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Conserved domains on  [gi|1842089067|ref|NP_001369504|]
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stromal interaction molecule 1 isoform 13 [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 ...
 268-367 3.80e-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: 179.37  E-value: 3.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 268 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 347
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 1842089067 348 ALRERLHRWQQIEILCGFQI 367
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 54-127 2.40e-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: 165.60  E-value: 2.40e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  54 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 127
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-263 2.35e-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: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 256
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1842089067 257 AEKELES 263
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 ...
 268-367 3.80e-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: 179.37  E-value: 3.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 268 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 347
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 1842089067 348 ALRERLHRWQQIEILCGFQI 367
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 54-127 2.40e-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: 165.60  E-value: 2.40e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  54 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 127
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 273-364 2.74e-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: 147.01  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 273 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRER 352
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                          90
                  ....*....|..
gi 1842089067 353 LHRWQQIEILCG 364
Cdd:cd11722    81 QHRWSQIESLCG 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-263 2.35e-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: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 256
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1842089067 257 AEKELES 263
Cdd:COG1196   349 AEEELEE 355
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 170-353 3.09e-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: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 170 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 248
Cdd:COG1579     2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 249 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKKrntlfgtfhvahsssL 328
Cdd:COG1579    70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE---------------L 126

                         170       180
                  ....*....|....*....|....*
gi 1842089067 329 DDVDHKILTAKQALSEVTAALRERL 353
Cdd:COG1579   127 AELEAELAELEAELEEKKAELDEEL 151
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 55-119 8.99e-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: 46.52  E-value: 8.99e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842089067   55 VYNWTVDEVVQWLITYVeLPQYEETFRKLQLSGHAMPRLavtNTTMTGTVLKMTDRSHRQKLQLK 119
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLL---TSEEDLKELGITKLGHRKKILKA 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 177-386 4.66e-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: 4.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 242
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  243 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGT- 319
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELq 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  320 ----FHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQI-EILCGF-----QIVNN----PGIHSLVAAL-NIDP 384
Cdd:TIGR02168  454 eeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEGFsegvkALLKNqsglSGILGVLSELiSVDE 533


                   ..
gi 1842089067  385 SW 386
Cdd:TIGR02168  534 GY 535
PRK12704 PRK12704
phosphodiesterase; Provisional
 140-312 2.23e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 140 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 206
Cdd:PRK12704    8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 207 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 278
Cdd:PRK12704   87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1842089067 279 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 312
Cdd:PRK12704  166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 164-260 3.24e-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: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 164 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 239
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 1842089067 240 QKYAEEELEQVREALRKAEKE 260
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-316 2.05e-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: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  179 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 251
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842089067  252 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTL 316
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL 384
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
165-352 2.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 165 EHMKKMMKDLEGL--HRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLK----EL--------- 229
Cdd:PRK03918  365 EEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpv 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 230 --REGTENER---------------SRQKYAEEELEQVREALRKAEKELESHSSwyapeaLQKWLQLTHEVEVQYYNIKK 292
Cdd:PRK03918  441 cgRELTEEHRkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKLKK 514

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842089067 293 QNAEKqLLVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILTAKQALSEVTAALRER 352
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 ...
 167-262 3.23e-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: 38.19  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 167 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 232
Cdd:cd06503    24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1842089067 233 TENERSRqkyAEEELEQ--VREALRKAEKELE 262
Cdd:cd06503   104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
57-122 7.17e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.32  E-value: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842089067  57 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPrLAVTNTTMTGtvLKMTDRSHRQKLQLKALD 122
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 ...
 268-367 3.80e-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: 179.37  E-value: 3.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 268 YAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTA 347
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 1842089067 348 ALRERLHRWQQIEILCGFQI 367
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 54-127 2.40e-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: 165.60  E-value: 2.40e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  54 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 127
Cdd:cd09573     1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 273-364 2.74e-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: 147.01  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 273 LQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRER 352
Cdd:cd11722     1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                          90
                  ....*....|..
gi 1842089067 353 LHRWQQIEILCG 364
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 ...
 54-127 2.33e-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: 135.92  E-value: 2.33e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  54 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 127
Cdd:cd09504     1 EVHNWTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDVVLFG 74
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 54-127 7.42e-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: 106.61  E-value: 7.42e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  54 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFG 127
Cdd:cd09574     1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-263 2.35e-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: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 256
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ....*..
gi 1842089067 257 AEKELES 263
Cdd:COG1196   349 AEEELEE 355
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 170-353 3.09e-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: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 170 MMKDLEglhraeqSLHDLQERLHKAQE-EHRTVEVEKVHleKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELE 248
Cdd:COG1579     2 MPEDLR-------ALLDLQELDSELDRlEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKR---LELEIE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 249 QVREALRKAEKELESHSSwyaPEALQkwlQLTHEVEVQyyNIKKQNAEKQLLVAKEGAEKIKKKrntlfgtfhvahsssL 328
Cdd:COG1579    70 EVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE---------------L 126

                         170       180
                  ....*....|....*....|....*
gi 1842089067 329 DDVDHKILTAKQALSEVTAALRERL 353
Cdd:COG1579   127 AELEAELAELEAELEEKKAELDEEL 151
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 55-119 8.99e-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: 46.52  E-value: 8.99e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842089067   55 VYNWTVDEVVQWLITYVeLPQYEETFRKLQLSGHAMPRLavtNTTMTGTVLKMTDRSHRQKLQLK 119
Cdd:smart00454   1 VSQWSPESVADWLESIG-LEQYADNFRKNGIDGALLLLL---TSEEDLKELGITKLGHRKKILKA 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
175-263 2.40e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 175 EGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREAL 254
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110


                  ....*....
gi 1842089067 255 RKAEKELES 263
Cdd:COG4372   111 EELQEELEE 119
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 177-386 4.66e-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: 4.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKL-RDEINLAKQEAQ-------------RLKELREGTENERSRQKY 242
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKleelkeelesleaELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  243 AEEELEQVREALRKAEKELESHSS--WYAPEALQkwlQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGT- 319
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNeiERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELq 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  320 ----FHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQI-EILCGF-----QIVNN----PGIHSLVAAL-NIDP 384
Cdd:TIGR02168  454 eeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEGFsegvkALLKNqsglSGILGVLSELiSVDE 533


                   ..
gi 1842089067  385 SW 386
Cdd:TIGR02168  534 GY 535
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-360 5.83e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKK---LRDEINLAKQE----AQRLKELREGTENERSRQKYAEEELEQ 249
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 250 VREALRKAEKELESHSswyapEALQKWLQlthevevqyyniKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHvAHSSSLD 329
Cdd:COG1196   321 LEEELAELEEELEELE-----EELEELEE------------ELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELE 382

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1842089067 330 DVDHKILTAKQALSEVTAALRERLHRWQQIE 360
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALL 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
163-278 1.69e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 163 SKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvEKVHLEKKLRDEINLAKQE------------AQRLKELR 230
Cdd:COG4717   120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEEleelleqlslatEEELQDLA 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1842089067 231 EGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ 278
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-316 2.06e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 165 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR---------DEINLAKQEAQRLKELREGTEN 235
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 236 ERSRQKY---AEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYniKKQNAEKQLLVAKEGAEKIKKK 312
Cdd:COG4717   151 LEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEE 228


                  ....
gi 1842089067 313 RNTL 316
Cdd:COG4717   229 LEQL 232
PRK12704 PRK12704
phosphodiesterase; Provisional
 140-312 2.23e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 140 FMLVVSIVIGVGGCWFAYI-----QNRYSKEHMKKMMKD--LEGLHRAEQSLHDLQERLHKAQEEH------RTVEVEKv 206
Cdd:PRK12704    8 LIALVALVVGAVIGYFVRKkiaeaKIKEAEEEAKRILEEakKEAEAIKKEALLEAKEEIHKLRNEFekelreRRNELQK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 207 hLEKKLRD-EINLAKQEA---QRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQ---- 278
Cdd:PRK12704   87 -LEKRLLQkEENLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1842089067 279 -LTHEVEVQYYNIKKQnaekqllvAKEGAEKIKKK 312
Cdd:PRK12704  166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 164-260 3.24e-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: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 164 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDeinlAKQEAQRLKELREGTENERS----R 239
Cdd:pfam20492   9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQE----AEEEKERLEESAEMEAEEKEqleaE 84

                          90       100
                  ....*....|....*....|.
gi 1842089067 240 QKYAEEELEQVREALRKAEKE 260
Cdd:pfam20492  85 LAEAQEEIARLEEEVERKEEE 105
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 57-97 3.95e-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: 3.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1842089067  57 NWTVDEVVQWlITYVELPQYEETFRKLQLSGH--------AMPRLAVTN 97
Cdd:cd09530     2 SWDTEDVAEW-IEGLGFPQYRECFTTNFIDGRklilvdasTLPRMGVTD 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-361 5.37e-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: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  165 EHMKKMMKDLE-GLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK---KLRDEINLAKQE----AQRLKELREGTENE 236
Cdd:TIGR02168  708 EELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERleeaEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  237 RSRQKYAEEELEQVREALRKAEKELESHSSWYA--PEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK----------- 303
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAAnlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeleel 867

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842089067  304 -----EGAEKIKKKRNTLFGTFHVAHS------SSLDDVDHKILTAKQALSEvtaaLRERLH----RWQQIEI 361
Cdd:TIGR02168  868 ieeleSELEALLNERASLEEALALLRSeleelsEELRELESKRSELRRELEE----LREKLAqlelRLEGLEV 936
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-355 6.47e-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: 6.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  164 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYA 243
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  244 EEELEQVREALRKAEKELESH-----SSWYAPEALQKWLQL------THEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 312
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALlneraSLEEALALLRSELEElseelrELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1842089067  313 RNTLFGTFHVAHSSSLDDvdhkILTAKQALSEVTAALRERLHR 355
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEE----AEALENKIEDDEEEARRRLKR 976
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-360 1.05e-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: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  165 EHMKKMMKDLEGLHR----AEQSLHDLqERLHKAQEEHRTVEVEKVHLEKkLRDEINL--AKQEAQRLKELREGTENERS 238
Cdd:COG4913    228 DALVEHFDDLERAHEaledAREQIELL-EPIRELAERYAAARERLAELEY-LRAALRLwfAQRRLELLEAELEELRAELA 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  239 RQKYAEEELEQVREALRKAEKELeshsswyapealqkwlqlthevEVQYYNI---KKQNAEKQLlvakEGAEKIKKKRNT 315
Cdd:COG4913    306 RLEAELERLEARLDALREELDEL----------------------EAQIRGNggdRLEQLEREI----ERLERELEERER 359

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1842089067  316 LFGTFHVAhsssLDDVDHKILTAKQALSEVTAALRERLHRWQQIE 360
Cdd:COG4913    360 RRARLEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 159-291 1.33e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 159 QNRYSKEHMK--KMMKDLEGLHR-AEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQR---------- 225
Cdd:PRK00409  508 KKLIGEDKEKlnELIASLEELEReLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeakkead 587

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842089067 226 --LKELREGTENERSRQKyaEEELEQVREALRKAEKELESHSswYAPEALQKWLQLTHEVEVQYYNIK 291
Cdd:PRK00409  588 eiIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKK--KKQKEKQEELKVGDEVKYLSLGQK 651
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
173-356 1.67e-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: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  173 DLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVRE 252
Cdd:COG4913    662 DVASAEREIAELEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQ---AEEELDELQD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  253 ALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQyynikkQNAEKQLLVAKEGAEKIKKKRNTLFGTF-------HVAHS 325
Cdd:COG4913    735 RLEAAEDLARLELRALLEERFAAALGDAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnrewpaeTADLD 808

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1842089067  326 SSLDDVDH--KILT--AKQALSEVTAALRERLHRW 356
Cdd:COG4913    809 ADLESLPEylALLDrlEEDGLPEYEERFKELLNEN 843
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 62-123 1.90e-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: 39.53  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842089067  62 EVVQWLITyVELPQYEETFRKLQLSGHAMPRLavTNTTMTGtvLKMTDRSHRQKLqLKALDT 123
Cdd:cd09487     1 DVAEWLES-LGLEQYADLFRKNEIDGDALLLL--TDEDLKE--LGITSPGHRKKI-LRAIQR 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-316 2.05e-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: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  179 RAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRL----KELREGTENERSRQKYAEEELEQVR 251
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLeqqkQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842089067  252 EALRKAEKELeshsswyapEALQKWLQLThEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTL 316
Cdd:TIGR02168  330 SKLDELAEEL---------AELEEKLEEL-KEELESLEAELEELEAELEELESRLEELEEQLETL 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-307 2.27e-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: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 165 EHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAE 244
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842089067 245 EELEQVREALRKAEKELEShsswyapEALQKWLQLTHEVEVQYYN---IKKQNAEKQLLVAKEGAE 307
Cdd:COG1196   470 EEAALLEAALAELLEELAE-------AAARLLLLLEAEADYEGFLegvKAALLLAGLRGLAGAVAV 528
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
164-313 3.03e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 164 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLR-------DEINL-----------------A 219
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEErlkelepfyneylelkdA 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 220 KQEAQRLKELREGTENERSRqkyAEEELEQVREALRKAEKELESHSSWYAPE----ALQKWLQLTHEV-----EVQYYNI 290
Cdd:PRK03918  611 EKELEREEKELKKLEEELDK---AFEELAETEKRLEELRKELEELEKKYSEEeyeeLREEYLELSRELaglraELEELEK 687

                         170       180
                  ....*....|....*....|...
gi 1842089067 291 KKQNAEKQLLVAKEGAEKIKKKR 313
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKAK 710
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
177-256 4.80e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKlrDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRK 256
Cdd:COG4717   434 LEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
177-263 6.54e-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: 6.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  177 LHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRqkyAEEELEQVREALRK 256
Cdd:COG4913    347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRE 423


                   ....*..
gi 1842089067  257 AEKELES 263
Cdd:COG4913    424 LEAEIAS 430
PTZ00121 PTZ00121
MAEBL; Provisional
 172-312 6.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  172 KDLEGLHRAEQSLHDlQERLHKAQEEHRTVEV---EKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELE 248
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKD-AEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  249 QVREALRKAEKELESHSSWYAPEALQKwlqlthevEVQYYNIKKQNAEKQLLVAKEGAEKIKKK 312
Cdd:PTZ00121  1303 KADEAKKKAEEAKKADEAKKKAEEAKK--------KADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
159-316 7.70e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 159 QNRYSKEHMKKMMKDLEGLHRAEQSLHDLQ---ERLHKAQEEHRTVEVEKVHLE---KKLRDEINLAKQEAQRLKELREG 232
Cdd:COG4717    55 ADELFKPQGRKPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEaelEELREELEKLEKLLQLLPLYQEL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 233 TENERSRQKYAE---------EELEQVREALRKAEKELESHSSwyAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAK 303
Cdd:COG4717   135 EALEAELAELPErleeleerlEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212

                         170
                  ....*....|...
gi 1842089067 304 EGAEKIKKKRNTL 316
Cdd:COG4717   213 EELEEAQEELEEL 225
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 57-116 8.21e-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: 8.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  57 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPRLavTNTTMTgTVLKMTDRSHRQKL 116
Cdd:cd09505     4 DWSEEDVCTWLRS-IGLEQYVEVFRANNIDGKELLNL--TKESLS-KDLKIESLGHRNKI 59
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
177-286 9.01e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 177 LHRAEQSLHDLQERLhkaQEEHRTVevekvhleKKLRDEINLAKQE-AQRLKELREGTENERSRQKYAEEELEQVREALR 255
Cdd:COG3206   272 LAELEAELAELSARY---TPNHPDV--------IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLE 340

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1842089067 256 KAEKELeshsswyaPEALQKWLQLTHEVEVQ 286
Cdd:COG3206   341 ARLAEL--------PELEAELRRLEREVEVA 363
PTZ00121 PTZ00121
MAEBL; Provisional
 156-311 1.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  156 AYIQNRYSKEHMKKMMK--DLEGLHRAEQSLHDLQER-----LHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQ---R 225
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  226 LKELREGTENERSRQ---KYAEEELEQVREALRKAEKELESHSSWYAPEA--LQKWLQLTHEVEVQyyNIKKQNAEKQLL 300
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAeeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeeKKKAEELKKAEEEN--KIKAEEAKKEAE 1740

                          170
                   ....*....|.
gi 1842089067  301 VAKEGAEKIKK 311
Cdd:PTZ00121  1741 EDKKKAEEAKK 1751
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
181-358 1.57e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 181 EQSLHDLQERLHKAQEEHRTVEVEKVhleKKLRDEINLAKQEAQRLKELREgtenersRQKYAEEELEQVREALRKAEKE 260
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKEL---KELEEELKEAEEKEEEYAELQE-------ELEELEEELEELEAELEELREE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 261 LESHSSWYAP-EALQKWLQLTHEVE---VQYYNIKKQ-----NAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDv 331
Cdd:COG4717   118 LEKLEKLLQLlPLYQELEALEAELAelpERLEELEERleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQD- 196

                         170       180
                  ....*....|....*....|....*..
gi 1842089067 332 dhkILTAKQALSEVTAALRERLHRWQQ 358
Cdd:COG4717   197 ---LAEELEELQQRLAELEEELEEAQE 220
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-316 1.64e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  164 KEHMKKMMKDLEG--------LHRAEQSLHDL-----QERLHKAQEEHRTVEVEKVHLEKKLRD---EINLAKQEAQRLK 227
Cdd:TIGR02169  753 IENVKSELKELEArieeleedLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLE 832

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  228 ELREGTENER----SRQKYAEEELEQVREALRKAEKELESHsswyapealQKWLQlthEVEVQYYNIKKQ--NAEKQLLV 301
Cdd:TIGR02169  833 KEIQELQEQRidlkEQIKSIEKEIENLNGKKEELEEELEEL---------EAALR---DLESRLGDLKKErdELEAQLRE 900

                          170
                   ....*....|....*
gi 1842089067  302 AKEGAEKIKKKRNTL 316
Cdd:TIGR02169  901 LERKIEELEAQIEKK 915
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
172-270 1.71e-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: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 172 KDLEG-LHRAEQSLHDLQERLHKAQEEHRTvevekvhlEKKLRDEINLAKQEAQRL-KELREgtenERSRQKYAEEELEQ 249
Cdd:COG2433   430 EELEAeLEEKDERIERLERELSEARSEERR--------EIRKDREISRLDREIERLeRELEE----ERERIEELKRKLER 497

                          90       100
                  ....*....|....*....|.
gi 1842089067 250 VREALRKaekeleSHSSWYAP 270
Cdd:COG2433   498 LKELWKL------EHSGELVP 512
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 164-254 1.85e-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: 38.36  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 164 KEHMKKMMKDLEglhRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEK-----------------KLRDEINLAKQEAQRL 226
Cdd:pfam20492  19 EEETKKAQEELE---ESEETAEELEEERRQAEEEAERLEQKRQEAEEekerleesaemeaeekeQLEAELAEAQEEIARL 95

                          90       100
                  ....*....|....*....|....*...
gi 1842089067 227 KELREGTENERSRqkyAEEELEQVREAL 254
Cdd:pfam20492  96 EEEVERKEEEARR---LQEELEEAREEE 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
165-352 2.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 165 EHMKKMMKDLEGL--HRAEQSLHDLQERLHKAQEEHRTVEVEkvhlEKKLRDEINLAKQEAQRLK----EL--------- 229
Cdd:PRK03918  365 EEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpv 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 230 --REGTENER---------------SRQKYAEEELEQVREALRKAEKELESHSSwyapeaLQKWLQLTHEVEVQYYNIKK 292
Cdd:PRK03918  441 cgRELTEEHRkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKLKK 514

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842089067 293 QNAEKqLLVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILTAKQALSEVTAALRER 352
Cdd:PRK03918  515 YNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKelekleelkKKLAELEKKLDELEEELAELLKELEEL 582
PTZ00121 PTZ00121
MAEBL; Provisional
 164-311 2.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  164 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEvekvhlEKKLRDEINLAKQEAQRlKELREGTENERSRQKYA 243
Cdd:PTZ00121  1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAEAAA-DEAEAAEEKAEAAEKKK 1373

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842089067  244 EEELEQVREALRKAEKELEshsswyAPEALQKwlqlTHEVEVQYYNIKKQNAEKQLL-VAKEGAEKIKK 311
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKK------ADEAKKK----AEEDKKKADELKKAAAAKKKAdEAKKKAEEKKK 1432
PTZ00121 PTZ00121
MAEBL; Provisional
 189-311 2.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  189 ERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKE-----------LREGTENERSRQKYAEEELEQVREALRKA 257
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeearieevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1842089067  258 EKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 311
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 179-308 2.33e-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: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 179 RAEQSLHDLqERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQ---------------------EAQRLKELREGTENER 237
Cdd:pfam15709 342 RAEMRRLEV-ERKRREQEEQRRLQQEQLERAEKMREELELEQQrrfeeirlrkqrleeerqrqeEEERKQRLQLQAAQER 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 238 SRQKYAE-----EELEQVR--EALRKAE------KELESHSSwyapEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKE 304
Cdd:pfam15709 421 ARQQQEEfrrklQELQRKKqqEEAERAEaekqrqKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE 496


                  ....
gi 1842089067 305 GAEK 308
Cdd:pfam15709 497 RRQK 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-360 2.38e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 179 RAEQSLHDLQERLHK---AQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENErsrqkyaEEELEQVREALR 255
Cdd:COG1196   219 KEELKELEAELLLLKlreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-------ELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 256 KAEKELeshsswyapEALQKWLQLTHEvEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHsSSLDDVDHKI 335
Cdd:COG1196   292 ELLAEL---------ARLEQDIARLEE-RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-EELEEAEAEL 360

                         170       180
                  ....*....|....*....|....*
gi 1842089067 336 LTAKQALSEVTAALRERLHRWQQIE 360
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELA 385
PTZ00121 PTZ00121
MAEBL; Provisional
 165-312 2.71e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  165 EHMKKM--MKDLEGLHRAEQSLHDLQER---LHKAQ-----EEHRTVEVEKVHLEKKLRDEINLAKQEAQRLK--ELREG 232
Cdd:PTZ00121  1549 DELKKAeeLKKAEEKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKA 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  233 TENERSRQKYAEEELEQVREA--LRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIK 310
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708


                   ..
gi 1842089067  311 KK 312
Cdd:PTZ00121  1709 KK 1710
PRK12705 PRK12705
hypothetical protein; Provisional
 140-307 3.02e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 140 FMLVVSIVIGVGGCWFAYI---QNRYSKEHMK-KMMKDLEGLHRAEQSLHDLQERLHKAQEEHRtvevekvhleKKLRDE 215
Cdd:PRK12705    6 LLVILLLLIGLLLGVLVVLlkkRQRLAKEAERiLQEAQKEAEEKLEAALLEAKELLLRERNQQR----------QEARRE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 216 INLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELEshsswyapealqkwlQLTHEVEVQYYNIKKQNA 295
Cdd:PRK12705   76 REELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE---------------ELEKQLDNELYRVAGLTP 140

                         170
                  ....*....|....
gi 1842089067 296 E--KQLLVAKEGAE 307
Cdd:PRK12705  141 EqaRKLLLKLLDAE 154
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 156-260 3.19e-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: 40.13  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 156 AYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTEN 235
Cdd:COG4942   134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

                          90       100
                  ....*....|....*....|....*
gi 1842089067 236 ERSRQKYAEEELEQVREALRKAEKE 260
Cdd:COG4942   214 ELAELQQEAEELEALIARLEAEAAA 238
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 167-262 3.23e-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: 38.19  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 167 MKKMMKD-----LEGLHRAEQSLHDLQERLHKAQEEHRTVEVE--------KVHLEKKLRDEINLAKQEAQRLKEL-REG 232
Cdd:cd06503    24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiieeaRKEAEKIKEEILAEAKEEAERILEQaKAE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1842089067 233 TENERSRqkyAEEELEQ--VREALRKAEKELE 262
Cdd:cd06503   104 IEQEKEK---ALAELRKevADLAVEAAEKILG 132
PTZ00121 PTZ00121
MAEBL; Provisional
 164-311 3.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  164 KEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENER------ 237
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkadeak 1476

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842089067  238 ---SRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKK 311
Cdd:PTZ00121  1477 kkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
PTZ00121 PTZ00121
MAEBL; Provisional
 189-312 5.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067  189 ERLHKAQEEHRTVEVEKVHlEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKEleshsswy 268
Cdd:PTZ00121  1281 DELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-------- 1351

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1842089067  269 aPEALQKWLQLTHEvevqyyniKKQNAEKQLLVAKEGAEKIKKK 312
Cdd:PTZ00121  1352 -AEAAADEAEAAEE--------KAEAAEKKKEEAKKKADAAKKK 1386
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
57-122 7.17e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.32  E-value: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842089067  57 NWTVDEVVQWLITyVELPQYEETFRKLQLSGHAMPrLAVTNTTMTGtvLKMTDRSHRQKLQLKALD 122
Cdd:pfam07647   3 SWSLESVADWLRS-IGLEQYTDNFRDQGITGAELL-LRLTLEDLKR--LGITSVGHRRKILKKIQE 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-313 7.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 163 SKEHMKKMMKDLEGLHR-------AEQSLHDLQERLHKAQEEhrtvevekvhLEKKlRDEINLAKQEAQRLKElregtEN 235
Cdd:PRK03918  586 SVEELEERLKELEPFYNeylelkdAEKELEREEKELKKLEEE----------LDKA-FEELAETEKRLEELRK-----EL 649

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842089067 236 ERSRQKYAEEELEQVREALRKAEKELESHSSWYapEALQKWLQlthEVEVQYYNIKKQNAEKQllVAKEGAEKIKKKR 313
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 ...
 179-262 8.17e-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: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842089067 179 RAEQSLHDLQERLHKAQEEHRTVEvekvhleKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAE 258
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKKAQ-------EELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75


                  ....
gi 1842089067 259 KELE 262
Cdd:pfam20492  76 EEKE 79
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 57-118 9.64e-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: 9.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842089067  57 NWTVDEVVQWLITYvELPQYEETFRKLQLSGHAMPRLavTNTTMTGtvLKMTDRSHRQKLQL 118
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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