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Conserved domains on  [gi|528502371|ref|XP_005173449|]
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stromal interaction molecule 1a isoform X1 [Danio rerio]

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 ...
 336-435 1.91e-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: 180.14  E-value: 1.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  336 SPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTA 415
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 528502371  416 ALRERLHRWQQIELLTGFTL 435
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 122-195 4.54e-45

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: 155.97  E-value: 4.54e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371 122 EVYNWTVDEVVKWLIDYVELTQYVEAIKKLNFSGTAMPRLAVKNNTLTQTVLKILDRSHVQKLQLKALDTVLFG 195
Cdd:cd09573    1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 238-421 1.12e-08

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


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 56.47  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 238 MMKDLdslqraeQSLHDLQQK-LQIAQEEHRsveVEKVNLE-QKLRDEINTAKQEAQRLKELREGTENELSRqkyAEEEL 315
Cdd:COG1579    2 MPEDL-------RALLDLQELdSELDRLEHR---LKELPAElAELEDELAALEARLEAAKTELEDLEKEIKR---LELEI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 316 EQVRMALKKAEKELESRSSwspPEALQkwlQLTHEVEVQyyNIKKQNAERQLQVAKEGAEKIKKKrntlfgtfhvahsss 395
Cdd:COG1579   69 EEVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE--------------- 125

                        170       180
                 ....*....|....*....|....*.
gi 528502371 396 LDDVDHKILAAKQALGEVTAALRERL 421
Cdd:COG1579  126 LAELEAELAELEAELEEKKAELDEEL 151
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 336-435 1.91e-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: 180.14  E-value: 1.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  336 SPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTA 415
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 528502371  416 ALRERLHRWQQIELLTGFTL 435
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 122-195 4.54e-45

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: 155.97  E-value: 4.54e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371 122 EVYNWTVDEVVKWLIDYVELTQYVEAIKKLNFSGTAMPRLAVKNNTLTQTVLKILDRSHVQKLQLKALDTVLFG 195
Cdd:cd09573    1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 341-432 6.03e-43

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: 150.47  E-value: 6.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 341 LQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTAALRER 420
Cdd:cd11722    1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                         90
                 ....*....|..
gi 528502371 421 LHRWQQIELLTG 432
Cdd:cd11722   81 QHRWSQIESLCG 92
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 238-421 1.12e-08

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: 56.47  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 238 MMKDLdslqraeQSLHDLQQK-LQIAQEEHRsveVEKVNLE-QKLRDEINTAKQEAQRLKELREGTENELSRqkyAEEEL 315
Cdd:COG1579    2 MPEDL-------RALLDLQELdSELDRLEHR---LKELPAElAELEDELAALEARLEAAKTELEDLEKEIKR---LELEI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 316 EQVRMALKKAEKELESRSSwspPEALQkwlQLTHEVEVQyyNIKKQNAERQLQVAKEGAEKIKKKrntlfgtfhvahsss 395
Cdd:COG1579   69 EEVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE--------------- 125

                        170       180
                 ....*....|....*....|....*.
gi 528502371 396 LDDVDHKILAAKQALGEVTAALRERL 421
Cdd:COG1579  126 LAELEAELAELEAELEEKKAELDEEL 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 245-430 1.91e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 245 LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMALKK 324
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 325 AEKELE-------------SRSSwsppEALQKWLQLTHEVEVQYYNIKKQ--NAERQLQVAKEGAEKIKKKRNtlfgtfh 389
Cdd:COG1196  349 AEEELEeaeaelaeaeealLEAE----AELAEAEEELEELAEELLEALRAaaELAAQLEELEEAEEALLERLE------- 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528502371 390 vAHSSSLDDVDHKILAAKQALGEVTAALRERLHRWQQIELL 430
Cdd:COG1196  418 -RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 238-359 7.24e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.91  E-value: 7.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 238 MMKDLDSLQR-AEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQR------------LKELREGTENE 304
Cdd:PRK00409 521 LIASLEELEReLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeakkeadeiIKELRQLQKGG 600

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528502371 305 LSRQKyaEEELEQVRMALKKAEKELESRSswSPPEALQKWLQLTHEVEVQYYNIK 359
Cdd:PRK00409 601 YASVK--AHELIEARKRLNKANEKKEKKK--KKQKEKQEELKVGDEVKYLSLGQK 651
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 233-380 7.99e-07

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: 52.76  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   233 DHMKKMMKDLDSLQ----RAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQ 308
Cdd:TIGR02169  681 ERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   309 KYAEEELEQVRM---ALKKAEKELESRSSWSP-----------PEALQKWLQLTHEVEV---------QYYNIKKQNAER 365
Cdd:TIGR02169  761 KELEARIEELEEdlhKLEEALNDLEARLSHSRipeiqaelsklEEEVSRIEARLREIEQklnrltlekEYLEKEIQELQE 840

                          170
                   ....*....|....*
gi 528502371   366 QLQVAKEGAEKIKKK 380
Cdd:TIGR02169  841 QRIDLKEQIKSIEKE 855
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 229-322 3.99e-06

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: 46.45  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  229 RHSKDHMKKMMKDLdslQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQ-----------------KLRDEINTAKQEA 291
Cdd:pfam20492  16 KQYEEETKKAQEEL---EESEETAEELEEERRQAEEEAERLEQKRQEAEEekerleesaemeaeekeQLEAELAEAQEEI 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 528502371  292 QRLKELREGTENELSRqkyAEEELEQVRMAL 322
Cdd:pfam20492  93 ARLEEEVERKEEEARR---LQEELEEAREEE 120
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 235-332 6.89e-05

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: 43.20  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 235 MKKMMKD-----LDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEkvnleqklRDEI-NTAKQEAQRLK-ELREGTENELSR 307
Cdd:cd06503   24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAE--------AQEIiEEARKEAEKIKeEILAEAKEEAER 95

                         90       100
                 ....*....|....*....|....*.
gi 528502371 308 QK-YAEEELEQVRmalKKAEKELESR 332
Cdd:cd06503   96 ILeQAKAEIEQEK---EKALAELRKE 118
 
Name Accession Description Interval E-value
SOAR pfam16533
STIM1 Orai1-activating region; SOAR is the Orai1-activating region of STIM1, where STIM1 are ...
 336-435 1.91e-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: 180.14  E-value: 1.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  336 SPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTA 415
Cdd:pfam16533   1 TPPTALQQWLQLTYEVEMQYYNIKRQAAEKQLQQAKEACEKLKKKRSSVFGSFRVAHSSSLDDVDNKILAAKNALEEVTK 80

                          90       100
                  ....*....|....*....|
gi 528502371  416 ALRERLHRWQQIELLTGFTL 435
Cdd:pfam16533  81 DLQERQHRWQQIEKLCGFPI 100
SAM_STIM1 cd09573
SAM domain of STIM1 subfamily proteins; SAM (sterile alpha motif) domain of STIM1 (Stromal ...
 122-195 4.54e-45

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: 155.97  E-value: 4.54e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371 122 EVYNWTVDEVVKWLIDYVELTQYVEAIKKLNFSGTAMPRLAVKNNTLTQTVLKILDRSHVQKLQLKALDTVLFG 195
Cdd:cd09573    1 EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDTVLFG 74
SOAR cd11722
STIM1 Orai1-activating region; STIM1 (stromal interaction module 1) is a metazoan ...
 341-432 6.03e-43

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: 150.47  E-value: 6.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 341 LQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTAALRER 420
Cdd:cd11722    1 LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQALEEVTRELQER 80

                         90
                 ....*....|..
gi 528502371 421 LHRWQQIELLTG 432
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 ...
 122-195 4.62e-33

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: 121.67  E-value: 4.62e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371 122 EVYNWTVDEVVKWLIDYVELTQYVEAIKKLNFSGTAMPRLAVKNNTLTQTVLKILDRSHVQKLQLKALDTVLFG 195
Cdd:cd09504    1 EVHNWTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDVVLFG 74
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 122-195 2.61e-25

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: 99.67  E-value: 2.61e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371 122 EVYNWTVDEVVKWLIDYVELTQYVEAIKKLNFSGTAMPRLAVKNNTLTQTVLKILDRSHVQKLQLKALDTVLFG 195
Cdd:cd09574    1 EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDVVLFG 74
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 238-421 1.12e-08

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: 56.47  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 238 MMKDLdslqraeQSLHDLQQK-LQIAQEEHRsveVEKVNLE-QKLRDEINTAKQEAQRLKELREGTENELSRqkyAEEEL 315
Cdd:COG1579    2 MPEDL-------RALLDLQELdSELDRLEHR---LKELPAElAELEDELAALEARLEAAKTELEDLEKEIKR---LELEI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 316 EQVRMALKKAEKELESRSSwspPEALQkwlQLTHEVEVQyyNIKKQNAERQLQVAKEGAEKIKKKrntlfgtfhvahsss 395
Cdd:COG1579   69 EEVEARIKKYEEQLGNVRN---NKEYE---ALQKEIESL--KRRISDLEDEILELMERIEELEEE--------------- 125

                        170       180
                 ....*....|....*....|....*.
gi 528502371 396 LDDVDHKILAAKQALGEVTAALRERL 421
Cdd:COG1579  126 LAELEAELAELEAELEEKKAELDEEL 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 245-430 1.91e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 245 LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMALKK 324
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 325 AEKELE-------------SRSSwsppEALQKWLQLTHEVEVQYYNIKKQ--NAERQLQVAKEGAEKIKKKRNtlfgtfh 389
Cdd:COG1196  349 AEEELEeaeaelaeaeealLEAE----AELAEAEEELEELAEELLEALRAaaELAAQLEELEEAEEALLERLE------- 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528502371 390 vAHSSSLDDVDHKILAAKQALGEVTAALRERLHRWQQIELL 430
Cdd:COG1196  418 -RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
244-384 3.22e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 244 SLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMALK 323
Cdd:COG4372   32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528502371 324 KAEKELESRssWSPPEALQKWL-QLTHEVEVQYYNI-----KKQNAERQLQVAKEGAEKIKKKRNTL 384
Cdd:COG4372  112 ELQEELEEL--QKERQDLEQQRkQLEAQIAELQSEIaereeELKELEEQLESLQEELAALEQELQAL 176
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
233-384 2.35e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 233 DHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRD------------EINTAKQEAQRLKELREG 300
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllplyqELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 301 TENELSRQKYAEEELEQVRMALKKAEKELESRSSWSPPEALQKWLQLTHEVEVQYYniKKQNAERQLQVAKEGAEKIKKK 380
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEE 228


                 ....
gi 528502371 381 RNTL 384
Cdd:COG4717  229 LEQL 232
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 238-359 7.24e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.91  E-value: 7.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 238 MMKDLDSLQR-AEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQR------------LKELREGTENE 304
Cdd:PRK00409 521 LIASLEELEReLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeakkeadeiIKELRQLQKGG 600

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528502371 305 LSRQKyaEEELEQVRMALKKAEKELESRSswSPPEALQKWLQLTHEVEVQYYNIK 359
Cdd:PRK00409 601 YASVK--AHELIEARKRLNKANEKKEKKK--KKQKEKQEELKVGDEVKYLSLGQK 651
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 233-380 7.99e-07

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: 52.76  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   233 DHMKKMMKDLDSLQ----RAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQ 308
Cdd:TIGR02169  681 ERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   309 KYAEEELEQVRM---ALKKAEKELESRSSWSP-----------PEALQKWLQLTHEVEV---------QYYNIKKQNAER 365
Cdd:TIGR02169  761 KELEARIEELEEdlhKLEEALNDLEARLSHSRipeiqaelsklEEEVSRIEARLREIEQklnrltlekEYLEKEIQELQE 840

                          170
                   ....*....|....*
gi 528502371   366 QLQVAKEGAEKIKKK 380
Cdd:TIGR02169  841 QRIDLKEQIKSIEKE 855
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
243-385 1.82e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 243 DSLQRAEQSLHDLQQKLQIAQEEHRSV--EVEKVNLEQ-KLRDEINTAKQEAQRLKELREGTENEL----SRQKYAEEEL 315
Cdd:COG4372   59 EELEQLEEELEQARSELEQLEEELEELneQLQAAQAELaQAQEELESLQEEAEELQEELEELQKERqdleQQRKQLEAQI 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 316 EQVRMALKKAEKELESRSswsppEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLF 385
Cdd:COG4372  139 AELQSEIAEREEELKELE-----EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 245-428 1.99e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 245 LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQK---LRDEINTAKQEAQRLKELREGTENELS----RQKYAEEELEQ 317
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEEYELLAELARLEQDIArleeRRRELEERLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 318 VRMALKKAEKELESRSswsppealqkwlQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLfgtfhvAHSSSLD 397
Cdd:COG1196  321 LEEELAELEEELEELE------------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA------EAEEELE 382

                        170       180       190
                 ....*....|....*....|....*....|.
gi 528502371 398 DVDHKILAAKQALGEVTAALRERLHRWQQIE 428
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEEAEEALL 413
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
232-381 3.49e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 232 KDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRD------------------------EINTA 287
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 288 KQEAQRLKELREGTENELSRqkyAEEELEQVRMALKKAEKELES-RSSWSPPE---ALQKWLQLTHEV-----EVQYYNI 358
Cdd:PRK03918 611 EKELEREEKELKKLEEELDK---AFEELAETEKRLEELRKELEElEKKYSEEEyeeLREEYLELSRELaglraELEELEK 687

                        170       180
                 ....*....|....*....|...
gi 528502371 359 KKQNAERQLQVAKEGAEKIKKKR 381
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAK 710
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 226-430 3.51e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 226 IQNRHSKDHMKKMMKDL-DSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKEL---REGT 301
Cdd:COG1196  298 ARLEQDIARLEERRRELeERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaeLAEA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 302 ENELSRQKYAEEELEQVRMALKKAEKELESRSswsppEALQKwLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKR 381
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAE-----EALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528502371 382 NTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTAALRERLHRWQQIELL 430
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 229-322 3.99e-06

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: 46.45  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  229 RHSKDHMKKMMKDLdslQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQ-----------------KLRDEINTAKQEA 291
Cdd:pfam20492  16 KQYEEETKKAQEEL---EESEETAEELEEERRQAEEEAERLEQKRQEAEEekerleesaemeaeekeQLEAELAEAQEEI 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 528502371  292 QRLKELREGTENELSRqkyAEEELEQVRMAL 322
Cdd:pfam20492  93 ARLEEEVERKEEEARR---LQEELEEAREEE 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
222-346 9.62e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 9.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 222 WFAYIQNRHSKDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKL----RDEINTAKQEAQRLKEl 297
Cdd:COG4717  128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQ- 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528502371 298 regtenelsRQKYAEEELEQVRMALKKAEKELESRSSWSPPEALQKWLQ 346
Cdd:COG4717  207 ---------RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-423 1.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 242 LDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMA 321
Cdd:COG1196  385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 322 LKKAEKELESRSswsppEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTfhvahsssLDDVDH 401
Cdd:COG1196  465 LAELLEEAALLE-----AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA--------VAVLIG 531

                        170       180
                 ....*....|....*....|..
gi 528502371 402 KILAAKQALGEVTAALRERLHR 423
Cdd:COG1196  532 VEAAYEAALEAALAAALQNIVV 553
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
233-428 1.29e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  233 DHMKKMMKDLDS----LQRAEQSLHDLQQkLQIAQEEHRSVEVEKVNLEQkLRDEIN--TAKQEAQRLKELREGTENELS 306
Cdd:COG4913   228 DALVEHFDDLERaheaLEDAREQIELLEP-IRELAERYAAARERLAELEY-LRAALRlwFAQRRLELLEAELEELRAELA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  307 RqkyAEEELEQVRMALKKAEKELEsrsswsppealqkwlqlthEVEVQYYNI---KKQNAERQLQVAKEGAEKIKKKRNT 383
Cdd:COG4913   306 R---LEAELERLEARLDALREELD-------------------ELEAQIRGNggdRLEQLEREIERLERELEERERRRAR 363

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528502371  384 LfgtfhvahSSSLDDVDHKILAAKQALGEVTAALRERLHRWQQIE 428
Cdd:COG4913   364 L--------EALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-430 1.30e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 244 SLQRAEQSLHDLQQKLQIAQEEHRSVEVEkvnlEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMALK 323
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 324 KAEKELESRSSwsppEALQKWLQLTHEVEVQyyNIKKQNAERQLQVAKEGAEKIKKKRNTLfgtfhvahSSSLDDVDHKI 403
Cdd:COG1196  372 AELAEAEEELE----ELAEELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEEL--------EEALAELEEEE 437

                        170       180
                 ....*....|....*....|....*..
gi 528502371 404 LAAKQALGEVTAALRERLHRWQQIELL 430
Cdd:COG1196  438 EEEEEALEEAAEEEAELEEEEEALLEL 464
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
245-433 1.50e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  245 LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLR----DEINTAKQEAQRLKELREGTENELSRQkyaEEELEQVRM 320
Cdd:COG4913   297 LEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARL---EALLAALGL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  321 ALKKAEKELESRSSwSPPEALQKWLQLTHEVEVQYYnikkqNAERQLQVAKEGAEKIKKKRNTLfgtfhVAHSSSLDDVD 400
Cdd:COG4913   374 PLPASAEEFAALRA-EAAALLEALEEELEALEEALA-----EAEAALRDLRRELRELEAEIASL-----ERRKSNIPARL 442

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528502371  401 HKILAA-KQALGEVTAAL---------RERLHRWQQ-IE-LLTGF 433
Cdd:COG4913   443 LALRDAlAEALGLDEAELpfvgelievRPEEERWRGaIErVLGGF 487
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 236-332 1.63e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.94  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  236 KKMMKDLDSLQRAEQSL-HDLQQKLQIAQEEHRSVEVE------KVNLEQKLRDEINTAKQEAQRLKELREGTENELSRq 308
Cdd:pfam07926  11 KRLKEEAADAEAQLQKLqEDLEKQAEIAREAQQNYERElvlhaeDIKALQALREELNELKAEIAELKAEAESAKAELEE- 89

                          90       100
                  ....*....|....*....|....
gi 528502371  309 kyAEEELEQVRMALKKAEKELESR 332
Cdd:pfam07926  90 --SEESWEEQKKELEKELSELEKR 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 229-429 1.83e-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: 48.51  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   229 RHSKDHMKKMMKDLDS-LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLE---QKLRDEINTAKQE----AQRLKELREG 300
Cdd:TIGR02168  704 RKELEELEEELEQLRKeLEELSRQISALRKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERleeaEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   301 TENELSRQKYAEEELEQVRMALKKAEKEL--ESRSSWSPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAK------- 371
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELtlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeiee 863

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528502371   372 ---------EGAEKIKKKRNTLFGTFHVAHS------SSLDDVDHKILAAKQALGEvtaaLRERLH----RWQQIEL 429
Cdd:TIGR02168  864 leelieeleSELEALLNERASLEEALALLRSeleelsEELRELESKRSELRRELEE----LREKLAqlelRLEGLEV 936
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 232-428 2.48e-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: 48.13  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   232 KDHMKKMMKDLDSLQRAEQSL----HDLQQKLQIAQEEHRSVEVEKVNLE----------QKLRDEINTAKQEAQRLKEL 297
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALaneiSRLEQQKQILRERLANLERQLEELEaqleelesklDELAEELAELEEKLEELKEE 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   298 REGTENEL-----------SRQKYAEEELEQVRMALKKAEKELES-RSSWSPPEALQKwlQLTHEVEVQYYNIKKQNAER 365
Cdd:TIGR02168  353 LESLEAELeeleaeleeleSRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLE--RLEDRRERLQQEIEELLKKL 430

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528502371   366 QLQVAKEGAEKIKKKRNTLFGT-----FHVAHSSSLDDVDHKILAAKQALGEVTAALRERLHRWQQIE 428
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEELqeeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-423 3.31e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   244 SLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMALK 323
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   324 KAEKELES----RSSWSPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKE-------GAEKIKKKRNTLFGTFHVAH 392
Cdd:TIGR02168  870 ELESELEAllneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREklaqlelRLEGLEVRIDNLQERLSEEY 949

                          170       180       190
                   ....*....|....*....|....*....|.
gi 528502371   393 SSSLDDvdhkILAAKQALGEVTAALRERLHR 423
Cdd:TIGR02168  950 SLTLEE----AEALENKIEDDEEEARRRLKR 976
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
241-433 3.92e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  241 DLDSLQRAeqsLHDLQQKLQIAQEEHRSVEVEKVNLEQkLRDEINTAKQEAQRLKELREGTENELSRqkyAEEELEQVRM 320
Cdd:COG4913   662 DVASAERE---IAELEAELERLDASSDDLAALEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQ---AEEELDELQD 734

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  321 ALKKAEKELESRSSWsppEALQKWLQLTHEvevQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTF-------HVAHS 393
Cdd:COG4913   735 RLEAAEDLARLELRA---LLEERFAAALGD---AVERELRENLEERIDALRARLNRAEEELERAMRAFnrewpaeTADLD 808

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528502371  394 SSLDDVDH--KILA--AKQALGEVTAALRERLHRWqQIELLTGF 433
Cdd:COG4913   809 ADLESLPEylALLDrlEEDGLPEYEERFKELLNEN-SIEFVADL 851
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 247-375 4.15e-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: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  247 RAEQSLHDLQQKLQIAQEEHRSVEvekvnleQKLRDEINTAKQEAQRLKELREGTEnELSRQKY-AEEELEQVRMALKKA 325
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKKAQ-------EELEESEETAEELEEERRQAEEEAE-RLEQKRQeAEEEKERLEESAEME 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528502371  326 EKE---LESRSSwsppEALQKWLQLTHEVEvqyyniKKQNAERQLQVAKEGAE 375
Cdd:pfam20492  75 AEEkeqLEAELA----EAQEEIARLEEEVE------RKEEEARRLQEELEEAR 117
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 238-427 4.73e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.27  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   238 MMKDLDSLQRAEQSLHDLQQKL------QIAQEEHRSVEVEKvNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYA 311
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLTLRSQLltlctpCMPDTYHERKQVLE-KELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   312 ------EEELEQVRMALKKAEKELESRSSWSPPEALQKWL-QLTHEVEVQYYNIKKQNAER------QLQVAKEGAEKIK 378
Cdd:TIGR00618  263 kqlrarIEELRAQEAVLEETQERINRARKAAPLAAHIKAVtQIEQQAQRIHTELQSKMRSRakllmkRAAHVKQQSSIEE 342

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 528502371   379 KKRntLFGTFHVAHssslddvDHKILAAKQALG-----EVTAALRERLHRWQQI 427
Cdd:TIGR00618  343 QRR--LLQTLHSQE-------IHIRDAHEVATSireisCQQHTLTQHIHTLQQQ 387
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 235-342 5.25e-05

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: 46.30  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 235 MKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEE 314
Cdd:COG4942  145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                         90       100
                 ....*....|....*....|....*...
gi 528502371 315 LEQVRMALKKAEKELESRSSWSPPEALQ 342
Cdd:COG4942  225 LEALIARLEAEAAAAAERTPAAGFAALK 252
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
245-423 5.42e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 245 LQRAEQSLHDLQQKLQIAQ----EEHRSVevekvnleQKLRDEINTAKQE-AQRLKELREGTENELsrqkyaeEELEQVR 319
Cdd:COG3206  265 IQQLRAQLAELEAELAELSarytPNHPDV--------IALRAQIAALRAQlQQEAQRILASLEAEL-------EALQARE 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 320 MALKKAEKELESRSSwSPPEALQKWLQLTHEVEV--QYYN-----IKKQNAERQLQVAK----------EGAEKIKKKRN 382
Cdd:COG3206  330 ASLQAQLAQLEARLA-ELPELEAELRRLEREVEVarELYEsllqrLEEARLAEALTVGNvrvidpavvpLKPVSPKKLLI 408

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528502371 383 TLFGTFhvahssslddvdhkiLAAkqALGEVTAALRERLHR 423
Cdd:COG3206  409 LALGLL---------------LGL--LLGLGLALLLELLDR 432
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 243-413 5.46e-05

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: 46.98  E-value: 5.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   243 DSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELR---EGTENELSRQKYAEEELEQVR 319
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRL 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   320 MALKKAEKELESRSSwsppeALQKWLQlthEVEVQyYNIKKQNAERQLQVAKEGAEKIKK-KRNTLFGTFHVAHSSSLDD 398
Cdd:TIGR02169  885 GDLKKERDELEAQLR-----ELERKIE---ELEAQ-IEKKRKRLSELKAKLEALEEELSEiEDPKGEDEEIPEEELSLED 955

                          170
                   ....*....|....*...
gi 528502371   399 VD---HKILAAKQALGEV 413
Cdd:TIGR02169  956 VQaelQRVEEEIRALEPV 973
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 235-332 6.89e-05

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: 43.20  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 235 MKKMMKD-----LDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEkvnleqklRDEI-NTAKQEAQRLK-ELREGTENELSR 307
Cdd:cd06503   24 ILKALDEreekiAESLEEAEKAKEEAEELLAEYEEKLAEARAE--------AQEIiEEARKEAEKIKeEILAEAKEEAER 95

                         90       100
                 ....*....|....*....|....*.
gi 528502371 308 QK-YAEEELEQVRmalKKAEKELESR 332
Cdd:cd06503   96 ILeQAKAEIEQEK---EKALAELRKE 118
PRK12704 PRK12704
phosphodiesterase; Provisional
 208-380 8.01e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 208 FMLVVSIVIGMGGCWFAYIQNRHSK-DHMKKMMKDLdsLQRAEQSLHDL-QQKLQIAQEE--HRSVEVEK---------V 274
Cdd:PRK12704   8 LIALVALVVGAVIGYFVRKKIAEAKiKEAEEEAKRI--LEEAKKEAEAIkKEALLEAKEEihKLRNEFEKelrerrnelQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 275 NLEQKLRDEINTAKQEAQRL----KELREGTENELSRQKYAEEELEQVRMALKKAEKELESRSSWSPPEALQKWLQ---- 346
Cdd:PRK12704  86 KLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEkvee 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 528502371 347 -LTHEVEVQYYNIKKQnaerqlqvAKEGAEKIKKK 380
Cdd:PRK12704 166 eARHEAAVLIKEIEEE--------AKEEADKKAKE 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-384 1.44e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   244 SLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRD----------EINTAKQEAQRLKELREGTENELSRQKYAEE 313
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelyalanEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528502371   314 ELEQ----VRMALKKAEKELESrsswsppeaLQKWLQLTHEvEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTL 384
Cdd:TIGR02168  327 ELESkldeLAEELAELEEKLEE---------LKEELESLEA-ELEELEAELEELESRLEELEEQLETLRSKVAQL 391
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
245-426 2.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 245 LQRAEQSLHDLQQKLQIAQEehrsvevekvNLEQKLRD---EINTAKQEAQRLKELREGTENELSRQkyaEEELEQVRMA 321
Cdd:COG4372    8 VGKARLSLFGLRPKTGILIA----------ALSEQLRKalfELDKLQEELEQLREELEQAREELEQL---EEELEQARSE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 322 LKKAEKELESRSswsppEALQKWLQLTHEVEVQYYNIKKQ--NAERQLQVAKEGAEKIKKKRNTLfgtfhvahSSSLDDV 399
Cdd:COG4372   75 LEQLEEELEELN-----EQLQAAQAELAQAQEELESLQEEaeELQEELEELQKERQDLEQQRKQL--------EAQIAEL 141

                        170       180
                 ....*....|....*....|....*..
gi 528502371 400 DHKILAAKQALgevtAALRERLHRWQQ 426
Cdd:COG4372  142 QSEIAEREEEL----KELEEQLESLQE 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 243-426 3.42e-04

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: 43.60  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 243 DSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRD---EINTAKQEAQRLKELREGTENELSRqkyAEEELEQVR 319
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerRIAALARRIRALEQELAALEAELAE---LEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 320 MALKKAEKELESR-------SSWSPPEAL---QKWLQLthEVEVQYYniKKQNAERQLQvakegAEKIKKKRNTlfgtfh 389
Cdd:COG4942   97 AELEAQKEELAELlralyrlGRQPPLALLlspEDFLDA--VRRLQYL--KYLAPARREQ-----AEELRADLAE------ 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528502371 390 vahsssLDDVDHKILAAKQALGEVTAALRERLHRWQQ 426
Cdd:COG4942  162 ------LAALRAELEAERAELEALLAELEEERAALEA 192
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
229-384 3.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 229 RHSKDHMKKMMKDLDSLQRAEQSLHDLQQKlqiaQEEHRSVEVEKVNLEQKLRDeintAKQEAQRLKELREGTENELSRQ 308
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELRE----IEKRLSRLEEEINGIEERIKEL 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 309 KYAEEELEQvrmaLKKAEKELESRSswsppEALQKWLQLTHEV---EVQYYNIKKQNA-------ERQLQVAKEGAEKIK 378
Cdd:PRK03918 334 EEKEERLEE----LKKKLKELEKRL-----EELEERHELYEEAkakKEELERLKKRLTgltpeklEKELEELEKAKEEIE 404


                 ....*.
gi 528502371 379 KKRNTL 384
Cdd:PRK03918 405 EEISKI 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 236-428 3.92e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 236 KKMMKDLDSLQRAEQSLHD--LQQKLQIAQEEHRSVEVEKVNLEQKLRD---EINTAKQEAQRLKELREGTENELSRQKY 310
Cdd:COG1196  216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 311 AEEELEQVRMALKKAEKELESRSSwsppEALQKWLQLTHEvevqyynikKQNAERQLQVAKEGAEKIKKKRNTLfgtfhv 390
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLE----ELEEELAELEEE---------LEELEEELEELEEELEEAEEELEEA------ 356

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528502371 391 ahssslddvDHKILAAKQALGEVTAALRERLHRWQQIE 428
Cdd:COG1196  357 ---------EAELAEAEEALLEAEAELAEAEEELEELA 385
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
229-331 3.95e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 229 RHSKDHMKKMMKDLDSLQR---AEQSLHDLQQKLQIAQEEHRSVEvEKVNLEQKLRDEINTAKQEAQRLKE-LREGTENE 304
Cdd:COG4717  115 REELEKLEKLLQLLPLYQEleaLEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEqLSLATEEE 193

                         90       100
                 ....*....|....*....|....*..
gi 528502371 305 LSRqkyAEEELEQVRMALKKAEKELES 331
Cdd:COG4717  194 LQD---LAEELEELQQRLAELEEELEE 217
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 248-380 4.06e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.64  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 248 AEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKY-AEEELEQVRMALKKAE 326
Cdd:PRK09510  85 EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAkAEAEAKRAAAAAKKAA 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528502371 327 KELESRSSwspPEALQKwlqltHEVEVQyyniKKQNAERQLQVAKEGAEKIKKK 380
Cdd:PRK09510 165 AEAKKKAE---AEAAKK-----AAAEAK----KKAEAEAAAKAAAEAKKKAEAE 206
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 245-332 4.18e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 41.86  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 245 LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEIntAKQEAQRLKELREGTENELS-RQKYAEEELEQ--VRMA 321
Cdd:PRK07352  66 LRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEI--EKQAIEDMARLKQTAAADLSaEQERVIAQLRReaAELA 143

                         90
                 ....*....|.
gi 528502371 322 LKKAEKELESR 332
Cdd:PRK07352 144 IAKAESQLPGR 154
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
243-451 4.24e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 243 DSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREG---TENELSR--QKYAEEELEQ 317
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlesLQEELAAleQELQALSEAE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 318 VRMALKKAEKELESRSSWSPPEALQKWLQLT--HEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSS 395
Cdd:COG4372  181 AEQALDELLKEANRNAEKEEELAEAEKLIESlpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528502371 396 LDDVDHKILAAKQALGEVTAALRERLHRWQQIELLTGFTLVHNPGLPSLASALNLD 451
Cdd:COG4372  261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 234-381 4.70e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   234 HMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEE-------HRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELS 306
Cdd:pfam02463  234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEklaqvlkENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528502371   307 RQKYAEEEleqvrmALKKAEKELESRSSWSppEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKR 381
Cdd:pfam02463  314 EKLKESEK------EKKKAEKELKKEKEEI--EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 235-328 5.97e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  235 MKKMMKDLDSL-QRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGtENELSRQKYAEE 313
Cdd:pfam03938  17 GKAAQAQLEKKfKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQ-ELQKKQQELLQP 95

                          90
                  ....*....|....*.
gi 528502371  314 ELEQVRMALKK-AEKE 328
Cdd:pfam03938  96 IQDKINKAIKEvAKEK 111
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
232-330 6.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 232 KDHMKKMMKDLD----SLQRAEQSLHDLQQKLqiAQEEHRSVEVEKVnleqKLRDEINTAKQEAQRLKELREGTENELSR 307
Cdd:PRK03918 625 EEELDKAFEELAetekRLEELRKELEELEKKY--SEEEYEELREEYL----ELSRELAGLRAELEELEKRREEIKKTLEK 698

                         90       100
                 ....*....|....*....|...
gi 528502371 308 QKYAEEELEQVRMALKKAEKELE 330
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKALE 721
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-420 8.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 236 KKMMKDLDSL--QRAEQSLHDLQQKLQIAQEEHRSVEVEkvnlEQKLRDEINTAKQEAQRLK----EL-----------R 298
Cdd:PRK03918 368 KAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKKEIKELKkaieELkkakgkcpvcgR 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 299 EGTENE---------------LSRQKYAEEELEQVRMALKKAEKELESRSSWSPPEALQKWLQLTHEvEVQYYNIKKqna 363
Cdd:PRK03918 444 ELTEEHrkelleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE-KLKKYNLEE--- 519

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528502371 364 erqLQVAKEGAEKIKKKRNTLFGTFHVAHS---------SSLDDVDHKILAAKQALGEVTAALRER 420
Cdd:PRK03918 520 ---LEKKAEEYEKLKEKLIKLKGEIKSLKKelekleelkKKLAELEKKLDELEEELAELLKELEEL 582
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 227-379 8.76e-04

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: 42.63  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  227 QNRHSKDHMKKmmkdldslQRAEQSLHDLQQKLQiAQEEHRSVEVEKVNLEQKLRDEINTAKQ---EAQRLKELREGTEn 303
Cdd:pfam15709 330 QEKASRDRLRA--------ERAEMRRLEVERKRR-EQEEQRRLQQEQLERAEKMREELELEQQrrfEEIRLRKQRLEEE- 399

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528502371  304 elsRQKYAEEELEQVRmaLKKAEKElesRSSWSPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKK 379
Cdd:pfam15709 400 ---RQRQEEEERKQRL--QLQAAQE---RARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKR 467
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 243-384 8.86e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 8.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 243 DSLQRAEQSLHDLQQKLQIAQEEhrsvevekvnlEQKLRDEINTAKQEAQRLKELREGTENELsrqKYAEEELEQVRMAL 322
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAE-----------LDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 323 KKAEKELESR------------------SSWSPPEALQKWLQLTHEVEVQYYNIKKQNAER-QLQVAKEGAEKIKKKRNT 383
Cdd:COG3883   82 EERREELGERaralyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKaELEAKKAELEAKLAELEA 161


                 .
gi 528502371 384 L 384
Cdd:COG3883  162 L 162
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
231-430 9.06e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 9.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 231 SKDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVekvnLEQKLRDEINTAKQEAQRLKELREgtenelsrqky 310
Cdd:COG4717  335 SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL----LAEAGVEDEEELRAALEQAEEYQE----------- 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 311 AEEELEQVRMALKKAEKELESRSSWSPPEALQKwlqlthevevqyyniKKQNAERQLQVAKEGAEKIKKKRNTLfgtfhV 390
Cdd:COG4717  400 LKEELEELEEQLEELLGELEELLEALDEEELEE---------------ELEELEEELEELEEELEELREELAEL-----E 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 528502371 391 AHSSSLDDvDHKILAAKQALGEVTAALRERLHRWQQIELL 430
Cdd:COG4717  460 AELEQLEE-DGELAELLQELEELKAELRELAEEWAALKLA 498
Caldesmon pfam02029
Caldesmon;
260-379 9.80e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.55  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  260 QIAQEEHRSVEVEKV---------NLEQKLRDEinTAKQEAQRLKELREgtenELSRQKYAEEEL--EQVRMALKKAEKE 328
Cdd:pfam02029  35 SVEPNEHNSYEEDSElkpsgqgglDEEEAFLDR--TAKREERRQKRLQE----ALERQKEFDPTIadEKESVAERKENNE 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528502371  329 LESRSSWSPPEALQKWLQLTHE-----VEVQYYNIKKQNAERqlQVAKEGAEKIKK 379
Cdd:pfam02029 109 EEENSSWEKEEKRDSRLGRYKEeeteiREKEYQENKWSTEVR--QAEEEGEEEEDK 162
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 227-380 1.03e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  227 QNRHSKDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELS 306
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371  307 RQKYAEEELEqvRMALKKAEKELESRsswsppEALQKWLQLTHEVEVQyynIKKQNAERQLQVAKEGAEKIKKK 380
Cdd:pfam13868 207 RAKLYQEEQE--RKERQKEREEAEKK------ARQRQELQQAREEQIE---LKERRLAEEAEREEEEFERMLRK 269
mukB PRK04863
chromosome partition protein MukB;
243-332 1.12e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  243 DSLQRAEQSLHDLQQKLQIAQEEHRSVEvEKVNLEQKLRDEI--NTAKQEAQRLkeLREGTEnelsrQKYAEEELEQVRM 320
Cdd:PRK04863  449 AKEQEATEELLSLEQKLSVAQAAHSQFE-QAYQLVRKIAGEVsrSEAWDVAREL--LRRLRE-----QRHLAEQLQQLRM 520

                          90
                  ....*....|..
gi 528502371  321 ALKKAEKELESR 332
Cdd:PRK04863  521 RLSELEQRLRQQ 532
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
237-384 1.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 237 KMMKDLDSLQRAEQSL--HDLQqKLQIAQEEHRSVEvEKVNleqKLRDEINTAKQEAQRLKELregtenelsrqkyaEEE 314
Cdd:PRK03918 497 KLKELAEQLKELEEKLkkYNLE-ELEKKAEEYEKLK-EKLI---KLKGEIKSLKKELEKLEEL--------------KKK 557

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528502371 315 LEQVRMALKKAEKELE------SRSSWSPPEALQKWLQlthEVEvQYYN--IKKQNAERQLQVAKegaEKIKKKRNTL 384
Cdd:PRK03918 558 LAELEKKLDELEEELAellkelEELGFESVEELEERLK---ELE-PFYNeyLELKDAEKELEREE---KELKKLEEEL 628
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 243-332 1.17e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.16  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 243 DSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKvnleQKLRDEintAKQEAQRLK-ELREGTENELSRQKY-AEEELEQVRm 320
Cdd:COG0711   38 DGLAEAERAKEEAEAALAEYEEKLAEARAEA----AEIIAE---ARKEAEAIAeEAKAEAEAEAERIIAqAEAEIEQER- 109

                         90
                 ....*....|..
gi 528502371 321 alKKAEKELESR 332
Cdd:COG0711  110 --AKALAELRAE 119
PRK12705 PRK12705
hypothetical protein; Provisional
 208-376 1.61e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.00  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 208 FMLVVSIVIGMGGCWFAYIQNRhskdhmKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTA 287
Cdd:PRK12705   6 LLVILLLLIGLLLGVLVVLLKK------RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 288 KQEAQRLKELREGTENELSRQKYAEEELEQVRMALKKAEKELESR-----------SSWSPPEALQKWLQ-LTHEVEVQy 355
Cdd:PRK12705  80 QREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELekqldnelyrvAGLTPEQARKLLLKlLDAELEEE- 158

                        170       180
                 ....*....|....*....|.
gi 528502371 356 yniKKQNAERQLQVAKEGAEK 376
Cdd:PRK12705 159 ---KAQRVKKIEEEADLEAER 176
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 244-330 1.63e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.80  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  244 SLQRAEQSLHDLQQKLQIAQEEH---RSVEVEKVNLEqKLRDEINTAKQEAQRLKELREGTENELSRQK--------YAE 312
Cdd:pfam07888 285 TLQLADASLALREGRARWAQEREtlqQSAEADKDRIE-KLSAELQRLEERLQEERMEREKLEVELGREKdcnrvqlsESR 363

                          90
                  ....*....|....*...
gi 528502371  313 EELEQVRMALKKAEKELE 330
Cdd:pfam07888 364 RELQELKASLRVAQKEKE 381
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 237-371 1.65e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   237 KMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKvNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELE 316
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH-EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528502371   317 QVRMALKKAEKELESRSswsppeALQKWLQLTH---EVEVQYYNIKKQNAERQLQVAK 371
Cdd:TIGR00618  404 ILQREQATIDTRTSAFR------DLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEK 455
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 288-431 2.17e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   288 KQEAQRLKELREGTENELSRQKYAEEELEQVRMALKKAEKELESRSSWSPPEALQKWLQLTHEvevQYYNIKKQNAERQL 367
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY---LKLNEERIDLLQEL 245

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528502371   368 QVAKEgaEKIKKKRNTLfgtfhVAHSSSLDDVD--HKILAAKQALGEVTAALRERLHRWQQIELLT 431
Cdd:pfam02463  246 LRDEQ--EEIESSKQEI-----EKEEEKLAQVLkeNKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 227-430 2.65e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   227 QNRHSKDHMKKMMKDLDSLQ----RAEQSLHDLQQKLQI-------------AQEEHRSV-EVEKVNLEQKLRDEINTAK 288
Cdd:pfam01576  265 KIRELEAQISELQEDLESERaarnKAEKQRRDLGEELEAlkteledtldttaAQQELRSKrEQEVTELKKALEEETRSHE 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   289 QEAQRLKELREGTENELSrqkyaeEELEQ---VRMALKKAEKELESRSSwsppeALQKWLQLTH-------------EVE 352
Cdd:pfam01576  345 AQLQEMRQKHTQALEELT------EQLEQakrNKANLEKAKQALESENA-----ELQAELRTLQqakqdsehkrkklEGQ 413

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528502371   353 VQYYNIKKQNAERQLQvakEGAEKIKKKRNTLFGTfhvahSSSLDDVDHK-ILAAKQAlgevtAALRERLHRWQqiELL 430
Cdd:pfam01576  414 LQELQARLSESERQRA---ELAEKLSKLQSELESV-----SSLLNEAEGKnIKLSKDV-----SSLESQLQDTQ--ELL 477
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 248-346 3.12e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 248 AEQSLHDLQQKLQIAQEEhrsvevekvnlEQKLRDEINTAKQEAQRLKELREGTENELSRqkyAEEELEQVRMALKKAEK 327
Cdd:COG3883   14 ADPQIQAKQKELSELQAE-----------LEAAQAELDALQAELEELNEEYNELQAELEA---LQAEIDKLQAEIAEAEA 79

                         90
                 ....*....|....*....
gi 528502371 328 ELESRSswsppEALQKWLQ 346
Cdd:COG3883   80 EIEERR-----EELGERAR 93
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-381 3.51e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   240 KDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEvekvNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKyaeEELEQVR 319
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIE----NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK---ERLEELE 743

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371   320 MALKKAEKELES-RSSWSPPEALQKWLQLT-HEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKR 381
Cdd:TIGR02169  744 EDLSSLEQEIENvKSELKELEARIEELEEDlHKLEEALNDLEARLSHSRIPEIQAELSKLEEEV 807
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 227-372 3.52e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 40.43  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  227 QNRHSKDHMKKMMKDLDS-LQRAEQSLHDLQQKLQIAQEEHRS--VEVEKVNLEQKLRDEI-NTAK-----QEAQRLKEL 297
Cdd:pfam15742 104 QSIKSQNSLQEKLAQEKSrVADAEEKILELQQKLEHAHKVCLTdtCILEKKQLEERIKEASeNEAKlkqqyQEEQQKRKL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  298 REGTENELSRQ----------------------KYAEEELEQVRMALKKAEKELESR--------SSWSPPEALQKWLQL 347
Cdd:pfam15742 184 LDQNVNELQQQvrslqdkeaqlemtnsqqqlriQQQEAQLKQLENEKRKSDEHLKSNqelseklsSLQQEKEALQEELQQ 263

                         170       180
                  ....*....|....*....|....*...
gi 528502371  348 THE---VEVQYYNIKKQNAERQLQVAKE 372
Cdd:pfam15742 264 VLKqldVHVRKYNEKHHHHKAKLRRAKD 291
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
244-319 3.53e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 244 SLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLR-----DEINTAKQEAQRLKELREGTENELSRQKYAEEELEQV 318
Cdd:COG4717  426 DEEELEEELEELEEELEELEEELEELREELAELEAELEqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEA 505


                 .
gi 528502371 319 R 319
Cdd:COG4717  506 R 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 249-375 3.75e-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: 40.82  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   249 EQSLHDLQQ-KLQIaqEEHRSVEVEKVNLEQKLRDEINTAK--QEAQRLKELREGTEnELSRQKYAEEELEQVRMALKKA 325
Cdd:TIGR02169  173 EKALEELEEvEENI--ERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEGYE-LLKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 528502371   326 EKELESRSSWSPPEA--LQKWLQLTHEVEVQyynIKKQNAERQLQVAKEGAE 375
Cdd:TIGR02169  250 EEELEKLTEEISELEkrLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGE 298
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 246-331 3.83e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 38.48  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  246 QRAEQSLHDLQQKLQIAQEEHRSvevekvnleqklrdeintakQEAQRLKELREGTENEL-SRQKYAEEELEQVRMALKK 324
Cdd:pfam00836  38 KKKDSSLEEIQKKLEAAEERRKS--------------------LEAQKLKQLAEKREKEEeALQKADEENNNFSKMAEEK 97


                  ....*..
gi 528502371  325 AEKELES 331
Cdd:pfam00836  98 LKQKMEA 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
232-421 4.44e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 232 KDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYA 311
Cdd:COG4372  107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 312 EEELEQVRMALKKAEKELESRSSWSPPEALQK---WLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTF 388
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEellEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266

                        170       180       190
                 ....*....|....*....|....*....|...
gi 528502371 389 HVAHSSSLDDVDHKILAAKQALGEVTAALRERL 421
Cdd:COG4372  267 ILVEKDTEEEELEIAALELEALEEAALELKLLA 299
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
246-426 4.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  246 QRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKlRDEINTAKQEAQRLKELRE------GTENELSRqkyAEEELEQVR 319
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWdeidvaSAEREIAE---LEAELERLD 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  320 ---MALKKAEKELEsrsswsppEALQKWLQLTHEVEVQYYNIKKqnAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSL 396
Cdd:COG4913   682 assDDLAALEEQLE--------ELEAELEELEEELDELKGEIGR--LEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                         170       180       190
                  ....*....|....*....|....*....|
gi 528502371  397 DDVdHKILAAKQALGEVTAALRERLHRWQQ 426
Cdd:COG4913   752 EER-FAAALGDAVERELRENLEERIDALRA 780
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
235-380 4.86e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 235 MKKMMKDLDSLQRAEQSLHDLQ------QKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREgtenELSRQ 308
Cdd:COG1340  142 IKELEKELEKAKKALEKNEKLKelraelKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD----ELHKE 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528502371 309 -KYAEEELEQVRMALKKAEKELesrsswsppealqkwlqltHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKK 380
Cdd:COG1340  218 iVEAQEKADELHEEIIELQKEL-------------------RELRKELKKLRKKQRALKREKEKEELEEKAEE 271
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
245-330 4.89e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  245 LQRAEQSLHDLQQKLQIAQEEHRSVEvEKVNLEQKLR----DEINTAKQEA------QRLKELREGTeNELSRqkyAEEE 314
Cdd:COG4913   619 LAELEEELAEAEERLEALEAELDALQ-ERREALQRLAeyswDEIDVASAEReiaeleAELERLDASS-DDLAA---LEEQ 693

                          90
                  ....*....|....*.
gi 528502371  315 LEQVRMALKKAEKELE 330
Cdd:COG4913   694 LEELEAELEELEEELD 709
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 225-330 5.59e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  225 YIQNRHSKDHMKKMMKDLDsLQRAEQSLHDLQQKLQI------AQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELR 298
Cdd:pfam13868  68 KEERKRYRQELEEQIEERE-QKRQEEYEEKLQEREQMdeiverIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528502371  299 egtenelsRQKYAEEELEQVRMALKKAEKELE 330
Cdd:pfam13868 147 --------KEEEREEDERILEYLKEKAEREEE 170
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
242-379 6.02e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 242 LDSL---QRAEqslhdLQQKLQIAQEE-HRSVEVEKvnlEQKLRDEiNTAKQEAQRLKELREG--TENELSRQKyAEEEL 315
Cdd:COG2268  186 LDALgrrKIAE-----IIRDARIAEAEaERETEIAI---AQANREA-EEAELEQEREIETARIaeAEAELAKKK-AEERR 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528502371 316 EQVRmALKKAEKELESRSswsppEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKK 379
Cdd:COG2268  256 EAET-ARAEAEAAYEIAE-----ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKP 313
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 227-384 6.08e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   227 QNRHSKDHMKKMMKDLDS-LQRAEQSLHDlQQKLQIAQEEHRSVEVEKvNLEQKLRDEINTAK---QEAQRLKELREGTE 302
Cdd:pfam01576  935 KSESARQQLERQNKELKAkLQEMEGTVKS-KFKSSIAALEAKIAQLEE-QLEQESRERQAANKlvrRTEKKLKEVLLQVE 1012

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371   303 NELSRQKYAEEELEQVRMALKKAEKELEsrsswsppEAlqkwlqlthEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRN 382
Cdd:pfam01576 1013 DERRHADQYKDQAEKGNSRMKQLKRQLE--------EA---------EEEASRANAARRKLQRELDDATESNESMNREVS 1075


                   ..
gi 528502371   383 TL 384
Cdd:pfam01576 1076 TL 1077
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 232-331 6.16e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 232 KDHMKKMMKDLDSLQ--RAEQSLHDLQQKLQ----IAQEE---HRSVEVEKVNLEQKL---RDEINTAKQEAQRLKELRE 299
Cdd:PRK04778 262 KEQIDENLALLEELDldEAEEKNEEIQERIDqlydILEREvkaRKYVEKNSDTLPDFLehaKEQNKELKEEIDRVKQSYT 341

                         90       100       110
                 ....*....|....*....|....*....|..
gi 528502371 300 GTENELSRQKYAEEELEQVRMALKKAEKELES 331
Cdd:PRK04778 342 LNESELESVRQLEKQLESLEKQYDEITERIAE 373
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
226-384 6.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 226 IQNRhSKDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQkLRDEINTAKQEAQRLKELREGTENEL 305
Cdd:PRK03918 191 IEEL-IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELESLEGSKRKLEEKIRELEERI 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 306 SRQKYAEEELEQVRMALKKAEKELESRSSWSppEALQKWLQLTHEVEVQY--YNIKKQNAERQLQVA---KEGAEKIKKK 380
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLS--EFYEEYLDELREIEKRLsrLEEEINGIEERIKELeekEERLEELKKK 346


                 ....
gi 528502371 381 RNTL 384
Cdd:PRK03918 347 LKEL 350
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
231-381 6.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 231 SKDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELregtenelsRQKY 310
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL---------EKKY 656

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528502371 311 AEEELEQVRMALKKAEKELESRSswSPPEALQKWLQlthEVEVQYYNIKKQNAERqlQVAKEGAEKIKKKR 381
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLR--AELEELEKRRE---EIKKTLEKLKEELEER--EKAKKELEKLEKAL 720
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 229-430 7.09e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  229 RHSKDHMKKMMKDLDS-LQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSR 307
Cdd:pfam07888  65 KRDREQWERQRRELESrVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371  308 QKYAEEELEQVRMALKKAEKELesRSSWSPPEALQKWLQLThEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGT 387
Cdd:pfam07888 145 VLERETELERMKERAKKAGAQR--KEEEAERKQLQAKLQQT-EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528502371  388 FHVAHSSSlddvdhkilAAKQALGEVTAALRERLHRWQQ-IELL 430
Cdd:pfam07888 222 LTTAHRKE---------AENEALLEELRSLQERLNASERkVEGL 256
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 243-360 7.97e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 39.92  E-value: 7.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 243 DSLQRAEQSLHDLQQKLqiaqEEHRSVEVEkvnLEQKLRDEINTAKQE-AQRLK--ELREGT----ENELSRQKYAEEEL 315
Cdd:PRK11091  78 EQLEESRQRLSRLVAKL----EEMRERDLE---LNVQLKDNIAQLNQEiAEREKaeEARQEAfeqlKNEIKEREETQIEL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 316 EQVRMALK-------------------------------KAEKELESRSSWS--PPEALQKWLQ-----------LTHEV 351
Cdd:PRK11091 151 EQQSSLLRsfldaspdlvyyrnedgefsgcnramelltgKSEKQLIGLTPKDvySPEAAEKVIEtdekvfrhnvsLTYEQ 230


                 ....*....
gi 528502371 352 EVQYYNIKK 360
Cdd:PRK11091 231 WLDYPDGRK 239
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 237-329 9.86e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 38.94  E-value: 9.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528502371 237 KMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQK---LRDEINTAKQEAQRLKELREGTENELSRQKYAEE 313
Cdd:COG4026  122 KSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESEleeLREEYKKLREENSILEEEFDNIKSEYSDLKSRFE 201

                         90       100
                 ....*....|....*....|
gi 528502371 314 ELEQVR----MALKKAEKEL 329
Cdd:COG4026  202 ELLKKRllevFSLEELWKEL 221
 
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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