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Conserved domains on  [gi|578827628|ref|XP_006720839|]
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homer protein homolog 2 isoform X3 [Homo sapiens]

Protein Classification

Homer/Vesl family protein( domain architecture ID 12913132)

Homer/Vesl family protein is a synaptic scaffolding protein, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation

Gene Ontology:  GO:0097110|GO:2001256|GO:0035256|GO:0007216

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 8.40e-77

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: 231.47  E-value: 8.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   3 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 578827628  83 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 111
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-333 2.78e-09

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: 58.53  E-value: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    93 EQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIA 172
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   173 LTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQ---- 248
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdies 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   249 LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKV 324
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*....
gi 578827628   325 ELKSFLEVL 333
Cdd:TIGR02168  937 RIDNLQERL 945
 
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 8.40e-77

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: 231.47  E-value: 8.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   3 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 578827628  83 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 111
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-107 5.11e-40

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: 137.20  E-value: 5.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    4 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 578827628   82 AntVFGLGFSSEQQLTKFAEKFQEVK 107
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-105 4.13e-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: 105.52  E-value: 4.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628     1 MREQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 578827628    79 DsrANTVFGLGFSSEQQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-333 2.78e-09

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: 58.53  E-value: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    93 EQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIA 172
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   173 LTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQ---- 248
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdies 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   249 LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKV 324
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*....
gi 578827628   325 ELKSFLEVL 333
Cdd:TIGR02168  937 RIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-340 9.23e-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: 9.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 241
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 242 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 321
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170
                 ....*....|....*....
gi 578827628 322 LKVELKSFLEVLDGKIDDL 340
Cdd:COG1196  398 LAAQLEELEEAEEALLERL 416
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-314 1.38e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQESGR-ETPSSTQASSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 173
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETlEAEIEDLRETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 174 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 253
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578827628 254 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 314
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 162-314 8.06e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.43  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 241
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  242 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 306
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 578827628  307 SLKTDIEE 314
Cdd:pfam10174 486 ALQPELTE 493
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 180-340 7.05e-03

LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) functions as an adapter protein linking the Par polarity complex (composed of Par3, Par6 and protein kinase C iota) to the Gpsm1/Gpsm2 complex, and is involved in cell polarity and spindle orientation during mitosis. Par3 interacts with INSC which binds directly to Pins (partner of Insc, homolog of vertebrate LGN/Gpsm2 and AGS3/Gpsm1). Pins then associates with the heterotrimeric G proteins and NuMA, which interacts directly with the cell spindle to control the orientation of the spindle and the division plane of mitotic cells. INSC may regulate cell proliferation and differentiation in the developing nervous system, may play a role in the asymmetric division of fibroblasts, and may also participate in the process of stratification of the squamous epithelium. This model corresponds to the Leu-Gly-Asn Repeat-Enriched Protein (LGN)-binding domain (LBD) of INSC. It interacts with the tetratricopeptide repeat (TPR) motifs of LGN, also called G-protein-signaling modulator 2 (Gpsm2).


Pssm-ID: 439320 [Multi-domain]  Cd Length: 300  Bit Score: 38.01  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 180 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 254
Cdd:cd21966    5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 255 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 328
Cdd:cd21966   83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                        170
                 ....*....|..
gi 578827628 329 FLEVLDGKIDDL 340
Cdd:cd21966  163 LVDSLEEPTSEL 174
 
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 8.40e-77

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: 231.47  E-value: 8.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   3 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 578827628  83 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 111
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-107 5.92e-42

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: 141.83  E-value: 5.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   5 PIFTTRAHVFQIDPNtKKNWMPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837    1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                         90       100
                 ....*....|....*....|....*.
gi 578827628  82 anTVFGLGFSSEQQLTKFAEKFQEVK 107
Cdd:cd00837   80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-107 5.11e-40

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: 137.20  E-value: 5.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    4 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 578827628   82 AntVFGLGFSSEQQLTKFAEKFQEVK 107
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-105 4.13e-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: 105.52  E-value: 4.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628     1 MREQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 578827628    79 DsrANTVFGLGFSSEQQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-100 2.97e-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: 62.33  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   5 PIFTTRAHVFQIDPNTKKnWMPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207    1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                         90       100
                 ....*....|....*....|
gi 578827628  81 RanTVFGLGFSSEQQLTKFA 100
Cdd:cd01207   80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-333 2.78e-09

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: 58.53  E-value: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    93 EQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIA 172
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   173 LTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQ---- 248
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdies 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   249 LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKV 324
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*....
gi 578827628   325 ELKSFLEVL 333
Cdd:TIGR02168  937 RIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-327 7.25e-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: 54.29  E-value: 7.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   163 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINRE 242
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   243 ----KEKNTQLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 318
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832


                   ....*....
gi 578827628   319 QRHLKVELK 327
Cdd:TIGR02168  833 IAATERRLE 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 93-326 1.67e-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: 53.15  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    93 EQQLTKFAEKFQE-VKEAAKIAKDKTQ--EKIETSSNHSQESGRETPSSTQA--SSVNGTDDEKASHAGPANTHLK---S 164
Cdd:TIGR02169  250 EEELEKLTEEISElEKRLEEIEQLLEElnKKIKDLGEEEQLRVKEKIGELEAeiASLERSIAEKERELEDAEERLAkleA 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   165 ENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKE 244
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   245 KntqLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAER-------DNQNLEDKVRSLKTDIEESKY 317
Cdd:TIGR02169  410 R---LQEELQRLSEELADLNAAIAGIEAK---INELEEEKEDKALEIKKQEWkleqlaaDLSKYEQELYDLKEEYDRVEK 483


                   ....*....
gi 578827628   318 RQRHLKVEL 326
Cdd:TIGR02169  484 ELSKLQREL 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-353 4.85e-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: 51.60  E-value: 4.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQcseINR 241
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   242 EKEKNTQLKRRIEELEAELREKETElkdLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 321
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEE---AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 578827628   322 LKVELKSFLEVLDGKIDDLHDFRRGLSKLGTD 353
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 186-351 7.64e-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: 51.22  E-value: 7.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   186 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCS-----EINREKEKNTQLKRRIEELEAEL 260
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   261 REKETELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKVELKSF 329
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 578827628   330 LEVLDGKIDDLHDFRRGLSKLG 351
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 186-334 8.27e-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: 50.84  E-value: 8.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   186 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKRRIEELEAELREKET 265
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEA 875

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578827628   266 ELKDLRKQSEIIpqlmseceyvSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 334
Cdd:TIGR02169  876 ALRDLESRLGDL----------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-340 9.23e-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: 9.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 241
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 242 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 321
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170
                 ....*....|....*....
gi 578827628 322 LKVELKSFLEVLDGKIDDL 340
Cdd:COG1196  398 LAAQLEELEEAEEALLERL 416
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
185-323 1.83e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.47  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 185 IELQTLRESNARLTTALQESAASVeqwkRQFSICRDENDRLRNKIDELEEQCSEInreKEKNTQLKRRIEELEAELRE-K 263
Cdd:COG2433  382 LEELIEKELPEEEPEAEREKEHEE----RELTEEEEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEaR 454

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 264 ETELKDLRKQSEIipqlmseceyvseklEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:COG2433  455 SEERREIRKDREI---------------SRLDREIERLERELEEERERIEELKRKLERLK 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
161-354 2.94e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  161 HLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRNKIDE 231
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  232 LEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 308
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578827628  309 KTDIEESKYRQRHLKVEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 354
Cdd:COG4913   772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-345 4.93e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  185 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKntQLKRRIEELEAELREKE 264
Cdd:COG4913   281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE--QLEREIERLERELEERE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  265 TELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGK 336
Cdd:COG4913   359 RRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSN 437

                         170
                  ....*....|
gi 578827628  337 ID-DLHDFRR 345
Cdd:COG4913   438 IPaRLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-314 5.43e-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: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTqsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKID----------- 230
Cdd:COG1196  218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 231 ELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 309
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                 ....*
gi 578827628 310 TDIEE 314
Cdd:COG1196  376 EAEEE 380
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-325 5.47e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 167 DKLKIALTQSAANVKKWEIELQTLRESNARLTTA------LQESAASVEQWKRQFSICRdENDRLRNKIDELEEQCSEIN 240
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELeaeleeLREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 241 REKEKNTQLKRRIEELEAELREKETELKDLRKQS-----EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES 315
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                        170
                 ....*....|
gi 578827628 316 KYRQRHLKVE 325
Cdd:COG4717  233 ENELEAAALE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 223-340 7.25e-06

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: 46.46  E-value: 7.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 223 DRLRNKIDELEEQCSEINREKEKN----TQLKRRIEELEAELREKETELKDLRKQ----SEIIPQLMSECEY--VSEKLE 292
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYeaLQKEIE 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578827628 293 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDL 340
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-314 1.38e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQESGR-ETPSSTQASSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 173
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETlEAEIEDLRETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 174 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 253
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578827628 254 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 314
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 219-349 1.85e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   219 RDENDRLRNKIDELEEQCS----EINREKEKNTQLKRRIEELEAELREKETEL----KDLRKQSEIIPQLMSECEYVSEK 290
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   291 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVEL-KSFLEVLDGKIDDLHDFRRGLSK 349
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 225-351 2.48e-05

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 45.49  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 225 LRNKIDELEEQCSEINREKEKntqLKRRIEELEAELREKETELKDLRKQSEIIpqlmseceyvsekleaaERDNQNLEDK 304
Cdd:COG4026  133 LREELLELKEKIDEIAKEKEK---LTKENEELESELEELREEYKKLREENSIL-----------------EEEFDNIKSE 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 578827628 305 VRSLKTDIEESKyRQRHLKV-ELKS-FLEVLDGKIDDLHDFRRGLSKLG 351
Cdd:COG4026  193 YSDLKSRFEELL-KKRLLEVfSLEElWKELFPEELPEEDFIYFATENLK 240
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-299 4.31e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 160 THLKSENDKLKIALtQSAANVKKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI 239
Cdd:COG4717  112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 240 NREKEKntQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 299
Cdd:COG4717  190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
184-275 4.68e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 184 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDEL-EEQCSEINREKEKnTQLKRRIEELEAELRE 262
Cdd:COG2433  405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREI-SRLDREIERLERELEE 483

                         90
                 ....*....|...
gi 578827628 263 KETELKDLRKQSE 275
Cdd:COG2433  484 ERERIEELKRKLE 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-347 6.17e-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: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  186 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLR-----NKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 260
Cdd:COG4913   243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDAL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  261 REKETELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKID 338
Cdd:COG4913   322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                  ....*....
gi 578827628  339 DLHDFRRGL 347
Cdd:COG4913   402 ALEEALAEA 410
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 223-314 7.70e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.69  E-value: 7.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 223 DRLRNKIDELEEQCSEInrEKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 302
Cdd:COG0542  414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                         90
                 ....*....|..
gi 578827628 303 DKVRSLKTDIEE 314
Cdd:COG0542  492 KELAELEEELAE 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 219-350 7.75e-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: 44.66  E-value: 7.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   219 RDENDRLRNKIDELEEQCSEINRE-KEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 297
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578827628   298 NQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 162-314 8.06e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.43  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 241
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  242 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 306
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 578827628  307 SLKTDIEE 314
Cdd:pfam10174 486 ALQPELTE 493
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
213-340 8.61e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 8.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 213 RQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLmseceyvsEKLE 292
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578827628 293 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKvELKSFLEVLDGKIDDL 340
Cdd:COG4717  136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-334 1.05e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   186 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKET 265
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578827628   266 ELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 334
Cdd:TIGR02168  366 ELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 241-340 1.16e-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: 44.29  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   241 REKEKNTQLKRRIEELEaelREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 320
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 578827628   321 HLKVEL---KSFLEVLDGKIDDL 340
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 164-340 1.37e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  164 SENDKLKIALTQSAANVKKweiELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEeqcSEINREK 243
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKK---ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  244 EKNTQLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481

                         170
                  ....*....|....*..
gi 578827628  324 VELKSFLEVLDGKIDDL 340
Cdd:TIGR04523 482 QNLEQKQKELKSKEKEL 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
217-323 1.46e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 217 ICRDEN--DRLRNKIDELEEQCSEINrekekntQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAA 294
Cdd:PRK03918 185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                         90       100
                 ....*....|....*....|....*....
gi 578827628 295 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK 286
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
184-350 1.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 184 EIELQTLRESNARLTTALQEsaasveqwkRQFSICRDENDRLR------NKIDELEEQCSEINREKEKNTQLKRRIEELE 257
Cdd:PRK03918 562 EKKLDELEEELAELLKELEE---------LGFESVEELEERLKelepfyNEYLELKDAEKELEREEKELKKLEEELDKAF 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 258 AELREKETELKDLRKQSEIIPQLMSECEY--VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSF------ 329
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekakke 712

                        170       180
                 ....*....|....*....|.
gi 578827628 330 LEVLDGKIDDLHDFRRGLSKL 350
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKY 733
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
162-349 1.58e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTQsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 241
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 242 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 314
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578827628 315 SKYRQ-RHLKVELKSFLEVLDGKIDDLHDFRRGLSK 349
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
181-314 2.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 181 KKWEIELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRNKIDELEeqcSEINREKEKNTQLKRRIEELEAEL 260
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578827628 261 REKETELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEE 314
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKE 739
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
211-323 2.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 211 WKRQFSICRDENDRLRNKIDEL--EEQCSEINREKEKN-TQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYV 287
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 578827628 288 SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
PLN02939 PLN02939
transferase, transferring glycosyl groups
 164-326 2.41e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 164 SENDKLKIALTQSAANVKKWEIELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREK 243
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 244 EKNTQLKRRIEELEAELREKETEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLEDKVRSL 308
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKL 336

                        170
                 ....*....|....*....
gi 578827628 309 KTDIEESK-YRQRHLKVEL 326
Cdd:PLN02939 337 EASLKEANvSKFSSYKVEL 355
PTZ00121 PTZ00121
MAEBL; Provisional
 101-336 2.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANV 180
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  181 KKWEIElqtlRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 260
Cdd:PTZ00121 1626 KKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578827628  261 REKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGK 336
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
PRK12704 PRK12704
phosphodiesterase; Provisional
 229-333 2.87e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 229 IDELEEQCSEINREK--EKNTQLKRRIEELEAELREKETELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNLEDKVR 306
Cdd:PRK12704  44 LEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEELEKKEK 117

                         90       100
                 ....*....|....*....|....*..
gi 578827628 307 SLKTDIEESKYRQRHLKVELKSFLEVL 333
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQEL 144
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 191-345 4.27e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   191 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKI-DELEEQCSEINREKEkntQLKRRIEELEAELREKETELKD 269
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAeDDLQALESELREQLE---AGKLEFNEEEYRLKSRLGELKL 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   270 LRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES--KYRQRHLKVE-----LKSFLEVLDG 335
Cdd:pfam12128  452 RLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQAseALRQASRRLEerqsaLDELELQLFP 531

                          170
                   ....*....|
gi 578827628   336 KIDDLHDFRR 345
Cdd:pfam12128  532 QAGTLLHFLR 541
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 106-340 4.33e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   106 VKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTddEKASHAGPANTHLKSEndkLKIALTQSAANVKKWEI 185
Cdd:pfam15921  243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLT--EKASSARSQANSIQSQ---LEIIQEQARNQNSMYMR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   186 ELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE------------------NDRLRNKIDELEEQCSEINREK 243
Cdd:pfam15921  318 QLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterdqfsqesgnlDDQLQKLLADLHKREKELSLEK 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   244 EKNTQLKRR-------IEELEAELREKETELKDLRKqseIIPQLMSECE-YVSEKLEAAERDNQNLEdKVRSLKTDIEES 315
Cdd:pfam15921  398 EQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQgQMERQMAAIQGKNESLE-KVSSLTAQLEST 473

                          250       260
                   ....*....|....*....|....*...
gi 578827628   316 KYRQRHLKVEL---KSFLEVLDGKIDDL 340
Cdd:pfam15921  474 KEMLRKVVEELtakKMTLESSERTVSDL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
201-350 4.62e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 201 LQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQL 280
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 281 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
223-326 5.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  223 DRLRNKIDELEEQCSEINREKEKNTQLKRRIEE--------------------LEAELREKETELKDLRKQSEIIPQLMS 282
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeidvasAEREIAELEAELERLDASSDDLAALEE 692

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 578827628  283 ECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVEL 326
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-308 1.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 184 EIELQTLRESNARL-TTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNT--QLKRRIEELEAEL 260
Cdd:COG4717  362 ELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEEL 441

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578827628 261 REKETELKDLRKQSEIIPQLMSECEyVSEKLEAAERDNQNLEDKVRSL 308
Cdd:COG4717  442 EELEEELEELREELAELEAELEQLE-EDGELAELLQELEELKAELREL 488
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 172-350 1.21e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 172 ALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKR 251
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 252 RIEELEAELREKETELKDLRKQSeiipQLMSECEYV-----SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHL---K 323
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRAL----YRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalR 166

                        170       180
                 ....*....|....*....|....*..
gi 578827628 324 VELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEAL 193
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 177-323 1.39e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   177 AANVKKWEIELQTLRESNARLTTaLQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR---------EKEKNT 247
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaaHIKAVT 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578827628   248 QLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLE---AAERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
224-316 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 224 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL-------------REKETELKDLRKQSEI--IPQLMSECEYVS 288
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerhelyeeaKAKKEELERLKKRLTGltPEKLEKELEELE 397

                         90       100
                 ....*....|....*....|....*...
gi 578827628 289 EKLEAAERDNQNLEDKVRSLKTDIEESK 316
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELK 425
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
149-314 2.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 149 DEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNK 228
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 229 IDELEEQcseINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 308
Cdd:COG4372   82 LEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKEL 155


                 ....*.
gi 578827628 309 KTDIEE 314
Cdd:COG4372  156 EEQLES 161
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
249-333 2.21e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 249 LKRRIEELEAELREKETELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 328
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                 ....*
gi 578827628 329 FLEVL 333
Cdd:COG3206  252 GPDAL 256
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-314 2.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 150 EKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKI 229
Cdd:COG1196  344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 230 DELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSeiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLK 309
Cdd:COG1196  424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL----------LEEAALLEAALAELLEELAEAAARL 493


                 ....*
gi 578827628 310 TDIEE 314
Cdd:COG1196  494 LLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-314 2.65e-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: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628    93 EQQLTKFAEKFQEVKEAAKIAKDK-TQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPAnTHLKSENDKLKI 171
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628   172 ALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWkrqfsicRDENDRLRNKIDELEEQCSEINREKEKntqLKR 251
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEG---LEV 936

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578827628   252 RIEELEAELREketelkdlrkqseiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 314
Cdd:TIGR02168  937 RIDNLQERLSE----------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
229-336 2.73e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 229 IDELEEQCSEINREKEKntQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSL 308
Cdd:PRK03918 505 LKELEEKLKKYNLEELE--KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582

                         90       100
                 ....*....|....*....|....*....
gi 578827628 309 K-TDIEESKYRQRHLKVELKSFLEVLDGK 336
Cdd:PRK03918 583 GfESVEELEERLKELEPFYNEYLELKDAE 611
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 149-328 3.04e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  149 DEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFS------------ 216
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvtefeattcs 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  217 ---ICRDENDRLRNKIDELEEQCSEINR---EKEKNTQLKR----RIEELEAELREKETELKDLRKQSEIIPQLMSECEY 286
Cdd:pfam05483 361 leeLLRTEQQRLEKNEDQLKIITMELQKkssELEEMTKFKNnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQE 440

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578827628  287 VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 328
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
181-333 3.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 181 KKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 260
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578827628 261 REKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKVELKSFLEVL 333
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
PRK01156 PRK01156
chromosome segregation protein; Provisional
 223-353 3.47e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 223 DRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKE-------TELKDLRKQSEIIPQLMSECEYVSEKLEAAE 295
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578827628 296 RDNQNLEDKVRSLKTDIEESKYRQRHLKVE----------LKSFLEVLDGKIDDLHDFRRGLSKLGTD 353
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKD 337
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 163-344 3.67e-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: 39.11  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  163 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI-NR 241
Cdd:pfam07888  65 KRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLtQR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  242 EKEKNTQLKR---RIEELEAELREKETELKDLR-------------------------KQSEIIPQLMSECEYVSEKLEA 293
Cdd:pfam07888 145 VLERETELERmkeRAKKAGAQRKEEEAERKQLQaklqqteeelrslskefqelrnslaQRDTQVLQLQDTITTLTQKLTT 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578827628  294 AER---DNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFR 344
Cdd:pfam07888 225 AHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 185-349 4.26e-03

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: 38.37  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 185 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIE---------- 254
Cdd:COG1579   10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnk 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 255 ELEAELREKETELKDLRKQSEIIPQLMseceyvsEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKVELKSFLEVLD 334
Cdd:COG1579   90 EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELE 155

                        170
                 ....*....|....*
gi 578827628 335 GKIDDLHDFRRGLSK 349
Cdd:COG1579  156 AELEELEAEREELAA 170
PRK01156 PRK01156
chromosome segregation protein; Provisional
 220-351 4.38e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 220 DENDRLRNKIDELEEQcsEINREKekntqLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQ 299
Cdd:PRK01156 626 NEANNLNNKYNEIQEN--KILIEK-----LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578827628 300 NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGKIDDLHDFRRGLSKLG 351
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLREAFDKSG 749
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 219-312 4.42e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 37.88  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  219 RDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKETELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 297
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 578827628  298 NQNLEDKVRSLKTDI 312
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
224-349 5.46e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 224 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRkqseiipqlmSECEYVSEKLEAAERDNQNLED 303
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE----------AEIEDLRETIAETEREREELAE 279

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578827628 304 KVRSLKTDIEESKYRQRHLKVElksfLEVLDGKIDDLHDFRRGLSK 349
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAE----AGLDDADAEAVEARREELED 321
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-318 6.20e-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: 38.21  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQE-----------SAASVEQWKRQFSI-------CRDEND 223
Cdd:COG4942   74 LEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYlkylapaRREQAE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 224 RLRNKIDELEEQCSEINREKEkntqlkrRIEELEAELREKETELKDLRK-QSEIIPQLMSECEYVSEKLEAAERDNQNLE 302
Cdd:COG4942  154 ELRADLAELAALRAELEAERA-------ELEALLAELEEERAALEALKAeRQKLLARLEKELAELAAELAELQQEAEELE 226

                        170
                 ....*....|....*.
gi 578827628 303 DKVRSLKTDIEESKYR 318
Cdd:COG4942  227 ALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
162-279 6.49e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628  162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES-AASVEQWKRQFSICRDENDRLRNKIDELEEQC---- 236
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLaalg 372

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578827628  237 -------------------------SEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQ 279
Cdd:COG4913   373 lplpasaeefaalraeaaallealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 225-330 6.72e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 38.13  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 225 LRNKIDELEEQCSeiNREKEKNTQlkrRIEELEAELREKETELKDLRKQ----SEIIPQLMSEceyvsekleaaERDNQN 300
Cdd:PRK05431   7 IRENPEAVKEALA--KRGFPLDVD---ELLELDEERRELQTELEELQAErnalSKEIGQAKRK-----------GEDAEA 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 578827628 301 LEDKVRSLKTDIEESKYRQRHLKVELKSFL 330
Cdd:PRK05431  71 LIAEVKELKEEIKALEAELDELEAELEELL 100
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-351 6.86e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 221 ENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKqsEIIPQLMSECEYVSEKLEAAER-DNQ 299
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK--ELEELGFESVEELEERLKELEPfYNE 603

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578827628 300 NLEdkVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKLG 351
Cdd:PRK03918 604 YLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 180-340 7.05e-03

LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) functions as an adapter protein linking the Par polarity complex (composed of Par3, Par6 and protein kinase C iota) to the Gpsm1/Gpsm2 complex, and is involved in cell polarity and spindle orientation during mitosis. Par3 interacts with INSC which binds directly to Pins (partner of Insc, homolog of vertebrate LGN/Gpsm2 and AGS3/Gpsm1). Pins then associates with the heterotrimeric G proteins and NuMA, which interacts directly with the cell spindle to control the orientation of the spindle and the division plane of mitotic cells. INSC may regulate cell proliferation and differentiation in the developing nervous system, may play a role in the asymmetric division of fibroblasts, and may also participate in the process of stratification of the squamous epithelium. This model corresponds to the Leu-Gly-Asn Repeat-Enriched Protein (LGN)-binding domain (LBD) of INSC. It interacts with the tetratricopeptide repeat (TPR) motifs of LGN, also called G-protein-signaling modulator 2 (Gpsm2).


Pssm-ID: 439320 [Multi-domain]  Cd Length: 300  Bit Score: 38.01  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 180 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 254
Cdd:cd21966    5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 255 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 328
Cdd:cd21966   83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                        170
                 ....*....|..
gi 578827628 329 FLEVLDGKIDDL 340
Cdd:cd21966  163 LVDSLEEPTSEL 174
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-314 8.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 241
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 242 EKEKNTQLKRRIEELE-----------------AELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDK 304
Cdd:PRK03918 274 EIEELEEKVKELKELKekaeeyiklsefyeeylDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353

                        170
                 ....*....|
gi 578827628 305 VRSLKTDIEE 314
Cdd:PRK03918 354 LEELEERHEL 363
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-350 8.51e-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: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 162 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 241
Cdd:COG4942   32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827628 242 EKEKN---------------TQLKRRIEELEAELREKETELKDLRKQSEIIPQLmseceyvSEKLEAAERDNQNLEDKVR 306
Cdd:COG4942  112 ALYRLgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------RAELEAERAELEALLAELE 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578827628 307 SLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:COG4942  185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
 
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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