NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217303388|ref|XP_047289313|]
View 

homer protein homolog 2 isoform X5 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 13-121 2.21e-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: 233.01  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  13 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 92
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 2217303388  93 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 121
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-332 2.21e-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: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  103 EQQLTKFAEKFQEVKEAAKiakDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKW 182
Cdd:TIGR02168  697 EKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  183 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLR--------------NKIDELEEQCSEINREKEKNTQ- 247
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEd 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  248 ---LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 320
Cdd:TIGR02168  854 iesLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250
                   ....*....|..
gi 2217303388  321 LKVELKSFLEVL 332
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, ...
 13-121 2.21e-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: 233.01  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  13 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 92
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 2217303388  93 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 121
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 14-117 5.86e-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: 136.81  E-value: 5.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  14 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 91
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 2217303388  92 AntVFGLGFSSEQQLTKFAEKFQEVK 117
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 11-115 1.04e-27

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


Pssm-ID: 214674  Cd Length: 106  Bit Score: 104.36  E-value: 1.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388   11 PREQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 88
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 2217303388   89 DsrANTVFGLGFSSEQQLTKFAEKFQE 115
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-332 2.21e-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: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  103 EQQLTKFAEKFQEVKEAAKiakDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKW 182
Cdd:TIGR02168  697 EKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  183 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLR--------------NKIDELEEQCSEINREKEKNTQ- 247
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEd 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  248 ---LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 320
Cdd:TIGR02168  854 iesLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250
                   ....*....|..
gi 2217303388  321 LKVELKSFLEVL 332
Cdd:TIGR02168  934 LEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-339 8.11e-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: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 161 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 240
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 241 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 320
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         170
                  ....*....|....*....
gi 2217303388 321 LKVELKSFLEVLDGKIDDL 339
Cdd:COG1196   398 LAAQLEELEEAEEALLERL 416
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
111-313 3.11e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 111 EKFQEVKEAAKIAKDKTQEKIETSSNHSQA------------SSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 172
Cdd:PRK02224  223 ERYEEQREQARETRDEADEVLEEHEERREEletleaeiedlrETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 173 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 252
Cdd:PRK02224  303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217303388 253 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 313
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 ...
 161-313 7.34e-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: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 161 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 240
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 241 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 305
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 2217303388 306 SLKTDIEE 313
Cdd:pfam10174 486 ALQPELTE 493
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 179-339 6.03e-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: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 179 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 253
Cdd:cd21966     5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 254 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 327
Cdd:cd21966    83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                         170
                  ....*....|..
gi 2217303388 328 FLEVLDGKIDDL 339
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, ...
 13-121 2.21e-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: 233.01  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  13 EQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 92
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 2217303388  93 NTVFGLGFSSEQQLTKFAEKFQEVKEAAK 121
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 15-117 3.61e-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: 142.22  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  15 PIFTTRAHVFQIDPNtKKNWMPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 91
Cdd:cd00837     1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                          90       100
                  ....*....|....*....|....*.
gi 2217303388  92 anTVFGLGFSSEQQLTKFAEKFQEVK 117
Cdd:cd00837    80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 14-117 5.86e-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: 136.81  E-value: 5.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  14 QPIFTTRAHVFQIDPNTKKNWMPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 91
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 2217303388  92 AntVFGLGFSSEQQLTKFAEKFQEVK 117
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 11-115 1.04e-27

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


Pssm-ID: 214674  Cd Length: 106  Bit Score: 104.36  E-value: 1.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388   11 PREQPIFTTRAHVFQIDPNTKKnWMPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 88
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 2217303388   89 DsrANTVFGLGFSSEQQLTKFAEKFQE 115
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 15-110 2.76e-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: 62.71  E-value: 2.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  15 PIFTTRAHVFQIDPNTKKnWMPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 90
Cdd:cd01207     1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                          90       100
                  ....*....|....*....|
gi 2217303388  91 RanTVFGLGFSSEQQLTKFA 110
Cdd:cd01207    80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-332 2.21e-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: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  103 EQQLTKFAEKFQEVKEAAKiakDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKW 182
Cdd:TIGR02168  697 EKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  183 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLR--------------NKIDELEEQCSEINREKEKNTQ- 247
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEd 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  248 ---LKRRIEELEAELREKETELKDLRKQSEIIPQLM----SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 320
Cdd:TIGR02168  854 iesLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250
                   ....*....|..
gi 2217303388  321 LKVELKSFLEVL 332
Cdd:TIGR02168  934 LEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-326 6.42e-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: 6.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  162 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINRE 241
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  242 ----KEKNTQLKRRIEELEAELREKETELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 317
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832


                   ....*....
gi 2217303388  318 QRHLKVELK 326
Cdd:TIGR02168  833 IAATERRLE 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 110-325 2.00e-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: 52.76  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  110 AEKFQEVKEAAKIAKDKTQE-----KIETSSNHSQASSVNGTDDEKASHAGPANTHLK---SENDKLKIALTQSAANVKK 181
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  182 WEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKntqLKRRIEELEAELRE 261
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR---LQEELQRLSEELAD 424

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217303388  262 KETELKDLRKQseiIPQLMSECEYVSEKLEAAER-------DNQNLEDKVRSLKTDIEESKYRQRHLKVEL 325
Cdd:TIGR02169  425 LNAAIAGIEAK---INELEEEKEDKALEIKKQEWkleqlaaDLSKYEQELYDLKEEYDRVEKELSKLQREL 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 161-352 4.37e-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: 4.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  161 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQcseINR 240
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  241 EKEKNTQLKRRIEELEAELREKETElkdLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 320
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEE---AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2217303388  321 LKVELKSFLEVLDGKIDDLHDFRRGLSKLGTD 352
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 104-333 7.53e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 7.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  104 QQLTKFAEKFQEVKEAAKIAKDKTQEKIEtsSNHSQASSVNGTDDEKASHAGpantHLKSENDKLKIALTQSaaNVKKWE 183
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLSSLEQEIE--NVKSELKELEARIEELEEDLH----KLEEALNDLEARLSHS--RIPEIQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  184 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKRRIEELEAELREKE 263
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELE 874

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  264 TELKDLRKQSEIIpqlmseceyvSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 333
Cdd:TIGR02169  875 AALRDLESRLGDL----------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 185-350 7.86e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 7.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  185 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCS-----EINREKEKNTQLKRRIEELEAEL 259
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  260 REKETELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKVELKSF 328
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 2217303388  329 LEVLDGKIDDLHDFRRGLSKLG 350
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-339 8.11e-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: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 161 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINR 240
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 241 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 320
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         170
                  ....*....|....*....
gi 2217303388 321 LKVELKSFLEVLDGKIDDL 339
Cdd:COG1196   398 LAAQLEELEEAEEALLERL 416
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
218-322 2.02e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.47  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 218 RDENDRLRNKIDELEEQCSEInreKEKNTQLKRRIEELEAELRE-KETELKDLRKQSEIipqlmseceyvseklEAAERD 296
Cdd:COG2433   412 EEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEaRSEERREIRKDREI---------------SRLDRE 473

                          90       100
                  ....*....|....*....|....*.
gi 2217303388 297 NQNLEDKVRSLKTDIEESKYRQRHLK 322
Cdd:COG2433   474 IERLERELEEERERIEELKRKLERLK 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
184-344 4.08e-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: 4.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  184 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKntQLKRRIEELEAELREKE 263
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE--QLEREIERLERELEERE 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  264 TELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGK 335
Cdd:COG4913    359 RRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSN 437

                          170
                   ....*....|
gi 2217303388  336 ID-DLHDFRR 344
Cdd:COG4913    438 IPaRLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-313 4.78e-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: 4.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 161 LKSENDKLKIALTqsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKID----------- 229
Cdd:COG1196   218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 230 ELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 308
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                  ....*
gi 2217303388 309 TDIEE 313
Cdd:COG1196   376 EAEEE 380
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-353 5.08e-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: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388   98 LGFSSEQQLtkfAEKFQEVKEAAKiAKDKTQEKIETSSNHSQAssvngTDDEKASHAGPANThlkSENDklkIALTQSAA 177
Cdd:COG4913    604 LGFDNRAKL---AALEAELAELEE-ELAEAEERLEALEAELDA-----LQERREALQRLAEY---SWDE---IDVASAER 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  178 NVKKWEIELQTLRESNARLTTALQEsaasVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKRRIEELEA 257
Cdd:COG4913    669 EIAELEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELD---ELQDRLEAAED 741

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  258 ELREKETELKDLRKQSEIIPQLmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEE--SKYRQRHlkvelKSFLEVLDGK 335
Cdd:COG4913    742 LARLELRALLEERFAAALGDAV------ERELRENLEERIDALRARLNRAEEELERamRAFNREW-----PAETADLDAD 810

                          250
                   ....*....|....*...
gi 2217303388  336 IDDLHDFRRGLSKLGTDN 353
Cdd:COG4913    811 LESLPEYLALLDRLEEDG 828
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
166-324 5.44e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 166 DKLKIALTQSAANVKKWEIELQTLRESNARLTTA------LQESAASVEQWKRQFSICRdENDRLRNKIDELEEQCSEIN 239
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELeaeleeLREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 240 REKEKNTQLKRRIEELEAELREKETELKDLRKQS-----EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES 314
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                         170
                  ....*....|
gi 2217303388 315 KYRQRHLKVE 324
Cdd:COG4717   233 ENELEAAALE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 222-339 9.00e-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: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 222 DRLRNKIDELEEQCSEINREKEKN----TQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSEC----EY--VSEKLE 291
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEYeaLQKEIE 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217303388 292 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDL 339
Cdd:COG1579   100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-348 1.84e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  218 RDENDRLRNKIDELEEQCS----EINREKEKNTQLKRRIEELEAELREKETEL----KDLRKQSEIIPQLMSECEYVSEK 289
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  290 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVEL-KSFLEVLDGKIDDLHDFRRGLSK 348
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
111-313 3.11e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 111 EKFQEVKEAAKIAKDKTQEKIETSSNHSQA------------SSVNGTDDEKASHAGPANTH------LKSENDKLKIAL 172
Cdd:PRK02224  223 ERYEEQREQARETRDEADEVLEEHEERREEletleaeiedlrETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 173 TQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNtqlKRRI 252
Cdd:PRK02224  303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217303388 253 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 313
Cdd:PRK02224  380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 224-350 3.15e-05

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 45.10  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 224 LRNKIDELEEQCSEINREKEKntqLKRRIEELEAELREKETELKDLRKQSEIIpqlmseceyvsekleaaERDNQNLEDK 303
Cdd:COG4026   133 LREELLELKEKIDEIAKEKEK---LTKENEELESELEELREEYKKLREENSIL-----------------EEEFDNIKSE 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217303388 304 VRSLKTDIEESKYRQRHLKVELKS-FLEVLDGKIDDLHDFRRGLSKLG 350
Cdd:COG4026   193 YSDLKSRFEELLKKRLLEVFSLEElWKELFPEELPEEDFIYFATENLK 240
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
159-298 4.44e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 159 THLKSENDKLKIALtQSAANVKKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI 238
Cdd:COG4717   112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 239 NREKEKntQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 298
Cdd:COG4717   190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-333 4.57e-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: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  110 AEKFQEVKEAAK------IAKDKTQEKIETSSNHSQASSVNgtDDEKASHAGPANTHLKSENDKLKIALTQSAANVKkwE 183
Cdd:TIGR02168  212 AERYKELKAELRelelalLVLRLEELREELEELQEELKEAE--EELEELTAELQELEEKLEELRLEVSELEEEIEEL--Q 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  184 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKE 263
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELE 364

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  264 TELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLD 333
Cdd:TIGR02168  365 AELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
183-274 5.00e-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: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 183 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDEL-EEQCSEINREKEKnTQLKRRIEELEAELRE 261
Cdd:COG2433   405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREI-SRLDREIERLERELEE 483

                          90
                  ....*....|...
gi 2217303388 262 KETELKDLRKQSE 274
Cdd:COG2433   484 ERERIEELKRKLE 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-346 5.11e-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: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  185 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLR-----NKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 259
Cdd:COG4913    243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDAL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  260 REKETELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKID 337
Cdd:COG4913    322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                   ....*....
gi 2217303388  338 DLHDFRRGL 346
Cdd:COG4913    402 ALEEALAEA 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 218-349 7.25e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 7.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  218 RDENDRLRNKIDELEEQCSEINRE-KEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 296
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217303388  297 NQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 349
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 161-313 7.34e-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: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 161 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRNKIDELEEQCseinR 240
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 241 EKEKN-TQLKRRIEELEAE--------------LREKETELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 305
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 2217303388 306 SLKTDIEE 313
Cdd:pfam10174 486 ALQPELTE 493
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 222-313 8.44e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.30  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 222 DRLRNKIDELEEQCSEInrEKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 301
Cdd:COG0542   414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                          90
                  ....*....|..
gi 2217303388 302 DKVRSLKTDIEE 313
Cdd:COG0542   492 KELAELEEELAE 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
212-339 8.95e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 212 RQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLmseceyvsEKLE 291
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217303388 292 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKvELKSFLEVLDGKIDDL 339
Cdd:COG4717   136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
161-348 1.06e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 161 LKSENDKLKIALTQsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR 240
Cdd:PRK02224  487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 241 EKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 313
Cdd:PRK02224  566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217303388 314 SKYRQ-RHLKVELKSFLEVLDGKIDDLHDFRRGLSK 348
Cdd:PRK02224  646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-339 1.17e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  240 REKEKNTQLKRRIEELEaelREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 319
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 2217303388  320 HLKVEL---KSFLEVLDGKIDDL 339
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
216-322 2.00e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 216 ICRDEN--DRLRNKIDELEEQCSEINrekekntQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAA 293
Cdd:PRK03918  185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                          90       100
                  ....*....|....*....|....*....
gi 2217303388 294 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 322
Cdd:PRK03918  258 EEKIRELEERIEELKKEIEELEEKVKELK 286
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
183-349 2.23e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 183 EIELQTLRESNARLTTALQEsaasveqwkRQFSICRDENDRLR------NKIDELEEQCSEINREKEKNTQLKRRIEELE 256
Cdd:PRK03918  562 EKKLDELEEELAELLKELEE---------LGFESVEELEERLKelepfyNEYLELKDAEKELEREEKELKKLEEELDKAF 632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 257 AELREKETELKDLRKQSEIIPQLMSECEY--VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSF------ 328
Cdd:PRK03918  633 EELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekakke 712

                         170       180
                  ....*....|....*....|.
gi 2217303388 329 LEVLDGKIDDLHDFRRGLSKL 349
Cdd:PRK03918  713 LEKLEKALERVEELREKVKKY 733
PLN02939 PLN02939
transferase, transferring glycosyl groups
 163-325 2.36e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 163 SENDKLKIALTQSAANVKKWEIELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREK 242
Cdd:PLN02939  180 SETDARIKLAAQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 243 EKNTQLKRRIEELEAELREKETEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLEDKVRSL 307
Cdd:PLN02939  257 ERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKL 336

                         170
                  ....*....|....*....
gi 2217303388 308 KTDIEESK-YRQRHLKVEL 325
Cdd:PLN02939  337 EASLKEANvSKFSSYKVEL 355
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
210-322 2.77e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 210 WKRQFSICRDENDRLRNKIDEL--EEQCSEINREKEKN-TQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYV 286
Cdd:PRK03918  164 YKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217303388 287 SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 322
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
180-313 2.77e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 180 KKWEIELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRNKIDELEeqcSEINREKEKNTQLKRRIEELEAEL 259
Cdd:PRK03918  622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217303388 260 REKETELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEE 313
Cdd:PRK03918  697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKE 739
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-313 2.78e-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: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 114 QEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESN 193
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 194 ARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQS 273
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217303388 274 eiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 313
Cdd:COG1196   469 ----------LEEAALLEAALAELLEELAEAAARLLLLLE 498
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 190-344 3.36e-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: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  190 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKI-DELEEQCSEINREKEkntQLKRRIEELEAELREKETELKD 268
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAeDDLQALESELREQLE---AGKLEFNEEEYRLKSRLGELKL 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  269 LRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES--KYRQRHLKVE-----LKSFLEVLDG 334
Cdd:pfam12128  452 RLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQAseALRQASRRLEerqsaLDELELQLFP 531

                          170
                   ....*....|
gi 2217303388  335 KIDDLHDFRR 344
Cdd:pfam12128  532 QAGTLLHFLR 541
PRK12704 PRK12704
phosphodiesterase; Provisional
 228-332 3.37e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 228 IDELEEQCSEINREK--EKNTQLKRRIEELEAELREKETELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNLEDKVR 305
Cdd:PRK12704   44 LEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEELEKKEK 117

                          90       100
                  ....*....|....*....|....*..
gi 2217303388 306 SLKTDIEESKYRQRHLKVELKSFLEVL 332
Cdd:PRK12704  118 ELEQKQQELEKKEEELEELIEEQLQEL 144
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 132-339 3.46e-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: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  132 ETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKK----WEIELQTLRESNARLTTALQESAASV 207
Cdd:pfam15921  286 KASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEELEKQLVLANSELTEARTER 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  208 EQWKRQFSicrDENDRLRNKIDELEEQCSEINREKEKNTQLKRR-------IEELEAELREKETELKDLRKqseIIPQLM 280
Cdd:pfam15921  366 DQFSQESG---NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMK 439

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217303388  281 SECE-YVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKVEL---KSFLEVLDGKIDDL 339
Cdd:pfam15921  440 SECQgQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDL 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-307 3.48e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 111 EKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAgpanTHLKSENDKLKIALTQSAANVKKWEIElQTLR 190
Cdd:COG4717   296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLE-ELEQ 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 191 ESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNT--QLKRRIEELEAELREKETELKD 268
Cdd:COG4717   371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEE 450

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217303388 269 LRKQSEIIPQLMSECEyVSEKLEAAERDNQNLEDKVRSL 307
Cdd:COG4717   451 LREELAELEAELEQLE-EDGELAELLQELEELKAELREL 488
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
200-349 5.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 200 LQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQL 279
Cdd:PRK03918  195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 280 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKL 349
Cdd:PRK03918  275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 171-349 1.05e-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: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 171 ALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEkntQLKR 250
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 251 RIEELEAELREKETELKDLRKQSeiipQLMSECEYV-----SEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHL---K 322
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRAL----YRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalR 166

                         170       180
                  ....*....|....*....|....*..
gi 2217303388 323 VELKSFLEVLDGKIDDLHDFRRGLSKL 349
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEAL 193
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 176-322 1.17e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  176 AANVKKWEIELQTLRESNARLTTaLQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINR---------EKEKNT 246
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaaHIKAVT 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217303388  247 QLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLE---AAERDNQNLEDKVRSLKTDIEESKYRQRHLK 322
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
148-313 1.49e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 148 DEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNK 227
Cdd:COG4372     2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 228 IDELEEQcseINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 307
Cdd:COG4372    82 LEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKEL 155


                  ....*.
gi 2217303388 308 KTDIEE 313
Cdd:COG4372   156 EEQLES 161
PTZ00121 PTZ00121
MAEBL; Provisional
 111-335 1.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  111 EKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEI-ELQTL 189
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEE 1631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  190 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDL 269
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217303388  270 RKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGK 335
Cdd:PTZ00121  1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-331 1.62e-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: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  103 EQQLTKFAEKFQEVK-EAAKIAKDKTQEKIETSSNHSQASSVNGtddekashagpANTHLKSENDKLKIALTQSAANVKK 181
Cdd:TIGR02168  767 EERLEEAEEELAEAEaEIEELEAQIEQLKEELKALREALDELRA-----------ELTLLNEEAANLRERLESLERRIAA 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  182 WEIELQTLRESNARLTTALQESAASVEQwkrqfsicrdendrLRNKIDELEEQCSEINREKEKNTQ----LKRRIEELEA 257
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIEELESELEALLNERASLEEalalLRSELEELSE 901

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  258 ELREKETELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRS---------------LKTDIEESKYRQRHLK 322
Cdd:TIGR02168  902 ELRELESKRSELRRELE---ELREKLAQLELRLEGLEVRIDNLQERLSEeysltleeaealenkIEDDEEEARRRLKRLE 978


                   ....*....
gi 2217303388  323 VELKSFLEV 331
Cdd:TIGR02168  979 NKIKELGPV 987
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 98-317 1.69e-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: 40.13  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  98 LGFSSEQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAA 177
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 178 NVKKWEIELQTLRESNARLTTALQE-----------SAASVEQWKRQFSI-------CRDENDRLRNKIDELEEQCSEIN 239
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYlkylapaRREQAEELRADLAELAALRAELE 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217303388 240 REKEkntqlkrRIEELEAELREKETELKDLRK-QSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 317
Cdd:COG4942   171 AERA-------ELEALLAELEEERAALEALKAeRQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 115-327 1.69e-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: 40.48  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 115 EVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNA 194
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 195 RLTTALQESAASVEQWKRQFS---------------ICRDENDRLRNKIDELEEQCSEINR---EKEKNTQLKR----RI 252
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSfvvtefeattcsleeLLRTEQQRLEKNEDQLKIITMELQKkssELEEMTKFKNnkevEL 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217303388 253 EELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 327
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
223-315 1.93e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 223 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL-------------REKETELKDLRKQSEI--IPQLMSECEYVS 287
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerhelyeeaKAKKEELERLKKRLTGltPEKLEKELEELE 397

                          90       100
                  ....*....|....*....|....*...
gi 2217303388 288 EKLEAAERDNQNLEDKVRSLKTDIEESK 315
Cdd:PRK03918  398 KAKEEIEEEISKITARIGELKKEIKELK 425
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
248-332 1.95e-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: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 248 LKRRIEELEAELREKETELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKS 327
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                  ....*
gi 2217303388 328 FLEVL 332
Cdd:COG3206   252 GPDAL 256
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 162-343 2.30e-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: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 162 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEI-NR 240
Cdd:pfam07888  65 KRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLtQR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 241 EKEKNTQLKR---RIEELEAELREKETELKDLR-------------------------KQSEIIPQLMSECEYVSEKLEA 292
Cdd:pfam07888 145 VLERETELERmkeRAKKAGAQRKEEEAERKQLQaklqqteeelrslskefqelrnslaQRDTQVLQLQDTITTLTQKLTT 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217303388 293 AER---DNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFR 343
Cdd:pfam07888 225 AHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 98-313 2.35e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  98 LGFSSEQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAA 177
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 178 NVKKWEIELQTLRESNAR--LTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNT----QLKRR 251
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEkkisSLEKE 618

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217303388 252 IEELEAELREKETELKDLRKQSEIIPQlmsECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 313
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQ---EVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
PRK01156 PRK01156
chromosome segregation protein; Provisional
 222-352 3.93e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 222 DRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKE-------TELKDLRKQSEIIPQLMSECEYVSEKLEAAE 294
Cdd:PRK01156  190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217303388 295 RDNQNLEDKVRSLKTDIEESKYRQRHLKVE----------LKSFLEVLDGKIDDLHDFRRGLSKLGTD 352
Cdd:PRK01156  270 EKNNYYKELEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKD 337
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
180-332 4.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 180 KKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAEL 259
Cdd:PRK03918  162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217303388 260 REKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKVELKSFLEVL 332
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
223-348 4.61e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 223 RLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRkqseiipqlmSECEYVSEKLEAAERDNQNLED 302
Cdd:PRK02224  210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE----------AEIEDLRETIAETEREREELAE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2217303388 303 KVRSLKTDIEESKYRQRHLKVElksfLEVLDGKIDDLHDFRRGLSK 348
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAE----AGLDDADAEAVEARREELED 321
PRK01156 PRK01156
chromosome segregation protein; Provisional
 219-350 4.72e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 219 DENDRLRNKIDELEEQcsEINREKekntqLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQ 298
Cdd:PRK01156  626 NEANNLNNKYNEIQEN--KILIEK-----LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217303388 299 NLEDKVRSLKTDIEESKYRQRHLKVELKSfLEVLDGKIDDLHDFRRGLSKLG 350
Cdd:PRK01156  699 RLESTIEILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLREAFDKSG 749
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 218-311 4.74e-03

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


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 37.88  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 218 RDENDRLRNKIDELEEqcsEINREKEKNTQLKRRIEELEAELREKETELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 296
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 2217303388 297 NQNLEDKVRSLKTDI 311
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
161-278 5.67e-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: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  161 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES-AASVEQWKRQFSICRDENDRLRNKIDELEEQC---- 235
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLaalg 372

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217303388  236 -------------------------SEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQ 278
Cdd:COG4913    373 lplpasaeefaalraeaaallealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 184-348 5.67e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 184 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIE---------- 253
Cdd:COG1579    10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 254 ELEAELREKETELKDLRKQSEIIPQLMseceyvsEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKVELKSFLEVLD 333
Cdd:COG1579    90 EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELE 155

                         170
                  ....*....|....*
gi 2217303388 334 GKIDDLHDFRRGLSK 348
Cdd:COG1579   156 AELEELEAEREELAA 170
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 179-339 6.03e-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: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 179 VKKWEIELQTLRESNArlTTALQESAASVEQW-KRQFSIC--RDENDRLRNKIDELEEQCSEINREKEKN--TQLKRRIE 253
Cdd:cd21966     5 VQQWLSELRLMTEPEC--MTTLQSKSIAGEEDqKVKLLVSsaTDSIRKLQQRAHIISAEFDKLYRKLEKGrwKQVHPLIQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 254 ELEAELRE--KETELKDLRKQS---EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE-SKYRQRHLKVELKS 327
Cdd:cd21966    83 SLTGHIRSllQEYNATLPELPPelqQYEQRLLEICEELRTAAERSLGSKPNLEELLKLLTTLGQSfSKLVDLLLLKELQI 162

                         170
                  ....*....|..
gi 2217303388 328 FLEVLDGKIDDL 339
Cdd:cd21966   163 LVDSLEEPTSEL 174
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 224-329 7.70e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 38.13  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 224 LRNKIDELEEQCSeiNREKEKNTQlkrRIEELEAELREKETELKDLRKQ----SEIIPQLMSEceyvsekleaaERDNQN 299
Cdd:PRK05431    7 IRENPEAVKEALA--KRGFPLDVD---ELLELDEERRELQTELEELQAErnalSKEIGQAKRK-----------GEDAEA 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217303388 300 LEDKVRSLKTDIEESKYRQRHLKVELKSFL 329
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 ...
 249-305 8.39e-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: 8.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217303388 249 KRRIEELEAELREKETELKDLRkqSEIipqlmseceyvsEKLEAaerDNQNLEDKVR 305
Cdd:pfam08172  95 RQRNAELEEELRKQFETISSLR--QEI------------ASLQK---DNLKLYEKTR 134
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
220-350 9.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388 220 ENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKqsEIIPQLMSECEYVSEKLEAAER-DNQ 298
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK--ELEELGFESVEELEERLKELEPfYNE 603

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217303388 299 NLEdkVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKLG 350
Cdd:PRK03918  604 YLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 176-313 9.60e-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: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303388  176 AANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICR----DENDRLRNKIDELEEQCSEINRE----KEKNTQ 247
Cdd:pfam12128  240 RPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNGElsaaDAAVAK 319

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217303388  248 LKRRIEELEAELREKETE-LKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 313
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH