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Conserved domains on  [gi|1841845163|ref|NP_001369510|]
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stromal interaction molecule 1 isoform 16 [Homo sapiens]

Protein Classification

SAM_superfamily and SOAR domain-containing protein( domain architecture ID 10977751)

SAM_superfamily and SOAR domain-containing protein

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 ...
 179-278 3.99e-54

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: 177.45  E-value: 3.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 179 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 258
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 1841845163 259 ALRERLHRWQQIEILCGFQI 278
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1-38 2.31e-20

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.


The actual alignment was detected with superfamily member cd09573:

Pssm-ID: 472832  Cd Length: 74  Bit Score: 85.09  E-value: 2.31e-20
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841845163   1 MPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 38
Cdd:cd09573    37 MPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-174 2.32e-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: 53.79  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 167
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1841845163 168 AEKELES 174
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 ...
 179-278 3.99e-54

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: 177.45  E-value: 3.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 179 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 258
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 1841845163 259 ALRERLHRWQQIEILCGFQI 278
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 184-275 3.74e-42

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: 145.47  E-value: 3.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 184 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRER 263
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                          90
                  ....*....|..
gi 1841845163 264 LHRWQQIEILCG 275
Cdd:cd11722    81 QHRWSQIESLCG 92
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 1-38 2.31e-20

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: 85.09  E-value: 2.31e-20
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841845163   1 MPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 38
Cdd:cd09573    37 MPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-174 2.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 167
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1841845163 168 AEKELES 174
Cdd:COG1196   349 AEEELEE 355
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 81-264 5.20e-07

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: 50.69  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  81 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 159
Cdd:COG1579     2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 160 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKKrntlfgtfhvahsssL 239
Cdd:COG1579    70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE---------------L 126

                         170       180
                  ....*....|....*....|....*
gi 1841845163 240 DDVDHKILTAKQALSEVTAALRERL 264
Cdd:COG1579   127 AELEAELAELEAELEEKKAELDEEL 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 88-297 5.87e-06

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: 49.28  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 153
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  154 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGT- 230
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELq 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  231 ----FHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQI-EILCGF-----QIVNN----PGIHSLVAAL-NIDP 295
Cdd:TIGR02168  454 eeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEGFsegvkALLKNqsglSGILGVLSELiSVDE 533


                   ..
gi 1841845163  296 SW 297
Cdd:TIGR02168  534 GY 535
PRK12704 PRK12704
phosphodiesterase; Provisional
 51-223 2.58e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  51 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 117
Cdd:PRK12704    8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 118 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 189
Cdd:PRK12704   87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1841845163 190 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 223
Cdd:PRK12704  166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 75-171 6.73e-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: 42.60  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  75 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 150
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 1841845163 151 QKYAEEELEQVREALRKAEKE 171
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 90-227 2.28e-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: 44.28  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   90 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 162
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841845163  163 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTL 227
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL 384
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
76-263 2.30e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  76 EHMKKMMKDLEGL--HRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLK----EL--------- 140
Cdd:PRK03918  365 EEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpv 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 141 --REGTENER---------------SRQKYAEEELEQVREALRKAEKELESHSSwyapeaLQKWLQLTHEVEVQYYNIKK 203
Cdd:PRK03918  441 cgRELTEEHRkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKLKK 514

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841845163 204 QNAEKqLLVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILTAKQALSEVTAALRER 263
Cdd:PRK03918  515 YNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKelekleelkKKLAELEKKLDELEEELAELLKELEEL 582
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 78-173 5.18e-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: 37.42  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  78 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 143
Cdd:cd06503    24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1841845163 144 TENERSRqkyAEEELEQ--VREALRKAEKELE 173
Cdd:cd06503   104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 179-278 3.99e-54

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: 177.45  E-value: 3.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 179 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 258
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 1841845163 259 ALRERLHRWQQIEILCGFQI 278
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 184-275 3.74e-42

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: 145.47  E-value: 3.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 184 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRER 263
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                          90
                  ....*....|..
gi 1841845163 264 LHRWQQIEILCG 275
Cdd:cd11722    81 QHRWSQIESLCG 92
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 1-38 2.31e-20

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: 85.09  E-value: 2.31e-20
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841845163   1 MPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 38
Cdd:cd09573    37 MPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 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 ...
 1-38 1.74e-15

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: 71.21  E-value: 1.74e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841845163   1 MPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 38
Cdd:cd09504    37 LPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDVVLFG 74
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 1-38 1.90e-10

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: 56.92  E-value: 1.90e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841845163   1 MPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 38
Cdd:cd09574    37 LPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-174 2.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 167
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1841845163 168 AEKELES 174
Cdd:COG1196   349 AEEELEE 355
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 81-264 5.20e-07

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: 50.69  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  81 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 159
Cdd:COG1579     2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 160 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKKrntlfgtfhvahsssL 239
Cdd:COG1579    70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE---------------L 126

                         170       180
                  ....*....|....*....|....*
gi 1841845163 240 DDVDHKILTAKQALSEVTAALRERL 264
Cdd:COG1579   127 AELEAELAELEAELEEKKAELDEEL 151
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
86-174 3.36e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  86 EGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREAL 165
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110


                  ....*....
gi 1841845163 166 RKAEKELES 174
Cdd:COG4372   111 EELQEELEE 119
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 88-297 5.87e-06

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: 49.28  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 153
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  154 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGT- 230
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELq 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  231 ----FHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQI-EILCGF-----QIVNN----PGIHSLVAAL-NIDP 295
Cdd:TIGR02168  454 eeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEGFsegvkALLKNqsglSGILGVLSELiSVDE 533


                   ..
gi 1841845163  296 SW 297
Cdd:TIGR02168  534 GY 535
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-271 7.24e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 7.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKK---LRDEINLAKQE----AQRLKELREGTENERSRQKYAEEELEQ 160
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 161 VREALRKAEKELESHSswyapEALQKWLQlthevevqyyniKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHvAHSSSLD 240
Cdd:COG1196   321 LEEELAELEEELEELE-----EELEELEE------------ELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELE 382

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1841845163 241 DVDHKILTAKQALSEVTAALRERLHRWQQIE 271
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALL 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-189 1.91e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  74 SKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvEKVHLEKKLRDEINLAKQE------------AQRLKELR 141
Cdd:COG4717   120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEEleelleqlslatEEELQDLA 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1841845163 142 EGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ 189
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
76-227 2.09e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  76 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR---------DEINLAKQEAQRLKELREGTEN 146
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 147 ERSRQKY---AEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYniKKQNAEKQLLVAKEGAEKIKKK 223
Cdd:COG4717   151 LEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEE 228


                  ....
gi 1841845163 224 RNTL 227
Cdd:COG4717   229 LEQL 232
PRK12704 PRK12704
phosphodiesterase; Provisional
 51-223 2.58e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  51 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 117
Cdd:PRK12704    8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 118 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 189
Cdd:PRK12704   87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1841845163 190 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 223
Cdd:PRK12704  166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 75-171 6.73e-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: 42.60  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  75 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 150
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 1841845163 151 QKYAEEELEQVREALRKAEKE 171
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 75-266 6.76e-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: 45.82  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   75 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYA 154
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  155 EEELEQVREALRKAEKELESH-----SSWYAPEALQKWLQL------THEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 223
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALlneraSLEEALALLRSELEElseelrELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1841845163  224 RNTLFGTFHVAHSSSLDDvdhkILTAKQALSEVTAALRERLHR 266
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEE----AEALENKIEDDEEEARRRLKR 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-272 6.94e-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: 45.82  E-value: 6.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   76 EHMKKMMKDLE-GLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK---KLRDEINLAKQE----AQRLKELREGTENE 147
Cdd:TIGR02168  708 EELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERleeaEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  148 RSRQKYAEEELEQVREALRKAEKELESHSSWYA--PEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK----------- 214
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAAnlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeleel 867

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841845163  215 -----EGAEKIKKKRNTLFGTFHVAHS------SSLDDVDHKILTAKQALSEvtaaLRERLH----RWQQIEI 272
Cdd:TIGR02168  868 ieeleSELEALLNERASLEEALALLRSeleelsEELRELESKRSELRRELEE----LREKLAqlelRLEGLEV 936
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
76-271 9.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 9.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   76 EHMKKMMKDLEGLHR----AEQSLHDLqERLHKAQEEHRTVEVEKVHLEKkLRDEINL--AKQEAQRLKELREGTENERS 149
Cdd:COG4913    228 DALVEHFDDLERAHEaledAREQIELL-EPIRELAERYAAARERLAELEY-LRAALRLwfAQRRLELLEAELEELRAELA 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  150 RQKYAEEELEQVREALRKAEKELeshsswyapealqkwlqlthevEVQYYNI---KKQNAEKQLlvakEGAEKIKKKRNT 226
Cdd:COG4913    306 RLEAELERLEARLDALREELDEL----------------------EAQIRGNggdRLEQLEREI----ERLERELEERER 359

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1841845163  227 LFGTFHVAhsssLDDVDHKILTAKQALSEVTAALRERLHRWQQIE 271
Cdd:COG4913    360 RRARLEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 70-202 1.28e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  70 QNRYSKEHMK--KMMKDLEGLHR-AEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQR---------- 136
Cdd:PRK00409  508 KKLIGEDKEKlnELIASLEELEReLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeakkead 587

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841845163 137 --LKELREGTENERSRQKyaEEELEQVREALRKAEKELESHSswYAPEALQKWLQLTHEVEVQYYNIK 202
Cdd:PRK00409  588 eiIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKK--KKQKEKQEELKVGDEVKYLSLGQK 651
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
84-267 1.39e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   84 DLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVRE 163
Cdd:COG4913    662 DVASAEREIAELEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQ---AEEELDELQD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  164 ALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQyynikkQNAEKQLLVAKEGAEKIKKKRNTLFGTF-------HVAHS 236
Cdd:COG4913    735 RLEAAEDLARLELRALLEERFAAALGDAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnrewpaeTADLD 808

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1841845163  237 SSLDDVDH--KILT--AKQALSEVTAALRERLHRW 267
Cdd:COG4913    809 ADLESLPEylALLDrlEEDGLPEYEERFKELLNEN 843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 90-227 2.28e-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: 44.28  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   90 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 162
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841845163  163 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTL 227
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 76-218 2.51e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  76 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAE 155
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841845163 156 EELEQVREALRKAEKELEShsswyapEALQKWLQLTHEVEVQYYN---IKKQNAEKQLLVAKEGAE 218
Cdd:COG1196   470 EEAALLEAALAELLEELAE-------AAARLLLLLEAEADYEGFLegvKAALLLAGLRGLAGAVAV 528
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
75-224 2.88e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  75 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR-------DEINL-----------------A 130
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEErlkelepfyneylelkdA 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 131 KQEAQRLKELREGTENERSRqkyAEEELEQVREALRKAEKELESHSSWYAPE----ALQKWLQLTHEV-----EVQYYNI 201
Cdd:PRK03918  611 EKELEREEKELKKLEEELDK---AFEELAETEKRLEELRKELEELEKKYSEEeyeeLREEYLELSRELaglraELEELEK 687

                         170       180
                  ....*....|....*....|...
gi 1841845163 202 KKQNAEKQLLVAKEGAEKIKKKR 224
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKAK 710
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-167 4.74e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKlrDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 167
Cdd:COG4717   434 LEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
88-174 5.47e-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: 5.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   88 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVREALRK 167
Cdd:COG4913    347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRE 423


                   ....*..
gi 1841845163  168 AEKELES 174
Cdd:COG4913    424 LEAEIAS 430
PTZ00121 PTZ00121
MAEBL; Provisional
 83-223 6.85e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   83 KDLEGLHRAEQSLHDlQERLHKAQEEHRTVEV---EKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELE 159
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKD-AEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841845163  160 QVREALRKAEKELESHSSWYAPEALQKwlqlthevEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 223
Cdd:PTZ00121  1303 KADEAKKKAEEAKKADEAKKKAEEAKK--------KADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
70-227 7.61e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  70 QNRYSKEHMKKMMKDLEGLHRAEQSLHDLQ---ERLHKAQEEHRTVEVEKVHLE---KKLRDEINLAKQEAQRLKELREG 143
Cdd:COG4717    55 ADELFKPQGRKPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEaelEELREELEKLEKLLQLLPLYQEL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 144 TENERSRQKYAE---------EELEQVREALRKAEKELESHSSwyAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK 214
Cdd:COG4717   135 EALEAELAELPErleeleerlEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212

                         170
                  ....*....|...
gi 1841845163 215 EGAEKIKKKRNTL 227
Cdd:COG4717   213 EELEEAQEELEEL 225
PTZ00121 PTZ00121
MAEBL; Provisional
 67-222 1.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   67 AYIQNRYSKEHMKKMMK--DLEGLHRAEQSLHDLQER-----LHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQ---R 136
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  137 LKELREGTENERSRQ---KYAEEELEQVREALRKAEKELESHSSWYAPEA--LQKWLQLTHEVEVQyyNIKKQNAEKQLL 211
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAeeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeeKKKAEELKKAEEEN--KIKAEEAKKEAE 1740

                          170
                   ....*....|.
gi 1841845163  212 VAKEGAEKIKK 222
Cdd:PTZ00121  1741 EDKKKAEEAKK 1751
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
83-181 1.39e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  83 KDLEG-LHRAEQSLHDLQERLHKAQEEHRTvevekvhlEKKLRDEINLAKQEAQRL-KELREgtenERSRQKYAEEELEQ 160
Cdd:COG2433   430 EELEAeLEEKDERIERLERELSEARSEERR--------EIRKDREISRLDREIERLeRELEE----ERERIEELKRKLER 497

                          90       100
                  ....*....|....*....|.
gi 1841845163 161 VREALRKaekeleSHSSWYAP 181
Cdd:COG2433   498 LKELWKL------EHSGELVP 512
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
88-197 1.59e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  88 LHRAEQSLHDLQERLhkaQEEHRTVevekvhleKKLRDEINLAKQE-AQRLKELREGTENERSRQKYAEEELEQVREALR 166
Cdd:COG3206   272 LAELEAELAELSARY---TPNHPDV--------IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLE 340

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1841845163 167 KAEKELeshsswyaPEALQKWLQLTHEVEVQ 197
Cdd:COG3206   341 ARLAEL--------PELEAELRRLEREVEVA 363
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 75-227 1.59e-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: 41.21  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   75 KEHMKKMMKDLEG--------LHRAEQSLHDL-----QERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRLK 138
Cdd:TIGR02169  753 IENVKSELKELEArieeleedLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLE 832

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  139 ELREGTENER----SRQKYAEEELEQVREALRKAEKELESHsswyapealQKWLQlthEVEVQYYNIKKQ--NAEKQLLV 212
Cdd:TIGR02169  833 KEIQELQEQRidlkEQIKSIEKEIENLNGKKEELEEELEEL---------EAALR---DLESRLGDLKKErdELEAQLRE 900

                          170
                   ....*....|....*
gi 1841845163  213 AKEGAEKIKKKRNTL 227
Cdd:TIGR02169  901 LERKIEELEAQIEKK 915
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
92-269 1.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  92 EQSLHDLQERLHKAQEEHRTVEVEKVhleKKLRDEINLAKQEAQRLKELREgtenersRQKYAEEELEQVREALRKAEKE 171
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKEL---KELEEELKEAEEKEEEYAELQE-------ELEELEEELEELEAELEELREE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 172 LESHSSWYAP-EALQKWLQLTHEVE---VQYYNIKKQ-----NAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDv 242
Cdd:COG4717   118 LEKLEKLLQLlPLYQELEALEAELAelpERLEELEERleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQD- 196

                         170       180
                  ....*....|....*....|....*..
gi 1841845163 243 dhkILTAKQALSEVTAALRERLHRWQQ 269
Cdd:COG4717   197 ---LAEELEELQQRLAELEEELEEAQE 220
PTZ00121 PTZ00121
MAEBL; Provisional
 100-222 2.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  100 ERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKE-----------LREGTENERSRQKYAEEELEQVREALRKA 168
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeearieevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1841845163  169 EKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 222
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
PTZ00121 PTZ00121
MAEBL; Provisional
 75-222 2.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   75 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvekvhlEKKLRDEINLAKQEAQRlKELREGTENERSRQKYA 154
Cdd:PTZ00121  1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAEAAA-DEAEAAEEKAEAAEKKK 1373

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841845163  155 EEELEQVREALRKAEKELEshsswyAPEALQKwlqlTHEVEVQYYNIKKQNAEKQLL-VAKEGAEKIKK 222
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKK------ADEAKKK----AEEDKKKADELKKAAAAKKKAdEAKKKAEEKKK 1432
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
76-263 2.30e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  76 EHMKKMMKDLEGL--HRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLK----EL--------- 140
Cdd:PRK03918  365 EEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpv 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 141 --REGTENER---------------SRQKYAEEELEQVREALRKAEKELESHSSwyapeaLQKWLQLTHEVEVQYYNIKK 203
Cdd:PRK03918  441 cgRELTEEHRkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKLKK 514

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841845163 204 QNAEKqLLVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILTAKQALSEVTAALRER 263
Cdd:PRK03918  515 YNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKelekleelkKKLAELEKKLDELEEELAELLKELEEL 582
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-271 2.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  90 RAEQSLHDLQERLHK---AQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENErsrqkyaEEELEQVREALR 166
Cdd:COG1196   219 KEELKELEAELLLLKlreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-------ELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 167 KAEKELeshsswyapEALQKWLQLTHEvEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHsSSLDDVDHKI 246
Cdd:COG1196   292 ELLAEL---------ARLEQDIARLEE-RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-EELEEAEAEL 360

                         170       180
                  ....*....|....*....|....*
gi 1841845163 247 LTAKQALSEVTAALRERLHRWQQIE 271
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELA 385
PTZ00121 PTZ00121
MAEBL; Provisional
 76-223 2.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   76 EHMKKM--MKDLEGLHRAEQSLHDLQER---LHKAQ-----EEHRTVEVEKVHLEKKLRDEINLAKQEAQRLK--ELREG 143
Cdd:PTZ00121  1549 DELKKAeeLKKAEEKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKA 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  144 TENERSRQKYAEEELEQVREA--LRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIK 221
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708


                   ..
gi 1841845163  222 KK 223
Cdd:PTZ00121  1709 KK 1710
PRK12705 PRK12705
hypothetical protein; Provisional
 51-218 2.99e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  51 FMLVVSIVIGVGGCWFAYI---QNRYSKEHMK-KMMKDLEGLHRAEQSLHDLQERLHKAQEEHRtvevekvhleKKLRDE 126
Cdd:PRK12705    6 LLVILLLLIGLLLGVLVVLlkkRQRLAKEAERiLQEAQKEAEEKLEAALLEAKELLLRERNQQR----------QEARRE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 127 INLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELEshsswyapealqkwlQLTHEVEVQYYNIKKQNA 206
Cdd:PRK12705   76 REELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE---------------ELEKQLDNELYRVAGLTP 140

                         170
                  ....*....|....
gi 1841845163 207 E--KQLLVAKEGAE 218
Cdd:PRK12705  141 EqaRKLLLKLLDAE 154
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-171 3.87e-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: 39.75  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  67 AYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTEN 146
Cdd:COG4942   134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

                          90       100
                  ....*....|....*....|....*
gi 1841845163 147 ERSRQKYAEEELEQVREALRKAEKE 171
Cdd:COG4942   214 ELAELQQEAEELEALIARLEAEAAA 238
PTZ00121 PTZ00121
MAEBL; Provisional
 75-222 3.98e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163   75 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENER------ 148
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkadeak 1476

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841845163  149 ---SRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 222
Cdd:PTZ00121  1477 kkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 75-165 4.11e-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: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  75 KEHMKKMMKDLEglhRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK-----------------KLRDEINLAKQEAQRL 137
Cdd:pfam20492  19 EEETKKAQEELE---ESEETAEELEEERRQAEEEAERLEQKRQEAEEekerleesaemeaeekeQLEAELAEAQEEIARL 95

                          90       100
                  ....*....|....*....|....*...
gi 1841845163 138 KELREGTENERSRqkyAEEELEQVREAL 165
Cdd:pfam20492  96 EEEVERKEEEARR---LQEELEEAREEE 120
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 78-173 5.18e-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: 37.42  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  78 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 143
Cdd:cd06503    24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1841845163 144 TENERSRqkyAEEELEQ--VREALRKAEKELE 173
Cdd:cd06503   104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
PTZ00121 PTZ00121
MAEBL; Provisional
 100-223 5.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  100 ERLHKAQEEHRTVEVEKVHlEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKEleshsswy 179
Cdd:PTZ00121  1281 DELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-------- 1351

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1841845163  180 aPEALQKWLQLTHEvevqyyniKKQNAEKQLLVAKEGAEKIKKK 223
Cdd:PTZ00121  1352 -AEAAADEAEAAEE--------KAEAAEKKKEEAKKKADAAKKK 1386
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 90-219 6.54e-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: 39.16  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  90 RAEQSLHDLqERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQ---------------------EAQRLKELREGTENER 148
Cdd:pfam15709 342 RAEMRRLEV-ERKRREQEEQRRLQQEQLERAEKMREELELEQQrrfeeirlrkqrleeerqrqeEEERKQRLQLQAAQER 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 149 SRQKYAE-----EELEQVR--EALRKAE------KELESHSSwyapEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKE 215
Cdd:pfam15709 421 ARQQQEEfrrklQELQRKKqqEEAERAEaekqrqKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE 496


                  ....
gi 1841845163 216 GAEK 219
Cdd:pfam15709 497 RRQK 500
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 75-223 6.81e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  75 KEHMKKMMKDLEGLH--RAEQSLHDLQER-------LHKAQEEHRTVEVEKVHLEKKL---RDEINLAKQEAQRLKELRE 142
Cdd:PRK04778  262 KEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFLehaKEQNKELKEEIDRVKQSYT 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163 143 GTENERSRQKYAEEELEQVREALRKAEKELESHSSWY--APEALQKWLQLTHEVEVQYYNIKK--QNAEKQLLVAKEGAE 218
Cdd:PRK04778  342 LNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYseLQEELEEILKQLEEIEKEQEKLSEmlQGLRKDELEAREKLE 421


                  ....*
gi 1841845163 219 KIKKK 223
Cdd:PRK04778  422 RYRNK 426
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-224 7.50e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841845163  74 SKEHMKKMMKDLEGLHR-------AEQSLHDLQERLHKAQEEhrtvevekvhLEKKlRDEINLAKQEAQRLKElregtEN 146
Cdd:PRK03918  586 SVEELEERLKELEPFYNeylelkdAEKELEREEKELKKLEEE----------LDKA-FEELAETEKRLEELRK-----EL 649

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841845163 147 ERSRQKYAEEELEQVREALRKAEKELESHSSWYapEALQKWLQlthEVEVQYYNIKKQNAEKQllVAKEGAEKIKKKR 224
Cdd:PRK03918  650 EELEKKYSEEEYEELREEYLELSRELAGLRAEL--EELEKRRE---EIKKTLEKLKEELEERE--KAKKELEKLEKAL 720
 
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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