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Conserved domains on  [gi|1958654096|ref|XP_038957083|]
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pleckstrin homology domain-containing family A member 7 isoform X20 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 15-44 1.74e-12

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13248:

Pssm-ID: 473070  Cd Length: 104  Bit Score: 64.60  E-value: 1.74e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958654096   15 AEHSGMRTYYFSADTLEDMNAWVRAMNQAA 44
Cdd:cd13248     75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 665-771 2.22e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSLSPTESKPAlQPSPPTSPVRTPL----------EVRLFPQLQTYVPY---RPHPPQLRKVVSPL 731
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPPPSLplggsvapggDVRRRPPSRSPAAKpaaPARPPVRRLARPAV 2891

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958654096  732 QSPTKATPQAEDEaPPRPPLPELYSPEDQPPAVPPLPREA 771
Cdd:PHA03247  2892 SRSTESFALPPDQ-PERPPQPQAPPPPQPQPQPPPPPQPQ 2930
CCDC90-like super family cl06708
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 538-638 3.36e-04

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


The actual alignment was detected with superfamily member pfam07798:

Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 42.50  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  538 IRALKEN---KDQLESVLEVLHRQTEQ-----YRD--QPQHLEKITCQQRllqEDLVHIRAEL-CRESTEMENAWNEYLK 606
Cdd:pfam07798    7 VRQLEEAgftEEQAEAIMKALRDLLNDslenvSKDlvTKEDLENETYLQK---ADLAELRSELqILEKSEFAALRSENEK 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958654096  607 LEKDVEQLKQTLQEQHRRAfffqeKSQIQKDL 638
Cdd:pfam07798   84 LRRELEKLKQRLREEITKL-----KADVRLDL 110
 
Name Accession Description Interval E-value
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 15-44 1.74e-12

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 64.60  E-value: 1.74e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958654096   15 AEHSGMRTYYFSADTLEDMNAWVRAMNQAA 44
Cdd:cd13248     75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
PHA03247 PHA03247
large tegument protein UL36; Provisional
 665-771 2.22e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSLSPTESKPAlQPSPPTSPVRTPL----------EVRLFPQLQTYVPY---RPHPPQLRKVVSPL 731
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPPPSLplggsvapggDVRRRPPSRSPAAKpaaPARPPVRRLARPAV 2891

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958654096  732 QSPTKATPQAEDEaPPRPPLPELYSPEDQPPAVPPLPREA 771
Cdd:PHA03247  2892 SRSTESFALPPDQ-PERPPQPQAPPPPQPQPQPPPPPQPQ 2930
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 671-771 1.27e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 43.62  E-value: 1.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096   671 PLFPHPSVPSLSPTESKPALQPSPPTSPVrtplevrlfpQLQTYVPYRPHPPQlrkvvsPLQSPtkatPQAEDEAPPRPP 750
Cdd:smart00818   72 PLMPVPGQHSMTPTQHHQPNLPQPAQQPF----------QPQPLQPPQPQQPM------QPQPP----VHPIPPLPPQPP 131

                            90       100
                    ....*....|....*....|.
gi 1958654096   751 LPELYSPEDQPPAVPPLPREA 771
Cdd:smart00818  132 LPPMFPMQPLPPLLPDLPLEA 152
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 538-638 3.36e-04

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 42.50  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  538 IRALKEN---KDQLESVLEVLHRQTEQ-----YRD--QPQHLEKITCQQRllqEDLVHIRAEL-CRESTEMENAWNEYLK 606
Cdd:pfam07798    7 VRQLEEAgftEEQAEAIMKALRDLLNDslenvSKDlvTKEDLENETYLQK---ADLAELRSELqILEKSEFAALRSENEK 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958654096  607 LEKDVEQLKQTLQEQHRRAfffqeKSQIQKDL 638
Cdd:pfam07798   84 LRRELEKLKQRLREEITKL-----KADVRLDL 110
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
526-653 1.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  526 EQDRILQDLEDKIRALKENKDQLESVLEVLHRQTEQYRDQPQHLEKITCQQRLLQEDLVHIRAELC-RESTEMENAWNEY 604
Cdd:COG4717    122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEEL 201

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958654096  605 LKLEKDVEQLKQTLQEQHrrafffQEKSQIQKDLWRIEDVMAGLSVNKE 653
Cdd:COG4717    202 EELQQRLAELEEELEEAQ------EELEELEEELEQLENELEAAALEER 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 531-654 3.14e-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: 41.97  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  531 LQDLEDKIRALKENKDQLESVLEVLHRQTEQYRDQPQHLEKITCQqrlLQEDLVHIRAELCRESTEMENAWNEYLKLEKD 610
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE---LEEKLEELKEELESLEAELEELEAELEELESR 373

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958654096  611 VEQLKQTLQEQhRRAFF--FQEKSQIQKDLWRIEDVMAGLSVNKEN 654
Cdd:TIGR02168  374 LEELEEQLETL-RSKVAqlELQIASLNNEIERLEARLERLEDRRER 418
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 665-790 5.57e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.91  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSlSPTESKPALQPSPPT-------SPVRTPLEVRlfPQLQTYVPY---RPHPPQLRKVVSPLQSP 734
Cdd:NF033839   363 PEVKPQPEKPKPEVKP-QPETPKPEVKPQPEKpkpevkpQPEKPKPEVK--PQPEKPKPEvkpQPEKPKPEVKPQPEKPK 439

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958654096  735 TKATPQAEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERK 790
Cdd:NF033839   440 PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKK 495
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 671-776 6.31e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  671 PLFPHPSVPSLSPTESKPAL--QPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDEAPPR 748
Cdd:pfam03154  187 PPPGTTQAATAGPTPSAPSVppQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPL 266

                           90       100
                   ....*....|....*....|....*...
gi 1958654096  749 PPlPELYSPedQPPAVPPLPREATIIRH 776
Cdd:pfam03154  267 PQ-PSLHGQ--MPPMPHSLQTGPSHMQH 291
PRK12704 PRK12704
phosphodiesterase; Provisional
 528-649 7.81e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  528 DRILQDLEDKIRALKENKdQLESVLEVLHRQTE---QYRDQPQHLEKItcQQRLLQ--EDLVHIRAELCRESTEMENAWN 602
Cdd:PRK12704    41 KRILEEAKKEAEAIKKEA-LLEAKEEIHKLRNEfekELRERRNELQKL--EKRLLQkeENLDRKLELLEKREEELEKKEK 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958654096  603 EYLKLEKDVEQLKQTLQEQHrrafffqeKSQIQKdLWRIedvmAGLS 649
Cdd:PRK12704   118 ELEQKQQELEKKEEELEELI--------EEQLQE-LERI----SGLT 151
 
Name Accession Description Interval E-value
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 15-44 1.74e-12

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 64.60  E-value: 1.74e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958654096   15 AEHSGMRTYYFSADTLEDMNAWVRAMNQAA 44
Cdd:cd13248     75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
PHA03247 PHA03247
large tegument protein UL36; Provisional
 665-771 2.22e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSLSPTESKPAlQPSPPTSPVRTPL----------EVRLFPQLQTYVPY---RPHPPQLRKVVSPL 731
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPPPSLplggsvapggDVRRRPPSRSPAAKpaaPARPPVRRLARPAV 2891

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958654096  732 QSPTKATPQAEDEaPPRPPLPELYSPEDQPPAVPPLPREA 771
Cdd:PHA03247  2892 SRSTESFALPPDQ-PERPPQPQAPPPPQPQPQPPPPPQPQ 2930
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 671-771 1.27e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 43.62  E-value: 1.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096   671 PLFPHPSVPSLSPTESKPALQPSPPTSPVrtplevrlfpQLQTYVPYRPHPPQlrkvvsPLQSPtkatPQAEDEAPPRPP 750
Cdd:smart00818   72 PLMPVPGQHSMTPTQHHQPNLPQPAQQPF----------QPQPLQPPQPQQPM------QPQPP----VHPIPPLPPQPP 131

                            90       100
                    ....*....|....*....|.
gi 1958654096   751 LPELYSPEDQPPAVPPLPREA 771
Cdd:smart00818  132 LPPMFPMQPLPPLLPDLPLEA 152
PHA03247 PHA03247
large tegument protein UL36; Provisional
 671-765 1.40e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  671 PLFPHPSVPSLS---------PTESKPALQPSP--PTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATP 739
Cdd:PHA03247  2840 PPPPGPPPPSLPlggsvapggDVRRRPPSRSPAakPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP 2919

                           90       100
                   ....*....|....*....|....*.
gi 1958654096  740 QAEDEAPPRPPLPELYSPEDQPPAVP 765
Cdd:PHA03247  2920 QPQPPPPPQPQPPPPPPPRPQPPLAP 2945
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
 21-51 1.42e-04

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270075  Cd Length: 110  Bit Score: 42.40  E-value: 1.42e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958654096   21 RTYYFSADTLEDMNAWVRAMNQAAQVLSRSS 51
Cdd:cd13255     76 RTFYVQADSKAEMESWISAINLARQALRATI 106
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
 14-45 3.31e-04

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269962  Cd Length: 114  Bit Score: 41.24  E-value: 3.31e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958654096   14 QAEHSGMRTYYFSADTLEDMNAWVRAMNQAAQ 45
Cdd:cd01260     80 KACHPKIKTFYFAAENLDDMNKWLSKLNMAIN 111
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 538-638 3.36e-04

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 42.50  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  538 IRALKEN---KDQLESVLEVLHRQTEQ-----YRD--QPQHLEKITCQQRllqEDLVHIRAEL-CRESTEMENAWNEYLK 606
Cdd:pfam07798    7 VRQLEEAgftEEQAEAIMKALRDLLNDslenvSKDlvTKEDLENETYLQK---ADLAELRSELqILEKSEFAALRSENEK 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958654096  607 LEKDVEQLKQTLQEQHRRAfffqeKSQIQKDL 638
Cdd:pfam07798   84 LRRELEKLKQRLREEITKL-----KADVRLDL 110
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 688-771 9.83e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 43.26  E-value: 9.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  688 PALQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPlqsPTKATPQAEDEAPPRPPlpelyspedQPPAVPPL 767
Cdd:PRK14950   364 PAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRET---ATPPPVPPRPVAPPVPH---------TPESAPKL 431


                   ....
gi 1958654096  768 PREA 771
Cdd:PRK14950   432 TRAA 435
PHA03247 PHA03247
large tegument protein UL36; Provisional
 665-768 1.22e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLfphPSVPSLSPTESKPALQPSPPTSPVrtPLevrlfPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDE 744
Cdd:PHA03247  2867 PSRSPAAK---PAAPARPPVRRLARPAVSRSTESF--AL-----PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936

                           90       100
                   ....*....|....*....|....
gi 1958654096  745 APPRPPLPELYSPEDQPPAVPPLP 768
Cdd:PHA03247  2937 PRPQPPLAPTTDPAGAGEPSGAVP 2960
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
526-653 1.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  526 EQDRILQDLEDKIRALKENKDQLESVLEVLHRQTEQYRDQPQHLEKITCQQRLLQEDLVHIRAELC-RESTEMENAWNEY 604
Cdd:COG4717    122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEEL 201

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958654096  605 LKLEKDVEQLKQTLQEQHrrafffQEKSQIQKDLWRIEDVMAGLSVNKE 653
Cdd:COG4717    202 EELQQRLAELEEELEEAQ------EELEELEEELEQLENELEAAALEER 244
PHA03378 PHA03378
EBNA-3B; Provisional
 656-770 2.68e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  656 RVLVGSVKNPERKTVPLFPHPSVP-SLSPTESKPALQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSP 734
Cdd:PHA03378   612 QSHIPETSAPRQWPMPLRPIPMRPlRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAP 691

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958654096  735 TKATPqaedeaPPRPPLPElyspedQPPAVPPLPRE 770
Cdd:PHA03378   692 GTMQP------PPRAPTPM------RPPAAPPGRAQ 715
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 531-654 3.14e-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: 41.97  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  531 LQDLEDKIRALKENKDQLESVLEVLHRQTEQYRDQPQHLEKITCQqrlLQEDLVHIRAELCRESTEMENAWNEYLKLEKD 610
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE---LEEKLEELKEELESLEAELEELEAELEELESR 373

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958654096  611 VEQLKQTLQEQhRRAFF--FQEKSQIQKDLWRIEDVMAGLSVNKEN 654
Cdd:TIGR02168  374 LEELEEQLETL-RSKVAqlELQIASLNNEIERLEARLERLEDRRER 418
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 23-47 4.08e-03

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 38.41  E-value: 4.08e-03
                           10        20
                   ....*....|....*....|....*
gi 1958654096   23 YYFSADTLEDMNAWVRAMNQAAQVL 47
Cdd:cd01263     96 VLLSADTKEERIEWLSALNQTLADL 120
PHA03247 PHA03247
large tegument protein UL36; Provisional
 665-789 4.63e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSLSPTESKPALQPSPPTSPvrtPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDE 744
Cdd:PHA03247  2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958654096  745 APPRPPLPELYSPEDQPPAVP----PLPREATIIRHTSVRGLKRQSDER 789
Cdd:PHA03247  2955 PSGAVPQPWLGALVPGRVAVPrfrvPQPAPSREAPASSTPPLTGHSLSR 3003
PHA03379 PHA03379
EBNA-3A; Provisional
 665-799 4.82e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.20  E-value: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVP---SLSPTESKPALQ-PSPPTSPVRTPLEVRLFP------QLQTYVPYRPHPPQLRKVVSPLQSP 734
Cdd:PHA03379   526 PQPMPVEPVPVPTVAlerPVCPAPPLIAMQgPGETSGIVRVRERWRPAPwtpnppRSPSQMSVRDRLARLRAEAQPYQAS 605

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958654096  735 TKATPQAEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDER--KRDREQGQCV 799
Cdd:PHA03379   606 VEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVPAMQPQYFDLplQQPISQGAPL 672
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 665-790 5.57e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.91  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSlSPTESKPALQPSPPT-------SPVRTPLEVRlfPQLQTYVPY---RPHPPQLRKVVSPLQSP 734
Cdd:NF033839   363 PEVKPQPEKPKPEVKP-QPETPKPEVKPQPEKpkpevkpQPEKPKPEVK--PQPEKPKPEvkpQPEKPKPEVKPQPEKPK 439

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958654096  735 TKATPQAEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERK 790
Cdd:NF033839   440 PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKK 495
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
529-621 5.99e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.44  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  529 RILQDLEDKIRALKENKDQLESV---LEVLHRQTEQYRDQ----PQHLEKItcQQRL-----LQ-------EDLVHIRAE 589
Cdd:COG0497    251 RALERLAEYDPSLAELAERLESAlieLEEAASELRRYLDSlefdPERLEEV--EERLallrrLArkygvtvEELLAYAEE 328

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958654096  590 LCRESTEMENAWNEYLKLEKDVEQLKQTLQEQ 621
Cdd:COG0497    329 LRAELAELENSDERLEELEAELAEAEAELLEA 360
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 671-776 6.31e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  671 PLFPHPSVPSLSPTESKPAL--QPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDEAPPR 748
Cdd:pfam03154  187 PPPGTTQAATAGPTPSAPSVppQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPL 266

                           90       100
                   ....*....|....*....|....*...
gi 1958654096  749 PPlPELYSPedQPPAVPPLPREATIIRH 776
Cdd:pfam03154  267 PQ-PSLHGQ--MPPMPHSLQTGPSHMQH 291
PHA03247 PHA03247
large tegument protein UL36; Provisional
 665-773 6.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  665 PERKTVPLFPHPSVPSLSPTESKPALQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDE 744
Cdd:PHA03247  2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821

                           90       100
                   ....*....|....*....|....*....
gi 1958654096  745 APPRPPLPELYSPEDQPPAVPPLPREATI 773
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 674-826 6.98e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  674 PHPSVPSLSPTESKPALQPSPPTSPVRTPLEVRLfPQLQTYVPYRPHPPQLRKVVSPLQSPTKATP-QAEDEAPPRPPLP 752
Cdd:PRK10263   382 QQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQP-AQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwQAEEQQSTFAPQS 460

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958654096  753 --ELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDREQGQCVNgdlKVELRSYVSEPELASFSGDVPRP 826
Cdd:PRK10263   461 tyQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFE---EVEEKRAREREQLAAWYQPIPEP 533
PRK12704 PRK12704
phosphodiesterase; Provisional
 528-649 7.81e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  528 DRILQDLEDKIRALKENKdQLESVLEVLHRQTE---QYRDQPQHLEKItcQQRLLQ--EDLVHIRAELCRESTEMENAWN 602
Cdd:PRK12704    41 KRILEEAKKEAEAIKKEA-LLEAKEEIHKLRNEfekELRERRNELQKL--EKRLLQkeENLDRKLELLEKREEELEKKEK 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958654096  603 EYLKLEKDVEQLKQTLQEQHrrafffqeKSQIQKdLWRIedvmAGLS 649
Cdd:PRK12704   118 ELEQKQQELEKKEEELEELI--------EEQLQE-LERI----SGLT 151
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 671-768 8.06e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  671 PLFPHPSVPSLSPTESKPALQPSPPTSPvRTPlEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDEAPPRPP 750
Cdd:PRK10263   339 PVTQTPPVASVDVPPAQPTVAWQPVPGP-QTG-EPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPA 416

                           90
                   ....*....|....*...
gi 1958654096  751 LPELYSPEDQPPAVPPLP 768
Cdd:PRK10263   417 QQPYYAPAPEQPAQQPYY 434
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 643-766 9.35e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 39.94  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654096  643 DVMAGLSVnkenYRVLVGSVKNPERKTVPL--FPHPSVPSLSPTESKPALQPSPPTSPVRTPlevRLFPQlQTYVPYRPH 720
Cdd:PHA03291   138 RAVVGLYV----LRVWVEGATNASLFPLGLaaFPAEGTLAAPPLGEGSADGSCDPALPLSAP---RLGPA-DVFVPATPR 209

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958654096  721 PPQlRKVVSPLQSPTKATPQAEDEAPPRPPLPELYSP--------EDQPPAVPP 766
Cdd:PHA03291   210 PTP-RTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPqagttpeaEGTPAPPTP 262
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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