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Conserved domains on  [gi|21070997|ref|NP_003147|]
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stromal interaction molecule 1 isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 342-441 1.06e-53

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


:

Pssm-ID: 465164 [Multi-domain]  Cd Length: 100  Bit Score: 179.37  E-value: 1.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   342 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 421
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 21070997   422 ALRERLHRWQQIEILCGFQI 441
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 128-201 3.20e-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: 3.20e-49
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21070997 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 2.31e-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: 54.17  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                ....*..
gi 21070997 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 ...
 342-441 1.06e-53

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


Pssm-ID: 465164 [Multi-domain]  Cd Length: 100  Bit Score: 179.37  E-value: 1.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   342 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 421
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 21070997   422 ALRERLHRWQQIEILCGFQI 441
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 128-201 3.20e-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: 3.20e-49
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21070997 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09573   1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 347-438 5.89e-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: 147.01  E-value: 5.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 347 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRER 426
Cdd:cd11722   1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                        90
                ....*....|..
gi 21070997 427 LHRWQQIEILCG 438
Cdd:cd11722  81 QHRWSQIESLCG 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-337 2.31e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                ....*..
gi 21070997 331 AEKELES 337
Cdd:COG1196 349 AEEELEE 355
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 244-427 3.14e-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: 51.85  E-value: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 244 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 322
Cdd:COG1579   2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 323 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKKrntlfgtfhvahsssL 402
Cdd:COG1579  70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE---------------L 126

                       170       180
                ....*....|....*....|....*
gi 21070997 403 DDVDHKILTAKQALSEVTAALRERL 427
Cdd:COG1579 127 AELEAELAELEAELEEKKAELDEEL 151
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 129-193 7.84e-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: 7.84e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21070997    129 VYNWTVDEVVQWLITYVeLPQYEETFRKLQLSGHAMPRLavtNTTMTGTVLKMTDRSHRQKLQLK 193
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLL---TSEEDLKELGITKLGHRKKILKA 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-460 4.67e-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: 50.06  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 316
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    317 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGT- 393
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELq 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    394 ----FHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQI-EILCGF-----QIVNN----PGIHSLVAAL-NIDP 458
Cdd:TIGR02168  454 eeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEGFsegvkALLKNqsglSGILGVLSELiSVDE 533


                   ..
gi 21070997    459 SW 460
Cdd:TIGR02168  534 GY 535
PRK12704 PRK12704
phosphodiesterase; Provisional
 214-386 2.55e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  214 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 280
Cdd:PRK12704   8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  281 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 352
Cdd:PRK12704  87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21070997  353 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 386
Cdd:PRK12704 166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 238-334 3.33e-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: 43.75  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 313
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 21070997   314 QKYAEEELEQVREALRKAEKE 334
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-390 2.07e-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: 44.66  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    253 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 325
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21070997    326 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTL 390
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL 384
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
239-426 2.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  239 EHMKKMMKDLEGL--HRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLK----EL--------- 303
Cdd:PRK03918 365 EEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpv 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  304 --REGTENER---------------SRQKYAEEELEQVREALRKAEKELESHSSwyapeaLQKWLQLTHEVEVQYYNIKK 366
Cdd:PRK03918 441 cgRELTEEHRkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKLKK 514

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21070997  367 QNAEKqLLVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILTAKQALSEVTAALRER 426
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 ...
 241-336 2.89e-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: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 241 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 306
Cdd:cd06503  24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                        90       100       110
                ....*....|....*....|....*....|..
gi 21070997 307 TENERSRqkyAEEELEQ--VREALRKAEKELE 336
Cdd:cd06503 104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
131-196 7.10e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 7.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21070997   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 ...
 342-441 1.06e-53

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


Pssm-ID: 465164 [Multi-domain]  Cd Length: 100  Bit Score: 179.37  E-value: 1.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   342 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 421
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 21070997   422 ALRERLHRWQQIEILCGFQI 441
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 128-201 3.20e-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: 3.20e-49
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21070997 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09573   1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 347-438 5.89e-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: 147.01  E-value: 5.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 347 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRER 426
Cdd:cd11722   1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                        90
                ....*....|..
gi 21070997 427 LHRWQQIEILCG 438
Cdd:cd11722  81 QHRWSQIESLCG 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 21070997 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 5.43e-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: 5.43e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21070997 128 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 201
Cdd:cd09574   1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-337 2.31e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                ....*..
gi 21070997 331 AEKELES 337
Cdd:COG1196 349 AEEELEE 355
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 244-427 3.14e-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: 51.85  E-value: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 244 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 322
Cdd:COG1579   2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 323 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKKrntlfgtfhvahsssL 402
Cdd:COG1579  70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE---------------L 126

                       170       180
                ....*....|....*....|....*
gi 21070997 403 DDVDHKILTAKQALSEVTAALRERL 427
Cdd:COG1579 127 AELEAELAELEAELEEKKAELDEEL 151
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 129-193 7.84e-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: 7.84e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21070997    129 VYNWTVDEVVQWLITYVeLPQYEETFRKLQLSGHAMPRLavtNTTMTGTVLKMTDRSHRQKLQLK 193
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLL---TSEEDLKELGITKLGHRKKILKA 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
249-374 1.67e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 249 EGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREAL 328
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21070997 329 RKAEKELESHSSwyAPEALQKWL-QLTHEVEVQYYNIKKQNAEKQLL 374
Cdd:COG4372 111 EELQEELEELQK--ERQDLEQQRkQLEAQIAELQSEIAEREEELKEL 155
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-460 4.67e-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: 50.06  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 316
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    317 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGT- 393
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELq 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    394 ----FHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQI-EILCGF-----QIVNN----PGIHSLVAAL-NIDP 458
Cdd:TIGR02168  454 eeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEGFsegvkALLKNqsglSGILGVLSELiSVDE 533


                   ..
gi 21070997    459 SW 460
Cdd:TIGR02168  534 GY 535
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-434 5.84e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 5.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKK---LRDEINLAKQE----AQRLKELREGTENERSRQKYAEEELEQ 323
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 324 VREALRKAEKELESHSswyapEALQKWLQlthevevqyyniKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHvAHSSSLD 403
Cdd:COG1196 321 LEEELAELEEELEELE-----EELEELEE------------ELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELE 382

                       170       180       190
                ....*....|....*....|....*....|.
gi 21070997 404 DVDHKILTAKQALSEVTAALRERLHRWQQIE 434
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALL 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
237-352 1.67e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 237 SKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvEKVHLEKKLRDEINLAKQE------------AQRLKELR 304
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEEleelleqlslatEEELQDLA 198

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 21070997 305 EGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ 352
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
239-390 1.74e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 239 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR---------DEINLAKQEAQRLKELREGTEN 309
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllPLYQELEALEAELAELPERLEE 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 310 ERSRQKY---AEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYniKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:COG4717 151 LEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEE 228


                ....
gi 21070997 387 RNTL 390
Cdd:COG4717 229 LEQL 232
PRK12704 PRK12704
phosphodiesterase; Provisional
 214-386 2.55e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  214 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 280
Cdd:PRK12704   8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  281 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 352
Cdd:PRK12704  87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21070997  353 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 386
Cdd:PRK12704 166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 238-334 3.33e-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: 43.75  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 313
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 21070997   314 QKYAEEELEQVREALRKAEKE 334
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 131-171 4.45e-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: 4.45e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21070997 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 ...
 239-435 5.53e-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: 46.59  E-value: 5.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    239 EHMKKMMKDLE-GLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK---KLRDEINLAKQE----AQRLKELREGTENE 310
Cdd:TIGR02168  708 EELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERleeaEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    311 RSRQKYAEEELEQVREALRKAEKELESHSSWYA--PEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK----------- 377
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAAnlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeleel 867

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21070997    378 -----EGAEKIKKKRNTLFGTFHVAHS------SSLDDVDHKILTAKQALSEvtaaLRERLH----RWQQIEI 435
Cdd:TIGR02168  868 ieeleSELEALLNERASLEEALALLRSeleelsEELRELESKRSELRRELEE----LREKLAqlelRLEGLEV 936
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 238-429 6.90e-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: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYA 317
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    318 EEELEQVREALRKAEKELESH-----SSWYAPEALQKWLQL------THEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALlneraSLEEALALLRSELEElseelrELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 21070997    387 RNTLFGTFHVAHSSSLDDvdhkILTAKQALSEVTAALRERLHR 429
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEE----AEALENKIEDDEEEARRRLKR 976
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
239-434 1.01e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  239 EHMKKMMKDLEGLHR----AEQSLHDLqERLHKAQEEHRTVEVEKVHLEKkLRDEINL--AKQEAQRLKELREGTENERS 312
Cdd:COG4913  228 DALVEHFDDLERAHEaledAREQIELL-EPIRELAERYAAARERLAELEY-LRAALRLwfAQRRLELLEAELEELRAELA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  313 RQKYAEEELEQVREALRKAEKELeshsswyapealqkwlqlthevEVQYYNI---KKQNAEKQLlvakEGAEKIKKKRNT 389
Cdd:COG4913  306 RLEAELERLEARLDALREELDEL----------------------EAQIRGNggdRLEQLEREI----ERLERELEERER 359

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 21070997  390 LFGTFHVAhsssLDDVDHKILTAKQALSEVTAALRERLHRWQQIE 434
Cdd:COG4913  360 RRARLEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 233-365 1.32e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  233 QNRYSKEHMK--KMMKDLEGLHR-AEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQR---------- 299
Cdd:PRK00409 508 KKLIGEDKEKlnELIASLEELEReLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeakkead 587

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21070997  300 --LKELREGTENERSRQKyaEEELEQVREALRKAEKELESHSswYAPEALQKWLQLTHEVEVQYYNIK 365
Cdd:PRK00409 588 eiIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKK--KKQKEKQEELKVGDEVKYLSLGQK 651
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
247-430 1.54e-04

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: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  247 DLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVRE 326
Cdd:COG4913  662 DVASAEREIAELEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQ---AEEELDELQD 734

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  327 ALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQyynikkQNAEKQLLVAKEGAEKIKKKRNTLFGTF-------HVAHS 399
Cdd:COG4913  735 RLEAAEDLARLELRALLEERFAAALGDAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnrewpaeTADLD 808

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21070997  400 SSLDDVDH--KILT--AKQALSEVTAALRERLHRW 430
Cdd:COG4913  809 ADLESLPEylALLDrlEEDGLPEYEERFKELLNEN 843
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 136-197 1.63e-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: 1.63e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21070997 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 ...
 253-390 2.07e-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: 44.66  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    253 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 325
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21070997    326 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTL 390
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 239-381 2.35e-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: 2.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 239 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAE 318
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21070997 319 EELEQVREALRKAEKELEShsswyapEALQKWLQLTHEVEVQYYN---IKKQNAEKQLLVAKEGAE 381
Cdd:COG1196 470 EEAALLEAALAELLEELAE-------AAARLLLLLEAEADYEGFLegvKAALLLAGLRGLAGAVAV 528
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
238-387 2.93e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR-------DEINL-----------------A 293
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEErlkelepfyneylelkdA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  294 KQEAQRLKELREGTENERSRqkyAEEELEQVREALRKAEKELESHSSWYAPE----ALQKWLQLTHEV-----EVQYYNI 364
Cdd:PRK03918 611 EKELEREEKELKKLEEELDK---AFEELAETEKRLEELRKELEELEKKYSEEeyeeLREEYLELSRELaglraELEELEK 687

                        170       180
                 ....*....|....*....|...
gi 21070997  365 KKQNAEKQLLVAKEGAEKIKKKR 387
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAK 710
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
251-330 4.39e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKlrDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 330
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
251-360 6.00e-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: 6.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 251 LHRAEQSLHDLQERLhkaQEEHRTVevekvhleKKLRDEINLAKQE-AQRLKELREGTENERSRQKYAEEELEQVREALR 329
Cdd:COG3206 272 LAELEAELAELSARY---TPNHPDV--------IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLE 340

                        90       100       110
                ....*....|....*....|....*....|.
gi 21070997 330 KAEKELeshsswyaPEALQKWLQLTHEVEVQ 360
Cdd:COG3206 341 ARLAEL--------PELEAELRRLEREVEVA 363
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
233-390 6.69e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 233 QNRYSKEHMKKMMKDLEGLHRAEQSLHDLQ---ERLHKAQEEHRTVEVEKVHLE---KKLRDEINLAKQEAQRLKELREG 306
Cdd:COG4717  55 ADELFKPQGRKPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEaelEELREELEKLEKLLQLLPLYQEL 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 307 TENERSRQKYAE---------EELEQVREALRKAEKELESHSSwyAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK 377
Cdd:COG4717 135 EALEAELAELPErleeleerlEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212

                       170
                ....*....|...
gi 21070997 378 EGAEKIKKKRNTL 390
Cdd:COG4717 213 EELEEAQEELEEL 225
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-337 6.94e-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: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  251 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVREALRK 330
Cdd:COG4913  347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRE 423


                 ....*..
gi 21070997  331 AEKELES 337
Cdd:COG4913  424 LEAEIAS 430
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 131-190 9.52e-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: 9.52e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 131 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPRLavTNTTMTgTVLKMTDRSHRQKL 190
Cdd:cd09505   4 DWSEEDVCTWLRS-IGLEQYVEVFRANNIDGKELLNL--TKESLS-KDLKIESLGHRNKI 59
PTZ00121 PTZ00121
MAEBL; Provisional
 246-386 9.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   246 KDLEGLHRAEQSLHDlQERLHKAQEEHRTVEV---EKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELE 322
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKD-AEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21070997   323 QVREALRKAEKELESHSSWYAPEALQKwlqlthevEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKK--------KADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
255-432 1.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 255 EQSLHDLQERLHKAQEEHRTVEVEKVhleKKLRDEINLAKQEAQRLKELREgtenersRQKYAEEELEQVREALRKAEKE 334
Cdd:COG4717  48 LERLEKEADELFKPQGRKPELNLKEL---KELEEELKEAEEKEEEYAELQE-------ELEELEEELEELEAELEELREE 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 335 LESHSSWYAP-EALQKWLQLTHEVE---VQYYNIKKQ-----NAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDv 405
Cdd:COG4717 118 LEKLEKLLQLlPLYQELEALEAELAelpERLEELEERleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQD- 196

                       170       180
                ....*....|....*....|....*..
gi 21070997 406 dhkILTAKQALSEVTAALRERLHRWQQ 432
Cdd:COG4717 197 ---LAEELEELQQRLAELEEELEEAQE 220
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 238-390 1.60e-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: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    238 KEHMKKMMKDLEG--------LHRAEQSLHDL-----QERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRLK 301
Cdd:TIGR02169  753 IENVKSELKELEArieeleedLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLE 832

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997    302 ELREGTENER----SRQKYAEEELEQVREALRKAEKELESHsswyapealQKWLQlthEVEVQYYNIKKQ--NAEKQLLV 375
Cdd:TIGR02169  833 KEIQELQEQRidlkEQIKSIEKEIENLNGKKEELEEELEEL---------EAALR---DLESRLGDLKKErdELEAQLRE 900

                          170
                   ....*....|....*
gi 21070997    376 AKEGAEKIKKKRNTL 390
Cdd:TIGR02169  901 LERKIEELEAQIEKK 915
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
246-344 1.69e-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: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 246 KDLEG-LHRAEQSLHDLQERLHKAQEEHRTvevekvhlEKKLRDEINLAKQEAQRL-KELREgtenERSRQKYAEEELEQ 323
Cdd:COG2433 430 EELEAeLEEKDERIERLERELSEARSEERR--------EIRKDREISRLDREIERLeRELEE----ERERIEELKRKLER 497

                        90       100
                ....*....|....*....|.
gi 21070997 324 VREALRKaekeleSHSSWYAP 344
Cdd:COG2433 498 LKELWKL------EHSGELVP 512
PTZ00121 PTZ00121
MAEBL; Provisional
 230-385 1.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   230 AYIQNRYSKEHMKKMMK--DLEGLHRAEQSLHDLQER-----LHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQ---R 299
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiK 1662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   300 LKELREGTENERSRQ---KYAEEELEQVREALRKAEKELESHSSWYAPEA--LQKWLQLTHEVEVQyyNIKKQNAEKQLL 374
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAeeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeeKKKAEELKKAEEEN--KIKAEEAKKEAE 1740

                         170
                  ....*....|.
gi 21070997   375 VAKEGAEKIKK 385
Cdd:PTZ00121 1741 EDKKKAEEAKK 1751
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 238-328 1.93e-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: 38.75  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   238 KEHMKKMMKDLEglhRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK-----------------KLRDEINLAKQEAQRL 300
Cdd:pfam20492  19 EEETKKAQEELE---ESEETAEELEEERRQAEEEAERLEQKRQEAEEekerleesaemeaeekeQLEAELAEAQEEIARL 95

                          90       100
                  ....*....|....*....|....*...
gi 21070997   301 KELREGTENERSRqkyAEEELEQVREAL 328
Cdd:pfam20492  96 EEEVERKEEEARR---LQEELEEAREEE 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
239-426 2.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  239 EHMKKMMKDLEGL--HRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLK----EL--------- 303
Cdd:PRK03918 365 EEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpv 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  304 --REGTENER---------------SRQKYAEEELEQVREALRKAEKELESHSSwyapeaLQKWLQLTHEVEVQYYNIKK 366
Cdd:PRK03918 441 cgRELTEEHRkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKLKK 514

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21070997  367 QNAEKqLLVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILTAKQALSEVTAALRER 426
Cdd:PRK03918 515 YNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKelekleelkKKLAELEKKLDELEEELAELLKELEEL 582
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 253-434 2.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 253 RAEQSLHDLQERLHK---AQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENErsrqkyaEEELEQVREALR 329
Cdd:COG1196 219 KEELKELEAELLLLKlreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-------ELELEEAQAEEY 291

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 330 KAEKELeshsswyapEALQKWLQLTHEvEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHsSSLDDVDHKI 409
Cdd:COG1196 292 ELLAEL---------ARLEQDIARLEE-RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-EELEEAEAEL 360

                       170       180
                ....*....|....*....|....*
gi 21070997 410 LTAKQALSEVTAALRERLHRWQQIE 434
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELA 385
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 253-382 2.72e-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: 40.71  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   253 RAEQSLHDLqERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQ---------------------EAQRLKELREGTENER 311
Cdd:pfam15709 342 RAEMRRLEV-ERKRREQEEQRRLQQEQLERAEKMREELELEQQrrfeeirlrkqrleeerqrqeEEERKQRLQLQAAQER 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   312 SRQKYAE-----EELEQVR--EALRKAE------KELESHSSwyapEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKE 378
Cdd:pfam15709 421 ARQQQEEfrrklQELQRKKqqEEAERAEaekqrqKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE 496


                  ....
gi 21070997   379 GAEK 382
Cdd:pfam15709 497 RRQK 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 230-334 2.82e-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: 2.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 230 AYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTEN 309
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

                        90       100
                ....*....|....*....|....*
gi 21070997 310 ERSRQKYAEEELEQVREALRKAEKE 334
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAA 238
PTZ00121 PTZ00121
MAEBL; Provisional
 238-385 2.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvekvhlEKKLRDEINLAKQEAQRlKELREGTENERSRQKYA 317
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAEAAA-DEAEAAEEKAEAAEKKK 1373

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21070997   318 EEELEQVREALRKAEKELEshsswyAPEALQKwlqlTHEVEVQYYNIKKQNAEKQLL-VAKEGAEKIKK 385
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKK------ADEAKKK----AEEDKKKADELKKAAAAKKKAdEAKKKAEEKKK 1432
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 241-336 2.89e-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: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997 241 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 306
Cdd:cd06503  24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                        90       100       110
                ....*....|....*....|....*....|..
gi 21070997 307 TENERSRqkyAEEELEQ--VREALRKAEKELE 336
Cdd:cd06503 104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
PTZ00121 PTZ00121
MAEBL; Provisional
 263-385 3.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   263 ERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENE-----------RSRQKYAEEELEQVREALRKA 331
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklyeeekkmKAEEAKKAEEAKIKAEELKKA 1628

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21070997   332 EKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 385
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
PRK12705 PRK12705
hypothetical protein; Provisional
 214-381 3.05e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.85  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  214 FMLVVSIVIGVGGCWFAYI---QNRYSKEHMK-KMMKDLEGLHRAEQSLHDLQERLHKAQEEHRtvevekvhleKKLRDE 289
Cdd:PRK12705   6 LLVILLLLIGLLLGVLVVLlkkRQRLAKEAERiLQEAQKEAEEKLEAALLEAKELLLRERNQQR----------QEARRE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  290 INLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELEshsswyapealqkwlQLTHEVEVQYYNIKKQNA 369
Cdd:PRK12705  76 REELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE---------------ELEKQLDNELYRVAGLTP 140

                        170
                 ....*....|....
gi 21070997  370 E--KQLLVAKEGAE 381
Cdd:PRK12705 141 EqaRKLLLKLLDAE 154
PTZ00121 PTZ00121
MAEBL; Provisional
 239-386 3.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   239 EHMKKM--MKDLEGLHRAEQSLHDLQER---LHKAQ-----EEHRTVEVEKVHLEKKLRDEINLAKQEAQRLK--ELREG 306
Cdd:PTZ00121 1549 DELKKAeeLKKAEEKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKA 1628

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   307 TENERSRQKYAEEELEQVREA--LRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIK 384
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708


                  ..
gi 21070997   385 KK 386
Cdd:PTZ00121 1709 KK 1710
PTZ00121 PTZ00121
MAEBL; Provisional
 238-385 5.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   238 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENER------ 311
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkadeak 1476

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21070997   312 ---SRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 385
Cdd:PTZ00121 1477 kkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
131-196 7.10e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 7.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21070997   131 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPrLAVTNTTMTGtvLKMTDRSHRQKLQLKALD 196
Cdd:pfam07647   3 SWSLESVADWLRS-IGLEQYTDNFRDQGITGAELL-LRLTLEDLKR--LGITSVGHRRKILKKIQE 64
PTZ00121 PTZ00121
MAEBL; Provisional
 263-386 7.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   263 ERLHKAQEEHRTVEVEKVHlEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKEleshsswy 342
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-------- 1351

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 21070997   343 aPEALQKWLQLTHEvevqyyniKKQNAEKQLLVAKEGAEKIKKK 386
Cdd:PTZ00121 1352 -AEAAADEAEAAEE--------KAEAAEKKKEEAKKKADAAKKK 1386
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
237-387 7.63e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997  237 SKEHMKKMMKDLEGLHR-------AEQSLHDLQERLHKAQEEhrtvevekvhLEKKlRDEINLAKQEAQRLKElregtEN 309
Cdd:PRK03918 586 SVEELEERLKELEPFYNeylelkdAEKELEREEKELKKLEEE----------LDKA-FEELAETEKRLEELRK-----EL 649

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21070997  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 8.26e-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: 36.82  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21070997   253 RAEQSLHDLQERLHKAQEEHRTVEvekvhleKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAE 332
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKKAQ-------EELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75


                  ....
gi 21070997   333 KELE 336
Cdd:pfam20492  76 EEKE 79
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 131-192 9.73e-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: 34.94  E-value: 9.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21070997   131 NWTVDEVVQWLITYvELPQYEETFRKLQLSGHAMPRLavTNTTMTGtvLKMTDRSHRQKLQL 192
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQL--TEDDLLK--LGVTLLGHRKKILY 58
 
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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