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Conserved domains on  [gi|312839860|ref|NP_001186164|]
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spectrin beta chain, non-erythrocytic 4 isoform sigma6 [Mus musculus]

Protein Classification

spectrin repeat-containing protein; PH domain-containing protein( domain architecture ID 10075188)

spectrin repeat-containing protein such as plectin, a prototypical plakin that tethers intermediate filaments to membrane-associated complexes| PH (pleckstrin homology) domain-containing protein similar to Caenorhabditis elegans protein C15H7.4

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 1098-1202 5.63e-51

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. 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: 269975  Cd Length: 106  Bit Score: 174.72  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1098 HEGFLLRKRELDA-NRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQT 1176
Cdd:cd10571     1 MEGFLERKHEWESgGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80

                          90       100
                  ....*....|....*....|....*.
gi 312839860 1177 QDGSEFLLQAKDEEEMNGWLEAVANS 1202
Cdd:cd10571    81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 192-403 6.24e-29

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 115.62  E-value: 6.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  192 ELHQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRG 271
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  272 QEQLQSAWTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEE 351
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312839860  352 SIAQLSRQCRALLEMGHPDS-EQISRRQSQVDRLYVALKELGEERRVSLEQQY 403
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 298-510 4.83e-26

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 107.15  E-value: 4.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  298 QVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRR 377
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  378 QSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGR 457
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEL-EAHE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 312839860  458 ERLAAVNQMVDELIE-CGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASR 510
Cdd:cd00176   160 PRLKSLNELAEELLEeGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 619-786 2.57e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.22  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  619 DALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQ 698
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  699 LDKLGSRKEEVSEKWDRHWEWLQQMLEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEE 778
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160


                  ....*...
gi 312839860  779 RFSSLRRL 786
Cdd:cd00176   161 RLKSLNEL 168
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2-190 2.58e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    2 LMARDGTREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQ 81
Cdd:cd00176    22 LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   82 LFEASKADQLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQ--ASK 159
Cdd:cd00176   102 LEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpDAD 181

                         170       180       190
                  ....*....|....*....|....*....|.
gi 312839860  160 ELVGERQSAVGERLVRLLEPLQERRRLLLAS 190
Cdd:cd00176   182 EEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 510-609 7.64e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


:

Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.77  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   510 RELHKFFSDARELQGQIEEKRrrlPRLTAPPEPR--PSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTvYAGEHAE 587
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKE---ALLSSEDYGKdlESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASE 76

                           90       100
                   ....*....|....*....|..
gi 312839860   588 AIASREQEVLQGWKELLAACED 609
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAE 98
 
Name Accession Description Interval E-value
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 1098-1202 5.63e-51

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. 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: 269975  Cd Length: 106  Bit Score: 174.72  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1098 HEGFLLRKRELDA-NRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQT 1176
Cdd:cd10571     1 MEGFLERKHEWESgGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80

                          90       100
                  ....*....|....*....|....*.
gi 312839860 1177 QDGSEFLLQAKDEEEMNGWLEAVANS 1202
Cdd:cd10571    81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 192-403 6.24e-29

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 115.62  E-value: 6.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  192 ELHQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRG 271
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  272 QEQLQSAWTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEE 351
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312839860  352 SIAQLSRQCRALLEMGHPDS-EQISRRQSQVDRLYVALKELGEERRVSLEQQY 403
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 298-510 4.83e-26

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 107.15  E-value: 4.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  298 QVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRR 377
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  378 QSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGR 457
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEL-EAHE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 312839860  458 ERLAAVNQMVDELIE-CGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASR 510
Cdd:cd00176   160 PRLKSLNELAEELLEeGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 619-786 2.57e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.22  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  619 DALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQ 698
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  699 LDKLGSRKEEVSEKWDRHWEWLQQMLEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEE 778
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160


                  ....*...
gi 312839860  779 RFSSLRRL 786
Cdd:cd00176   161 RLKSLNEL 168
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 1098-1204 1.04e-21

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 91.72  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  1098 HEGFLLRKRELDANRKSS---NRSWVSLYCVLSKGELGFYKDSKGPASGGT-------HGGEPLLSLHKATSEVASDYKK 1167
Cdd:pfam15410    2 KKGIVMRKCCFESKGKKTprgKRSWKMVYAVLKDLVLYLYKDEHPPESSQFedkkslkNAPVGKIRLHHALATPAPDYTK 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 312839860  1168 KKHVFKLQTQDGSEFLLQAKDEEEMNGWLEAVaNSVA 1204
Cdd:pfam15410   82 KSHVFRLQTADGAEYLFQTGSPKELQEWVDTL-NYWA 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2-190 2.58e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    2 LMARDGTREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQ 81
Cdd:cd00176    22 LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   82 LFEASKADQLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQ--ASK 159
Cdd:cd00176   102 LEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpDAD 181

                         170       180       190
                  ....*....|....*....|....*....|.
gi 312839860  160 ELVGERQSAVGERLVRLLEPLQERRRLLLAS 190
Cdd:cd00176   182 EEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
194-294 7.75e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 74.29  E-value: 7.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    194 HQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRGQE 273
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 312839860    274 QLQSAWTGLREAAERRQQTLD 294
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1096-1198 1.73e-15

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 73.35  E-value: 1.73e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   1096 VQHEGFLLRKReldanrKSSNRSWVSLYCVLSKGELGFYKDSKGpASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQ 1175
Cdd:smart00233    1 VIKEGWLYKKS------GGGKKSWKKRYFVLFNSTLLYYKSKKD-KKSYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIK 73

                            90       100
                    ....*....|....*....|...
gi 312839860   1176 TQDGSEFLLQAKDEEEMNGWLEA 1198
Cdd:smart00233   74 TSDRKTLLLQAESEEEREKWVEA 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 191-295 3.51e-15

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 72.35  E-value: 3.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   191 KELHQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRR 270
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                           90       100
                   ....*....|....*....|....*
gi 312839860   271 GQEQLQSAWTGLREAAERRQQTLDA 295
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
406-506 2.53e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.97  E-value: 2.53e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    406 YQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGRERLAAVNQMVDELIECGHTAAATMAEWK 485
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAEL-EAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|.
gi 312839860    486 DGLNEAWAELLELMGTRAQLL 506
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
622-721 5.85e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.20  E-value: 5.85e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    622 RFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQLDK 701
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90       100
                    ....*....|....*....|
gi 312839860    702 LGSRKEEVSEKWDRHWEWLQ 721
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 619-722 1.19e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 65.42  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   619 DALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQ 698
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81

                           90       100
                   ....*....|....*....|....
gi 312839860   699 LDKLGSRKEEVSEKWDRHWEWLQQ 722
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 403-506 8.67e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 62.72  E-value: 8.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   403 YWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGRERLAAVNQMVDELIECGHTAAATMA 482
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAEL-AAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                           90       100
                   ....*....|....*....|....
gi 312839860   483 EWKDGLNEAWAELLELMGTRAQLL 506
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
2-82 3.91e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 3.91e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860      2 LMARDGTREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQ 81
Cdd:smart00150   20 LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEELNERWEELKELAEERRQK 99


                    .
gi 312839860     82 L 82
Cdd:smart00150  100 L 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 21-84 3.50e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 49.62  E-value: 3.50e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312839860    21 RHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFE 84
Cdd:pfam00435   42 KHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 510-609 7.64e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.77  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   510 RELHKFFSDARELQGQIEEKRrrlPRLTAPPEPR--PSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTvYAGEHAE 587
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKE---ALLSSEDYGKdlESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASE 76

                           90       100
                   ....*....|....*....|..
gi 312839860   588 AIASREQEVLQGWKELLAACED 609
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAE 98
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 17-768 1.28e-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: 49.67  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    17 KRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQL--------FEASKA 88
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqILRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    89 DQLVQSFAELDKRLLHMESQLQDV---------DPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASK 159
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELaeelaeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   160 ELVGERQSAVGERLVRLLEPLQERRRLLLASKELHQVAHDlDDELAWVQERLPL--AMQTERGTGLQAVQQHIKKNQGLR 237
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-EAELKELQAELEEleEELEELQEELERLEEALEELREEL 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   238 REIQahgprlEEVLERAGVLASLRSpEAEAVRRGQEQLQSAWTGLREAAERRQQ------TLDAAFQVEQYYfdVAEVEA 311
Cdd:TIGR02168  471 EEAE------QALDAAERELAQLQA-RLDSLERLQENLEGFSEGVKALLKNQSGlsgilgVLSELISVDEGY--EAAIEA 541

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   312 WLGE--QELLMMSEDKGKDEQstlqllkkhlqleqgvenyeESIAQLSRQCRALLEM-----GHPDSEQISRRQSQVDRL 384
Cdd:TIGR02168  542 ALGGrlQAVVVENLNAAKKAI--------------------AFLKQNELGRVTFLPLdsikgTEIQGNDREILKNIEGFL 601

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   385 YVALKELGEERRVSLEQQYWLYQLsRQVDELEHWIAEkevvagSPELGQDFEHVSVLQEKFSEFASETGTAGRERLAAVN 464
Cdd:TIGR02168  602 GVAKDLVKFDPKLRKALSYLLGGV-LVVDDLDNALEL------AKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   465 --QMVDELIECGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTAPPEP 542
Cdd:TIGR02168  675 rrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   543 RPSASSMQRT------------LRAFEHDLQLLVSQVRQLQEGAAQLRTvyAGEHAEAIASREQEVLQGWKELLAACEDA 610
Cdd:TIGR02168  755 ELTELEAEIEeleerleeaeeeLAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERR 832

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   611 RLHVSSTADALrfHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVlmNYHQGLKTELEARVPELATCQELGRSLLLNKSA 690
Cdd:TIGR02168  833 IAATERRLEDL--EEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNERASLEEALALLRSELEELSEELRELES 908

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312839860   691 MADEIQAQLDKLGSRKEEVSEKWDRhwewLQQMLevhQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEA 768
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEG----LEVRI---DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SPEC smart00150
Spectrin repeats;
513-609 3.86e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 3.86e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    513 HKFFSDARELQGQIEEKRRRLpRLTAPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVyAGEHAEAIASR 592
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78

                            90
                    ....*....|....*..
gi 312839860    593 EQEVLQGWKELLAACED 609
Cdd:smart00150   79 LEELNERWEELKELAEE 95
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-392 7.91e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   27 AELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFEASKADQLVQSFAELDKRLLhME 106
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-LL 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  107 SQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASKELVGERQSAVGERLVRLLEPLQERRRL 186
Cdd:COG1196   497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  187 LLASKELHQVAHDLDDELAWVQERLPLAMQTERGtgLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAE 266
Cdd:COG1196   577 LPLDKIRARAALAAALARGAIGAAVDLVASDLRE--ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  267 AVRRGQEQLQSAWTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGV 346
Cdd:COG1196   655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 312839860  347 ENYEESIAQLSRQCRALLEMGHPDSEQISRRQSQVDRLYVALKELG 392
Cdd:COG1196   735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 121-631 1.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  121 VNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASKELVGERQSAVGERLVRLLEPLQERRRLLLASKE--LHQVAH 198
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELArlEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  199 DLDDELAWVQERlpLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRGQEQLQSA 278
Cdd:COG1196   307 LEERRRELEERL--EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  279 WTGLREAAERRQQTLDAAFQVEQyyfdvAEVEAwlgEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSR 358
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEE-----AEEAL---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  359 QCRALLemghpdsEQISRRQSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQdfeHV 438
Cdd:COG1196   457 EEEALL-------ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG---AV 526

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  439 SVLQEKfsEFASETGTAGRERLAAVNQMVDELiecghTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSD 518
Cdd:COG1196   527 AVLIGV--EAAYEAALEAALAAALQNIVVEDD-----EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  519 ARELQGQIEEKRRRLPRL--------TAPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVYAGEHAEAIA 590
Cdd:COG1196   600 AVDLVASDLREADARYYVlgdtllgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 312839860  591 SREQEVLQGWKELLAACEDARLHVSSTADALRFHSQARDLL 631
Cdd:COG1196   680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
PRK11281 PRK11281
mechanosensitive channel MscK;
27-130 5.49e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   27 AELAQNKEWLEKIEREGQQLMQEKPELAASVRKklgeIRQCWAELES---TTQAKARQLFEAskadqlvQSFAELDKRLL 103
Cdd:PRK11281   63 QDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK----LRQAQAELEAlkdDNDEETRETLST-------LSLRQLESRLA 131

                          90       100
                  ....*....|....*....|....*..
gi 312839860  104 HMESQLQDVDpgGDLATVNSQLKKLQS 130
Cdd:PRK11281  132 QTLDQLQNAQ--NDLAEYNSQLVSLQT 156
PTZ00121 PTZ00121
MAEBL; Provisional
 30-469 6.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   30 AQNKEWLEKIEREGQQLMQEKPEL--AASVRKKLGEIRQCWAELESTTQAKaRQLFEASKADQLVQSfAELDKRLLHMES 107
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAK-KKAEEAKKADEAKKK-AEEAKKAEEAKK 1464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  108 QLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAAlpleqasKELVGERQSAVGERLVRLLEPLQERRRLL 187
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-------KKKADEAKKAEEAKKADEAKKAEEAKKAD 1537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  188 LASK-ELHQVAhdldDELAWVQErlpLAMQTERGTGLQAVQQHIKKNQGLRR-EI--QAHGPRLEEVLEragVLASLRSP 263
Cdd:PTZ00121 1538 EAKKaEEKKKA----DELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKaEEakKAEEARIEEVMK---LYEEEKKM 1607

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  264 EAEAVRRGQEQLQSAwTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAwlGEQELLMMSEDKGKDEQSTLQLLKKHLQLE 343
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  344 QGVENYEESIAQLSRQCRallemghpDSEQISRRQSQVDRLYVALKELGEERRVSLEqqywlyQLSRQVDElehwiaEKE 423
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAK--------KAEELKKKEAEEKKKAEELKKAEEENKIKAE------EAKKEAEE------DKK 1744

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 312839860  424 vvaGSPELGQDFEHVSVLQEKFSEFASETGTAGRERLAAVNQMVDE 469
Cdd:PTZ00121 1745 ---KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
 
Name Accession Description Interval E-value
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 1098-1202 5.63e-51

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. 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: 269975  Cd Length: 106  Bit Score: 174.72  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1098 HEGFLLRKRELDA-NRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQT 1176
Cdd:cd10571     1 MEGFLERKHEWESgGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80

                          90       100
                  ....*....|....*....|....*.
gi 312839860 1177 QDGSEFLLQAKDEEEMNGWLEAVANS 1202
Cdd:cd10571    81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 192-403 6.24e-29

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 115.62  E-value: 6.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  192 ELHQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRG 271
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  272 QEQLQSAWTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEE 351
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312839860  352 SIAQLSRQCRALLEMGHPDS-EQISRRQSQVDRLYVALKELGEERRVSLEQQY 403
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 298-510 4.83e-26

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 107.15  E-value: 4.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  298 QVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRR 377
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  378 QSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGR 457
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEL-EAHE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 312839860  458 ERLAAVNQMVDELIE-CGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASR 510
Cdd:cd00176   160 PRLKSLNELAEELLEeGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 619-786 2.57e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.22  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  619 DALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQ 698
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  699 LDKLGSRKEEVSEKWDRHWEWLQQMLEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEE 778
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160


                  ....*...
gi 312839860  779 RFSSLRRL 786
Cdd:cd00176   161 RLKSLNEL 168
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 87-296 2.20e-23

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 99.83  E-value: 2.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   87 KADQLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLE-QASKELVGER 165
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEgHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  166 QSAVGERLVRLLEPLQERRRLLLASKELHQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGP 245
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 312839860  246 RLEEVLERAGVLASLRSPEA-EAVRRGQEQLQSAWTGLREAAERRQQTLDAA 296
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 511-724 6.83e-23

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 98.29  E-value: 6.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  511 ELHKFFSDARELQGQIEEKRRRLPRlTAPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVYAgEHAEAIA 590
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  591 SREQEVLQGWKELLAACEDARLHVSSTADALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEAR 670
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 312839860  671 VPELATCQELGRSLLLNKS-AMADEIQAQLDKLGSRKEEVSEKWDRHWEWLQQML 724
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 1098-1204 6.92e-23

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. 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: 270107  Cd Length: 126  Bit Score: 95.09  E-value: 6.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1098 HEGFLLRKRELDANRKSS---NRSWVSLYCVLSKGELGFYKDSKGPASGG-THGGEPLLSLHKATSEVASDYKKKKHVFK 1173
Cdd:cd13295     8 KKGYLMRKCCADPDGKKTpfgKRGWKMFYATLKGLVLYLHKDEYGCKKALrYESLRNAISVHHSLATKATDYTKKPHVFR 87

                          90       100       110
                  ....*....|....*....|....*....|.
gi 312839860 1174 LQTQDGSEFLLQAKDEEEMNGWLEAVaNSVA 1204
Cdd:cd13295    88 LRTADWREYLFQASDTKEMQSWIEAI-NLVA 117
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 1098-1204 1.04e-21

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 91.72  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  1098 HEGFLLRKRELDANRKSS---NRSWVSLYCVLSKGELGFYKDSKGPASGGT-------HGGEPLLSLHKATSEVASDYKK 1167
Cdd:pfam15410    2 KKGIVMRKCCFESKGKKTprgKRSWKMVYAVLKDLVLYLYKDEHPPESSQFedkkslkNAPVGKIRLHHALATPAPDYTK 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 312839860  1168 KKHVFKLQTQDGSEFLLQAKDEEEMNGWLEAVaNSVA 1204
Cdd:pfam15410   82 KSHVFRLQTADGAEYLFQTGSPKELQEWVDTL-NYWA 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 405-609 2.28e-21

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 93.66  E-value: 2.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  405 LYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGRERLAAVNQMVDELIECGHTAAATMAEW 484
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL-AAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  485 KDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTAPPEPrPSASSMQRTLRAFEHDLQLLV 564
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDL-ESVEELLKKHKELEEELEAHE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 312839860  565 SQVRQLQEGAAQLRTVYAGEHAEAIASREQEVLQGWKELLAACED 609
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 1099-1205 2.67e-19

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. 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: 270053  Cd Length: 110  Bit Score: 84.26  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRKRELDANRKSsNRSWVSLYCVLSKGELGFYKDSKGPASGGTHGGEPLLS--LHKATSEVASDYKKKKHVFKLQT 1176
Cdd:cd13233     3 QGLLNKTKIAENGKKL-RKNWSTSWVVLTSSHLLFYKDAKSAAKSGNPYSKPESSvdLRGASIEWAKEKSSRKNVFQIST 81

                          90       100
                  ....*....|....*....|....*....
gi 312839860 1177 QDGSEFLLQAKDEEEMNGWLEAVANSVAE 1205
Cdd:cd13233    82 VTGTEFLLQSDNDTEIREWFDAIKAVIQR 110
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 1099-1205 2.99e-19

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. 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: 269955  Cd Length: 113  Bit Score: 84.34  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRKRELDAN-RKSSNRSWVSLYCVLSKGELGFYKDSK--GPASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQ 1175
Cdd:cd01253     3 EGWLHYKQIVTDKgKRVSDRSWKQAWAVLRGHSLYLYKDKReqTPALSIELGSEQRISIRGCIVDIAYSYTKRKHVFRLT 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 312839860 1176 TQDGSEFLLQAKDEEEMNGWLEAV-ANSVAE 1205
Cdd:cd01253    83 TSDFSEYLFQAEDRDDMLGWIKAIqENSNAE 113
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2-190 2.58e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    2 LMARDGTREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQ 81
Cdd:cd00176    22 LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   82 LFEASKADQLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQ--ASK 159
Cdd:cd00176   102 LEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpDAD 181

                         170       180       190
                  ....*....|....*....|....*....|.
gi 312839860  160 ELVGERQSAVGERLVRLLEPLQERRRLLLAS 190
Cdd:cd00176   182 EEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
194-294 7.75e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 74.29  E-value: 7.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    194 HQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRGQE 273
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 312839860    274 QLQSAWTGLREAAERRQQTLD 294
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1096-1198 1.73e-15

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 73.35  E-value: 1.73e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   1096 VQHEGFLLRKReldanrKSSNRSWVSLYCVLSKGELGFYKDSKGpASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQ 1175
Cdd:smart00233    1 VIKEGWLYKKS------GGGKKSWKKRYFVLFNSTLLYYKSKKD-KKSYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIK 73

                            90       100
                    ....*....|....*....|...
gi 312839860   1176 TQDGSEFLLQAKDEEEMNGWLEA 1198
Cdd:smart00233   74 TSDRKTLLLQAESEEEREKWVEA 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 191-295 3.51e-15

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 72.35  E-value: 3.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   191 KELHQVAHDLDDELAWVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRR 270
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                           90       100
                   ....*....|....*....|....*
gi 312839860   271 GQEQLQSAWTGLREAAERRQQTLDA 295
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1096-1198 1.14e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 68.36  E-value: 1.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  1096 VQHEGFLLRKRELDANrkssnrSWVSLYCVLSKGELGFYKDSKGPASGGTHGgepLLSLHKATSE--VASDYKKKKHVFK 1173
Cdd:pfam00169    1 VVKEGWLLKKGGGKKK------SWKKRYFVLFDGSLLYYKDDKSGKSKEPKG---SISLSGCEVVevVASDSPKRKFCFE 71

                           90       100
                   ....*....|....*....|....*...
gi 312839860  1174 LQTQDGSE---FLLQAKDEEEMNGWLEA 1198
Cdd:pfam00169   72 LRTGERTGkrtYLLQAESEEERKDWIKA 99
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 1098-1199 2.49e-13

Pleckstrin homology (PH) domain; 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: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 66.80  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1098 HEGFLLRKRELdanrksSNRSWVSLYCVLSKGELGFYKDSKGPASGGTHggepLLSLHKATSEVASDYKKKKHVFKLQTQ 1177
Cdd:cd00821     1 KEGYLLKRGGG------GLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKG----SIPLSGILEVEEVSPKERPHCFELVTP 70

                          90       100
                  ....*....|....*....|..
gi 312839860 1178 DGSEFLLQAKDEEEMNGWLEAV 1199
Cdd:cd00821    71 DGRTYYLQADSEEERQEWLKAL 92
SPEC smart00150
Spectrin repeats;
406-506 2.53e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.97  E-value: 2.53e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    406 YQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGRERLAAVNQMVDELIECGHTAAATMAEWK 485
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAEL-EAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|.
gi 312839860    486 DGLNEAWAELLELMGTRAQLL 506
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
622-721 5.85e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.20  E-value: 5.85e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    622 RFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQLDK 701
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90       100
                    ....*....|....*....|
gi 312839860    702 LGSRKEEVSEKWDRHWEWLQ 721
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
300-400 6.39e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.81  E-value: 6.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    300 EQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRRQS 379
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 312839860    380 QVDRLYVALKELGEERRVSLE 400
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 619-722 1.19e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 65.42  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   619 DALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELATCQELGRSLLLNKSAMADEIQAQ 698
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81

                           90       100
                   ....*....|....*....|....
gi 312839860   699 LDKLGSRKEEVSEKWDRHWEWLQQ 722
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 300-401 6.80e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 63.11  E-value: 6.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   300 EQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRRQS 379
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 312839860   380 QVDRLYVALKELGEERRVSLEQ 401
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 403-506 8.67e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 62.72  E-value: 8.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   403 YWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETgTAGRERLAAVNQMVDELIECGHTAAATMA 482
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAEL-AAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                           90       100
                   ....*....|....*....|....
gi 312839860   483 EWKDGLNEAWAELLELMGTRAQLL 506
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
2-82 3.91e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 3.91e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860      2 LMARDGTREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQ 81
Cdd:smart00150   20 LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEELNERWEELKELAEERRQK 99


                    .
gi 312839860     82 L 82
Cdd:smart00150  100 L 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 724-801 5.78e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 51.94  E-value: 5.78e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312839860   724 LEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEERFSSLrrLTTIEKLKAEQSKQPP 801
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEAL--NELAEKLIDEGHYASE 76
SPEC smart00150
Spectrin repeats;
727-802 1.28e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 1.28e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312839860    727 HQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEERFSSLRRLTtiEKLKAEQSKQPPT 802
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELG--EQLIEEGHPDAEE 74
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 21-84 3.50e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 49.62  E-value: 3.50e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312839860    21 RHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFE 84
Cdd:pfam00435   42 KHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
PH_DOCK-D cd13267
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also ...
 1099-1206 3.70e-07

Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. 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: 270087  Cd Length: 126  Bit Score: 50.40  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRKRELdANRKSSN---RSWVSLYCVLSKGE-----LGFYKDSKGPASGGThggeplLSLhKATSEVASDYKKKKH 1170
Cdd:cd13267     9 EGYLYKGPEN-SSDSFISlamKSFKRRFFHLKQLVdgsyiLEFYKDEKKKEAKGT------IFL-DSCTGVVQNSKRRKF 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 312839860 1171 VFKLQTQDGSEFLLQAKDEEEMNGWLEAVaNSVAEH 1206
Cdd:cd13267    81 CFELRMQDKKSYVLAAESEAEMDEWISKL-NKILQS 115
PH_CNK_insect-like cd13326
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
 1099-1199 2.53e-06

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 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 insects, spiders, mollusks, and nematodes. 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: 270135  Cd Length: 91  Bit Score: 46.95  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRKREldanRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGGthggepLLSLHKATSEVASDYKKKKHVFKLQtQD 1178
Cdd:cd13326     2 QGWLYQRRR----KGKGGGKWAKRWFVLKGSNLYGFRSQESTKADC------VIFLPGFTVSPAPEVKSRKYAFKVY-HT 70

                          90       100
                  ....*....|....*....|.
gi 312839860 1179 GSEFLLQAKDEEEMNGWLEAV 1199
Cdd:cd13326    71 GTVFYFAAESQEDMKKWLDLL 91
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 510-609 7.64e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.77  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   510 RELHKFFSDARELQGQIEEKRrrlPRLTAPPEPR--PSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTvYAGEHAE 587
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKE---ALLSSEDYGKdlESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASE 76

                           90       100
                   ....*....|....*....|..
gi 312839860   588 AIASREQEVLQGWKELLAACED 609
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAE 98
SPEC smart00150
Spectrin repeats;
90-187 1.05e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.40  E-value: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860     90 QLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQ-ASKELVGERQSA 168
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhPDAEEIEERLEE 81

                            90
                    ....*....|....*....
gi 312839860    169 VGERLVRLLEPLQERRRLL 187
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 17-768 1.28e-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: 49.67  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    17 KRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQL--------FEASKA 88
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqILRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    89 DQLVQSFAELDKRLLHMESQLQDV---------DPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASK 159
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELaeelaeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   160 ELVGERQSAVGERLVRLLEPLQERRRLLLASKELHQVAHDlDDELAWVQERLPL--AMQTERGTGLQAVQQHIKKNQGLR 237
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-EAELKELQAELEEleEELEELQEELERLEEALEELREEL 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   238 REIQahgprlEEVLERAGVLASLRSpEAEAVRRGQEQLQSAWTGLREAAERRQQ------TLDAAFQVEQYYfdVAEVEA 311
Cdd:TIGR02168  471 EEAE------QALDAAERELAQLQA-RLDSLERLQENLEGFSEGVKALLKNQSGlsgilgVLSELISVDEGY--EAAIEA 541

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   312 WLGE--QELLMMSEDKGKDEQstlqllkkhlqleqgvenyeESIAQLSRQCRALLEM-----GHPDSEQISRRQSQVDRL 384
Cdd:TIGR02168  542 ALGGrlQAVVVENLNAAKKAI--------------------AFLKQNELGRVTFLPLdsikgTEIQGNDREILKNIEGFL 601

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   385 YVALKELGEERRVSLEQQYWLYQLsRQVDELEHWIAEkevvagSPELGQDFEHVSVLQEKFSEFASETGTAGRERLAAVN 464
Cdd:TIGR02168  602 GVAKDLVKFDPKLRKALSYLLGGV-LVVDDLDNALEL------AKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   465 --QMVDELIECGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTAPPEP 542
Cdd:TIGR02168  675 rrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   543 RPSASSMQRT------------LRAFEHDLQLLVSQVRQLQEGAAQLRTvyAGEHAEAIASREQEVLQGWKELLAACEDA 610
Cdd:TIGR02168  755 ELTELEAEIEeleerleeaeeeLAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERR 832

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   611 RLHVSSTADALrfHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVlmNYHQGLKTELEARVPELATCQELGRSLLLNKSA 690
Cdd:TIGR02168  833 IAATERRLEDL--EEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNERASLEEALALLRSELEELSEELRELES 908

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312839860   691 MADEIQAQLDKLGSRKEEVSEKWDRhwewLQQMLevhQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEA 768
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEG----LEVRI---DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SPEC smart00150
Spectrin repeats;
513-609 3.86e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 3.86e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    513 HKFFSDARELQGQIEEKRRRLpRLTAPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVyAGEHAEAIASR 592
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78

                            90
                    ....*....|....*..
gi 312839860    593 EQEVLQGWKELLAACED 609
Cdd:smart00150   79 LEELNERWEELKELAEE 95
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 1099-1203 4.00e-05

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. 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: 270113  Cd Length: 108  Bit Score: 43.90  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRKRELDANrkssnrsWVSLYCVLSKGELGFYKDSkgpaSGGTHGGEPLLSLHKATSEvASDYKKKKHVFKLQTQD 1178
Cdd:cd13301     6 EGYLVKKGHVVNN-------WKARWFVLKEDGLEYYKKK----TDSSPKGMIPLKGCTITSP-CLEYGKRPLVFKLTTAK 73

                          90       100
                  ....*....|....*....|....*
gi 312839860 1179 GSEFLLQAKDEEEMNGWLEAVANSV 1203
Cdd:cd13301    74 GQEHFFQACSREERDAWAKDITKAI 98
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
 1096-1206 6.09e-05

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. 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: 270118  Cd Length: 113  Bit Score: 43.55  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1096 VQHEGFLLRKreldANRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGGthggepLLSLHKATSEVASDY-KKKKHVFKL 1174
Cdd:cd13308     9 VIHSGTLTKK----GGSQKTLQNWQLRYVIIHQGCVYYYKNDQSAKPKG------VFSLNGYNRRAAEERtSKLKFVFKI 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 312839860 1175 Q--TQDGSEFLLQAKDEEEMNGWLEAVANSVAEH 1206
Cdd:cd13308    79 IhlSPDHRTWYFAAKSEDEMSEWMEYIRREIDHY 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-392 7.91e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   27 AELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFEASKADQLVQSFAELDKRLLhME 106
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-LL 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  107 SQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASKELVGERQSAVGERLVRLLEPLQERRRL 186
Cdd:COG1196   497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  187 LLASKELHQVAHDLDDELAWVQERLPLAMQTERGtgLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAE 266
Cdd:COG1196   577 LPLDKIRARAALAAALARGAIGAAVDLVASDLRE--ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  267 AVRRGQEQLQSAWTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGV 346
Cdd:COG1196   655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 312839860  347 ENYEESIAQLSRQCRALLEMGHPDSEQISRRQSQVDRLYVALKELG 392
Cdd:COG1196   735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 1096-1199 8.03e-05

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. 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: 270110  Cd Length: 106  Bit Score: 43.00  E-value: 8.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1096 VQHEGFLLRKREldaNRKSSNRSWVslycVLSKGELGFYKDSKgpasggthggE-------PLLSLHkATSEVASdyKKK 1168
Cdd:cd13298     6 VLKSGYLLKRSR---KTKNWKKRWV----VLRPCQLSYYKDEK----------EyklrrviNLSELL-AVAPLKD--KKR 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 312839860 1169 KHVFKLQTQDgSEFLLQAKDEEEMNGWLEAV 1199
Cdd:cd13298    66 KNVFGIYTPS-KNLHFRATSEKDANEWVEAL 95
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
 1096-1200 5.17e-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: 40.86  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1096 VQHEGFLLRKREldaNRKSSNRSWVslycVLSKGELGFYKDSKgpasggthggE----PLLSLHKATSEVASDYKKKKHV 1171
Cdd:cd13255     6 VLKAGYLEKKGE---RRKTWKKRWF----VLRPTKLAYYKNDK----------EyrllRLIDLTDIHTCTEVQLKKHDNT 68

                          90       100
                  ....*....|....*....|....*....
gi 312839860 1172 FKLQTQDGSeFLLQAKDEEEMNGWLEAVA 1200
Cdd:cd13255    69 FGIVTPART-FYVQADSKAEMESWISAIN 96
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 1117-1198 6.37e-04

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: 40.33  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1117 RSWVSLYCVLSKGELGFYKDSKgpaSGGTHGGEPLLSlHKATSEVASDYKKKKHVFKLQTQDGSEFLLQAKDEEEMNGWL 1196
Cdd:cd13248    22 KNWRKRWFVLKDNCLYYYKDPE---EEKALGSILLPS-YTISPAPPSDEISRKFAFKAEHANMRTYYFAADTAEEMEQWM 97


                  ..
gi 312839860 1197 EA 1198
Cdd:cd13248    98 NA 99
PH_SKIP cd13309
SifA and kinesin-interacting protein Pleckstrin homology (PH) domain; SKIP (also called ...
 1099-1204 7.90e-04

SifA and kinesin-interacting protein Pleckstrin homology (PH) domain; SKIP (also called PLEKHM2/Pleckstrin homology domain-containing family M member 2) is a soluble cytosolic protein that contains a RUN domain and a PH domain separated by a unstructured linker region. SKIP is a target of the Salmonella effector protein SifA and the SifA-SKIP complex regulates kinesin-1 on the bacterial vacuole. The PH domain of SKIP binds to the N-terminal region of SifA while the N-terminus of SKIP is proposed to bind the TPR domain of the kinesin light chain. The opposite side of the SKIP PH domain is proposed to bind phosphoinositides. TSifA, SKIP, SseJ, and RhoA family GTPases are also thought to promote host membrane tubulation. Recently, it was shown that the lysosomal GTPase Arl8 binds to the kinesin-1 linker SKIP and that both are required for the normal intracellular distribution of lysosomes. Interestingly, two kinesin light chain binding motifs (WD) in SKIP have now been identified to match a consensus sequence for a kinesin light chain binding site found in several proteins including calsyntenin-1/alcadein, caytaxin, and vaccinia virus A36. SKIP has also been shown to interact with Rab1A. 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: 270119  Cd Length: 103  Bit Score: 40.06  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRKReldANRKSSNRSWVSLYCVLSKGELGFYKDSkgpasggtHGGEPLLSLHKATSEVA----SDYKKKKHVFKL 1174
Cdd:cd13309     3 EGMLMYKT---GTSYLGGETWKPGYFLLKNGVLYQYPDR--------SDRLPLLSISLGGEQCGgcrrINNTERPHTFEL 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 312839860 1175 QTQDGSEFLLQAKDEEEMNGWLEAVANSVA 1204
Cdd:cd13309    72 ILTDRSSLELAAPDEYEASEWLQSLCQSAS 101
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
 1095-1204 9.43e-04

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). 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: 269939  Cd Length: 103  Bit Score: 39.88  E-value: 9.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1095 TVQHEGFLLRKREldanrksSNRSWVSLYCVLSKGELGFYKDSKGPASGGthggepLLSLHKATSEVASDYK---KKKHV 1171
Cdd:cd01233     5 VVSKRGYLLFLED-------ATDGWVRRWVVLRRPYLHIYSSEKDGDERG------VINLSTARVEYSPDQEallGRPNV 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 312839860 1172 FKLQTQDGSeFLLQAKDEEEMNGWLEAVANSVA 1204
Cdd:cd01233    72 FAVYTPTNS-YLLQARSEKEMQDWLYAIDPLLA 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 121-631 1.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  121 VNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASKELVGERQSAVGERLVRLLEPLQERRRLLLASKE--LHQVAH 198
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELArlEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  199 DLDDELAWVQERlpLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRGQEQLQSA 278
Cdd:COG1196   307 LEERRRELEERL--EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  279 WTGLREAAERRQQTLDAAFQVEQyyfdvAEVEAwlgEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSR 358
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEE-----AEEAL---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  359 QCRALLemghpdsEQISRRQSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQdfeHV 438
Cdd:COG1196   457 EEEALL-------ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG---AV 526

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  439 SVLQEKfsEFASETGTAGRERLAAVNQMVDELiecghTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSD 518
Cdd:COG1196   527 AVLIGV--EAAYEAALEAALAAALQNIVVEDD-----EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  519 ARELQGQIEEKRRRLPRL--------TAPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVYAGEHAEAIA 590
Cdd:COG1196   600 AVDLVASDLREADARYYVlgdtllgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 312839860  591 SREQEVLQGWKELLAACEDARLHVSSTADALRFHSQARDLL 631
Cdd:COG1196   680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
PH2_AFAP cd13307
Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are ...
 1115-1196 1.15e-03

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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: 270117  Cd Length: 101  Bit Score: 39.67  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1115 SNRSWVSLYCVLSKGELGFYKDskgpaSGGTHGGEPLLSLHKAtsEVASDY-KKKKHVFKLqTQDGSEF-LLQAKDEEEM 1192
Cdd:cd13307    12 VNQQWRSRWCCVKDGQLHFYQD-----RNKTKSPQQSLPLHGC--EVVPGPdPKHPYSFRI-LRNGEEVaALEASSSEDM 83


                  ....
gi 312839860 1193 NGWL 1196
Cdd:cd13307    84 GRWL 87
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 90-189 1.23e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.61  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    90 QLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAAL-PLEQASKELVGERQSA 168
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQERLEE 84

                           90       100
                   ....*....|....*....|.
gi 312839860   169 VGERLVRLLEPLQERRRLLLA 189
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-563 1.64e-03

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: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860    8 TREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQcwAELESTTQAKARQLFEASK 87
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE--LELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   88 AdQLVQSFAELDKRLLHMESQLQDVDpggdlATVNSQLKKLQSMESQVEEWCREVGELQAQTAAL-----PLEQASKELV 162
Cdd:COG1196   298 A-RLEQDIARLEERRRELEERLEELE-----EELAELEEELEELEEELEELEEELEEAEEELEEAeaelaEAEEALLEAE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  163 GERQSAVGERLVRLLEPLQERRRLLLASKELHQVAHDLDDELAwVQERLPLAMQTERGTGLQAVQQHIKKNQGLRREIQA 242
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  243 HGPRLEEVLERAGVLASLRSPEAEAVRRGQEQLQSawtgLREAAERRQQTLDAAFQVEQYYFDVAE---VEAWLGEQELL 319
Cdd:COG1196   451 EAELEEEEEALLELLAELLEEAALLEAALAELLEE----LAEAAARLLLLLEAEADYEGFLEGVKAallLAGLRGLAGAV 526

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  320 MMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALL-----------EMGHPDSEQISRRQSQVDRLYVAL 388
Cdd:COG1196   527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpldkiRARAALAAALARGAIGAAVDLVAS 606

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  389 KELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETGTAGRERLAAVNQMVD 468
Cdd:COG1196   607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  469 ELIEcgHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTAPPEPRPSASS 548
Cdd:COG1196   687 RLAE--EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764

                         570
                  ....*....|....*
gi 312839860  549 MQRTLRAFEHDLQLL 563
Cdd:COG1196   765 LERELERLEREIEAL 779
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
 1099-1195 1.70e-03

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. 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: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 38.84  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1099 EGFLLRkreLDANRKSSNRSWVslycVLSKGELGFYKDSKGPasggthggEPL--LSLHKATSEVASDYKKKKHVFKLQT 1176
Cdd:cd10573     6 EGYLTK---LGGIVKNWKTRWF----VLRRNELKYFKTRGDT--------KPIrvLDLRECSSVQRDYSQGKVNCFCLVF 70

                          90
                  ....*....|....*....
gi 312839860 1177 QDgSEFLLQAKDEEEMNGW 1195
Cdd:cd10573    71 PE-RTFYMYANTEEEADEW 88
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
 1096-1202 1.79e-03

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single PH domain. 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: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 39.53  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1096 VQHEGFLLRKRELdanrkssNRSWVSLYCVLsKGELGFYKDSKGpasggthGGEPL--LSLHKATSEVASDykKKKHVFK 1173
Cdd:cd13288     8 VDKEGYLWKKGER-------NTSYQKRWFVL-KGNLLFYFEKKG-------DREPLgvIVLEGCTVELAED--AEPYAFA 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 312839860 1174 LQTQDGSE--FLLQAKDEEEMNGWLEAVANS 1202
Cdd:cd13288    71 IRFDGPGArsYVLAAENQEDMESWMKALSRA 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
22-421 2.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   22 HQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFEASKAdqlvqsFAELDKR 101
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE------LEELREE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  102 LLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQtaalpLEQASKELVGERQSAVGERLVRLLEPLQ 181
Cdd:COG4717   118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-----LEELEAELAELQEELEELLEQLSLATEE 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  182 ERRRLLLASKELHQVAHDLDDELAWVQERL-PLAMQTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASL 260
Cdd:COG4717   193 ELQDLAEELEELQQRLAELEEELEEAQEELeELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  261 RSPEAEAVRRGQEQLQSAWTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHL 340
Cdd:COG4717   273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  341 QLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRRQSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIA 420
Cdd:COG4717   353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE 432


                  .
gi 312839860  421 E 421
Cdd:COG4717   433 E 433
PRK11281 PRK11281
mechanosensitive channel MscK;
27-130 5.49e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   27 AELAQNKEWLEKIEREGQQLMQEKPELAASVRKklgeIRQCWAELES---TTQAKARQLFEAskadqlvQSFAELDKRLL 103
Cdd:PRK11281   63 QDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK----LRQAQAELEAlkdDNDEETRETLST-------LSLRQLESRLA 131

                          90       100
                  ....*....|....*....|....*..
gi 312839860  104 HMESQLQDVDpgGDLATVNSQLKKLQS 130
Cdd:PRK11281  132 QTLDQLQNAQ--NDLAEYNSQLVSLQT 156
PTZ00121 PTZ00121
MAEBL; Provisional
 30-469 6.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860   30 AQNKEWLEKIEREGQQLMQEKPEL--AASVRKKLGEIRQCWAELESTTQAKaRQLFEASKADQLVQSfAELDKRLLHMES 107
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAK-KKAEEAKKADEAKKK-AEEAKKAEEAKK 1464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  108 QLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAAlpleqasKELVGERQSAVGERLVRLLEPLQERRRLL 187
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-------KKKADEAKKAEEAKKADEAKKAEEAKKAD 1537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  188 LASK-ELHQVAhdldDELAWVQErlpLAMQTERGTGLQAVQQHIKKNQGLRR-EI--QAHGPRLEEVLEragVLASLRSP 263
Cdd:PTZ00121 1538 EAKKaEEKKKA----DELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKaEEakKAEEARIEEVMK---LYEEEKKM 1607

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  264 EAEAVRRGQEQLQSAwTGLREAAERRQQTLDAAFQVEQYYFDVAEVEAwlGEQELLMMSEDKGKDEQSTLQLLKKHLQLE 343
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860  344 QGVENYEESIAQLSRQCRallemghpDSEQISRRQSQVDRLYVALKELGEERRVSLEqqywlyQLSRQVDElehwiaEKE 423
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAK--------KAEELKKKEAEEKKKAEELKKAEEENKIKAE------EAKKEAEE------DKK 1744

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 312839860  424 vvaGSPELGQDFEHVSVLQEKFSEFASETGTAGRERLAAVNQMVDE 469
Cdd:PTZ00121 1745 ---KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 1117-1206 6.27e-03

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. 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: 270095  Cd Length: 106  Bit Score: 37.68  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1117 RSWVSLYCVLSKGELGFYKDSKGPASGGTHGgepLLSLHKATS-EVASDYKKKKHVFKLQTQDGSeFLLQAKDEEEMNGW 1195
Cdd:cd13276    13 KTWRRRWFVLKQGKLFWFKEPDVTPYSKPRG---VIDLSKCLTvKSAEDATNKENAFELSTPEET-FYFIADNEKEKEEW 88

                          90
                  ....*....|.
gi 312839860 1196 LEAVANSVAEH 1206
Cdd:cd13276    89 IGAIGRAIVKH 99
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
 1098-1204 8.01e-03

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. 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: 270070  Cd Length: 98  Bit Score: 37.20  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1098 HEGFLLRKreldanrkSSN--RSWVSLYCVLSKGELGFYKDSKGPaSGGTHGGEPLLSLHKATSEvaSDykkKKHVFKLQ 1175
Cdd:cd13250     1 KEGYLFKR--------SSNafKTWKRRWFSLQNGQLYYQKRDKKD-EPTVMVEDLRLCTVKPTED--SD---RRFCFEVI 66

                          90       100
                  ....*....|....*....|....*....
gi 312839860 1176 TQDGSeFLLQAKDEEEMNGWLEAVANSVA 1204
Cdd:cd13250    67 SPTKS-YMLQAESEEDRQAWIQAIQSAIA 94
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
 1101-1211 8.31e-03

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn domain. 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: 269937  Cd Length: 127  Bit Score: 37.82  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312839860 1101 FLLRKRELD---ANRKSSNRSWVSLycvlsKG-ELGFYK-DSKGPASggtHGGEP--LLSLHKATSEVASDYKKKKHVFK 1173
Cdd:cd01230    14 FLVHKKNKKvelATRRKWKKYWVCL-----KGcTLLFYEcDERSGID---ENSEPkhALFVEGSIVQAVPEHPKKDFVFC 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 312839860 1174 LQTQDGSEFLLQAKDEEEMNGWLEAVANSVAehAEIAR 1211
Cdd:cd01230    86 LSNSFGDAYLFQATSQTELENWVTAIHSACA--SAFAR 121
 
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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