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Conserved domains on  [gi|46249349|ref|NP_004830|]
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homer protein homolog 2 isoform 1 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 2.85e-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: 2.85e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   3 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 46249349  83 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-322 1.99e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     93 EQQLTKFAEKFQEVKEAAKiakDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKW 172
Cdd:TIGR02168  697 EKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    173 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLR--------------NKIDELEEQCSEINREKEKNTQ- 237
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEd 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    238 ---LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  854 iesLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250
                   ....*....|..
gi 46249349    311 LKVELKSFLEVL 322
Cdd:TIGR02168  934 LEVRIDNLQERL 945
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 2.85e-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: 2.85e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   3 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 46249349  83 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-107 5.87e-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: 136.43  E-value: 5.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     4 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 46249349    82 AntVFGLGFSSEQQLTKFAEKFQEVK 107
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-105 5.49e-29

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: 107.83  E-value: 5.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349      1 MGEQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 46249349     79 DsrANTVFGLGFSSEQQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-322 1.99e-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: 55.83  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     93 EQQLTKFAEKFQEVKEAAKiakDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKW 172
Cdd:TIGR02168  697 EKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    173 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLR--------------NKIDELEEQCSEINREKEKNTQ- 237
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEd 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    238 ---LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  854 iesLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250
                   ....*....|..
gi 46249349    311 LKVELKSFLEVL 322
Cdd:TIGR02168  934 LEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-329 7.59e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 7.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 230
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 231 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                       170
                ....*....|....*....
gi 46249349 311 LKVELKSFLEVLDGKIDDL 329
Cdd:COG1196 398 LAAQLEELEEAEEALLERL 416
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-303 2.84e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQA------------SSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 162
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREEletleaeiedlrETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  163 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 242
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46249349  243 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 303
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 ...
 151-303 5.68e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   231 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 46249349   296 SLKTDIEE 303
Cdd:pfam10174 486 ALQPELTE 493
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 169-329 5.87e-03

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


Pssm-ID: 439320 [Multi-domain]  Cd Length: 300  Bit Score: 38.01  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 169 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 243
Cdd:cd21966   5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 244 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 317
Cdd:cd21966  83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                       170
                ....*....|..
gi 46249349 318 FLEVLDGKIDDL 329
Cdd:cd21966 163 LVDSLEEPTSEL 174
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 2.85e-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: 2.85e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   3 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 46249349  83 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-107 4.09e-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: 4.09e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   5 PIFTTRAHVFQIDPNtKKNWMPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837   1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                        90       100
                ....*....|....*....|....*.
gi 46249349  82 anTVFGLGFSSEQQLTKFAEKFQEVK 107
Cdd:cd00837  80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-107 5.87e-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: 136.43  E-value: 5.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     4 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 46249349    82 AntVFGLGFSSEQQLTKFAEKFQEVK 107
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-105 5.49e-29

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: 107.83  E-value: 5.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349      1 MGEQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 46249349     79 DsrANTVFGLGFSSEQQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-100 3.06e-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: 3.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   5 PIFTTRAHVFQIDPNTKKnWMPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207   1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                        90       100
                ....*....|....*....|
gi 46249349  81 RanTVFGLGFSSEQQLTKFA 100
Cdd:cd01207  80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-322 1.99e-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: 55.83  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     93 EQQLTKFAEKFQEVKEAAKiakDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKW 172
Cdd:TIGR02168  697 EKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    173 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLR--------------NKIDELEEQCSEINREKEKNTQ- 237
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEd 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    238 ---LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  854 iesLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250
                   ....*....|..
gi 46249349    311 LKVELKSFLEVL 322
Cdd:TIGR02168  934 LEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-316 5.90e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 5.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    152 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINRE 231
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    232 ----KEKNTQLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 307
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832


                   ....*....
gi 46249349    308 QRHLKVELK 316
Cdd:TIGR02168  833 IAATERRLE 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-315 1.48e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    100 AEKFQEVKEAAKIAKDKTQE-----KIETSSNHSQASSVNGTDDEKASHAGPANTHLK---SENDKLKIALTQSAANVKK 171
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    172 WEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKntqLKRRIEELEAELRE 251
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR---LQEELQRLSEELAD 424

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46249349    252 KETELKDLRKQseiIPQLMSECEYVSEKLEAAER-------DNQNLEDKVRSLKTDIEESKYRQRHLKVEL 315
Cdd:TIGR02169  425 LNAAIAGIEAK---INELEEEKEDKALEIKKQEWkleqlaaDLSKYEQELYDLKEEYDRVEKELSKLQREL 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-342 3.90e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQcseINR 230
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    231 EKEKNTQLKRRIEELEAELREKETElkdLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEE---AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 46249349    311 LKVELKSFLEVLDGKIDDLHDFRRGLSKLGTD 342
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 175-340 6.01e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 6.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCS-----EINREKEKNTQLKRRIEELEAEL 249
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    250 REKETELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKVELKSF 318
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 46249349    319 LEVLDGKIDDLHDFRRGLSKLG 340
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 94-323 6.11e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 6.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     94 QQLTKFAEKFQEVKEAAKIAKDKTQEKIEtsSNHSQASSVNGTDDEKASHAGpantHLKSENDKLKIALTQSaaNVKKWE 173
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLSSLEQEIE--NVKSELKELEARIEELEEDLH----KLEEALNDLEARLSHS--RIPEIQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    174 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKRRIEELEAELREKE 253
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELE 874

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    254 TELKDLRKQSEIIpqlmseceyvSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 323
Cdd:TIGR02169  875 AALRDLESRLGDL----------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-329 7.59e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 7.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 230
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 231 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                       170
                ....*....|....*....
gi 46249349 311 LKVELKSFLEVLDGKIDDL 329
Cdd:COG1196 398 LAAQLEELEEAEEALLERL 416
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
174-312 1.52e-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: 1.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 174 IELQTLRESNARLTTALQESAASVeqwkRQFSICRDENDRLRNKIDELEEQCSEInreKEKNTQLKRRIEELEAELRE-K 252
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEE----RELTEEEEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEaR 454

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 253 ETELKDLRKQSEIipqlmseceyvseklEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:COG2433 455 SEERREIRKDREI---------------SRLDREIERLERELEEERERIEELKRKLERLK 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
174-334 4.11e-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: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  174 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKntQLKRRIEELEAELREKE 253
Cdd:COG4913  281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE--QLEREIERLERELEERE 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  254 TELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGK 325
Cdd:COG4913  359 RRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSN 437

                        170
                 ....*....|
gi 46249349  326 ID-DLHDFRR 334
Cdd:COG4913  438 IPaRLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-303 4.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 151 LKSENDKLKIALTqsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKID----------- 219
Cdd:COG1196 218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 220 ELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 298
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                ....*
gi 46249349 299 TDIEE 303
Cdd:COG1196 376 EAEEE 380
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
156-314 4.77e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 4.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 156 DKLKIALTQSAANVKKWEIELQTLRESNARLTTA------LQESAASVEQWKRQFSICRdENDRLRNKIDELEEQCSEIN 229
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELeaeleeLREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELE 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 230 REKEKNTQLKRRIEELEAELREKETELKDLRKQS-----EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES 304
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                       170
                ....*....|
gi 46249349 305 KYRQRHLKVE 314
Cdd:COG4717 233 ENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
88-343 5.54e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   88 LGFSSEQQLtkfAEKFQEVKEAAKiAKDKTQEKIETSSNHSQAssvngTDDEKASHAGPANThlkSENDklkIALTQSAA 167
Cdd:COG4913  604 LGFDNRAKL---AALEAELAELEE-ELAEAEERLEALEAELDA-----LQERREALQRLAEY---SWDE---IDVASAER 668

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  168 NVKKWEIELQTLRESNARLTTALQEsaasVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKRRIEELEA 247
Cdd:COG4913  669 EIAELEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELD---ELQDRLEAAED 741

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  248 ELREKETELKDLRKQSEIIPQLmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEE--SKYRQRHlkvelKSFLEVLDGK 325
Cdd:COG4913  742 LARLELRALLEERFAAALGDAV------ERELRENLEERIDALRARLNRAEEELERamRAFNREW-----PAETADLDAD 810

                        250
                 ....*....|....*...
gi 46249349  326 IDDLHDFRRGLSKLGTDN 343
Cdd:COG4913  811 LESLPEYLALLDRLEEDG 828
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 212-329 6.89e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 6.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 212 DRLRNKIDELEEQCSEINREKEKN----TQLKRRIEELEAELREKETELKDLRKQ----SEIIPQLMSECEY--VSEKLE 281
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYeaLQKEIE 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46249349 282 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDL 329
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-338 1.48e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    208 RDENDRLRNKIDELEEQCS----EINREKEKNTQLKRRIEELEAELREKETEL----KDLRKQSEIIPQLMSECEYVSEK 279
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    280 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVEL-KSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 214-340 2.35e-05

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 45.49  E-value: 2.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 214 LRNKIDELEEQCSEINREKEKntqLKRRIEELEAELREKETELKDLRKQSEIIpqlmseceyvsekleaaERDNQNLEDK 293
Cdd:COG4026 133 LREELLELKEKIDEIAKEKEK---LTKENEELESELEELREEYKKLREENSIL-----------------EEEFDNIKSE 192

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46249349 294 VRSLKTDIEESKyRQRHLKV-ELKS-FLEVLDGKIDDLHDFRRGLSKLG 340
Cdd:COG4026 193 YSDLKSRFEELL-KKRLLEVfSLEElWKELFPEELPEEDFIYFATENLK 240
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-303 2.84e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQA------------SSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 162
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREEletleaeiedlrETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  163 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 242
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46249349  243 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 303
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-288 3.74e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 149 THLKSENDKLKIALtQSAANVKKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI 228
Cdd:COG4717 112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 229 NREKEKntQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 288
Cdd:COG4717 190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
173-264 3.96e-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: 3.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 173 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDEL-EEQCSEINREKEKnTQLKRRIEELEAELRE 251
Cdd:COG2433 405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREI-SRLDREIERLERELEE 483

                        90
                ....*....|...
gi 46249349 252 KETELKDLRKQSE 264
Cdd:COG2433 484 ERERIEELKRKLE 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-323 4.35e-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: 4.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    100 AEKFQEVKEAAK------IAKDKTQEKIETSSNHSQASSVNgtDDEKASHAGPANTHLKSENDKLKIALTQSAANVKkwE 173
Cdd:TIGR02168  212 AERYKELKAELRelelalLVLRLEELREELEELQEELKEAE--EELEELTAELQELEEKLEELRLEVSELEEEIEEL--Q 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    174 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKE 253
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELE 364

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    254 TELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 323
Cdd:TIGR02168  365 AELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-336 5.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  175 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLR-----NKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 249
Cdd:COG4913  243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDAL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  250 REKETELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKID 327
Cdd:COG4913  322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                 ....*....
gi 46249349  328 DLHDFRRGL 336
Cdd:COG4913  402 ALEEALAEA 410
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 151-303 5.68e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   231 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 46249349   296 SLKTDIEE 303
Cdd:pfam10174 486 ALQPELTE 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 208-339 6.68e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    208 RDENDRLRNKIDELEEQCSEINRE-KEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 46249349    287 NQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-329 7.30e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 7.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 202 RQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLmseceyvsEKLE 281
Cdd:COG4717  64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46249349 282 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKvELKSFLEVLDGKIDDL 329
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 212-303 7.37e-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: 7.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 212 DRLRNKIDELEEQCSEInrEKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 291
Cdd:COG0542 414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                        90
                ....*....|..
gi 46249349 292 DKVRSLKTDIEE 303
Cdd:COG0542 492 KELAELEEELAE 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 230-329 9.80e-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: 44.29  E-value: 9.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    230 REKEKNTQLKRRIEELEaelREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 46249349    310 HLKVEL---KSFLEVLDGKIDDL 329
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-338 1.02e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  151 LKSENDKLKIALTQsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 230
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  231 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 303
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46249349  304 SKYRQ-RHLKVELKSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
173-339 1.22e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  173 EIELQTLRESNARLTTALQEsaasveqwkRQFSICRDENDRLR------NKIDELEEQCSEINREKEKNTQLKRRIEELE 246
Cdd:PRK03918 562 EKKLDELEEELAELLKELEE---------LGFESVEELEERLKelepfyNEYLELKDAEKELEREEKELKKLEEELDKAF 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  247 AELREKETELKDLRKQSEIIPQLMSECEY--VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSF------ 318
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekakke 712

                        170       180
                 ....*....|....*....|.
gi 46249349  319 LEVLDGKIDDLHDFRRGLSKL 339
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKY 733
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
206-312 1.28e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  206 ICRDEN--DRLRNKIDELEEQCSEINrekekntQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918 185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                         90       100
                 ....*....|....*....|....*....
gi 46249349  284 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK 286
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-303 1.71e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  170 KKWEIELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRNKIDELEeqcSEINREKEKNTQLKRRIEELEAEL 249
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 46249349  250 REKETELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKE 739
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
200-312 1.80e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  200 WKRQFSICRDENDRLRNKIDEL--EEQCSEINREKEKN-TQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYV 276
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 46249349  277 SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
PLN02939 PLN02939
transferase, transferring glycosyl groups
 153-315 2.14e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.35  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  153 SENDKLKIALTQSAANVKKWEIELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREK 232
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  233 EKNTQLKRRIEELEAELREKETEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLEDKVRSL 297
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKL 336

                        170
                 ....*....|....*....
gi 46249349  298 KTDIEESK-YRQRHLKVEL 315
Cdd:PLN02939 337 EASLKEANvSKFSSYKVEL 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-303 2.64e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 104 QEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESN 183
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 184 ARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQS 263
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46249349 264 eiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:COG1196 469 ----------LEEAALLEAALAELLEELAEAAARLLLLLE 498
PRK12704 PRK12704
phosphodiesterase; Provisional
 218-322 2.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  218 IDELEEQCSEINREK--EKNTQLKRRIEELEAELREKETELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:PRK12704  44 LEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEELEKKEK 117

                         90       100
                 ....*....|....*....|....*..
gi 46249349  296 SLKTDIEESKYRQRHLKVELKSFLEVL 322
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQEL 144
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 122-329 3.09e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    122 ETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKK----WEIELQTLRESNARLTTALQESAASV 197
Cdd:pfam15921  286 KASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEELEKQLVLANSELTEARTER 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    198 EQWKRQFSicrDENDRLRNKIDELEEQCSEINREKEKNTQLKRR-------IEELEAELREKETELKDLRKqseIIPQLM 270
Cdd:pfam15921  366 DQFSQESG---NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMK 439

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46249349    271 SECE-YVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKVEL---KSFLEVLDGKIDDL 329
Cdd:pfam15921  440 SECQgQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDL 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
101-297 3.24e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 3.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAgpanTHLKSENDKLKIALTQSAANVKKWEIElQTLR 180
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLE-ELEQ 370

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 181 ESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNT--QLKRRIEELEAELREKETELKD 258
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEE 450

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 46249349 259 LRKQSEIIPQLMSECEyVSEKLEAAERDNQNLEDKVRSL 297
Cdd:COG4717 451 LREELAELEAELEQLE-EDGELAELLQELEELKAELREL 488
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 180-334 3.41e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    180 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKI-DELEEQCSEINREKEkntQLKRRIEELEAELREKETELKD 258
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAeDDLQALESELREQLE---AGKLEFNEEEYRLKSRLGELKL 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    259 LRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES--KYRQRHLKVE-----LKSFLEVLDG 324
Cdd:pfam12128  452 RLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQAseALRQASRRLEerqsaLDELELQLFP 531

                          170
                   ....*....|
gi 46249349    325 KIDDLHDFRR 334
Cdd:pfam12128  532 QAGTLLHFLR 541
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
190-339 4.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  190 LQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQL 269
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  270 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 166-312 9.58e-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: 41.11  E-value: 9.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    166 AANVKKWEIELQTLRESNARLTTaLQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR---------EKEKNT 236
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaaHIKAVT 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46249349    237 QLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLE---AAERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 161-339 1.11e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 161 ALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKR 240
Cdd:COG4942  14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 241 RIEELEAELREKETELKDLRKQSeiipQLMSECEYV-----SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHL---K 312
Cdd:COG4942  91 EIAELRAELEAQKEELAELLRAL----YRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalR 166

                       170       180
                ....*....|....*....|....*..
gi 46249349 313 VELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-305 1.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  213 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL-------------REKETELKDLRKQSEI--IPQLMSECEYVS 277
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerhelyeeaKAKKEELERLKKRLTGltPEKLEKELEELE 397

                         90       100
                 ....*....|....*....|....*...
gi 46249349  278 EKLEAAERDNQNLEDKVRSLKTDIEESK 305
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELK 425
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 105-317 1.20e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   105 EVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNA 184
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   185 RLTTALQESAASVEQWKRQFS---------------ICRDENDRLRNKIDELEEQCSEINR---EKEKNTQLKR----RI 242
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSfvvtefeattcsleeLLRTEQQRLEKNEDQLKIITMELQKkssELEEMTKFKNnkevEL 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46249349   243 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 317
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
PTZ00121 PTZ00121
MAEBL; Provisional
 101-325 1.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   101 EKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEI-ELQTL 179
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEE 1631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   180 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDL 259
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46249349   260 RKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGK 325
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-303 1.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 138 DEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNK 217
Cdd:COG4372   2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 218 IDELEEQcseINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 297
Cdd:COG4372  82 LEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKEL 155


                ....*.
gi 46249349 298 KTDIEE 303
Cdd:COG4372 156 EEQLES 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-297 1.54e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349     93 EQQLTKFAEKFQEVK-EAAKIAKDKTQEKIETSSNHSQASSVNGtddekashagpANTHLKSENDKLKIALTQSAANVKK 171
Cdd:TIGR02168  767 EERLEEAEEELAEAEaEIEELEAQIEQLKEELKALREALDELRA-----------ELTLLNEEAANLRERLESLERRIAA 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    172 WEIELQTLRESNARLTTALQESAASVEQwkrqfsicrdendrLRNKIDELEEQCSEINREKEKNTQ----LKRRIEELEA 247
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIEELESELEALLNERASLEEalalLRSELEELSE 901

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 46249349    248 ELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 297
Cdd:TIGR02168  902 ELRELESKRSELRRELE---ELREKLAQLELRLEGLEVRIDNLQERLSEE 948
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 152-333 1.73e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   152 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEIN-R 230
Cdd:pfam07888  65 KRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTqR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   231 EKEKNTQLKR---RIEELEAELREKETELKDLR-------------------------KQSEIIPQLMSECEYVSEKLEA 282
Cdd:pfam07888 145 VLERETELERmkeRAKKAGAQRKEEEAERKQLQaklqqteeelrslskefqelrnslaQRDTQVLQLQDTITTLTQKLTT 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46249349   283 AER---DNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFR 333
Cdd:pfam07888 225 AHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 88-307 1.77e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  88 LGFSSEQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAA 167
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 168 NVKKWEIELQTLRESNARLTTALQE-----------SAASVEQWKRQFSI-------CRDENDRLRNKIDELEEQCSEIN 229
Cdd:COG4942  91 EIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYlkylapaRREQAEELRADLAELAALRAELE 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46249349 230 REKEkntqlkrRIEELEAELREKETELKDLRK-QSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 307
Cdd:COG4942 171 AERA-------ELEALLAELEEERAALEALKAeRQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
238-322 1.86e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 238 LKRRIEELEAELREKETELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 317
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                ....*
gi 46249349 318 FLEVL 322
Cdd:COG3206 252 GPDAL 256
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 88-303 1.98e-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: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    88 LGFSSEQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAA 167
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   168 NVKKWEIELQTLRESNAR--LTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNT----QLKRR 241
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEkkisSLEKE 618

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46249349   242 IEELEAELREKETELKDLRKQSEIIPQlmsECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQ---EVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-322 2.84e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  170 KKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 249
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46249349  250 REKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKVELKSFLEVL 322
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
PRK01156 PRK01156
chromosome segregation protein; Provisional
 212-342 3.06e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  212 DRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKE-------TELKDLRKQSEIIPQLMSECEYVSEKLEAAE 284
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46249349  285 RDNQNLEDKVRSLKTDIEESKYRQRHLKVE----------LKSFLEVLDGKIDDLHDFRRGLSKLGTD 342
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKD 337
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 208-301 3.78e-03

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


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 37.88  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   208 RDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKETELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 46249349   287 NQNLEDKVRSLKTDI 301
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
PRK01156 PRK01156
chromosome segregation protein; Provisional
 209-340 3.84e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  209 DENDRLRNKIDELEEQcsEINREKekntqLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQ 288
Cdd:PRK01156 626 NEANNLNNKYNEIQEN--KILIEK-----LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46249349  289 NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGKIDDLHDFRRGLSKLG 340
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLREAFDKSG 749
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 174-338 4.03e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 4.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 174 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIE---------- 243
Cdd:COG1579  10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnk 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 244 ELEAELREKETELKDLRKQSEIIPQLMseceyvsEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKVELKSFLEVLD 323
Cdd:COG1579  90 EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELE 155

                       170
                ....*....|....*
gi 46249349 324 GKIDDLHDFRRGLSK 338
Cdd:COG1579 156 AELEELEAEREELAA 170
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
213-338 4.24e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  213 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRkqseiipqlmSECEYVSEKLEAAERDNQNLED 292
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE----------AEIEDLRETIAETEREREELAE 279

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46249349  293 KVRSLKTDIEESKYRQRHLKVElksfLEVLDGKIDDLHDFRRGLSK 338
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAE----AGLDDADAEAVEARREELED 321
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-268 5.49e-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: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES-AASVEQWKRQFSICRDENDRLRNKIDELEEQC---- 225
Cdd:COG4913  293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLaalg 372

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46249349  226 -------------------------SEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQ 268
Cdd:COG4913  373 lplpasaeefaalraeaaallealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 169-329 5.87e-03

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


Pssm-ID: 439320 [Multi-domain]  Cd Length: 300  Bit Score: 38.01  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 169 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 243
Cdd:cd21966   5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349 244 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 317
Cdd:cd21966  83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                       170
                ....*....|..
gi 46249349 318 FLEVLDGKIDDL 329
Cdd:cd21966 163 LVDSLEEPTSEL 174
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
210-340 6.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  210 ENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKqsEIIPQLMSECEYVSEKLEAAER-DNQ 288
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK--ELEELGFESVEELEERLKELEPfYNE 603

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46249349  289 NLEdkVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKLG 340
Cdd:PRK03918 604 YLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 214-319 6.50e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 38.13  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  214 LRNKIDELEEQCSeiNREKEKNTQlkrRIEELEAELREKETELKDLRKQ----SEIIPQLMSEceyvsekleaaERDNQN 289
Cdd:PRK05431   7 IRENPEAVKEALA--KRGFPLDVD---ELLELDEERRELQTELEELQAErnalSKEIGQAKRK-----------GEDAEA 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 46249349  290 LEDKVRSLKTDIEESKYRQRHLKVELKSFL 319
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 ...
 239-295 7.55e-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: 37.27  E-value: 7.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46249349   239 KRRIEELEAELREKETELKDLRkqSEIipqlmseceyvsEKLEAaerDNQNLEDKVR 295
Cdd:pfam08172  95 RQRNAELEEELRKQFETISSLR--QEI------------ASLQK---DNLKLYEKTR 134
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
151-303 7.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 230
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349  231 EKEKNTQLKRRIEELE-----------------AELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDK 293
Cdd:PRK03918 274 EIEELEEKVKELKELKekaeeyiklsefyeeylDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353

                        170
                 ....*....|
gi 46249349  294 VRSLKTDIEE 303
Cdd:PRK03918 354 LEELEERHEL 363
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 230-321 8.14e-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: 36.80  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349   230 REKEKNTQLKRRIEELEAELREKETELKDLRKQSEI-----IPQLMSECEYVSEKLEAAERDNQNLEDKVRSlktdieES 304
Cdd:pfam15619  78 RLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDknlaeREELQKKLEQLEAKLEDKDEKIQDLERKLEL------EN 151

                          90
                  ....*....|....*..
gi 46249349   305 KYRQRHLKVELKSFLEV 321
Cdd:pfam15619 152 KSFRRQLAAEKKKHKEA 168
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 166-303 9.39e-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: 37.90  E-value: 9.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46249349    166 AANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICR----DENDRLRNKIDELEEQCSEINRE----KEKNTQ 237
Cdd:pfam12128  240 RPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNGElsaaDAAVAK 319

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46249349    238 LKRRIEELEAELREKETE-LKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:pfam12128  320 DRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
 
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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