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Conserved domains on  [gi|32880035|gb|AAP88848|]
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homer homolog 1 (Drosophila) [Homo sapiens]

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, ...
 3-111 2.66e-79

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: 237.63  E-value: 2.66e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   3 EQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 32880035  83 NTVYGLGFSSEHHLSKFAEKFQEFKEAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-352 2.58e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 181 KHWEAELATLKGNNAKLTAALLESTANVKQwkQQLAAYQEEAERLHKRVTELECVSSQAN-AVHTHKTELNQTIQELEET 259
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELE--AELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAELARL 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 260 LKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFE 339
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170
                ....*....|...
gi 32880035 340 LTELRDNLAKLLE 352
Cdd:COG1196 381 LEELAEELLEALR 393
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 2.66e-79

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: 237.63  E-value: 2.66e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   3 EQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 32880035  83 NTVYGLGFSSEHHLSKFAEKFQEFKEAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-105 2.16e-39

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: 135.27  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035     4 QPIFSTRAHVFQIDPNTKKNWVPTsKHAVTVSYFYDSTRNVYRIISLD--GSKAIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....
gi 32880035    82 AntVYGLGFSSEHHLSKFAEKFQE 105
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQE 109
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-107 6.04e-35

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: 123.62  E-value: 6.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035      1 MGEQPIFSTRAHVFQIDPNTKKnWVPTSKH-AVTVSYFYDSTRNVYRIISLDGS-KAIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*....
gi 32880035     79 DsrANTVYGLGFSSEHHLSKFAEKFQEFK 107
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLKAL 106
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-352 2.58e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 181 KHWEAELATLKGNNAKLTAALLESTANVKQwkQQLAAYQEEAERLHKRVTELECVSSQAN-AVHTHKTELNQTIQELEET 259
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELE--AELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAELARL 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 260 LKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFE 339
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170
                ....*....|...
gi 32880035 340 LTELRDNLAKLLE 352
Cdd:COG1196 381 LEELAEELLEALR 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-333 1.27e-07

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: 53.52  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTE----LECVSSQANAVHTHKTELNQTIQELEET 259
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlrerLESLERRIAATERRLEDLEEQIEELSED 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    260 LKLKEEEIERLKQEIDNARE------------------LQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEA 321
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESeleallnerasleealalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170
                   ....*....|..
gi 32880035    322 FRNNLKTLLEIL 333
Cdd:TIGR02168  934 LEVRIDNLQERL 945
PRK12704 PRK12704
phosphodiesterase; Provisional
 267-352 2.42e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  267 IERLKQEIDnaRELQEQRdsltQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 346
Cdd:PRK12704  66 IHKLRNEFE--KELRERR----NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139


                 ....*.
gi 32880035  347 LAKLLE 352
Cdd:PRK12704 140 QLQELE 145
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 212-349 6.47e-04

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 40.84  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   212 KQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARELQEQRDSLTQKL 291
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLE---SQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTL 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32880035   292 QEVEIRNKDLEG--------------QLSDLEQRLEKSQNEQEAFRNnlktLLEILDGKIFELTELRDNLAK 349
Cdd:pfam15294 209 NASTALQKSLEEdlastkhellkvqeQLEMAEKELEKKFQQTAAYRN----MKEMLTKKNEQIKELRKRLSK 276
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 2.66e-79

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: 237.63  E-value: 2.66e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   3 EQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 32880035  83 NTVYGLGFSSEHHLSKFAEKFQEFKEAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-107 7.14e-44

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: 146.84  E-value: 7.14e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   5 PIFSTRAHVFQIDPNtKKNWVPTS-KHAVTVSYFYDSTRNVYRIISLDGS--KAIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837   1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                        90       100
                ....*....|....*....|....*.
gi 32880035  82 anTVYGLGFSSEHHLSKFAEKFQEFK 107
Cdd:cd00837  80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-105 2.16e-39

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: 135.27  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035     4 QPIFSTRAHVFQIDPNTKKNWVPTsKHAVTVSYFYDSTRNVYRIISLD--GSKAIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....
gi 32880035    82 AntVYGLGFSSEHHLSKFAEKFQE 105
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQE 109
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-107 6.04e-35

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: 123.62  E-value: 6.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035      1 MGEQPIFSTRAHVFQIDPNTKKnWVPTSKH-AVTVSYFYDSTRNVYRIISLDGS-KAIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*....
gi 32880035     79 DsrANTVYGLGFSSEHHLSKFAEKFQEFK 107
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLKAL 106
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-100 3.12e-11

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: 59.63  E-value: 3.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   5 PIFSTRAHVFQIDPNTKKnWVPT-SKHAVTVSYFYDSTR-NVYRIIS--LDGSKAIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207   1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGrkLQDHEVVINCAILKGLKYNQATPTFHQWRDA 79

                        90       100
                ....*....|....*....|
gi 32880035  81 RanTVYGLGFSSEHHLSKFA 100
Cdd:cd01207  80 R--QVYGLNFASKEEATEFA 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-352 2.58e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 181 KHWEAELATLKGNNAKLTAALLESTANVKQwkQQLAAYQEEAERLHKRVTELECVSSQAN-AVHTHKTELNQTIQELEET 259
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELE--AELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAELARL 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 260 LKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFE 339
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170
                ....*....|...
gi 32880035 340 LTELRDNLAKLLE 352
Cdd:COG1196 381 LEELAEELLEALR 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-333 1.27e-07

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: 53.52  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTE----LECVSSQANAVHTHKTELNQTIQELEET 259
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlrerLESLERRIAATERRLEDLEEQIEELSED 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    260 LKLKEEEIERLKQEIDNARE------------------LQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEA 321
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESeleallnerasleealalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170
                   ....*....|..
gi 32880035    322 FRNNLKTLLEIL 333
Cdd:TIGR02168  934 LEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-352 1.51e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 181 KHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELecvSSQANAVHTHKTELNQTIQELEETL 260
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA---QAEEYELLAELARLEQDIARLEERR 311

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 261 KLKEEEIERLKQEIdnaRELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFEL 340
Cdd:COG1196 312 RELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                       170
                ....*....|..
gi 32880035 341 TELRDNLAKLLE 352
Cdd:COG1196 389 LEALRAAAELAA 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-352 2.58e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLK 263
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEELEEL 335

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 264 EEEIERLKQEIDNA----RELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFE 339
Cdd:COG1196 336 EEELEELEEELEEAeeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                       170
                ....*....|...
gi 32880035 340 LTELRDNLAKLLE 352
Cdd:COG1196 416 LERLEEELEELEE 428
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 195-352 4.55e-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: 51.61  E-value: 4.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    195 AKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLklkeeeiERLKQEI 274
Cdd:TIGR02169  290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE---AEIDKLLAEIEELEREIEEERKRR-------DKLTEEY 359

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32880035    275 DnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:TIGR02169  360 A---ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-352 8.76e-07

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: 8.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvssqanavhthkTELNQTIQELEETLKLK 263
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-------------EELEEAEAELAEAEEAL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 264 EEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTEL 343
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447


                ....*....
gi 32880035 344 RDNLAKLLE 352
Cdd:COG1196 448 AEEEAELEE 456
PRK12704 PRK12704
phosphodiesterase; Provisional
 267-352 2.42e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  267 IERLKQEIDnaRELQEQRdsltQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 346
Cdd:PRK12704  66 IHKLRNEFE--KELRERR----NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139


                 ....*.
gi 32880035  347 LAKLLE 352
Cdd:PRK12704 140 QLQELE 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 195-352 2.61e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    195 AKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEI 274
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR---KELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    275 DNARE----LQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKL 350
Cdd:TIGR02168  743 EQLEEriaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822


                   ..
gi 32880035    351 LE 352
Cdd:TIGR02168  823 RE 824
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 181-352 3.25e-06

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: 48.91  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    181 KHWEAELATLKGNNAKLTAAL--LESTANVKQWKQ---QLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQE 255
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALndLEARLSHSRIPEiqaELSKLEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    256 LEETLKLKEEEIERLKQEIDNareLQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQR----------LEKSQNEQEA---- 321
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIEN---LNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaqlreLERKIEELEAqiek 914

                          170       180       190
                   ....*....|....*....|....*....|.
gi 32880035    322 FRNNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-352 3.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 3.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLK 263
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE---EELEELEEELEELEEELEEAEEELEEA 356

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 264 EEEIERLKQEIDNA----RELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFE 339
Cdd:COG1196 357 EAELAEAEEALLEAeaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                       170
                ....*....|...
gi 32880035 340 LTELRDNLAKLLE 352
Cdd:COG1196 437 EEEEEEALEEAAE 449
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-352 4.52e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 181 KHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvssqaNAVHTHKTELNQTIQELEETL 260
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAE 378

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 261 KLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFEL 340
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                       170
                ....*....|..
gi 32880035 341 TELRDNLAKLLE 352
Cdd:COG1196 459 EALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-350 4.82e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVhthKTELNQTIQELEETLKLK 263
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IEELEERLEEAEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    264 EEEIERLKQEIDNareLQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTEL 343
Cdd:TIGR02168  781 EAEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857


                   ....*..
gi 32880035    344 RDNLAKL 350
Cdd:TIGR02168  858 AAEIEEL 864
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-352 6.78e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 6.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    194 NAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQE 273
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    274 IdnaRELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILD---GKIFELTELRDNLAKL 350
Cdd:TIGR02168  304 K---QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQ 380


                   ..
gi 32880035    351 LE 352
Cdd:TIGR02168  381 LE 382
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-320 7.06e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 7.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAAL--LESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHTHKTELNQTIQELEETLK 261
Cdd:COG4717 108 EAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32880035 262 LKEEeiERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQE 320
Cdd:COG4717 188 LATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-352 1.30e-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: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLK 263
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL---AELARLEQDIARLEERRRELEERLEEL 321

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 264 EEEIERLKQEIDNAR----ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFE 339
Cdd:COG1196 322 EEELAELEEELEELEeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                       170
                ....*....|...
gi 32880035 340 LTELRDNLAKLLE 352
Cdd:COG1196 402 LEELEEAEEALLE 414
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-321 2.23e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  101 EKFQEFKEAARLAKEKSQEKME-----LTSTPSQESAGGDLQspltpESINGTDDERTPDVTQNSEPRAEPTQNALPFSH 175
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEeheerREELETLEAEIEDLR-----ETIAETEREREELAEEVRDLRERLEELEEERDD 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  176 SSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQE 255
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE---ERAEELREEAAELESELEE 374

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32880035  256 LEETLKLKEEEIERLKQEIDNARE-----------LQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEA 321
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRErfgdapvdlgnAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 185-352 2.87e-05

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: 44.92  E-value: 2.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 185 AELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKtELNQtiqeleetlklke 264
Cdd:COG1579  31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLGNVRNNK-EYEA------------- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 265 eeierLKQEIDNareLQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELR 344
Cdd:COG1579  94 -----LQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165


                ....*...
gi 32880035 345 DNLAKLLE 352
Cdd:COG1579 166 EELAAKIP 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-348 4.83e-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: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  212 KQQLAAYQEEAERLHKRVTELECVSSQANAVHTHKTELNQTIQELEETL------KLKEEEIERLKQEIDNA-------R 278
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLdassddlA 688

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32880035  279 ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILD-GKIFELTELRDNLA 348
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAAL 759
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
213-352 5.96e-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: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  213 QQLAAYQEEAERLHKRVTELECVSSQANAVHTHK--TELNQTIQELEETLKLKEEEIERLKQEIDnarELQEQRDSLTQK 290
Cdd:COG4913  255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRrlELLEAELEELRAELARLEAELERLEARLD---ALREELDELEAQ 331

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32880035  291 LQEVEIRNKD-LEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:COG4913  332 IRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-350 6.80e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 6.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLK 263
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLLNEEAANLRERLESL 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    264 EEEIERLKQEIdnaRELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNE---QEAFRNNLKTLLEILDGKIFEL 340
Cdd:TIGR02168  830 ERRIAATERRL---EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasLEEALALLRSELEELSEELREL 906

                          170
                   ....*....|....
gi 32880035    341 ----TELRDNLAKL 350
Cdd:TIGR02168  907 eskrSELRRELEEL 920
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
181-352 7.61e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  181 KHWEAELatlkgnnAKLTAALLESTANVKQWKQQLAAYQEEAErLHKRVTELECVSSQANAVHTHKTELNQTIQeleeTL 260
Cdd:COG4913  613 AALEAEL-------AELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAEREIAELEAELE----RL 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  261 KLKEEEIERLKQEIDNAR----ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQN--------------EQEAF 322
Cdd:COG4913  681 DASSDDLAALEEQLEELEaeleELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelralleerfAAALG 760

                        170       180       190
                 ....*....|....*....|....*....|
gi 32880035  323 RNNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:COG4913  761 DAVERELRENLEERIDALRARLNRAEEELE 790
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
184-349 8.26e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 8.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  184 EAELATLKgNNAKLTAALLEstanvkQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLK 263
Cdd:PRK02224 508 EDRIERLE-ERREDLEELIA------ERRETIEEKRERAEELRERAAELE---AEAEEKREAAAEAEEEAEEAREEVAEL 577

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  264 EEEIERLKQEIDNAR-----------------ELQEQRDSLTQ-------KLQEVEIRNKDLEGQLSdlEQRLEKSQNEQ 319
Cdd:PRK02224 578 NSKLAELKERIESLErirtllaaiadaedeieRLREKREALAElnderreRLAEKRERKRELEAEFD--EARIEEAREDK 655

                        170       180       190
                 ....*....|....*....|....*....|
gi 32880035  320 EafrnNLKTLLEILDGKIFELTELRDNLAK 349
Cdd:PRK02224 656 E----RAEEYLEQVEEKLDELREERDDLQA 681
PRK09039 PRK09039
peptidoglycan -binding protein;
176-312 1.72e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  176 SSAISKHwEAELATLKGNNAKLTAAL-LESTAN------VKQWKQQLAAYQEEAERLHKRVTELecvSSQANAVHTHKTE 248
Cdd:PRK09039  45 SREISGK-DSALDRLNSQIAELADLLsLERQGNqdlqdsVANLRASLSAAEAERSRLQALLAEL---AGAGAAAEGRAGE 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32880035  249 LNQTIQELEETLKLKEEEIERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRL 312
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIA---ALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
213-337 2.23e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 2.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 213 QQLAAYQEEAERLHKRVTELEcvssqanavhTHKTELNQTIQELEETlklkeeeIERLKQEIDNARELQEQRDSLTQKLQ 292
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDER-------IERLERELSEARSEERREIRKDREIS 468

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32880035 293 EVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKtlLEILDGKI 337
Cdd:COG2433 469 RLDREIERLERELEEERERIEELKRKLERLKELWK--LEHSGELV 511
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 185-352 3.18e-04

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: 42.75  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    185 AELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELE----CVSSQANAVHTHKTELNQTIQELEETL 260
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedlsSLEQEIENVKSELKELEARIEELEEDL 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    261 KLKEEEIERLKqeidnARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDgkifEL 340
Cdd:TIGR02169  775 HKLEEALNDLE-----ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI----DL 845

                          170
                   ....*....|..
gi 32880035    341 TELRDNLAKLLE 352
Cdd:TIGR02169  846 KEQIKSIEKEIE 857
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
199-350 3.99e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 3.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 199 AALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHTHKTELNQTIQELEETLKLKE---------EEIER 269
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelpERLEE 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 270 LKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLS-DLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLA 348
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                ..
gi 32880035 349 KL 350
Cdd:COG4717 231 QL 232
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 235-333 5.09e-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: 41.67  E-value: 5.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 235 VSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIdnaRELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEK 314
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE---KALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                        90
                ....*....|....*....
gi 32880035 315 SQNEQEAFRNNLKTLLEIL 333
Cdd:COG4942  88 LEKEIAELRAELEAQKEEL 106
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 184-329 5.41e-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: 41.67  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHkRVTELECVSSQANAVHTHKT-----ELNQTIQELEE 258
Cdd:COG4942  75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAE 153

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32880035 259 TLKLKEEEIERLKQEIDNAR--------ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTL 329
Cdd:COG4942 154 ELRADLAELAALRAELEAERaeleallaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 212-349 6.47e-04

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 40.84  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   212 KQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARELQEQRDSLTQKL 291
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLE---SQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTL 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32880035   292 QEVEIRNKDLEG--------------QLSDLEQRLEKSQNEQEAFRNnlktLLEILDGKIFELTELRDNLAK 349
Cdd:pfam15294 209 NASTALQKSLEEdlastkhellkvqeQLEMAEKELEKKFQQTAAYRN----MKEMLTKKNEQIKELRKRLSK 276
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
186-347 6.48e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  186 ELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTEL-----------ECVSSQANAVHTHKTELNQTIQ 254
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  255 ELEETLKLKEEEIERLKQEIDN----ARELQEQRDSLTQKLQ--EVEIRNK-----DLEGQLSDLEQRLEKSQNEQEAFR 323
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDleerAEELREEAAELESELEeaREAVEDRreeieELEEEIEELRERFGDAPVDLGNAE 411

                        170       180
                 ....*....|....*....|....
gi 32880035  324 NNLKTLLEILDGKIFELTELRDNL 347
Cdd:PRK02224 412 DFLEELREERDELREREAELEATL 435
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
176-331 7.36e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 7.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 176 SSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQE 255
Cdd:COG4372  29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---EQLQAAQAELAQAQEELES 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32880035 256 LEETLKLKEEEIERLKQEIdnaRELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLE 331
Cdd:COG4372 106 LQEEAEELQEELEELQKER---QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
213-352 1.66e-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: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  213 QQLAAYQEEAERLHKRVTELECVSSQANAVHTHKTELNQTIQELEETLK-LKEEEIERLKQEIDnarELQEQRDSLTQKL 291
Cdd:COG4913  235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELE---ELRAELARLEAEL 311

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32880035  292 QEVEIRNKDLEGQLSDLEQRLEKSQNEQEAfrnNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:COG4913  312 ERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEALLA 369
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 213-353 1.73e-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: 40.43  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    213 QQLAAYQEEAERLHKRVTELECVS--SQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIdnaRELQEQRDSLTQK 290
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEV---SELEEEIEELQKE 289

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32880035    291 LQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLEC 353
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 195-353 1.87e-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: 40.43  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    195 AKLTAALLESTANVKQWKQQLAAYQEEAERLHK----RVTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERL 270
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    271 KQEIDNA----RELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIF-----ELT 341
Cdd:TIGR02168  364 EAELEELesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELE 443

                          170
                   ....*....|..
gi 32880035    342 ELRDNLAKLLEC 353
Cdd:TIGR02168  444 ELEEELEELQEE 455
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 240-350 2.35e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   240 NAVHTHKTELNQTIQELEETLKLKEEEIERLKQ-------EIDNARELQEQRDSL-------TQKLQEVEIRNKDLEGQL 305
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlnenELERVRGLEKQLEELekrydeiVERLEEKEVAYSELQEEL 366

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 32880035   306 SDLEQRLEKSQNEQEAFRNNLKTL-------LEILDGKIFELTELRDNLAKL 350
Cdd:pfam06160 367 EEILEQLEEIEEEQEEFKESLQSLrkdeleaREKLDEFKLELREIKRLVEKS 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 183-309 2.63e-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: 39.65  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    183 WEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcVSSQANAVHTHKTELNQTIQELEETLKL 262
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELEEELEELQEE 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 32880035    263 KEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLE 309
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 184-352 2.63e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvssqaNAVHTHKTELNQTI---------- 253
Cdd:COG4942  47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------AELEAQKEELAELLralyrlgrqp 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 254 -------QELEETLKLKEEEIERLKQEI-DNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQ---RLEKSQNEQEAF 322
Cdd:COG4942 121 plalllsPEDFLDAVRRLQYLKYLAPARrEQAEELRADLAELAALRAELEAERAELEALLAELEEeraALEALKAERQKL 200

                       170       180       190
                ....*....|....*....|....*....|
gi 32880035 323 RNNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIA 230
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
208-352 4.72e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 4.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 208 VKQWKQQLAAYQEEAERLHKRVTELEcvssqanavhthktELNQTIQELEETLKLKEEEIERLKQEIDnARELQEQRDSL 287
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELE--------------ELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEAL 137

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32880035 288 TQKLQEVEIRNKDLEGQ---LSDLEQRLEKSQNEQEAFRNNLKTLLEILD-GKIFELTELRDNLAKLLE 352
Cdd:COG4717 138 EAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 267-350 4.88e-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: 38.59  E-value: 4.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 267 IERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 346
Cdd:COG4942  22 AAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98


                ....
gi 32880035 347 LAKL 350
Cdd:COG4942  99 LEAQ 102
Knl1_RWD_C pfam18210
Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, ...
 279-350 5.41e-03

Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, present in Homo sapiens. The KMN network is the core of the outer kinetochore which is responsible for microtubule binding/stabilization and controls the spindle assembly checkpoint. This domain is the second of two RING finger, WD repeat, DEAD-like helicase (RWD) domains. The tandem RWD domains mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex. The Mis12 complex is a KMN sub-complex that tethers directly onto the underlying chromatin layer.


Pssm-ID: 465680 [Multi-domain]  Cd Length: 152  Bit Score: 37.05  E-value: 5.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32880035   279 ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRnnLKTLLEILDGK-IFELTELRDNLAKL 350
Cdd:pfam18210   1 ELKEELEELEEKLEELEERKQELLAAIGEAERIREECWTSEEVLR--LKEELEALESLhGWRITEVSDDTLVF 71
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-334 5.87e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEcvsSQANAVHTHKTELNQTIQELEETLKLK 263
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAEL 433

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32880035 264 EEEIERLKQEIDNARELQEQrdsLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILD 334
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAE---LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 185-350 6.42e-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: 38.51  E-value: 6.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    185 AELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELEC--------VSSQANAVHTHKTELN---QTI 253
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEReieeerkrRDKLTEEYAELKEELEdlrAEL 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    254 QELEETLKLKEEEIERLKQEIDNAR----ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFR------ 323
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYREKLEKLKreinELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleikkq 453

                          170       180
                   ....*....|....*....|....*...
gi 32880035    324 -NNLKTLLEILDGKIFELTELRDNLAKL 350
Cdd:TIGR02169  454 eWKLEQLAADLSKYEQELYDLKEEYDRV 481
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 199-350 6.67e-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: 38.34  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   199 AALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNAR 278
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035   279 ELQEQRDSLTQKLQEV--------------EIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELR 344
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTittltqklttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278


                  ....*.
gi 32880035   345 DNLAKL 350
Cdd:pfam07888 279 LQAAQL 284
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
184-297 7.70e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.07  E-value: 7.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVteLECVSSQANAVHTHKTELNQTIQELEETLKL- 262
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI--LASLEAELEALQAREASLQAQLAQLEARLAEl 346

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 32880035 263 --KEEEIERLKQEIDNARELQEQrdsLTQKLQEVEIR 297
Cdd:COG3206 347 peLEAELRRLEREVEVARELYES---LLQRLEEARLA 380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 217-352 8.24e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 8.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 217 AYQEEAERLHKRVTELEcvssqANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNAR----ELQEQRDSLTQKLQ 292
Cdd:COG1196 217 ELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRleleELELELEEAQAEEY 291

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035 293 EVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 352
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
PRK12704 PRK12704
phosphodiesterase; Provisional
 212-314 8.46e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035  212 KQQLAAYQEEAERLHKrvtelECVSSQANAVHTHKTELNQTIQELEETLKLKEEEI----ERLKQEIDNA----RELQEQ 283
Cdd:PRK12704  41 KRILEEAKKEAEAIKK-----EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLlqkeENLDRKLELLekreEELEKK 115

                         90       100       110
                 ....*....|....*....|....*....|.
gi 32880035  284 RDSLTQKLQEVEIRNKDLEGQLSDLEQRLEK 314
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELER 146
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 184-331 8.50e-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: 38.23  E-value: 8.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    184 EAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQ-----------EEAERLHKRVTELECVSSQANAVHTHKTELNQT 252
Cdd:pfam01576  383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlseserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32880035    253 IQELEETLKLKEEEI-ERLKQEIDNA---RELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKT 328
Cdd:pfam01576  463 VSSLESQLQDTQELLqEETRQKLNLStrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542


                   ...
gi 32880035    329 LLE 331
Cdd:pfam01576  543 LEE 545
 
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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