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Conserved domains on  [gi|767985825|ref|XP_011520535|]
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homer protein homolog 2 isoform X2 [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, ...
 11-119 4.95e-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: 232.24  E-value: 4.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  11 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 90
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 767985825  91 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 119
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-341 1.50e-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: 59.69  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   101 EQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIA 180
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   181 LTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQ---- 256
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdies 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   257 LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKV 332
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*....
gi 767985825   333 ELKSFLEVL 341
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, ...
 11-119 4.95e-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: 232.24  E-value: 4.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  11 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 90
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 767985825  91 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 119
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 12-115 4.70e-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: 4.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   12 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 89
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 767985825   90 AntVFGLGFSSEQQLTKFAEKFQEVK 115
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 11-113 1.41e-27

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: 104.36  E-value: 1.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825    11 EQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWADs 88
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 767985825    89 rANTVFGLGFSSEQQLTKFAEKFQE 113
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-341 1.50e-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: 59.69  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   101 EQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIA 180
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   181 LTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQ---- 256
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdies 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   257 LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKV 332
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*....
gi 767985825   333 ELKSFLEVL 341
Cdd:TIGR02168  937 RIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-348 6.49e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 249
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 250 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 329
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170
                 ....*....|....*....
gi 767985825 330 LKVELKSFLEVLDGKIDDL 348
Cdd:COG1196  398 LAAQLEELEEAEEALLERL 416
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
109-322 7.60e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 109 EKFQEVKEAAKIAKDKTQEKIETSSNHSQESGR-ETPSSTQASSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 181
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETlEAEIEDLRETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 182 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 261
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767985825 262 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 322
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 ...
 170-322 3.02e-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: 45.97  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 249
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  250 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 314
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 767985825  315 SLKTDIEE 322
Cdd:pfam10174 486 ALQPELTE 493
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 188-348 4.27e-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: 38.39  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 188 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 262
Cdd:cd21966    5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 263 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 336
Cdd:cd21966   83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                        170
                 ....*....|..
gi 767985825 337 FLEVLDGKIDDL 348
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, ...
 11-119 4.95e-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: 232.24  E-value: 4.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  11 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 90
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 767985825  91 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 119
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 13-115 6.29e-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: 6.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  13 PIFTTRAHVFQIDPNtKKNWMPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 89
Cdd:cd00837    1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                         90       100
                 ....*....|....*....|....*.
gi 767985825  90 anTVFGLGFSSEQQLTKFAEKFQEVK 115
Cdd:cd00837   80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 12-115 4.70e-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: 4.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   12 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 89
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 767985825   90 AntVFGLGFSSEQQLTKFAEKFQEVK 115
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 11-113 1.41e-27

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: 104.36  E-value: 1.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825    11 EQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWADs 88
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 767985825    89 rANTVFGLGFSSEQQLTKFAEKFQE 113
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 13-108 3.12e-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: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  13 PIFTTRAHVFQIDPNTKKnWMPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 88
Cdd:cd01207    1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                         90       100
                 ....*....|....*....|
gi 767985825  89 RanTVFGLGFSSEQQLTKFA 108
Cdd:cd01207   80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-341 1.50e-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: 59.69  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   101 EQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIA 180
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   181 LTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQ---- 256
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdies 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   257 LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKV 332
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*....
gi 767985825   333 ELKSFLEVL 341
Cdd:TIGR02168  937 RIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-335 4.07e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   171 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINRE 250
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   251 ----KEKNTQLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 326
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832


                   ....*....
gi 767985825   327 QRHLKVELK 335
Cdd:TIGR02168  833 IAATERRLE 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-334 6.94e-08

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: 54.30  E-value: 6.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   101 EQQLTKFAEKFQE-VKEAAKIAKDKTQ--EKIETSSNHSQESGRETPSSTQA--SSVNGTDDEKASHAGPANTHLK---S 172
Cdd:TIGR02169  250 EEELEKLTEEISElEKRLEEIEQLLEElnKKIKDLGEEEQLRVKEKIGELEAeiASLERSIAEKERELEDAEERLAkleA 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   173 ENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKE 252
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   253 KntqLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAER-------DNQNLEDKVRSLKTDIEESKY 325
Cdd:TIGR02169  410 R---LQEELQRLSEELADLNAAIAGIEAK---INELEEEKEDKALEIKKQEWkleqlaaDLSKYEQELYDLKEEYDRVEK 483


                   ....*....
gi 767985825   326 RQRHLKVEL 334
Cdd:TIGR02169  484 ELSKLQREL 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-361 2.76e-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: 52.37  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQcseINR 249
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   250 EKEKNTQLKRRIEELEAELREKETElkdLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 329
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEE---AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 767985825   330 LKVELKSFLEVLDGKIDDLHDFRRGLSKLGTD 361
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 194-359 3.78e-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: 51.99  E-value: 3.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   194 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCS-----EINREKEKNTQLKRRIEELEAEL 268
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   269 REKETELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKVELKSF 337
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 767985825   338 LEVLDGKIDDLHDFRRGLSKLG 359
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 194-342 4.88e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 4.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   194 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKRRIEELEAELREKET 273
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEA 875

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985825   274 ELKDLRKQSEIIpqlmseceyvSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 342
Cdd:TIGR02169  876 ALRDLESRLGDL----------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-348 6.49e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 249
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 250 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 329
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170
                 ....*....|....*....
gi 767985825 330 LKVELKSFLEVLDGKIDDL 348
Cdd:COG1196  398 LAAQLEELEEAEEALLERL 416
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
193-331 1.50e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.86  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 193 IELQTLRESNARLTTALQESAASVeqwkRQFSICRDENDRLRNKIDELEEQCSEInreKEKNTQLKRRIEELEAELRE-K 271
Cdd:COG2433  382 LEELIEKELPEEEPEAEREKEHEE----RELTEEEEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEaR 454

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 272 ETELKDLRKQSEIipqlmseceyvseklEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 331
Cdd:COG2433  455 SEERREIRKDREI---------------SRLDREIERLERELEEERERIEELKRKLERLK 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
169-362 1.99e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  169 HLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRNKIDE 239
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  240 LEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 316
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767985825  317 KTDIEESKYRQRHLKVEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 362
Cdd:COG4913   772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
175-333 2.51e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 175 DKLKIALTQSAANVKKWEIELQTLRESNARLTTA------LQESAASVEQWKRQFSICRdENDRLRNKIDELEEQCSEIN 248
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELeaeleeLREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 249 REKEKNTQLKRRIEELEAELREKETELKDLRKQS-----EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES 323
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                        170
                 ....*....|
gi 767985825 324 KYRQRHLKVE 333
Cdd:COG4717  233 ENELEAAALE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 231-348 3.05e-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: 47.61  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 231 DRLRNKIDELEEQCSEINREKEKN----TQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSEC----EY--VSEKLE 300
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEYeaLQKEIE 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767985825 301 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDL 348
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
193-353 3.68e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  193 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKntQLKRRIEELEAELREKE 272
Cdd:COG4913   281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE--QLEREIERLERELEERE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  273 TELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGK 344
Cdd:COG4913   359 RRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSN 437

                         170
                  ....*....|
gi 767985825  345 ID-DLHDFRR 353
Cdd:COG4913   438 IPaRLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-322 3.74e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTqsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKID----------- 238
Cdd:COG1196  218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 239 ELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 317
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                 ....*
gi 767985825 318 TDIEE 322
Cdd:COG1196  376 EAEEE 380
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
109-322 7.60e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 109 EKFQEVKEAAKIAKDKTQEKIETSSNHSQESGR-ETPSSTQASSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 181
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETlEAEIEDLRETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 182 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 261
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767985825 262 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 322
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 227-357 1.05e-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: 47.37  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   227 RDENDRLRNKIDELEEQCS----EINREKEKNTQLKRRIEELEAELREKETEL----KDLRKQSEIIPQLMSECEYVSEK 298
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   299 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVEL-KSFLEVLDGKIDDLHDFRRGLSK 357
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 233-359 1.19e-05

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 46.26  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 233 LRNKIDELEEQCSEINREKEKntqLKRRIEELEAELREKETELKDLRKQSEIIpqlmseceyvsekleaaERDNQNLEDK 312
Cdd:COG4026  133 LREELLELKEKIDEIAKEKEK---LTKENEELESELEELREEYKKLREENSIL-----------------EEEFDNIKSE 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767985825 313 VRSLKTDIEESKyRQRHLKV-ELKS-FLEVLDGKIDDLHDFRRGLSKLG 359
Cdd:COG4026  193 YSDLKSRFEELL-KKRLLEVfSLEElWKELFPEELPEEDFIYFATENLK 240
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
168-307 2.04e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 168 THLKSENDKLKIALtQSAANVKKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI 247
Cdd:COG4717  112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 248 NREKEKntQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 307
Cdd:COG4717  190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 172-348 2.65e-05

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: 46.17  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  172 SENDKLKIALTQSAANVKKweiELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEeqcSEINREK 251
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKK---ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  252 EKNTQLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 331
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481

                         170
                  ....*....|....*..
gi 767985825  332 VELKSFLEVLDGKIDDL 348
Cdd:TIGR04523 482 QNLEQKQKELKSKEKEL 498
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 170-322 3.02e-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: 45.97  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 249
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  250 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 314
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 767985825  315 SLKTDIEE 322
Cdd:pfam10174 486 ALQPELTE 493
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
192-283 4.25e-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: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 192 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDEL-EEQCSEINREKEKnTQLKRRIEELEAELRE 270
Cdd:COG2433  405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREI-SRLDREIERLERELEE 483

                         90
                 ....*....|...
gi 767985825 271 KETELKDLRKQSE 283
Cdd:COG2433  484 ERERIEELKRKLE 496
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
221-348 4.70e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 221 RQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLmseceyvsEKLE 300
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767985825 301 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKvELKSFLEVLDGKIDDL 348
Cdd:COG4717  136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
194-355 4.75e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  194 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLR-----NKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 268
Cdd:COG4913   243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDAL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  269 REKETELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKID 346
Cdd:COG4913   322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                  ....*....
gi 767985825  347 DLHDFRRGL 355
Cdd:COG4913   402 ALEEALAEA 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 227-358 4.97e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 4.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   227 RDENDRLRNKIDELEEQCSEINRE-KEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 305
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767985825   306 NQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 358
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-358 6.30e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 192 EIELQTLRESNARLTTALQEsaasveqwkRQFSICRDENDRLR------NKIDELEEQCSEINREKEKNTQLKRRIEELE 265
Cdd:PRK03918 562 EKKLDELEEELAELLKELEE---------LGFESVEELEERLKelepfyNEYLELKDAEKELEREEKELKKLEEELDKAF 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 266 AELREKETELKDLRKQSEIIPQLMSECEY--VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSF------ 337
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekakke 712

                        170       180
                 ....*....|....*....|.
gi 767985825 338 LEVLDGKIDDLHDFRRGLSKL 358
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKY 733
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 249-348 6.91e-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: 45.06  E-value: 6.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   249 REKEKNTQLKRRIEELEaelREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 328
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 767985825   329 HLKVEL---KSFLEVLDGKIDDL 348
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-342 6.92e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 6.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   194 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKET 273
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985825   274 ELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 342
Cdd:TIGR02168  366 ELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 231-322 7.18e-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: 7.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 231 DRLRNKIDELEEQCSEInrEKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 310
Cdd:COG0542  414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                         90
                 ....*....|..
gi 767985825 311 DKVRSLKTDIEE 322
Cdd:COG0542  492 KELAELEEELAE 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
225-331 7.31e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 225 ICRDEN--DRLRNKIDELEEQCSEINrekekntQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAA 302
Cdd:PRK03918 185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                         90       100
                 ....*....|....*....|....*....
gi 767985825 303 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 331
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK 286
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
189-322 9.01e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 189 KKWEIELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRNKIDELEeqcSEINREKEKNTQLKRRIEELEAEL 268
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767985825 269 REKETELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEE 322
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKE 739
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-357 9.41e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 9.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 249
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 250 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 322
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767985825 323 SKYRQ-RHLKVELKSFLEVLDGKIDDLHDFRRGLSK 357
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-331 1.08e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 219 WKRQFSICRDENDRLRNKIDEL--EEQCSEINREKEKN-TQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYV 295
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767985825 296 SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 331
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 114-348 1.22e-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: 43.95  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   114 VKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTddEKASHAGPANTHLKSEndkLKIALTQSAANVKKWEI 193
Cdd:pfam15921  243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLT--EKASSARSQANSIQSQ---LEIIQEQARNQNSMYMR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   194 ELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE------------------NDRLRNKIDELEEQCSEINREK 251
Cdd:pfam15921  318 QLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterdqfsqesgnlDDQLQKLLADLHKREKELSLEK 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   252 EKNTQLKRR-------IEELEAELREKETELKDLRKqseIIPQLMSECE-YVSEKLEAAERDNQNLEdKVRSLKTDIEES 323
Cdd:pfam15921  398 EQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQgQMERQMAAIQGKNESLE-KVSSLTAQLEST 473

                          250       260
                   ....*....|....*....|....*...
gi 767985825   324 KYRQRHLKVEL---KSFLEVLDGKIDDL 348
Cdd:pfam15921  474 KEMLRKVVEELtakKMTLESSERTVSDL 501
PTZ00121 PTZ00121
MAEBL; Provisional
 109-344 1.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  109 EKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANV 188
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  189 KKWEIElqtlRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 268
Cdd:PTZ00121 1626 KKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767985825  269 REKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGK 344
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
PLN02939 PLN02939
transferase, transferring glycosyl groups
 172-334 1.95e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.35  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 172 SENDKLKIALTQSAANVKKWEIELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREK 251
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 252 EKNTQLKRRIEELEAELREKETEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLEDKVRSL 316
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKL 336

                        170
                 ....*....|....*....
gi 767985825 317 KTDIEESK-YRQRHLKVEL 334
Cdd:PLN02939 337 EASLKEANvSKFSSYKVEL 355
PRK12704 PRK12704
phosphodiesterase; Provisional
 237-341 2.29e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 237 IDELEEQCSEINREK--EKNTQLKRRIEELEAELREKETELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNLEDKVR 314
Cdd:PRK12704  44 LEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEELEKKEK 117

                         90       100
                 ....*....|....*....|....*..
gi 767985825 315 SLKTDIEESKYRQRHLKVELKSFLEVL 341
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQEL 144
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 199-353 2.64e-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: 42.90  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   199 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKI-DELEEQCSEINREKEkntQLKRRIEELEAELREKETELKD 277
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAeDDLQALESELREQLE---AGKLEFNEEEYRLKSRLGELKL 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   278 LRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES--KYRQRHLKVE-----LKSFLEVLDG 343
Cdd:pfam12128  452 RLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQAseALRQASRRLEerqsaLDELELQLFP 531

                          170
                   ....*....|
gi 767985825   344 KIDDLHDFRR 353
Cdd:pfam12128  532 QAGTLLHFLR 541
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
209-358 2.73e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 209 LQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQL 288
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 289 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 358
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
157-322 3.38e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 157 DEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNK 236
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 237 IDELEEQcseINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 316
Cdd:COG4372   82 LEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKEL 155


                 ....*.
gi 767985825 317 KTDIEE 322
Cdd:COG4372  156 EEQLES 161
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
231-334 4.37e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  231 DRLRNKIDELEEQCSEINREKEKNTQLKRRIEE--------------------LEAELREKETELKDLRKQSEIIPQLMS 290
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeidvasAEREIAELEAELERLDASSDDLAALEE 692

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767985825  291 ECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVEL 334
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 185-355 5.12e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   185 AANVKKWEIELQTLRESNARLTTaLQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR---------EKEKNT 255
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaaHIKAVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   256 QLKRRIEELEAELREKETEL--------------KDLRKQSEIIPQLMSECEYVS-----EKLEAAERDNQ-NLEDKVRS 315
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRakllmkraahvkqqSSIEEQRRLLQTLHSQEIHIRdahevATSIREISCQQhTLTQHIHT 383

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 767985825   316 LKTDIEESKYRQRHLKvELKSFLEVLDGKIDDLHDFRRGL 355
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLC-KELDILQREQATIDTRTSAFRDL 422
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
192-316 5.73e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 192 EIELQTLRESNARL-TTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNT--QLKRRIEELEAEL 268
Cdd:COG4717  362 ELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEEL 441

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767985825 269 REKETELKDLRKQSEIIPQLMSECEyVSEKLEAAERDNQNLEDKVRSL 316
Cdd:COG4717  442 EELEEELEELREELAELEAELEQLE-EDGELAELLQELEELKAELREL 488
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
232-324 6.92e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 232 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL-------------REKETELKDLRKQSEI--IPQLMSECEYVS 296
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerhelyeeaKAKKEELERLKKRLTGltPEKLEKELEELE 397

                         90       100
                 ....*....|....*....|....*...
gi 767985825 297 EKLEAAERDNQNLEDKVRSLKTDIEESK 324
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELK 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 180-358 8.89e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 8.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 180 ALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKR 259
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 260 RIEELEAELREKETELKDLRKQSeiipQLMSECEYV-----SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHL---K 331
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRAL----YRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalR 166

                        170       180
                 ....*....|....*....|....*..
gi 767985825 332 VELKSFLEVLDGKIDDLHDFRRGLSKL 358
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEAL 193
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 157-336 8.93e-04

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: 41.25  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  157 DEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLT----TALQES-----AASVEQWKRQFSIC- 226
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTeekeAQMEELnkakaAHSFVVTEFEATTCs 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  227 -----RDENDRLRNKIDELEEQCSEINR---EKEKNTQLKR----RIEELEAELREKETELKDLRKQSEIIPQLMSECEY 294
Cdd:pfam05483 361 leellRTEQQRLEKNEDQLKIITMELQKkssELEEMTKFKNnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQE 440

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767985825  295 VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 336
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-322 1.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   101 EQQLTKFAEKFQEVKEAAKIAKDK-TQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPAnTHLKSENDKLKI 179
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   180 ALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWkrqfsicRDENDRLRNKIDELEEQCSEINREKEKntqLKR 259
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEG---LEV 936

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767985825   260 RIEELEAELREketelkdlrkqseiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 322
Cdd:TIGR02168  937 RIDNLQERLSE----------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
237-344 1.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 237 IDELEEQCSEINREKEKntQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSL 316
Cdd:PRK03918 505 LKELEEKLKKYNLEELE--KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582

                         90       100
                 ....*....|....*....|....*....
gi 767985825 317 K-TDIEESKYRQRHLKVELKSFLEVLDGK 344
Cdd:PRK03918 583 GfESVEELEERLKELEPFYNEYLELKDAE 611
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
257-341 1.65e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 257 LKRRIEELEAELREKETELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 336
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                 ....*
gi 767985825 337 FLEVL 341
Cdd:COG3206  252 GPDAL 256
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
189-341 1.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 189 KKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 268
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767985825 269 REKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKVELKSFLEVL 341
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 171-352 1.66e-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: 40.26  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  171 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEIN-R 249
Cdd:pfam07888  65 KRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTqR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  250 EKEKNTQLKR---RIEELEAELREKETELKDLR-------------------------KQSEIIPQLMSECEYVSEKLEA 301
Cdd:pfam07888 145 VLERETELERmkeRAKKAGAQRKEEEAERKQLQaklqqteeelrslskefqelrnslaQRDTQVLQLQDTITTLTQKLTT 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767985825  302 AER---DNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFR 352
Cdd:pfam07888 225 AHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278
PRK01156 PRK01156
chromosome segregation protein; Provisional
 231-361 1.83e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 231 DRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKE-------TELKDLRKQSEIIPQLMSECEYVSEKLEAAE 303
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767985825 304 RDNQNLEDKVRSLKTDIEESKYRQRHLKVE----------LKSFLEVLDGKIDDLHDFRRGLSKLGTD 361
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKD 337
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-322 1.87e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 158 EKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKI 237
Cdd:COG1196  344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 238 DELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSeiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLK 317
Cdd:COG1196  424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL----------LEEAALLEAALAELLEELAEAAARL 493


                 ....*
gi 767985825 318 TDIEE 322
Cdd:COG1196  494 LLLLE 498
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 193-357 1.98e-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: 39.14  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 193 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIE---------- 262
Cdd:COG1579   10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnk 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 263 ELEAELREKETELKDLRKQSEIIPQLMseceyvsEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKVELKSFLEVLD 342
Cdd:COG1579   90 EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELE 155

                        170
                 ....*....|....*
gi 767985825 343 GKIDDLHDFRRGLSK 357
Cdd:COG1579  156 AELEELEAEREELAA 170
PRK01156 PRK01156
chromosome segregation protein; Provisional
 228-359 2.21e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 228 DENDRLRNKIDELEEQcsEINREKekntqLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQ 307
Cdd:PRK01156 626 NEANNLNNKYNEIQEN--KILIEK-----LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767985825 308 NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGKIDDLHDFRRGLSKLG 359
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLREAFDKSG 749
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 227-320 2.34e-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: 38.65  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  227 RDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKETELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 305
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 767985825  306 NQNLEDKVRSLKTDI 320
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 168-350 2.39e-03

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: 40.00  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  168 THLKSENDKLKIALTQSaanvkkwEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI 247
Cdd:TIGR04523 352 TNSESENSEKQRELEEK-------QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  248 NRE----KEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEK------------------LEAAERD 305
Cdd:TIGR04523 425 EKEierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKikqnleqkqkelkskekeLKKLNEE 504

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767985825  306 NQNLEDKVRSLKTDIEESKYRQRHLKVELKSflevLDGKIDDLHD 350
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKE----KESKISDLED 545
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
229-359 3.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 229 ENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKqsEIIPQLMSECEYVSEKLEAAER-DNQ 307
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK--ELEELGFESVEELEERLKELEPfYNE 603

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767985825 308 NLEdkVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKLG 359
Cdd:PRK03918 604 YLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
232-357 3.84e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 232 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRkqseiipqlmSECEYVSEKLEAAERDNQNLED 311
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE----------AEIEDLRETIAETEREREELAE 279

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767985825 312 KVRSLKTDIEESKYRQRHLKVElksfLEVLDGKIDDLHDFRRGLSK 357
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAE----AGLDDADAEAVEARREELED 321
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 188-348 4.27e-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: 38.39  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 188 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 262
Cdd:cd21966    5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 263 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 336
Cdd:cd21966   83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                        170
                 ....*....|..
gi 767985825 337 FLEVLDGKIDDL 348
Cdd:cd21966  163 LVDSLEEPTSEL 174
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 170-326 4.39e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQE-----------SAASVEQWKRQFSI-------CRDEND 231
Cdd:COG4942   74 LEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYlkylapaRREQAE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 232 RLRNKIDELEEQCSEINREKEkntqlkrRIEELEAELREKETELKDLRK-QSEIIPQLMSECEYVSEKLEAAERDNQNLE 310
Cdd:COG4942  154 ELRADLAELAALRAELEAERA-------ELEALLAELEEERAALEALKAeRQKLLARLEKELAELAAELAELQQEAEELE 226

                        170
                 ....*....|....*.
gi 767985825 311 DKVRSLKTDIEESKYR 326
Cdd:COG4942  227 ALIARLEAEAAAAAER 242
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 249-340 4.55e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 37.96  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  249 REKEKNTQLKRRIEELEAELREKETELKDLRKQSEI-----IPQLMSECEYVSEKLEAAERDNQNLEDKVRSlktdieES 323
Cdd:pfam15619  78 RLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDknlaeREELQKKLEQLEAKLEDKDEKIQDLERKLEL------EN 151

                          90
                  ....*....|....*..
gi 767985825  324 KYRQRHLKVELKSFLEV 340
Cdd:pfam15619 152 KSFRRQLAAEKKKHKEA 168
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-287 5.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES-AASVEQWKRQFSICRDENDRLRNKIDELEEQC---- 244
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLaalg 372

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767985825  245 -------------------------SEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQ 287
Cdd:COG4913   373 lplpasaeefaalraeaaallealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-322 5.11e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 249
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 250 EKEKNTQLKRRIEELE-----------------AELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDK 312
Cdd:PRK03918 274 EIEELEEKVKELKELKekaeeyiklsefyeeylDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353

                        170
                 ....*....|
gi 767985825 313 VRSLKTDIEE 322
Cdd:PRK03918 354 LEELEERHEL 363
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 170-358 6.59e-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: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 249
Cdd:COG4942   32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 250 EKEKN---------------TQLKRRIEELEAELREKETELKDLRKQSEIIPQLmseceyvSEKLEAAERDNQNLEDKVR 314
Cdd:COG4942  112 ALYRLgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------RAELEAERAELEALLAELE 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767985825 315 SLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 358
Cdd:COG4942  185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 233-338 6.61e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 38.13  E-value: 6.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 233 LRNKIDELEEQCSeiNREKEKNTQlkrRIEELEAELREKETELKDLRKQ----SEIIPQLMSEceyvsekleaaERDNQN 308
Cdd:PRK05431   7 IRENPEAVKEALA--KRGFPLDVD---ELLELDEERRELQTELEELQAErnalSKEIGQAKRK-----------GEDAEA 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 767985825 309 LEDKVRSLKTDIEESKYRQRHLKVELKSFL 338
Cdd:PRK05431  71 LIAEVKELKEEIKALEAELDELEAELEELL 100
CASP_C pfam08172
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ...
 258-314 7.40e-03

CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.


Pssm-ID: 462392 [Multi-domain]  Cd Length: 247  Bit Score: 37.65  E-value: 7.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767985825  258 KRRIEELEAELREKETELKDLRkqSEIipqlmseceyvsEKLEAaerDNQNLEDKVR 314
Cdd:pfam08172  95 RQRNAELEEELRKQFETISSLR--QEI------------ASLQK---DNLKLYEKTR 134
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 185-322 7.91e-03

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: 38.28  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   185 AANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICR----DENDRLRNKIDELEEQCSEINRE----KEKNTQ 256
Cdd:pfam12128  240 RPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNGElsaaDAAVAK 319

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767985825   257 LKRRIEELEAELREKETE-LKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 322
Cdd:pfam12128  320 DRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
194-284 7.98e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 7.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 194 ELQTLRESNARLTTALQESAASVEQWKRQFSIcrDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKET 273
Cdd:COG4717  157 ELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                         90
                 ....*....|.
gi 767985825 274 ELKDLRKQSEI 284
Cdd:COG4717  235 ELEAAALEERL 245
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 229-348 8.23e-03

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: 38.08  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825  229 ENDRLRNKIDELEEQCSEINREKEKNTQlkrRIEELEAELREKETELKDLR-KQSEIIPQLmsecEYVSEKLEAAERDNQ 307
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTQLNQLKdEQNKIKKQL----SEKQKELEQNNKKIK 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767985825  308 NLEDKVRSLKTDIEE-SKYRQRHLKVELKSFLEVLDGKIDDL 348
Cdd:TIGR04523 285 ELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEI 326
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 200-358 9.11e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   200 ESNARLTTALQESAASVEQWKRQFSIcrdenDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLR 279
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELELALLV-----LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825   280 KQSEIIP-------QLMSECE-----------YVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVL 341
Cdd:TIGR02168  281 EEIEELQkelyalaNEISRLEqqkqilrerlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360

                          170
                   ....*....|....*..
gi 767985825   342 DGKIDDLHDFRRGLSKL 358
Cdd:TIGR02168  361 EELEAELEELESRLEEL 377
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 170-285 9.68e-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: 37.21  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 170 LKSENDKLKIALTQSAANVKKWEIELQTLResNARLTTALQesaASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 249
Cdd:COG1579   57 LEKEIKRLELEIEEVEARIKKYEEQLGNVR--NNKEYEALQ---KEIESLKRRISDLEDEILELMERIEELEEELAELEA 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767985825 250 EKEKntqLKRRIEELEAELREK----ETELKDLRKQSEII 285
Cdd:COG1579  132 ELAE---LEAELEEKKAELDEElaelEAELEELEAEREEL 168
PRK01156 PRK01156
chromosome segregation protein; Provisional
 213-322 9.76e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 37.96  E-value: 9.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985825 213 AASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQ-LMSE 291
Cdd:PRK01156 331 LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDaIKKE 410

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767985825 292 CEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 322
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALRENLDE 441
 
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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