAEEKAEAAEKKK 1373

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841838619  318 EEELEQVREALRKAEKELEshsswyAPEALQKwlqlTHEVEVQYYNIKKQNAEKQLL-VAKEGAEKIKK 385
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKK------ADEAKKK----AEEDKKKADELKKAAAAKKKAdEAKKKAEEKKK 1432
PTZ00121 PTZ00121
MAEBL; Provisional
 263-385 2.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  263 ERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKE-----------LREGTENERSRQKYAEEELEQVREALRKA 331
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeearieevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1841838619  332 EKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 385
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 230-334 2.66e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 230 AYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTEN 309
Cdd:COG4942   134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

                          90       100
                  ....*....|....*....|....*
gi 1841838619 310 ERSRQKYAEEELEQVREALRKAEKE 334
Cdd:COG4942   214 ELAELQQEAEELEALIARLEAEAAA 238
PRK12705 PRK12705
hypothetical protein; Provisional
 214-381 2.99e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.85  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 214 FMLVVSIVIGVGGCWFAYI---QNRYSKEHMK-KMMKDLEGLHRAEQSLHDLQERLHKAQEEHRtvevekvhleKKLRDE 289
Cdd:PRK12705    6 LLVILLLLIGLLLGVLVVLlkkRQRLAKEAERiLQEAQKEAEEKLEAALLEAKELLLRERNQQR----------QEARRE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 290 INLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELEshsswyapealqkwlQLTHEVEVQYYNIKKQNA 369
Cdd:PRK12705   76 REELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE---------------ELEKQLDNELYRVAGLTP 140

                         170
                  ....*....|....
gi 1841838619 370 E--KQLLVAKEGAE 381
Cdd:PRK12705  141 EqaRKLLLKLLDAE 154
PTZ00121 PTZ00121
MAEBL; Provisional
 239-386 3.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  239 EHMKKM--MKDLEGLHRAEQSLHDLQER---LHKAQ-----EEHRTVEVEKVHLEKKLRDEINLAKQEAQRLK--ELREG 306
Cdd:PTZ00121  1549 DELKKAeeLKKAEEKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKA 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  307 TENERSRQKYAEEELEQVREA--LRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIK 384
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708


                   ..
gi 1841838619  385 KK 386
Cdd:PTZ00121  1709 KK 1710
PTZ00121 PTZ00121
MAEBL; Provisional
 238-385 4.68e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENER------ 311
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkadeak 1476

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841838619  312 ---SRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 385
Cdd:PTZ00121  1477 kkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
237-387 5.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 237 SKEHMKKMMKDLEGLHR-------AEQSLHDLQERLHKAQEEhrtvevekvhLEKKlRDEINLAKQEAQRLKElregtEN 309
Cdd:PRK03918  586 SVEELEERLKELEPFYNeylelkdAEKELEREEKELKKLEEE----------LDKA-FEELAETEKRLEELRK-----EL 649

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841838619 310 ERSRQKYAEEELEQVREALRKAEKELESHSSWYapEALQKWLQlthEVEVQYYNIKKQNAEKQllVAKEGAEKIKKKR 387
Cdd:PRK03918  650 EELEKKYSEEEYEELREEYLELSRELAGLRAEL--EELEKRRE---EIKKTLEKLKEELEERE--KAKKELEKLEKAL 720
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 253-336 6.56e-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: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 253 RAEQSLHDLQERLHKAQEEHRTVEvekvhleKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAE 332
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKKAQ-------EELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75


                  ....
gi 1841838619 333 KELE 336
Cdd:pfam20492  76 EEKE 79
PTZ00121 PTZ00121
MAEBL; Provisional
 263-386 6.68e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  263 ERLHKAQEEHRTVEVEKVHlEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKEleshsswy 342
Cdd:PTZ00121  1281 DELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-------- 1351

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1841838619  343 aPEALQKWLQLTHEvevqyyniKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:PTZ00121  1352 -AEAAADEAEAAEE--------KAEAAEKKKEEAKKKADAAKKK 1386
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
131-196 6.77e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 6.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841838619 131 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPrLAVTNTTMTGtvLKMTDRSHRQKLQLKALD 196
Cdd:pfam07647   3 SWSLESVADWLRS-IGLEQYTDNFRDQGITGAELL-LRLTLEDLKR--LGITSVGHRRKILKKIQE 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 131-192 9.18e-03

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: 35.32  E-value: 9.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841838619 131 NWTVDEVVQWLITYvELPQYEETFRKLQLSGHAMPRLavTNTTMTGtvLKMTDRSHRQKLQL 192
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQL--TEDDLLK--LGVTLLGHRKKILY 58
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 229-440 9.24e-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: 39.57  E-value: 9.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  229 FAYIQNRYSKEHmKKMMKDLEGLHRAEQ----------SLHDLQERLHK--------AQEEHRTVEVEKVHLEKKLRDEI 290
Cdd:TIGR00618  154 FAQFLKAKSKEK-KELLMNLFPLDQYTQlalmefakkkSLHGKAELLTLrsqlltlcTPCMPDTYHERKQVLEKELKHLR 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  291 NLAKQEAQRLKELREGTENERSRQKYaEEELEQVREALRKAEKELESHSSwyAPEALQ---KWLQLTHEVE-VQYYNIKK 366
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKK-QQLLKQLRARIEELRAQEAVLEE--TQERINrarKAAPLAAHIKaVTQIEQQA 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619  367 QNAEKQLLVAKEGAEKIKKKRNTlfgtfHVAHSSSLDDVDHKILTANSLSSVFRQALSEVTA---------ALRERLHRW 437
Cdd:TIGR00618  310 QRIHTELQSKMRSRAKLLMKRAA-----HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireiscqqhTLTQHIHTL 384


                   ...
gi 1841838619  438 QQI 440
Cdd:TIGR00618  385 QQQ 387
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 238-386 9.60e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 238 KEHMKKMMKDLEGLH--RAEQSLHDLQER-------LHKAQEEHRTVEVEKVHLEKKL---RDEINLAKQEAQRLKELRE 305
Cdd:PRK04778  262 KEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFLehaKEQNKELKEEIDRVKQSYT 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841838619 306 GTENERSRQKYAEEELEQVREALRKAEKELESHSSWY--APEALQKWLQLTHEVEVQYYNIKK--QNAEKQLLVAKEGAE 381
Cdd:PRK04778  342 LNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYseLQEELEEILKQLEEIEKEQEKLSEmlQGLRKDELEAREKLE 421


                  ....*
gi 1841838619 382 KIKKK 386
Cdd:PRK04778  422 RYRNK 426
 
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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