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Conserved domains on  [gi|1958683518|ref|XP_038950361|]
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homer protein homolog 3 isoform X7 [Rattus norvegicus]

Protein Classification

Homer/Vesl family EVH1 domain-containing protein( domain architecture ID 10100433)

Homer/Vesl family EVH1 (WH1, RanBP1-WASP) domain-containing protein is a synaptic scaffolding protein, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation

CATH:  2.30.29.30
Gene Ontology:  GO:0007216|GO:0035256|GO:0005515
PubMed:  11911879|17316461
SCOP:  4002440

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 6-114 5.75e-78

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


:

Pssm-ID: 269917  Cd Length: 109  Bit Score: 233.78  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958683518  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-312 4.15e-08

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   95 SEQQLTQFAEKFQEVKEAARLAREKSQDGGELTSTALAMASHQVppsplvstngpeEKLFRSQSADAPGPTERERLKKML 174
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR------------ERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  175 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSV 254
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARL 409

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683518  255 EQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 6-114 5.75e-78

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269917  Cd Length: 109  Bit Score: 233.78  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958683518  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 7-110 4.97e-43

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 144.51  E-value: 4.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 1958683518  85 AntVYGLGFGSEQQLTQFAEKFQEVK 110
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 6-108 1.62e-28

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 106.29  E-value: 1.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518    6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 1958683518   84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-312 4.15e-08

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: 55.06  E-value: 4.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   95 SEQQLTQFAEKFQEVKEAARLAREKSQDGGELTSTALAMASHQVppsplvstngpeEKLFRSQSADAPGPTERERLKKML 174
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR------------ERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  175 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSV 254
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARL 409

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683518  255 EQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-312 2.31e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 103 AEKFQEVKEAARLAreksqdggELTSTALAMASHQVppsplvstngpEEKLFRSQSADApgPTERERLKKMLSEGSVGEV 182
Cdd:COG1196   212 AERYRELKEELKEL--------EAELLLLKLRELEA-----------ELEELEAELEEL--EAELEELEAELAELEAELE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQ 262
Cdd:COG1196   271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELEEELEELEEELE 347

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958683518 263 TKDQEIQTLKNQstgpREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:COG1196   348 EAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
mukB PRK04863
chromosome partition protein MukB;
168-309 2.58e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  168 ERLKKMLSEGSVGEVQWEAEFFALQdsnQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELE--------AQVAA 239
Cdd:PRK04863   536 ERLLAEFCKRLGKNLDDEDELEQLQ---EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawlaAQDAL 612

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683518  240 EPVRA--GEKEATSQSVEQLearvqtkdqeIQTLknqstgpreapdtAERE-ETQQQVQDLETRNAELEQQLR 309
Cdd:PRK04863   613 ARLREqsGEEFEDSQDVTEY----------MQQL-------------LERErELTVERDELAARKQALDEEIE 662
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 190-315 3.75e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 190 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAgeKEATSQSVEQLEARVQtkdQEIQ 269
Cdd:pfam04012  19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKA--QAALTKGNEELAREAL---AEKK 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958683518 270 TLKNQSTGPREAPDTAE--REETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:pfam04012  94 SLEKQAEALETQLAQQRsaVEQLRKQLAALETKIQQLKAKKNLLKARL 141
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 6-114 5.75e-78

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269917  Cd Length: 109  Bit Score: 233.78  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958683518  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 7-110 4.97e-43

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 144.51  E-value: 4.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 1958683518  85 AntVYGLGFGSEQQLTQFAEKFQEVK 110
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 8-110 7.02e-38

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 131.04  E-value: 7.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   8 PIFSTRAHVFQIDPATKrNWIPA-GKHALTVSYFYDATRNVYRIISIGGA--KAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:cd00837     1 SIFSARAHVMQIDDSNK-NWVPAgGKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                          90       100
                  ....*....|....*....|....*.
gi 1958683518  85 anTVYGLGFGSEQQLTQFAEKFQEVK 110
Cdd:cd00837    80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 6-108 1.62e-28

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 106.29  E-value: 1.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518    6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 1958683518   84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 8-103 5.91e-12

Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269918  Cd Length: 108  Bit Score: 61.55  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   8 PIFSTRAHVFQIDPATKRnWIPAG-KHALTVSYFYDATR-NVYRIIsigGAKA-----IINSTVTPNMTFTKTSQKFGQW 80
Cdd:cd01207     1 SVASARASVMVYDDENKR-WVPSGgSQGLSRVQIYHNTRnNTFRVV---GRKLqdhevVINCAILKGLKYNQATPTFHQW 76

                          90       100
                  ....*....|....*....|...
gi 1958683518  81 ADSRanTVYGLGFGSEQQLTQFA 103
Cdd:cd01207    77 RDAR--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-312 4.15e-08

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: 55.06  E-value: 4.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   95 SEQQLTQFAEKFQEVKEAARLAREKSQDGGELTSTALAMASHQVppsplvstngpeEKLFRSQSADAPGPTERERLKKML 174
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR------------ERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  175 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSV 254
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARL 409

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683518  255 EQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-312 2.31e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 103 AEKFQEVKEAARLAreksqdggELTSTALAMASHQVppsplvstngpEEKLFRSQSADApgPTERERLKKMLSEGSVGEV 182
Cdd:COG1196   212 AERYRELKEELKEL--------EAELLLLKLRELEA-----------ELEELEAELEEL--EAELEELEAELAELEAELE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQ 262
Cdd:COG1196   271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELEEELEELEEELE 347

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958683518 263 TKDQEIQTLKNQstgpREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:COG1196   348 EAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-315 3.24e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEvQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683518 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREE---TQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEEL 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-315 1.05e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 202 LREANAAATQWR---QQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQ--ST 276
Cdd:COG1196   224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAElaRL 300

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958683518 277 GPREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-315 1.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 167 RERLKKMLSEGSVGEVQW-EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAEL---EAQVAAEPV 242
Cdd:COG1196   219 KEELKELEAELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELA 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683518 243 RA-GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGpreapDTAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG1196   299 RLeQDIARLEERRRELEERLEELEEELAELEEELEE-----LEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-315 2.22e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 166 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVA-AEPVRA 244
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeAEEELE 354

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683518 245 GEKEATSQSVEQLEARVQTKDQEIQTLKN-----QSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEElaeelLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-315 5.14e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 5.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  196 QRLAGALREANAAATQWRQQLEVQRAEAEHLR--------QRVAELEAQVAAEPVRAGEKEATSQSVEQLEARVQ-TKDQ 266
Cdd:COG4913    298 EELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGlPLPA 377

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958683518  267 EIQTLKNQSTGPREAPDT--AEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG4913    378 SAEEFAALRAEAAALLEAleEELEALEEALAEAEAALRDLRRELRELEAEI 428
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-315 5.71e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 5.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  185 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEH--LRQRVAELEAQVAAEpvragekEATSQSVEQLEARVQ 262
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERL-------DASSDDLAALEEQLE 695

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958683518  263 TKDQEIQTLKnqstgpreapdtAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG4913    696 ELEAELEELE------------EELDELKGEIGRLEKELEQAEEELDELQDRL 736
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
191-311 1.79e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 191 LQDSNQRLAGA---LREANAAATQWRQQLEVQRAEA---------EHLRQRVAELEAQVAAEPVRAGEKeatSQSVEQLE 258
Cdd:COG3206   221 LSELESQLAEAraeLAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPN---HPDVIALR 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958683518 259 ARVQTKDQEIQTLKNQSTGPREApdtaEREETQQQVQDLETRNAELEQQLRAM 311
Cdd:COG3206   298 AQIAALRAQLQQEAQRILASLEA----ELEALQAREASLQAQLAQLEARLAEL 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 183-321 2.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQV-AAEPVRAGEKEATSQSVEQLEARV 261
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeEAEAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683518 262 QTKDQEIQTLKNQSTgpREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEA--------RAE 321
Cdd:COG1196   379 EELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeeeeeeEAL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-312 2.38e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 166 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAG 245
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA---LR 393

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683518 246 EKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-315 2.64e-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: 42.74  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   96 EQQLTQFAEKFQEVKEAARLAREKSQDggelTSTALAMASHQVPPSPLVSTNGpEEKLFRSQSADAPGPTERERLKKMLS 175
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  176 EGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGE----KEATS 251
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqIEELS 851

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683518  252 QSVEQLEARVQTKDQEIQTLKNQSTGpreapDTAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEA-----LLNERASLEEALALLRSELEELSEELRELESKR 910
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-312 2.80e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  202 LREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGEKEATS--QSVEQLEARVQTKDQEIQTLKNQ---ST 276
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARleAELERLEARLDALREELDELEAQirgNG 336

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958683518  277 GPREAPDTAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:COG4913    337 GDRLEQLEREIERLERELEERERRRARLEALLAALG 372
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 151-306 3.85e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  151 EKLFRSQSadapgptERERLKKMLSEGSVGEVQWEAEFFALQDSNQ----RLAGALREANAAATQWRQQLEVQRAEAEHL 226
Cdd:COG3096    525 EQRLRQQQ-------NAERLLEEFCQRIGQQLDAAEELEELLAELEaqleELEEQAAEAVEQRSELRQQLEQLRARIKEL 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  227 RQRV-AELEAQVAAEPVRA--GEKEATSQSVeqLEARVQTKDQEiqtlknqstgpREApdTAEREETQQQVQDLETRNAE 303
Cdd:COG3096    598 AARApAWLAAQDALERLREqsGEALADSQEV--TAAMQQLLERE-----------REA--TVERDELAARKQALESQIER 662


                   ...
gi 1958683518  304 LEQ 306
Cdd:COG3096    663 LSQ 665
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 205-311 5.38e-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: 41.29  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 205 ANAAATQWRQQLEVQRAEaehLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDT 284
Cdd:COG4942    14 AAAAQADAAAEAEAELEQ---LQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                          90       100
                  ....*....|....*....|....*..
gi 1958683518 285 AEREETQQQvQDLETRNAELEQQLRAM 311
Cdd:COG4942    88 LEKEIAELR-AELEAQKEELAELLRAL 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 196-316 6.20e-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: 41.58  E-value: 6.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  196 QRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958683518  276 TGPREAPD--TAEREETQQQVQDLETRNAELEQQLRAMESNLE 316
Cdd:TIGR02168  764 EELEERLEeaEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-323 1.96e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  186 AEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAaepvragekEATSQSVEQLEARVQTKD 265
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---------GNGGDRLEQLEREIERLE 351

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683518  266 QEIQTLKNQSTGPREA--------PDTAE-----REETQQQVQDLETRNAELEQQLRAMESNLEEARAERE 323
Cdd:COG4913    352 RELEERERRRARLEALlaalglplPASAEefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
202-319 1.98e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 39.83  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 202 LREANAAATQWRQQLEV--QRAEAEHLRQRVAELEAQVAAEPVRAGEKEAT----SQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:COG3524   193 LRDAREALLAFRNRNGIldPEATAEALLQLIATLEGQLAELEAELAALRSYlspnSPQVRQLRRRIAALEKQIAAERARL 272

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958683518 276 TGPREAPDTAEReetQQQVQDLETRNAELEQQLRAMESNLEEAR 319
Cdd:COG3524   273 TGASGGDSLASL---LAEYERLELEREFAEKAYTSALAALEQAR 313
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-308 2.39e-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: 40.05  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  166 ERERLKKMLSE---------GSVGEVQWEAEffALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQ 236
Cdd:TIGR02169  696 ELRRIENRLDElsqelsdasRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  237 VAAE----------------PVRAGEKEATSQSVEQLEARVQTKDQEIQTLKnqstgPREAPDTAEREETQQQVQDLETR 300
Cdd:TIGR02169  774 LHKLeealndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLT-----LEKEYLEKEIQELQEQRIDLKEQ 848


                   ....*...
gi 1958683518  301 NAELEQQL 308
Cdd:TIGR02169  849 IKSIEKEI 856
mukB PRK04863
chromosome partition protein MukB;
168-309 2.58e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  168 ERLKKMLSEGSVGEVQWEAEFFALQdsnQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELE--------AQVAA 239
Cdd:PRK04863   536 ERLLAEFCKRLGKNLDDEDELEQLQ---EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawlaAQDAL 612

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683518  240 EPVRA--GEKEATSQSVEQLearvqtkdqeIQTLknqstgpreapdtAERE-ETQQQVQDLETRNAELEQQLR 309
Cdd:PRK04863   613 ARLREqsGEEFEDSQDVTEY----------MQQL-------------LERErELTVERDELAARKQALDEEIE 662
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
161-311 3.20e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 161 APGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAE 240
Cdd:COG4717   298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683518 241 PVRAGEKEATSQSVEQLEARVQTKdQEIQTLKNQ----STGPREAPDTAEREETQQQVQDLETRNAELEQQLRAM 311
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEYQELK-EELEELEEQleelLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
PRK09039 PRK09039
peptidoglycan -binding protein;
201-315 3.22e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 201 ALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQV-AAEPVRAGEKEAT---SQSVEQLEARVQTKDQEIQTLKNQSt 276
Cdd:PRK09039   54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLsAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQVS- 132

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958683518 277 gpreapdtaerEETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:PRK09039  133 -----------ARALAQVELLNQQIAALRRQLAALEAAL 160
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-315 3.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 191 LQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAG-----------EKEATSQSVEQLEA 259
Cdd:PRK02224  354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfleelreERDELREREAELEA 433

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683518 260 RVQTKD---QEIQTLKNQSTGP------REAPDTAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:PRK02224  434 TLRTARervEEAEALLEAGKCPecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL 498
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 190-315 3.75e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 190 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAgeKEATSQSVEQLEARVQtkdQEIQ 269
Cdd:pfam04012  19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKA--QAALTKGNEELAREAL---AEKK 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958683518 270 TLKNQSTGPREAPDTAE--REETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:pfam04012  94 SLEKQAEALETQLAQQRsaVEQLRKQLAALETKIQQLKAKKNLLKARL 141
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-314 4.70e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 149 PEEKLFRSQSADAPGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlEVQRAEAEHLRQ 228
Cdd:COG4717   300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 229 RVAELEAQVAAEPVRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGP----REAPDTAEREETQQQVQDLETRNAEL 304
Cdd:COG4717   379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeELEELEEELEELEEELEELREELAEL 458

                         170
                  ....*....|
gi 1958683518 305 EQQLRAMESN 314
Cdd:COG4717   459 EAELEQLEED 468
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
167-315 5.58e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 167 RERLKKMLSEGSVGEvqweAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGE 246
Cdd:PRK02224  292 EEERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683518 247 KEATSQS----VEQLEARVQTKDQEIQTLKNQSTGPREAPDTAE--REETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:PRK02224  368 LESELEEareaVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdfLEELREERDELREREAELEATLRTARERV 442
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-309 5.86e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518   91 LGFGSEQQLTQFAekfqevKEAARLAREKSQDGGELTSTALAMASHQvppsplvstngpeeklfrsqsadapgptERERL 170
Cdd:COG4913    604 LGFDNRAKLAALE------AELAELEEELAEAEERLEALEAELDALQ----------------------------ERREA 649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  171 KKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEAT 250
Cdd:COG4913    650 LQRLAEYSWDEIDVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL---EKELEQA 725

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683518  251 SQSVEQLEARVQTKDQEIQTLKNQSTGPR---EAPDTAE---REETQQQVQDLETRNAELEQQLR 309
Cdd:COG4913    726 EEELDELQDRLEAAEDLARLELRALLEERfaaALGDAVErelRENLEERIDALRARLNRAEEELE 790
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 167-310 6.82e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 167 RERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGE 246
Cdd:COG4942   103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683518 247 KEATSQSVEQLEARVQTKDQEIQTlknqstgpREAPDTAEREETQQQVQDLETRNAELEQQLRA 310
Cdd:COG4942   183 LEEERAALEALKAERQKLLARLEK--------ELAELAAELAELQQEAEELEALIARLEAEAAA 238
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 190-289 7.11e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  190 ALQDSNQRLaGALREANAAATQwrQQLEVQRAEAEHLRQRVAELE-AQVAAEpvraGEKEATSQSVEQLEARVQTKDQEI 268
Cdd:PRK10929   152 QLNEIERRL-QTLGTPNTPLAQ--AQLTALQAESAALKALVDELElAQLSAN----NRQELARLRSELAKKRSQQLDAYL 224

                           90       100
                   ....*....|....*....|...
gi 1958683518  269 QTLKNQ--STGPREAPDTAEREE 289
Cdd:PRK10929   225 QALRNQlnSQRQREAERALESTE 247
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 185-312 7.41e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.39  E-value: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  185 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQ---RVAELEAQVAAEpvRAGEKEATSQSVEQLEARV 261
Cdd:COG3096    835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpQANLLADETLAD--RLEELREELDAAQEAQAFI 912

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958683518  262 QTKDQEIQTLKNQSTGPREAPdtAEREETQQQVQDLETRNAELEQQLRAME 312
Cdd:COG3096    913 QQHGKALAQLEPLVAVLQSDP--EQFEQLQADYLQAKEQQRRLKQQIFALS 961
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-315 7.46e-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: 38.13  E-value: 7.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  166 ERERLKKMLSEGSVGEVQWEAEFfaLQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQvaaepvrag 245
Cdd:TIGR02169  780 ALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--------- 848

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  246 eKEATSQSVEQLEARVQTKDQEIQTLKnqstgpreapdtAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:TIGR02169  849 -IKSIEKEIENLNGKKEELEEELEELE------------AALRDLESRLGDLKKERDELEAQLRELERKI 905
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
190-315 8.25e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 190 ALQDSNQRLAGALREANAAatqwRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARvqtKDQEIQ 269
Cdd:PRK02224  259 EIEDLRETIAETEREREEL----AEEVRDLRERLEELEEERDDLLAEAGLD---DADAEAVEARREELEDR---DEELRD 328

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683518 270 TLKNQSTGPREAPDTAEREetQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:PRK02224  329 RLEECRVAAQAHNEEAESL--REDADDLEERAEELREEAAELESEL 372
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 214-312 8.38e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 37.43  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 214 QQLEVQR-AEAEHLRQRVAELEAQVAAEPVRAGEKEAT---------------SQSVEQLEARVQTKDQEIQTLKNQSTG 277
Cdd:pfam09787  78 QELEAQQqEEAESSREQLQELEEQLATERSARREAEAElerlqeelryleeelRRSKATLQSRIKDREAEIEKLRNQLTS 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958683518 278 pREAPDTAERE-------------ETQQQVQDLETRNAELEQQLRAME 312
Cdd:pfam09787 158 -KSQSSSSQSElenrlhqltetliQKQTMLEALSTEKNSLVLQLERME 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 219-315 8.66e-03

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: 38.11  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518  219 QRAEAEHLRQRVAELEAQvaaepVRAGEKE--ATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQ--QQV 294
Cdd:TIGR02168  675 RRREIEELEEKIEELEEK-----IAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleERI 749

                           90       100
                   ....*....|....*....|.
gi 1958683518  295 QDLETRNAELEQQLRAMESNL 315
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERL 770
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-305 8.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683518 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG1196   641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683518 245 GEKEATSQSVEQLEARVQTKDQEIQTLkNQSTGPREAPDTAEREETQQQVQDLETRNAELE 305
Cdd:COG1196   721 LEEEALEEQLEAEREELLEELLEEEEL-LEEEALEELPEPPDLEELERELERLEREIEALG 780
 
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.
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