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Conserved domains on  [gi|93102364|ref|NP_055870|]
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switch-associated protein 70 isoform 1 [Homo sapiens]

Protein Classification

PH_SWAP-70 domain-containing protein( domain architecture ID 10192778)

PH_SWAP-70 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
204-313 4.18e-61

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal 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: 270092  Cd Length: 110  Bit Score: 197.52  E-value: 4.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 204 FNELILDVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKT 283
Cdd:cd13273   1 YDELILDVIKKGYLWKKGHLLPTWTERWFVLKPNSLSYYKSEDLKEKKGEIALDSNCCVESLPDREGKKCRFLVKTPDKT 80
                        90       100       110
                ....*....|....*....|....*....|
gi 93102364 284 FEISASDKKKKQEWIQAIHSTIHLLKLGSP 313
Cdd:cd13273  81 YELSASDHKTRQEWIAAIQTAIRLSQEGKS 110
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-525 3.55e-17

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 3.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQL----AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARfSTELE 392
Cdd:COG1196 220 EELKELEAELLLLKLreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-LAELA 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 393 REKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQ 472
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 93102364 473 QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
 
Name Accession Description Interval E-value
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
204-313 4.18e-61

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal 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: 270092  Cd Length: 110  Bit Score: 197.52  E-value: 4.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 204 FNELILDVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKT 283
Cdd:cd13273   1 YDELILDVIKKGYLWKKGHLLPTWTERWFVLKPNSLSYYKSEDLKEKKGEIALDSNCCVESLPDREGKKCRFLVKTPDKT 80
                        90       100       110
                ....*....|....*....|....*....|
gi 93102364 284 FEISASDKKKKQEWIQAIHSTIHLLKLGSP 313
Cdd:cd13273  81 YELSASDHKTRQEWIAAIQTAIRLSQEGKS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-525 3.55e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 3.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQL----AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARfSTELE 392
Cdd:COG1196 220 EELKELEAELLLLKLreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-LAELA 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 393 REKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQ 472
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 93102364 473 QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
211-306 2.98e-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: 71.81  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    211 VLKQGYMMKKG-HRRKNWTERWFVLKPNIISYYVSEDLKDK---KGDILLDENCCVESL-PDKDGKKCLFLVKCFD-KTF 284
Cdd:smart00233   1 VIKEGWLYKKSgGGKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPdPDSSKKPHCFEIKTSDrKTL 80
                           90       100
                   ....*....|....*....|..
gi 93102364    285 EISASDKKKKQEWIQAIHSTIH 306
Cdd:smart00233  81 LLQAESEEEREKWVEALRKAIA 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
332-549 1.45e-14

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: 77.40  E-value: 1.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    332 AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEeKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSE 411
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    412 LEQYLQRVRELEDMYLKLQEAL-EDERQARQDEETVRKLQARLLEEESSKRaELEKWHLEQQQAIQTTEAEKQELENQRV 490
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELaEAEAEIEELEAQIEQLKEELKALREALD-ELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364    491 LKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGLIRLIE 549
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
PH pfam00169
PH domain; PH stands for pleckstrin homology.
211-306 1.48e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 66.82  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   211 VLKQGYMMKKGH-RRKNWTERWFVLKPNIISYYVSED---LKDKKGDILLDENCCVESL-PDKDGKKCLFLVK----CFD 281
Cdd:pfam00169   1 VVKEGWLLKKGGgKKKSWKKRYFVLFDGSLLYYKDDKsgkSKEPKGSISLSGCEVVEVVaSDSPKRKFCFELRtgerTGK 80
                          90       100
                  ....*....|....*....|....*
gi 93102364   282 KTFEISASDKKKKQEWIQAIHSTIH 306
Cdd:pfam00169  81 RTYLLQAESEEERKDWIKAIQSAIR 105
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
321-532 2.77e-12

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 69.77  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   321 QRRKELRKKQLAEQEELERQM---KELQAANESKQQELEAVRKKleeaasRAAEEEKKRLQTQVELQARFSTELEREKLI 397
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAaiyAEQERMAMERERELERIRQE------ERKRELERIRQEEIAMEISRMRELERLQME 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   398 RQQMEEQVAQkssELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKraELEKWHLEQQQAIQT 477
Cdd:pfam17380 387 RQQKNERVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQ 461
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93102364   478 TEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTK 532
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK 516
PTZ00121 PTZ00121
MAEBL; Provisional
317-584 7.14e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRK--ELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELERE 394
Cdd:PTZ00121 1528 KKAEEAKKadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   395 KLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEE--TVRKLQARLLEEESSKRAELEKWHLEQQ 472
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   473 ----QAIQTTEAEKQELENQRVLKEQALQEAmEQLEQLELERKQALEQY----EEVKKKLEMAtNKTKSWKDKVAHhegl 544
Cdd:PTZ00121 1688 kkaaEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAkkeaEEDKKKAEEA-KKDEEEKKKIAH---- 1761
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 93102364   545 irLIEPGSKNPHLITNWGPAAFTEAELEEREKNWKEKKTT 584
Cdd:PTZ00121 1762 --LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
 
Name Accession Description Interval E-value
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
204-313 4.18e-61

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal 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: 270092  Cd Length: 110  Bit Score: 197.52  E-value: 4.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 204 FNELILDVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKT 283
Cdd:cd13273   1 YDELILDVIKKGYLWKKGHLLPTWTERWFVLKPNSLSYYKSEDLKEKKGEIALDSNCCVESLPDREGKKCRFLVKTPDKT 80
                        90       100       110
                ....*....|....*....|....*....|
gi 93102364 284 FEISASDKKKKQEWIQAIHSTIHLLKLGSP 313
Cdd:cd13273  81 YELSASDHKTRQEWIAAIQTAIRLSQEGKS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-525 3.55e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 3.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQL----AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARfSTELE 392
Cdd:COG1196 220 EELKELEAELLLLKLreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-LAELA 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 393 REKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQ 472
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 93102364 473 QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-525 1.28e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 83.83  E-value: 1.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKkRLQTQVELQARFSTELEREKL 396
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEE 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 397 IRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQ 476
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 93102364 477 TTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
288-525 6.11e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 6.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 288 ASDKKKKQEWIQAIHSTIHLLKLGspppHKEARQRRKELRKKQLAEQEELERQMKELQAANEsKQQELEAVRKKLEEAAS 367
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELA 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 368 RAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVR 447
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93102364 448 KLQARLLEEESSKRAELEkwhlEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 407 EAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
318-525 2.06e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.98  E-value: 2.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 318 EARQRRKELRKKQLAEQEELERQMKELQ------AANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTEL 391
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELArleqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 392 EREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQ 471
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 93102364 472 QQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
211-306 2.98e-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: 71.81  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    211 VLKQGYMMKKG-HRRKNWTERWFVLKPNIISYYVSEDLKDK---KGDILLDENCCVESL-PDKDGKKCLFLVKCFD-KTF 284
Cdd:smart00233   1 VIKEGWLYKKSgGGKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPdPDSSKKPHCFEIKTSDrKTL 80
                           90       100
                   ....*....|....*....|..
gi 93102364    285 EISASDKKKKQEWIQAIHSTIH 306
Cdd:smart00233  81 LLQAESEEEREKWVEALRKAIA 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-573 5.57e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 5.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQ------ELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTE 390
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEEleeelaELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 391 LEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARL---LEEESSKRAELEKW 467
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELeeaLAELEEEEEEEEEA 443
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 468 HLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKdKVAHHEGLIRL 547
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGL 522
                       250       260
                ....*....|....*....|....*.
gi 93102364 548 IEPGsknpHLITNWGPAAFTEAELEE 573
Cdd:COG1196 523 AGAV----AVLIGVEAAYEAALEAAL 544
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
332-549 1.45e-14

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: 77.40  E-value: 1.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    332 AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEeKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSE 411
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    412 LEQYLQRVRELEDMYLKLQEAL-EDERQARQDEETVRKLQARLLEEESSKRaELEKWHLEQQQAIQTTEAEKQELENQRV 490
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELaEAEAEIEELEAQIEQLKEELKALREALD-ELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364    491 LKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGLIRLIE 549
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
315-525 3.14e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 3.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 315 PHKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELERE 394
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 395 KLIRQQMEEQvAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQA 474
Cdd:COG1196 386 EELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 93102364 475 IQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
213-301 4.53e-14

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: 67.95  E-value: 4.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHR-RKNWTERWFVLKPNIISYY--VSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKTFEISAS 289
Cdd:cd00821   1 KEGYLLKRGGGgLKSWKKRWFVLFEGVLLYYksKKDSSYKPKGSIPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80
                        90
                ....*....|..
gi 93102364 290 DKKKKQEWIQAI 301
Cdd:cd00821  81 SEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
211-306 1.48e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 66.82  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   211 VLKQGYMMKKGH-RRKNWTERWFVLKPNIISYYVSED---LKDKKGDILLDENCCVESL-PDKDGKKCLFLVK----CFD 281
Cdd:pfam00169   1 VVKEGWLLKKGGgKKKSWKKRYFVLFDGSLLYYKDDKsgkSKEPKGSISLSGCEVVEVVaSDSPKRKFCFELRtgerTGK 80
                          90       100
                  ....*....|....*....|....*
gi 93102364   282 KTFEISASDKKKKQEWIQAIHSTIH 306
Cdd:pfam00169  81 RTYLLQAESEEERKDWIKAIQSAIR 105
PH2_TAPP1_2 cd13271
Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal ...
211-314 3.34e-13

Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal repeat; The binding of TAPP1 (also called PLEKHA1/pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1) and 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). TAPP1 and TAPP2 contain 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. 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: 270090  Cd Length: 114  Bit Score: 66.22  E-value: 3.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDE-----NCCVESLPDKDGkkcLFLVKCFDKTFE 285
Cdd:cd13271   8 VIKSGYCVKQGAVRKNWKRRFFILDDNTISYYKSETDKEPLRTIPLREvlkvhECLVKSLLMRDN---LFEIITTSRTFY 84
                        90       100
                ....*....|....*....|....*....
gi 93102364 286 ISASDKKKKQEWIQAIHSTIHLLKLGSPP 314
Cdd:cd13271  85 IQADSPEEMHSWIKAISGAIVARRGPSRS 113
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
211-304 4.96e-13

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: 65.34  E-value: 4.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCfDKTFEISASD 290
Cdd:cd13298   6 VLKSGYLLKRSRKTKNWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSELLAVAPLKDKKRKNVFGIYTP-SKNLHFRATS 84
                        90
                ....*....|....
gi 93102364 291 KKKKQEWIQAIHST 304
Cdd:cd13298  85 EKDANEWVEALREE 98
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
319-530 6.68e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 6.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 319 ARQRRKELRKKQLAEQEElERQMKELQAANESKQQELEAVRKKLEEAasraaeeeKKRLQTQVELQARFSTELEREKLIR 398
Cdd:COG1196 206 ERQAEKAERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLEL 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 399 QQMEEQVAQKSSELEQYLQRVRELEDmylKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAiqtt 478
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQ---DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA---- 349
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 93102364 479 EAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNK 530
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
321-532 2.77e-12

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 69.77  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   321 QRRKELRKKQLAEQEELERQM---KELQAANESKQQELEAVRKKleeaasRAAEEEKKRLQTQVELQARFSTELEREKLI 397
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAaiyAEQERMAMERERELERIRQE------ERKRELERIRQEEIAMEISRMRELERLQME 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   398 RQQMEEQVAQkssELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKraELEKWHLEQQQAIQT 477
Cdd:pfam17380 387 RQQKNERVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQ 461
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93102364   478 TEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTK 532
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK 516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
320-539 3.27e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 3.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 320 RQRRKE-LRKKQLAEQ---------EELERQMKEL--QAANESKQQELEAVRKKLEEAASRaaeeekKRLQTQVELQARF 387
Cdd:COG1196 171 KERKEEaERKLEATEEnlerledilGELERQLEPLerQAEKAERYRELKEELKELEAELLL------LKLRELEAELEEL 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 388 STELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDmylKLQEALEDERQARQDEETVRKLQARLLEEESskraelekw 467
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYELLAELARLEQDIARLEERRR--------- 312
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93102364 468 hlEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVA 539
Cdd:COG1196 313 --ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
213-344 4.09e-12

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: 63.41  E-value: 4.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLdENCCVESLPDKDgkKCLFLVkCFD----KTFEISA 288
Cdd:cd13288  10 KEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKKGDREPLGVIVL-EGCTVELAEDAE--PYAFAI-RFDgpgaRSYVLAA 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364 289 SDKKKKQEWIQAI-HSTIHLLKLgsppphkearqrrkelrkkqlaEQEELERQMKEL 344
Cdd:cd13288  86 ENQEDMESWMKALsRASYDYLRL----------------------TVEELEKQLEEL 120
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
211-306 6.53e-12

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: 62.39  E-value: 6.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDeNCCVESlPDKDGKKCLFLVKCFDKTFE---IS 287
Cdd:cd13301   3 IIKEGYLVKKGHVVNNWKARWFVLKEDGLEYYKKKTDSSPKGMIPLK-GCTITS-PCLEYGKRPLVFKLTTAKGQehfFQ 80
                        90
                ....*....|....*....
gi 93102364 288 ASDKKKKQEWIQAIHSTIH 306
Cdd:cd13301  81 ACSREERDAWAKDITKAIT 99
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
213-314 6.93e-12

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. 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: 270094  Cd Length: 104  Bit Score: 61.97  E-value: 6.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRKNWTERWFVLKPNIISYYvsEDLKDKKGDIL---LDENCCVESLPDKDGKKCLFLVKCFD-KTFEISA 288
Cdd:cd13275   1 KKGWLMKQGSRQGEWSKHWFVLRGAALKYY--RDPSAEEAGELdgvIDLSSCTEVTELPVSRNYGFQVKTWDgKVYVLSA 78
                        90       100
                ....*....|....*....|....*.
gi 93102364 289 SDKKKKQEWIQAIHSTIHLLKLGSPP 314
Cdd:cd13275  79 MTSGIRTNWIQALRKAAGLPSPPALP 104
PH2_Pleckstrin_2 cd13302
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 2; Pleckstrin is a protein found in ...
211-303 1.93e-10

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 2; 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 second 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: 270114  Cd Length: 109  Bit Score: 58.29  E-value: 1.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLK--PNIISYYVSEDLKDKKGDILLdENCCVESLPDK-DGKK-----CLFLVKCFDK 282
Cdd:cd13302   7 IVKQGCLLKQGHRRKNWKVRKFVLRddPAYLHYYDPAKGEDPLGAIHL-RGCVVTAVEDNsNPRKgsvegNLFEIITADE 85
                        90       100
                ....*....|....*....|..
gi 93102364 283 T-FEISASDKKKKQEWIQAIHS 303
Cdd:cd13302  86 VhYYLQAATPAERTEWIKAIQM 107
PH_Skap_family cd13266
Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain; Skap adaptor ...
211-301 2.14e-10

Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain; Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270086  Cd Length: 106  Bit Score: 57.92  E-value: 2.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKghRRKN------WTERWFVLKPNIISYYVSEDLKDKKGDILLDeNCCVESLP--DKDGKK-CLFLVKCFD 281
Cdd:cd13266   1 VIKAGYLEKR--RKDHsffgseWQKRWCAISKNVFYYYGSDKDKQQKGEFAIN-GYDVRMNPtlRKDGKKdCCFELVCPD 77
                        90       100
                ....*....|....*....|.
gi 93102364 282 K-TFEISASDKKKKQEWIQAI 301
Cdd:cd13266  78 KrTYQFTAASPEDAEDWVDQI 98
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
321-527 2.31e-10

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 63.50  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 321 QRRKELRKKQLAEQEE-LERQMKELQAANESKQQELEAVRKKLE----EAASRAAEEEKKRLQTQ-VELQARFSTELERE 394
Cdd:COG3206 163 EQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQlAEARAELAEAEARL 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 395 KLIRQQMEEQVAQKSSELEQylQRVRELEDMYLKLQEALEDERQARQDE-ETVRKLQARLLEEESSKRAELEKWHLEQQQ 473
Cdd:COG3206 243 AALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNhPDVIALRAQIAALRAQLQQEAQRILASLEA 320
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364 474 AIQTTEAEKQELENQRV-LKEQALQEAMEQLEQLELERKQAL--EQYEEVKKKLEMA 527
Cdd:COG3206 321 ELEALQAREASLQAQLAqLEARLAELPELEAELRRLEREVEVarELYESLLQRLEEA 377
PH2_MyoX cd13296
Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular ...
213-305 2.74e-10

Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the second 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: 270108  Cd Length: 103  Bit Score: 57.48  E-value: 2.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGH-----RRKNWTERWFVLKPNIISYYVSEDLKDK-KGDILLDENCCVeslPDKDGKKCLFLVKCFDKTFEI 286
Cdd:cd13296   1 KSGWLTKKGGgsstlSRRNWKSRWFVLRDTVLKYYENDQEGEKlLGTIDIRSAKEI---VDNDPKENRLSITTEERTYHL 77
                        90
                ....*....|....*....
gi 93102364 287 SASDKKKKQEWIQAIHSTI 305
Cdd:cd13296  78 VAESPEDASQWVNVLTRVI 96
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
213-303 2.98e-10

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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: 241436  Cd Length: 96  Bit Score: 57.31  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKK--GDILLDENCCVEslpdKDGKKCLFLVKCFDKTFEISASD 290
Cdd:cd13282   1 KAGYLTKLGGKVKTWKRRWFVLKNGELFYYKSPNDVIRKpqGQIALDGSCEIA----RAEGAQTFEIVTEKRTYYLTADS 76
                        90
                ....*....|...
gi 93102364 291 KKKKQEWIQAIHS 303
Cdd:cd13282  77 ENDLDEWIRVIQN 89
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
211-306 6.36e-10

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. 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: 269954  Cd Length: 119  Bit Score: 56.94  E-value: 6.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLdENCCVESLPDKDGKKC--LFLVKCFDK------ 282
Cdd:cd01252   3 PDREGWLLKLGGRVKSWKRRWFILTDNCLYYFEYTTDKEPRGIIPL-ENLSVREVEDKKKPFCfeLYSPSNGQVikackt 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 93102364 283 ------------TFEISASDKKKKQEWIQAIHSTIH 306
Cdd:cd01252  82 dsdgkvvegnhtVYRISAASEEERDEWIKSIKASIS 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-527 6.43e-10

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: 62.38  E-value: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    317 KEARQRRKELRKKQlAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEeKKRLQTQVELQARfsteLEREKL 396
Cdd:TIGR02168  232 LRLEELREELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-QKELYALANEISR----LEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    397 IRQQMEEQVAQKSSELEQYLQrvrELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQ 476
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 93102364    477 TTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMA 527
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
318-525 7.84e-10

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: 62.00  E-value: 7.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    318 EARQRRKELRKkqlaEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQA----RFSTELER 393
Cdd:TIGR02168  695 ELEKALAELRK----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    394 EKLI---------RQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLL-------EEE 457
Cdd:TIGR02168  771 EEAEeelaeaeaeIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedleeqiEEL 850
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93102364    458 SSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEA-------MEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrseleelSEELRELESKRSELRRELEELREKLA 925
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
211-314 9.68e-10

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: 56.27  E-value: 9.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSedlkDKKGDIL-----LDENCCVE-SLPDKDGkkcLFLVKCFDKTF 284
Cdd:cd13255   6 VLKAGYLEKKGERRKTWKKRWFVLRPTKLAYYKN----DKEYRLLrlidlTDIHTCTEvQLKKHDN---TFGIVTPARTF 78
                        90       100       110
                ....*....|....*....|....*....|
gi 93102364 285 EISASDKKKKQEWIQAIHSTIHLLKLGSPP 314
Cdd:cd13255  79 YVQADSKAEMESWISAINLARQALRATITP 108
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
271-516 1.02e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.55  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 271 KKCLFLVKCFDKTFEISASDKKKKQEWIQAIHSTIHLLKlgsppphkEARQRRKELRKKQLAEQEELERQMKELQAANES 350
Cdd:COG4942   2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 351 KQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFST-----ELEREKLIRQQMEEQVAQKSSELEQYLqrVRELEDM 425
Cdd:COG4942  74 LEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyrlgRQPPLALLLSPEDFLDAVRRLQYLKYL--APARREQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 426 YLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQ 505
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
                       250
                ....*....|.
gi 93102364 506 LELERKQALEQ 516
Cdd:COG4942 232 LEAEAAAAAER 242
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
210-301 1.07e-09

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 270083  Cd Length: 114  Bit Score: 56.24  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDEN--CCVESLPDKDGkKCLFLVKCFD------ 281
Cdd:cd13263   2 RPIKSGWLKKQGSIVKNWQQRWFVLRGDQLYYYKDEDDTKPQGTIPLPGNkvKEVPFNPEEPG-KFLFEIIPGGggdrmt 80
                        90       100
                ....*....|....*....|...
gi 93102364 282 ---KTFEISASDKKKKQEWIQAI 301
Cdd:cd13263  81 snhDSYLLMANSQAEMEEWVKVI 103
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
213-305 3.19e-09

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: 54.63  E-value: 3.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKK---GDILLDENCCVESLPDKDGKKCLFLVKCFDKTFEISAS 289
Cdd:cd13276   1 KAGWLEKQGEFIKTWRRRWFVLKQGKLFWFKEPDVTPYSkprGVIDLSKCLTVKSAEDATNKENAFELSTPEETFYFIAD 80
                        90
                ....*....|....*.
gi 93102364 290 DKKKKQEWIQAIHSTI 305
Cdd:cd13276  81 NEKEKEEWIGAIGRAI 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
307-525 4.24e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.62  E-value: 4.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 307 LLKLGSPPPHKEARQRRKELRKKQlAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQAr 386
Cdd:COG4942  10 LLALAAAAQADAAAEAEAELEQLQ-QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 387 fsTELEREKLiRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALED--------ERQARQDEETVRKLQARLlEEES 458
Cdd:COG4942  88 --LEKEIAEL-RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADL-AELA 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364 459 SKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-519 5.00e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 5.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    317 KEARQRRKELRKKQL-AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREK 395
Cdd:TIGR02168  300 LEQQKQILRERLANLeRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    396 LIRQ------QMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEEtvrklqarlLEEESSKRAELEKWHL 469
Cdd:TIGR02168  380 QLETlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELE 450
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 93102364    470 EQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLElERKQALEQYEE 519
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQ-ARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-545 5.40e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 5.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKL 396
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    397 IRQQMEEQ----------VAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEK 466
Cdd:TIGR02168  801 LREALDELraeltllneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    467 WHLEQQQAI-------QTTEAEKQELENQRVLKEQALQEAMEQLEQLELeRKQALEQ----------------YEEVKKK 523
Cdd:TIGR02168  881 ERASLEEALallrselEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVridnlqerlseeysltLEEAEAL 959
                          250       260
                   ....*....|....*....|..
gi 93102364    524 LEMATNKTKSWKDKVAHHEGLI 545
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKI 981
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
317-531 5.41e-09

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 58.98  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAE--QEELE---RQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVEL----QARF 387
Cdd:pfam17380 348 RELERIRQEERKRELERirQEEIAmeiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKvemeQIRA 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   388 STELEREKLIRQQME------EQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQD-EETVRKLQARLLE----- 455
Cdd:pfam17380 428 EQEEARQREVRRLEEeraremERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaEEQRRKILEKELEerkqa 507
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   456 --EESSKRAELEKWHLEQQQAI----QTTEAE-----KQELENQRVLKEQALQ--EAMEQLEQLELERK--QALEQYEEV 520
Cdd:pfam17380 508 miEEERKRKLLEKEMEERQKAIyeeeRRREAEeerrkQQEMEERRRIQEQMRKatEERSRLEAMEREREmmRQIVESEKA 587
                         250
                  ....*....|.
gi 93102364   521 KKKLEMATNKT 531
Cdd:pfam17380 588 RAEYEATTPIT 598
PTZ00121 PTZ00121
MAEBL; Provisional
317-584 7.14e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRK--ELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELERE 394
Cdd:PTZ00121 1528 KKAEEAKKadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   395 KLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEE--TVRKLQARLLEEESSKRAELEKWHLEQQ 472
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   473 ----QAIQTTEAEKQELENQRVLKEQALQEAmEQLEQLELERKQALEQY----EEVKKKLEMAtNKTKSWKDKVAHhegl 544
Cdd:PTZ00121 1688 kkaaEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAkkeaEEDKKKAEEA-KKDEEEKKKIAH---- 1761
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 93102364   545 irLIEPGSKNPHLITNWGPAAFTEAELEEREKNWKEKKTT 584
Cdd:PTZ00121 1762 --LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
323-525 8.36e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 8.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    323 RKELRKKQ--LAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQV-ELQARFST---ELEREKL 396
Cdd:TIGR02168  195 LNELERQLksLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELeELTAELQEleeKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    397 IRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALED-ERQARQDEETVRKLQARLLEEESSKrAELEKWHLEQQQAI 475
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlERQLEELEAQLEELESKLDELAEEL-AELEEKLEELKEEL 353
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 93102364    476 QTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
335-516 9.44e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 9.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  335 EELERQMKELQAANEsKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKlirQQMEEQVAQKSSELEQ 414
Cdd:COG4913  245 EDAREQIELLEPIRE-LAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL---ARLEAELERLEARLDA 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  415 YLQRVRELEDMYLK--------LQEALEDERQARQDEETVRKLQARLLE----EESSKRAELEKWHLEQQQAIQTTEAEK 482
Cdd:COG4913  321 LREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEEL 400
                        170       180       190
                 ....*....|....*....|....*....|....
gi 93102364  483 QELENQRVLKEQALQEAMEQLEQLELERkQALEQ 516
Cdd:COG4913  401 EALEEALAEAEAALRDLRRELRELEAEI-ASLER 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
332-525 1.02e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.54  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    332 AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVElQARFSTELEREKLIRQQMEEQVAQKSSE 411
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-EEKLKERLEELEEDLSSLEQEIENVKSE 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    412 LEQYLQRVRELEDMYLKLQEALED-------------ERQARQDEETVRKLQARLLEEEsskrAELEKWHLEQQQA---I 475
Cdd:TIGR02169  760 LKELEARIEELEEDLHKLEEALNDlearlshsripeiQAELSKLEEEVSRIEARLREIE----QKLNRLTLEKEYLekeI 835
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 93102364    476 QTTEAEKQELENQRVLKEQALQEAMEQLEQL--ELERKQ-ALEQYEEVKKKLE 525
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELeeELEELEaALRDLESRLGDLK 888
PH_Skap-hom_Skap2 cd13381
Src kinase-associated phosphoprotein homolog and Skap 2 Pleckstrin homology (PH) domain; ...
211-301 1.45e-08

Src kinase-associated phosphoprotein homolog and Skap 2 Pleckstrin homology (PH) domain; Adaptor protein Skap-hom, a homolog of Skap55, which interacts with actin and with ADAP (adhesion and degranulation promoting adapter protein) undergoes tyrosine phosphorylation in response to plating of bone marrow-derived macrophages on fibronectin. Skap-hom has an N-terminal coiled-coil conformation that is involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap-hom PH domain regulates intracellular targeting; its interaction with the DM domain inhibits Skap-hom actin-based ruffles in macrophages and its binding to 3'-phosphoinositides reverses this autoinhibition. The Skap-hom PH domain binds PI[3,4]P2 and PI[3,4,5]P3, but not to PI[3]P, PI[5]P, or PI[4,5]P2. Skap2 is a downstream target of Heat shock transcription factor 4 (HSF4) and functions in the regulation of actin reorganization during lens differentiation. It is thought that SKAP2 anchors the complex of tyrosine kinase adaptor protein 2 (NCK20/focal adhesion to fibroblast growth factor receptors at the lamellipodium in lens epithelial cells. Skap2 has an N-terminal coiled-coil conformation which interacts with the SH2 domain of NCK2, a central PH domain and a C-terminal SH3 domain that associates with ADAP (adhesion and degranulation promoting adapter protein)/FYB (the Fyn binding protein). Skap2 PH domain binds to membrane lipids. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-hom have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. 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: 270181  Cd Length: 106  Bit Score: 52.65  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKkghRRKN-------WTERWFVLKPNIISYYVSEDLKDKKGDILLD-ENCCVESLPDKDGKK-CLFLVKCFD 281
Cdd:cd13381   1 VLKAGYLEK---RRKDhsffgfeWQKRWCALSNSVFYYYGSDKDKQQKGEFAIDgYDVKMNNTLRKDAKKdCCFEICAPD 77
                        90       100
                ....*....|....*....|.
gi 93102364 282 K-TFEISASDKKKKQEWIQAI 301
Cdd:cd13381  78 KrVYQFTAASPKEAEEWVQQI 98
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
213-308 1.51e-08

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: 52.22  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGH-RRKNWTERWFVLKPNIISYYvsedlKDKKG--------DILLdenCCVESLPDKDGKKClFLVKCFDKT 283
Cdd:cd13250   1 KEGYLFKRSSnAFKTWKRRWFSLQNGQLYYQ-----KRDKKdeptvmveDLRL---CTVKPTEDSDRRFC-FEVISPTKS 71
                        90       100
                ....*....|....*....|....*
gi 93102364 284 FEISASDKKKKQEWIQAIHSTIHLL 308
Cdd:cd13250  72 YMLQAESEEDRQAWIQAIQSAIASA 96
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
213-305 1.82e-08

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: 51.94  E-value: 1.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDlkDKKGDILLDENCCVESLPDKD-GKKCLFLVKCFDKTFEISASDK 291
Cdd:cd10573   5 KEGYLTKLGGIVKNWKTRWFVLRRNELKYFKTRG--DTKPIRVLDLRECSSVQRDYSqGKVNCFCLVFPERTFYMYANTE 82
                        90
                ....*....|....
gi 93102364 292 KKKQEWIQAIHSTI 305
Cdd:cd10573  83 EEADEWVKLLKWKL 96
PTZ00121 PTZ00121
MAEBL; Provisional
317-585 1.86e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQtqvelQARFSTELEREKL 396
Cdd:PTZ00121 1118 EEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE-----AARKAEEVRKAEE 1192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   397 IRQQMEEQVAQ--KSSELEQYLQRVRELEDMylKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQA 474
Cdd:PTZ00121 1193 LRKAEDARKAEaaRKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   475 IQTTEAEKQELEnqrVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVahhEGLIRLIEPGSKN 554
Cdd:PTZ00121 1271 AIKAEEARKADE---LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA---DAAKKKAEEAKKA 1344
                         250       260       270
                  ....*....|....*....|....*....|.
gi 93102364   555 PHLITNWGPAAFTEAELEEREKNWKEKKTTE 585
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
314-539 2.33e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 56.38  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 314 PPHKEARQRRKELRKKQLAEQEELERQMKELQAANE---SKQQELEAVRKKLeeaasraaeeekKRLQTQV-ELQARFST 389
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEeynELQAELEALQAEI------------DKLQAEIaEAEAEIEE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 390 ELER-EKLIRQQMEEQVAQK-------SSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKR 461
Cdd:COG3883  84 RREElGERARALYRSGGSVSyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93102364 462 AELEkwhlEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVA 539
Cdd:COG3883 164 AELE----AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
PH_Skap1 cd13380
Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain; Adaptor protein Skap1 ...
211-301 4.22e-08

Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain; Adaptor protein Skap1 (also called Skap55/Src kinase-associated phosphoprotein of 55 kDa) and its partner, ADAP (adhesion and degranulation promoting adapter protein) help reorganize the cytoskeleton and/or promote integrin-mediated adhesion upon immunoreceptor activation. Skap1 is also involved in T Cell Receptor (TCR)-induced RapL-Rap1 complex formation and LFA-1 activation. Skap1 has an N-terminal coiled-coil conformation which is proposed to be involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap1 PH domain plays a role in controlling integrin function via recruitment of ADAP-SKAP complexes to integrins as well as in controlling the ability of ADAP to interact with the CBM signalosome and regulate NF-kappaB. SKAP1 is necessary for RapL binding to membranes in a PH domain-dependent manner and the PI3K pathway. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Skap55/Skap1, Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. 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: 270180  Cd Length: 106  Bit Score: 51.40  E-value: 4.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRK----NWTERWFVLKPNIISYYVSEDLKDKKGDILLdENCCVESLPD--KDGKK-CLFLVKCFDK- 282
Cdd:cd13380   1 ILKQGYLEKRSKDHSffgsEWQKRWCVLTNRAFYYYASEKSKQPKGGFLI-KGYSAQMAPHlrKDSRRdSCFELTTPGRr 79
                        90
                ....*....|....*....
gi 93102364 283 TFEISASDKKKKQEWIQAI 301
Cdd:cd13380  80 TYQFTAASPSEARDWVDQI 98
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
295-505 4.46e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  295 QEWIQAIHSTIHLLKLGSPPPHKEARQRRKELRkkqlAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEK 374
Cdd:COG4913  262 ERYAAARERLAELEYLRAALRLWFAQRRLELLE----AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  375 KRLQtqvelqarfstELEREkliRQQMEEQVAQKSSELEQYLQRVRELE-DMYLKLQEALEDERQARQDEETVRKLQARL 453
Cdd:COG4913  338 DRLE-----------QLERE---IERLERELEERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEAL 403
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 93102364  454 LEEESSKRAELEkwhlEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQ 505
Cdd:COG4913  404 EEALAEAEAALR----DLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
225-305 5.31e-08

Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 is proposed to function in regulation of Akt phosphorylation. ORP9 has 2 forms, a long (ORP9L) and a short (ORP9S). ORP9L contains an N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains a FFAT motif and an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF 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: 241444  Cd Length: 102  Bit Score: 50.91  E-value: 5.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 225 KNWTERWFVLKPN--IISYYVSEDlKDKKGDilldENCCVE------SLPDKDgkKCLFLVKCFDKTFEISASDKKKKQE 296
Cdd:cd13290  13 KGWQYRWFVLDDNagLLSYYTSKE-KMMRGS----RRGCVRlkgavvGIDDED--DSTFTITVDQKTFHFQARDAEERER 85

                ....*....
gi 93102364 297 WIQAIHSTI 305
Cdd:cd13290  86 WIRALEDTI 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
318-525 7.89e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 7.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    318 EARQRRKELRKKQLAEQEELERQMKELQAaNESKQQELEAvRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKli 397
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRA-ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-- 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    398 rQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQT 477
Cdd:TIGR02168  848 -EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364    478 TEAEKQELENQR----------------------VLKEQALQEAMEQLEQLELERKQ-------ALEQYEEVKKKLE 525
Cdd:TIGR02168  927 LELRLEGLEVRIdnlqerlseeysltleeaealeNKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYD 1003
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
349-532 9.13e-08

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 54.96  E-value: 9.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   349 ESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTEL---EREKLIRQQMEEQVAQKSSELEQYLQRVRELEDM 425
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERkrrEQEEQRRLQQEQLERAEKMREELELEQQRRFEEI 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   426 YLKLQEaLEDERQARQDEETVRKLQARLLEEES-SKRAELEKWHLEQQQAIQTTEAEKQELENQRvLKEQALQEAMEQLE 504
Cdd:pfam15709 390 RLRKQR-LEEERQRQEEEERKQRLQLQAAQERArQQQEEFRRKLQELQRKKQQEEAERAEAEKQR-QKELEMQLAEEQKR 467
                         170       180       190
                  ....*....|....*....|....*....|...
gi 93102364   505 QLELERKQALE-----QYEEVKKKLEMATNKTK 532
Cdd:pfam15709 468 LMEMAEEERLEyqrqkQEAEEKARLEAEERRQK 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
317-525 9.35e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 9.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    317 KEARQRRKELRKKQ--------LAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQ---------- 378
Cdd:TIGR02169  207 REKAERYQALLKEKreyegyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlge 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    379 -TQVELQARF-STELEREKLIR---------QQMEEQVAQKSSELEQYLQRVRELE---DMYLKLQEALEDERQARQDEE 444
Cdd:TIGR02169  287 eEQLRVKEKIgELEAEIASLERsiaekerelEDAEERLAKLEAEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEEL 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    445 tvRKLQARlLEEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKL 524
Cdd:TIGR02169  367 --EDLRAE-LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443

                   .
gi 93102364    525 E 525
Cdd:TIGR02169  444 E 444
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
320-523 9.82e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 9.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 320 RQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQArfstelereklirQ 399
Cdd:COG4717  62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-------------L 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 400 QMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESskraelekwhLEQQQAIQTTE 479
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS----------LATEEELQDLA 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 93102364 480 AEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKK 523
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PH_Sbf1_hMTMR5 cd01235
Set binding factor 1 (also called Human MTMR5) Pleckstrin Homology (PH) domain; Sbf1 is a ...
215-305 2.18e-07

Set binding factor 1 (also called Human MTMR5) Pleckstrin Homology (PH) domain; Sbf1 is a myotubularin-related pseudo-phosphatase. Both Sbf1 and myotubularin interact with the SET domains of Hrx and other epigenetic regulatory proteins, but Sbf1 lacks phosphatase activity due to several amino acid changes in its structurally preserved catalytic pocket. It contains pleckstrin (PH), GEF, and myotubularin homology domains that are thought to be responsible for signaling and growth control. Sbf1 functions as an inhibitor of cellular growth. The N-terminal GEF homology domain serves to inhibit the transforming effects of Sbf1. 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: 269941  Cd Length: 106  Bit Score: 49.25  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 215 GYMMKKGHRRKNWTERWFVLKPNI--ISYYVSEDLKDKKGDILLDEnccVESL---------PDKDGKKCLFLVKCFDKT 283
Cdd:cd01235   7 GYLYKRGALLKGWKQRWFVLDSTKhqLRYYESREDTKCKGFIDLAE---VESVtpatpiigaPKRADEGAFFDLKTNKRV 83
                        90       100
                ....*....|....*....|..
gi 93102364 284 FEISASDKKKKQEWIQAIHSTI 305
Cdd:cd01235  84 YNFCAFDAESAQQWIEKIQSCL 105
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
318-512 2.30e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.87  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 318 EARQRRKELRKKQ----LAEQEE-LERQMKELQAANESKQQELEAVRKKLeeaasraaeeekKRLQTQVELQARFSTELE 392
Cdd:COG3206 193 EAEAALEEFRQKNglvdLSEEAKlLLQQLSELESQLAEARAELAEAEARL------------AALRAQLGSGPDALPELL 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 393 REKLIrQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDE-----ETVRKLQARLLEEESSKRAELEKw 467
Cdd:COG3206 261 QSPVI-QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqrilASLEAELEALQAREASLQAQLAQ- 338
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 93102364 468 hLEQQ-QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQ 512
Cdd:COG3206 339 -LEARlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
PH_RhoGap24 cd13379
Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ...
209-305 3.04e-07

Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241530  Cd Length: 114  Bit Score: 49.20  E-value: 3.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 209 LDVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVE-SLPDKDGKKCLFLV---------K 278
Cdd:cd13379   1 LEVIKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLPGNRVTEhPCNEEEPGKFLFEVvpggdrermT 80
                        90       100
                ....*....|....*....|....*..
gi 93102364 279 CFDKTFEISASDKKKKQEWIQAIHSTI 305
Cdd:cd13379  81 ANHETYLLMASTQNDMEDWVKSIRRVI 107
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
213-305 3.94e-07

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 49.53  E-value: 3.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRK-----NWTERWFVLKPNIISYYVSEDLKD--KKGDILLDENCCVESLPD--KDGKKCLFLVKCFDKT 283
Cdd:cd01238   1 LEGLLVKRSQGKKrfgpvNYKERWFVLTKSSLSYYEGDGEKRgkEKGSIDLSKVRCVEEVKDeaFFERKYPFQVVYDDYT 80
                        90       100
                ....*....|....*....|..
gi 93102364 284 FEISASDKKKKQEWIQAIHSTI 305
Cdd:cd01238  81 LYVFAPSEEDRDEWIAALRKVC 102
PH_RasGRF1_2 cd13261
Ras-specific guanine nucleotide-releasing factors 1 and 2 Pleckstrin homology (PH) domain; ...
210-302 3.96e-07

Ras-specific guanine nucleotide-releasing factors 1 and 2 Pleckstrin homology (PH) domain; RasGRF1 (also called GRF1; CDC25Mm/Ras-specific nucleotide exchange factor CDC25; GNRP/Guanine nucleotide-releasing protein) and RasGRF2 (also called GRF2; Ras guanine nucleotide exchange factor 2) are a family of guanine nucleotide exchange factors (GEFs). They both promote the exchange of Ras-bound GDP by GTP, thereby regulating the RAS signaling pathway. RasGRF1 and RasGRF2 form homooligomers and heterooligomers. GRF1 has 3 isoforms and GRF2 has 2 isoforms. The longest isoforms of RasGRF1 and RasGRF2 contain the following domains: a Rho-GEF domain sandwiched between 2 PH domains, IQ domains, a REM (Ras exchanger motif) domain, and a Ras-GEF domainwhich gives them the capacity to activate both Ras and Rac GTPases in response to signals from a variety of neurotransmitter receptors. Their IQ domains allow them to act as calcium sensors to mediate the actions of NMDA-type and calcium-permeable AMPA-type glutamate receptors. GRF1 also mediates the action of dopamine receptors that signal through cAMP. GRF1 and GRF2 play strikingly different roles in regulating MAP kinase family members, neuronal synaptic plasticity, specific forms of learning and memory, and behavioral responses to psychoactive drugs. 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: 270081  Cd Length: 136  Bit Score: 49.35  E-value: 3.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLdENCCVESLP----DKDGKKCLFLVKCF----- 280
Cdd:cd13261   4 DGTKRGYLSKKTSDSGKWHERWFALYQNLLFYFENESSSRPSGLYLL-EGCYCERLPtpkgALKGKDHLEKQHYFtisfr 82
                        90       100
                ....*....|....*....|....*
gi 93102364 281 ---DKTFEISASDKKKKQEWIQAIH 302
Cdd:cd13261  83 henQRQYELRAETESDCDEWVEAIK 107
PTZ00121 PTZ00121
MAEBL; Provisional
318-544 5.19e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQEELERQMKELQAANESKqqelEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLI 397
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   398 RQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQ- 476
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEa 1488
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93102364   477 ---TTEAEKQELENQRvlKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGL 544
Cdd:PTZ00121 1489 kkkAEEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
211-305 5.57e-07

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241529  Cd Length: 116  Bit Score: 48.40  E-value: 5.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVE--SLPDKDGKKCLFL----------VK 278
Cdd:cd13378   3 VLKAGWLKKQRSIMKNWQQRWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNElpPNPEEPGKHLFEIlpggagdrekVP 82
                        90       100
                ....*....|....*....|....*..
gi 93102364 279 CFDKTFEISASDKKKKQEWIQAIHSTI 305
Cdd:cd13378  83 MNHEAFLLMANSQSDMEDWVKAIRRVI 109
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
374-525 7.45e-07

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 52.26  E-value: 7.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  374 KKRLQTQVELQARFStELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALED-ERQARQDEETVRKLQAR 452
Cdd:COG3096  508 QALAQRLQQLRAQLA-ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEElEEQAAEAVEQRSELRQQ 586
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364  453 LlEEESSKRAELEK----WHLEQQQAIQTTEAEKQELENQRVLKEqALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG3096  587 L-EQLRARIKELAArapaWLAAQDALERLREQSGEALADSQEVTA-AMQQLLEREREATVERDELAARKQALESQIE 661
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-496 8.42e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 8.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQlAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARfstELEREKL 396
Cdd:COG4717  81 KEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE---ELEERLE 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 397 IRQQMEEQVAQKSSELEQYLQRVRELEDmylklQEALEDERQARQDEETVRKLQARlLEEESSKRAELEKWHLEQQQAIQ 476
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLE-----QLSLATEEELQDLAEELEELQQR-LAELEEELEEAQEELEELEEELE 230
                       170       180
                ....*....|....*....|
gi 93102364 477 TTEAEKQELENQRVLKEQAL 496
Cdd:COG4717 231 QLENELEAAALEERLKEARL 250
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
330-539 1.01e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.30  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 330 QLAEQEELERQMKELQAANESKQQELEAVRKKleeaaSRAAEEEKKRLQTQVELQARFSTELEREkliRQQMEEQVAQKS 409
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-----EKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 410 SELEQYLQRVRELEDMYLKLQEALEdeRQARQDEETVrklqarLLEEESSKRAE-----LEKWHLEQQQAIQTTEAEKQE 484
Cdd:COG4942  90 KEIAELRAELEAQKEELAELLRALY--RLGRQPPLAL------LLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAE 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 93102364 485 LENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVA 539
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
PTZ00121 PTZ00121
MAEBL; Provisional
318-535 1.51e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLI 397
Cdd:PTZ00121 1203 EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   398 RQQMEE----------QVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKW 467
Cdd:PTZ00121 1283 LKKAEEkkkadeakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   468 HLEQQQAIQTTEAEKQELENQRVlKEQALQEAMEQLEQLELERKQA--LEQYEEVKKKLEMATNKTKSWK 535
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKK-KAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKK 1431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
307-525 1.51e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 307 LLKLGSPPPHKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEekkRLQTQVELQAR 386
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG---RLREVTLEGEG 655
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 387 FSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEK 466
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102364 467 WHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQlELERK-----QALEQYEEVKKKLE 525
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLER-EIEALgpvnlLAIEEYEELEERYD 798
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
214-301 2.44e-06

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. 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: 270126  Cd Length: 97  Bit Score: 46.21  E-value: 2.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 214 QGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDEN--CCVESLPDKDGKKCLFLV-KCFDKTFEISASD 290
Cdd:cd13316   3 SGWMKKRGERYGTWKTRYFVLKGTRLYYLKSENDDKEKGLIDLTGHrvVPDDSNSPFRGSYGFKLVpPAVPKVHYFAVDE 82
                        90
                ....*....|.
gi 93102364 291 KKKKQEWIQAI 301
Cdd:cd13316  83 KEELREWMKAL 93
PTZ00121 PTZ00121
MAEBL; Provisional
318-538 3.09e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQ--EELERQMKELQAANESKQQ--ELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELER 393
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   394 EKLIRQQME-EQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQ 472
Cdd:PTZ00121 1554 AEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93102364   473 QAIQ---TTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQA--LEQYEEVKKKLEMATNKTKSWKDKV 538
Cdd:PTZ00121 1634 KVEQlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKA 1704
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
390-534 3.34e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  390 ELEREkliRQQMEEQVAQ---KSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARL--LEEESSKRAEL 464
Cdd:COG4913  614 ALEAE---LAELEEELAEaeeRLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerLDASSDDLAAL 690
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  465 EkwhleqqQAIQTTEAEKQELEnqrvlkeQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSW 534
Cdd:COG4913  691 E-------EQLEELEAELEELE-------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
PTZ00121 PTZ00121
MAEBL; Provisional
285-511 4.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   285 EISASDKKKKQEWIQAIHSTIHLLKLGSPPPHKEARQRRKELRKkqlaeQEELERQMKELQAANESKQQELEAVRKKlee 364
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKA--- 1655
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   365 aaSRAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSEleqylqrVRELEDMYLKLQEALEDERQARQDEE 444
Cdd:PTZ00121 1656 --EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-------AKKAEELKKKEAEEKKKAEELKKAEE 1726
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102364   445 tVRKLQARLL----EEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQ---LELERK 511
Cdd:PTZ00121 1727 -ENKIKAEEAkkeaEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEkrrMEVDKK 1799
PRK12704 PRK12704
phosphodiesterase; Provisional
349-523 5.49e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  349 ESKQQELEAVRKKLEEAASRAAEEEKKrlqtQVELQARfstelEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLK 428
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEAEAIKK----EALLEAK-----EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  429 LQEALEDERQARQDEEtvrKLQARLLEEESSKRAELEKWHLEQQQAIQ-----TTEAEKQELENQrvLKEQALQEAMEQL 503
Cdd:PRK12704 101 KLELLEKREEELEKKE---KELEQKQQELEKKEEELEELIEEQLQELErisglTAEEAKEILLEK--VEEEARHEAAVLI 175
                        170       180
                 ....*....|....*....|
gi 93102364  504 EQLELERKqaleqyEEVKKK 523
Cdd:PRK12704 176 KEIEEEAK------EEADKK 189
PTZ00121 PTZ00121
MAEBL; Provisional
288-522 5.66e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   288 ASDKKKKQEWIQAiHSTIHLLKLGSPPPHKEARQRRKELRKKQlaeQEELERQMKELQAANESKQQELEAVRKKLEEAAS 367
Cdd:PTZ00121 1338 AEEAKKAAEAAKA-EAEAAADEAEAAEEKAEAAEKKKEEAKKK---ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   368 RAAEEEKKRLQTQVElqarfstELEREKLIRQQMEEqvAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVR 447
Cdd:PTZ00121 1414 AAAKKKADEAKKKAE-------EKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   448 KLQARLLEEESSKRA-ELEKWHLEQQQAIQTTEAEKQELENQRVLKEQA-----LQEAMEQLEQLELERKQALEQYEEVK 521
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKAdEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKKAEEKK 1564

                  .
gi 93102364   522 K 522
Cdd:PTZ00121 1565 K 1565
PRK01294 PRK01294
lipase secretion chaperone;
343-517 5.79e-06

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 48.52  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  343 ELQAANESKQQELEAVRKKLEEAASRaaeeeKKRLQTQVELQARFSTE-------LEREKLIRQQM--EEQVAQKSSELE 413
Cdd:PRK01294 142 AQLEDDGPGKLDLQALQQLLDARLAL-----RARFFSDWEIQAFFGEEnqyqryaLERLRIAQDPSlsDAQKAARLAALE 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  414 Q--------YLQRVRELEDmylkLQEALEDERQARQDEETVRKLQARLLEEESSKR-AELEKWHLEQQQAIQTTEAEKQE 484
Cdd:PRK01294 217 AqlpedlraALQESQRQQA----LLQQLAQLQASGASPQELRLMRAQLVGPEAAQRlEQLDQQRAAWQQRYDDYLAQRAQ 292
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 93102364  485 LENQRVLKEQALQEAMEQLEQL-----ELERKQALEQY 517
Cdd:PRK01294 293 ILNAAGLSPQDRQAQIAQLRQQrfspqEALRLAALERI 330
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
298-517 7.72e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 7.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 298 IQAIHSTIHLLKLGSPPPHKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKkrL 377
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--L 359
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 378 QTQVELQARfstELEREKLIRQ---QMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALeDERQARQDEETVRKLQARLL 454
Cdd:COG4717 360 EEELQLEEL---EQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELL-GELEELLEALDEEELEEELE 435
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 93102364 455 EEESsKRAELEKWHLEQQQAIQTTEAEKQELENqrvlkEQALQEAMEQLEQLELERKQALEQY 517
Cdd:COG4717 436 ELEE-ELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEW 492
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
315-536 7.84e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  315 PHKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEaasraaeeekkrlQTQVELQARFSTELERE 394
Cdd:PRK09510  81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK-------------QKQAEEAAAKAAAAAKA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  395 KLIRQQMEEQVAQKSSeleqylqrvreledmylklqealEDERQARQDEETVRKlqarlLEEESSKRAELEKWHLEQQQA 474
Cdd:PRK09510 148 KAEAEAKRAAAAAKKA-----------------------AAEAKKKAEAEAAKK-----AAAEAKKKAEAEAAAKAAAEA 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93102364  475 IQTTEAEKQElENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKD 536
Cdd:PRK09510 200 KKKAEAEAKK-KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
210-301 8.07e-06

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but 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: 275402  Cd Length: 116  Bit Score: 45.31  E-value: 8.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVS-EDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKTFEISA 288
Cdd:cd13215  20 AVIKSGYLSKRSKRTLRYTRYWFVLKGDTLSWYNSsTDLYFPAGTIDLRYATSIELSKSNGEATTSFKIVTNSRTYKFKA 99
                        90
                ....*....|...
gi 93102364 289 SDKKKKQEWIQAI 301
Cdd:cd13215 100 DSETSADEWVKAL 112
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
319-513 8.35e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 8.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  319 ARQRRKELRkkqlAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEE--EKKRLQTQVELQArfsTELEREKL 396
Cdd:COG4913  608 NRAKLAALE----AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAE---LEAELERL 680
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  397 IR-----QQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVrkLQARLLEEESSKRAELEKwHLEQ 471
Cdd:COG4913  681 DAssddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--LEAAEDLARLELRALLEE-RFAA 757
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 93102364  472 QQAIQTTEAEKQELENQRvlkeQALQEAMEQLEQlELERKQA 513
Cdd:COG4913  758 ALGDAVERELRENLEERI----DALRARLNRAEE-ELERAMR 794
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
317-527 8.42e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 48.79  E-value: 8.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQEELERQMKELQaaneskqqeleavrkkleeaasraaeeeKKRLQTQVELQARFSTELEREKl 396
Cdd:pfam15709 332 KASRDRLRAERAEMRRLEVERKRREQEEQ----------------------------RRLQQEQLERAEKMREELELEQ- 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   397 irQQMEEQVAQKSSELEQYLQRvRELEDMYLKLQEALEDERQARQDEETVRKLQ--ARLLEEESSKRAELEKwhleQQQa 474
Cdd:pfam15709 383 --QRRFEEIRLRKQRLEEERQR-QEEEERKQRLQLQAAQERARQQQEEFRRKLQelQRKKQQEEAERAEAEK----QRQ- 454
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 93102364   475 iqtTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMA 527
Cdd:pfam15709 455 ---KELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEA 504
PTZ00121 PTZ00121
MAEBL; Provisional
317-537 8.81e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 8.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQ----EELERQMKELQAANESKQQELEAvrKKLEEAASRAAEEEKKRLQTQVELQARFSTELE 392
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   393 REKLIRQQMEEQVAQKSSELEQyLQRVRELEdmylKLQEALEDERQARQDEETVRKL-QARLLEEESSKRAELEKWHLEQ 471
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADE-LKKAEELK----KAEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEE 1603
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93102364   472 QQAIQTTEAEKQELEN---QRVLKEQALQEAMEQLEQLELERKQALEQY--EEVKKKLEMATNKTKSWKDK 537
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDK 1674
PH_GPBP cd13283
Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called ...
213-304 9.11e-06

Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called Collagen type IV alpha-3-binding protein/hCERT; START domain-containing protein 11/StARD11; StAR-related lipid transfer protein 11) is a kinase that phosphorylates an N-terminal region of the alpha 3 chain of type IV collagen, which is commonly known as the goodpasture antigen. Its splice variant the ceramide transporter (CERT) mediates the cytosolic transport of ceramide. There have been additional splice variants identified, but all of them function as ceramide transport proteins. GPBP and CERT both contain an N-terminal PH domain, followed by a serine rich domain, and a C-terminal START domain. However, GPBP has an additional serine rich domain just upstream of its START domain. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF 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: 270100 [Multi-domain]  Cd Length: 100  Bit Score: 44.59  E-value: 9.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDK--KGDILLDENCCVESLPDkdgkKCLFLVKCFDKTFEISASD 290
Cdd:cd13283   1 LRGVLSKWTNYIHGWQDRYFVLKDGTLSYYKSESEKEYgcRGSISLSKAVIKPHEFD----ECRFDVSVNDSVWYLRAES 76
                        90
                ....*....|....
gi 93102364 291 KKKKQEWIQAIHST 304
Cdd:cd13283  77 PEERQRWIDALESH 90
PH2_ADAP cd01251
ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 2; ADAP (also called ...
210-305 1.38e-05

ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 2; ADAP (also called centaurin alpha) is a phophatidlyinositide binding protein consisting of an N-terminal ArfGAP domain and two PH domains. In response to growth factor activation, PI3K phosphorylates phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 1 is recruited to the plasma membrane following growth factor stimulation by specific binding of its PH domain to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 2 is constitutively bound to the plasma membrane since it binds phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate with equal affinity. This cd contains the second 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: 241282  Cd Length: 105  Bit Score: 44.12  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKKGHRRKN-WTERWFVLKPNIISYYvsedlKDK-----KGDILL---DENCCV-ESLP--DKDGKKCLFLV 277
Cdd:cd01251   1 DFLKEGYLEKTGPKQTDgFRKRWFTLDDRRLMYF-----KDPldafpKGEIFIgskEEGYSVrEGLPpgIKGHWGFGFTL 75
                        90       100
                ....*....|....*....|....*...
gi 93102364 278 KCFDKTFEISASDKKKKQEWIQAIHSTI 305
Cdd:cd01251  76 VTPDRTFLLSAETEEERREWITAIQKVL 103
DUF4175 pfam13779
Domain of unknown function (DUF4175);
317-524 1.68e-05

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 48.06  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKE-LRKKqlAEQEELERQMKELQAANESKQQELEavrkkleeaasraaEEEKKRLQTQVELQARFSTELEREK 395
Cdd:pfam13779 492 RAAQERLSEaLERG--ASDEEIAKLMQELREALDDYMQALA--------------EQAQQNPQDLQQPDDPNAQEMTQQD 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   396 LIR--QQMEEqvAQKSSELEQYLQRVRELEDMYLKLQEAL-EDERQARQDE---------ETVRKlQARLLEEESSKRAE 463
Cdd:pfam13779 556 LQRmlDRIEE--LARSGRRAEAQQMLSQLQQMLENLQAGQpQQQQQQGQSEmqqamdelgDLLRE-QQQLLDETFRQLQQ 632
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   464 LEKWHLEQQ----QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQleleRKQAL-EQYEEVKKKL 524
Cdd:pfam13779 633 QGGQQQGQPgqqgQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAE----RQQALrRRLEELQDEL 694
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
322-532 1.82e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  322 RRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLeEAASRAAEEEKKRLQTQVELQARFsTELEREKLIR--- 398
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL-PELREELEKLEKEVKELEELKEEI-EELEKELESLegs 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  399 --------QQMEEQVAQKSSELEQYLQRVRELEDM------YLKLQEALEDERQARQD-EETVRKLQARL--LEEESSKR 461
Cdd:PRK03918 254 krkleekiRELEERIEELKKEIEELEEKVKELKELkekaeeYIKLSEFYEEYLDELREiEKRLSRLEEEIngIEERIKEL 333
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93102364  462 AELEKWHLEQQQAIQTTEAEKQELENqrvlKEQALQEAMEQLEQLE-LERKQALEQYEEVKKKLEMATNKTK 532
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEKAKE 401
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
399-525 1.87e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 399 QQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEkwhlEQQQAIQTT 478
Cdd:COG1579  13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE----EQLGNVRNN 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 93102364 479 ------EAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG1579  89 keyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
210-301 2.05e-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: 43.93  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKKGHRRK---NWTERWFVLKPNIISYYVSEDLKDKKGDILLDE-NCCVESLPDKDGK---KCLFLVKCfDK 282
Cdd:cd13308   8 DVIHSGTLTKKGGSQKtlqNWQLRYVIIHQGCVYYYKNDQSAKPKGVFSLNGyNRRAAEERTSKLKfvfKIIHLSPD-HR 86
                        90
                ....*....|....*....
gi 93102364 283 TFEISASDKKKKQEWIQAI 301
Cdd:cd13308  87 TWYFAAKSEDEMSEWMEYI 105
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
335-525 2.32e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  335 EELERQMKELQAANESKQQELEAVRKKLEeaasraaeeekkRLQTQVELQARFSTELEREKLIRQQMEEQ---VAQKSSE 411
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLE------------RAEDLVEAEDRIERLEERREDLEELIAERretIEEKRER 538
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  412 LEQYLQRVRELEDmylklqEALEDERQARQDEETVRKLQARLLEEESsKRAELEKwHLEQQQAIQTTEAEKQELENQRvl 491
Cdd:PRK02224 539 AEELRERAAELEA------EAEEKREAAAEAEEEAEEAREEVAELNS-KLAELKE-RIESLERIRTLLAAIADAEDEI-- 608
                        170       180       190
                 ....*....|....*....|....*....|....
gi 93102364  492 keQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:PRK02224 609 --ERLREKREALAELNDERRERLAEKRERKRELE 640
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
375-530 2.50e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.76  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   375 KRLQTQVELQARfsTELEREKLIRQQMEEQVAQKSSELeqylQRVRELEDMYLKLQEALEDERQARQDEEtvrklQARLL 454
Cdd:TIGR02794  53 NRIQQQKKPAAK--KEQERQKKLEQQAEEAEKQRAAEQ----ARQKELEQRAAAEKAAKQAEQAAKQAEE-----KQKQA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   455 EEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQAL--QEAMEQLEQLELERKQALE-----QYEEVKKKLEMA 527
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEaeakaKAEEAKAKAEAA 201

                  ...
gi 93102364   528 TNK 530
Cdd:TIGR02794 202 KAK 204
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-525 2.81e-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: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAvRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKL 396
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA-EAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 397 IRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEesskRAELEKWHLEqqqAI- 475
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE----IEALGPVNLL---AIe 788
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364 476 --QTTEAEKQELENQRvlkeQALQEAMEQLEQ----LELERKQAL-EQYEEVKKKLE 525
Cdd:COG1196 789 eyEELEERYDFLSEQR----EDLEEARETLEEaieeIDRETRERFlETFDAVNENFQ 841
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
316-524 2.88e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    316 HKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREK 395
Cdd:pfam02463  252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    396 LIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDErqaRQDEETVRKLQARLLEEESSKRAELEKWHLEQQQA- 474
Cdd:pfam02463  332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE---EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAq 408
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 93102364    475 IQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKL 524
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
PTZ00121 PTZ00121
MAEBL; Provisional
317-542 2.98e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQ-----EELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQA--RFST 389
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAE 1388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   390 ELEREKLIRQQMEEQvAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHL 469
Cdd:PTZ00121 1389 EKKKADEAKKKAEED-KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364   470 EQQQA--IQTTEAEKQELENQRVLKEQALQEAmEQLEQLELERKQA--LEQYEEVKKKLEMATNKTKSWKDKVAHHE 542
Cdd:PTZ00121 1468 EAKKAdeAKKKAEEAKKADEAKKKAEEAKKKA-DEAKKAAEAKKKAdeAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
212-305 3.01e-05

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. 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: 270073  Cd Length: 94  Bit Score: 42.76  E-value: 3.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 212 LKQGYMMKKGHRRKN--WTERWFVLKPNIISYYVSEDLKDKKGDILLdeNCCVESLPDKDGKkclFLVKCFDKTFEISAS 289
Cdd:cd13253   1 IKSGYLDKQGGQGNNkgFQKRWVVFDGLSLRYFDSEKDAYSKRIIPL--SAISTVRAVGDNK---FELVTTNRTFVFRAE 75
                        90
                ....*....|....*.
gi 93102364 290 DKKKKQEWIQAIHSTI 305
Cdd:cd13253  76 SDDERNLWCSTLQAAI 91
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
316-524 3.20e-05

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 46.61  E-value: 3.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 316 HKEARQRRKELRKKQ---LAEQEELERQMKELQAAN--ESKQQELEAVRKkleeaasraaeeekkRLQTQVELQARFSTE 390
Cdd:COG0497 167 WRALKKELEELRADEaerARELDLLRFQLEELEAAAlqPGEEEELEEERR---------------RLSNAEKLREALQEA 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 391 LER--------EKLIRQQME--EQVAQKSSELEQYLQRvreLEDMYLKLQEALED-ERQARQ---DEETVRKLQARLLEE 456
Cdd:COG0497 232 LEAlsggeggaLDLLGQALRalERLAEYDPSLAELAER---LESALIELEEAASElRRYLDSlefDPERLEEVEERLALL 308
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93102364 457 ESSKRaeleKWHLEQQQAIQTTEAEKQELEnqrvlkeqALQEAMEQLEQLELERKQALEQYEEVKKKL 524
Cdd:COG0497 309 RRLAR----KYGVTVEELLAYAEELRAELA--------ELENSDERLEELEAELAEAEAELLEAAEKL 364
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
321-525 3.59e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.89  E-value: 3.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    321 QRRKELRKKQLAEQEELERQmKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQQ 400
Cdd:TIGR00618  601 EKLSEAEDMLACEQHALLRK-LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    401 MEEQVAQksSELEQYLQRVRELEDMYLKLQEALEDE----RQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQ 476
Cdd:TIGR00618  680 LALQKMQ--SEKEQLTYWKEMLAQCQTLLRELETHIeeydREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK 757
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 93102364    477 TTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:TIGR00618  758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
mukB PRK04863
chromosome partition protein MukB;
325-524 4.19e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   325 ELRKKQlAEQEELERQMKELQAANESKQQELEAVRKKLEEAAsraaeeekkRLQTQVELQARfSTELEREKLIRQQMEE- 403
Cdd:PRK04863  838 ELRQLN-RRRVELERALADHESQEQQQRSQLEQAKEGLSALN---------RLLPRLNLLAD-ETLADRVEEIREQLDEa 906
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   404 QVAQKSseLEQYLQRVRELEDMYLKLQ------EALEDE-RQARQDEETVRKlQARLLEEESSKRAelekwHLEQQQAIQ 476
Cdd:PRK04863  907 EEAKRF--VQQHGNALAQLEPIVSVLQsdpeqfEQLKQDyQQAQQTQRDAKQ-QAFALTEVVQRRA-----HFSYEDAAE 978
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 93102364   477 tteaekqelenqRVLKEQALQEAM-EQLEQLELERKQALEQYEEVKKKL 524
Cdd:PRK04863  979 ------------MLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQL 1015
PH_PLD cd01254
Phospholipase D pleckstrin homology (PH) domain; PLD hydrolyzes phosphatidylcholine to ...
213-301 4.36e-05

Phospholipase D pleckstrin homology (PH) domain; PLD hydrolyzes phosphatidylcholine to phosphatidic acid (PtdOH), which can bind target proteins. PLD contains a PH domain, a PX domain and four conserved PLD signature domains. The PLD PH domain is specific for bisphosphorylated inositides. 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: 269956  Cd Length: 136  Bit Score: 43.40  E-value: 4.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 213 KQGYMMKK--GHRR---------------KNWTERWFVLKPniiSY--YVSEDLKDKKGDILL-DENCCVESLPDKD--G 270
Cdd:cd01254  26 KEGYLKKRsgGHRQgwrvchfyccckamcGRWSKRWFIVKD---SFlaYVKDPDSGAILDVFLfDQEFKVSRGGKETkyG 102
                        90       100       110
                ....*....|....*....|....*....|.
gi 93102364 271 KKCLFLVKCFDKTFEISASDKKKKQEWIQAI 301
Cdd:cd01254 103 SRHGLKITNLSRKLKLKCKSERKAKQWVESI 133
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
398-539 4.50e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  398 RQQME--EQVAQKSSELEQYLQRVRELEDM------------YLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAE 463
Cdd:COG4913  248 REQIEllEPIRELAERYAAARERLAELEYLraalrlwfaqrrLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364  464 LEKWHLEQQ-QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVA 539
Cdd:COG4913  328 LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
390-549 5.54e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 5.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 390 ELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQ---EALEDERQARQDEETVRKLQARLLEEEsskrAELEK 466
Cdd:COG4717  75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReelEKLEKLLQLLPLYQELEALEAELAELP----ERLEE 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 467 WhLEQQQAIQTTEAEKQELENQRVLKEQALQEAmeqLEQLELERKQAL----EQYEEVKKKLEMATNKTKSWKDKVAHHE 542
Cdd:COG4717 151 L-EERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELqdlaEELEELQQRLAELEEELEEAQEELEELE 226

                ....*..
gi 93102364 543 GLIRLIE 549
Cdd:COG4717 227 EELEQLE 233
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
316-525 6.79e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 6.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    316 HKEARQRRKEL------RKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFST 389
Cdd:TIGR02169  715 SRKIGEIEKEIeqleqeEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    390 ELERE----KLIRQQMEEQVA------QKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDE--ETVRKLQARLlEEE 457
Cdd:TIGR02169  795 EIQAElsklEEEVSRIEARLReieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlnGKKEELEEEL-EEL 873
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93102364    458 SSKRAELEKWHLEQQQAIQTTEAEKQELENqrvlKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEAQLRELER----KIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
PRK09039 PRK09039
peptidoglycan -binding protein;
403-516 6.92e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.34  E-value: 6.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  403 EQVAQKSSELEQYLQRVRELEDMylklqeaLEDERQARQD-EETVRKLQARLLEEESsKRAELEKWHLEQQQAIQTTEAE 481
Cdd:PRK09039  46 REISGKDSALDRLNSQIAELADL-------LSLERQGNQDlQDSVANLRASLSAAEA-ERSRLQALLAELAGAGAAAEGR 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 93102364  482 KQELENQRVLKEQALQEAMEQLE----QLELERKQ--ALEQ 516
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVEllnqQIAALRRQlaALEA 158
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
330-532 6.95e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.94  E-value: 6.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    330 QLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQ---ARFSTELE--REKLIRQQMEEQ 404
Cdd:pfam01576  167 NLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQeqiAELQAQIAelRAQLAKKEEELQ 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    405 VAQKSSELE-----QYLQRVRELEDMYLKLQEALEDERQARQDEETVRKlqaRLLEEESSKRAELEKwhleqqqaIQTTE 479
Cdd:pfam01576  247 AALARLEEEtaqknNALKKIRELEAQISELQEDLESERAARNKAEKQRR---DLGEELEALKTELED--------TLDTT 315
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102364    480 AEKQELENQRVLKEQALQEAME--------QLEQLELERKQALEQYEE---VKKKLEMATNKTK 532
Cdd:pfam01576  316 AAQQELRSKREQEVTELKKALEeetrsheaQLQEMRQKHTQALEELTEqleQAKRNKANLEKAK 379
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
316-539 8.53e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 45.27  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   316 HKEARQRRKELRKKQLAEQEELERQMKELqaanESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREk 395
Cdd:pfam07888  50 QEAANRQREKEKERYKRDREQWERQRREL----ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQR- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   396 lirqqmeeqvaqksselEQYLQRVRELEDMYLKL-QEALEDERQARQDEETVRKLQARLLEEESSKRAeLEKWHLEQQQA 474
Cdd:pfam07888 125 -----------------AAHEARIRELEEDIKTLtQRVLERETELERMKERAKKAGAQRKEEEAERKQ-LQAKLQQTEEE 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93102364   475 IQTTEAEKQELEN---QRVLKEQALQEAMEQLEQL-------ELERKQALEQYEEVKKKLEMATNKTKSWKDKVA 539
Cdd:pfam07888 187 LRSLSKEFQELRNslaQRDTQVLQLQDTITTLTQKlttahrkEAENEALLEELRSLQERLNASERKVEGLGEELS 261
PH_RASA1 cd13260
RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...
211-301 8.54e-05

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. 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: 270080  Cd Length: 103  Bit Score: 41.95  E-value: 8.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCV-----ESLPDKDgkKC-------LFLVK 278
Cdd:cd13260   3 IDKKGYLLKKGGKNKKWKNLYFVLEGKEQHLYFFDNEKRTKPKGLIDLSYCSlypvhDSLFGRP--NCfqivvraLNEST 80
                        90       100
                ....*....|....*....|...
gi 93102364 279 CFDktfeISASDKKKKQEWIQAI 301
Cdd:cd13260  81 ITY----LCADTAELAQEWMRAL 99
PH_ORP10_ORP11 cd13291
Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin ...
215-298 9.02e-05

Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin homology (PH) domain; Human ORP10 is involvedt in intracellular transport or organelle positioning and is proposed to function as a regulator of cellular lipid metabolism. Human ORP11 localizes at the Golgi-late endosome interface and is thought to form a dimer with ORP9 functioning as an intracellular lipid sensor or transporter. Both ORP10 and ORP11 contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF 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: 270106  Cd Length: 107  Bit Score: 41.90  E-value: 9.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 215 GYMMKKGHRRKNWTERWFVLKPN--IISYYVSEDLKDKKGDILLDENCCVESLPDKDGKkcLFLVKCFD-KTFEISASDK 291
Cdd:cd13291   3 GQLLKYTNVVKGWQNRWFVLDPDtgILEYFLSEESKNQKPRGSLSLAGAVISPSDEDSH--TFTVNAANgEMYKLRAADA 80

                ....*..
gi 93102364 292 KKKQEWI 298
Cdd:cd13291  81 KERQEWV 87
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
318-544 9.86e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  318 EARQRRKELRK--KQLAEQEELERQMKE----LQAANESKQQELEAVRKKLEEAASRAAEEEKKR--LQTQVELQARFST 389
Cdd:PRK02224 210 GLESELAELDEeiERYEEQREQARETRDeadeVLEEHEERREELETLEAEIEDLRETIAETEREReeLAEEVRDLRERLE 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  390 ELEREkliRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQ----DEETVRKlQARLLEEES----SKR 461
Cdd:PRK02224 290 ELEEE---RDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahneEAESLRE-DADDLEERAeelrEEA 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  462 AELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHH 541
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA 445

                 ...
gi 93102364  542 EGL 544
Cdd:PRK02224 446 EAL 448
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
385-525 9.86e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 9.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 385 ARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDER------QARQDE-ETVRKLQARLLEEE 457
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyEEQLGNvRNNKEYEALQKEIE 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102364 458 SSKR--AELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLE----QLELERKQALEQYEEVKKKLE 525
Cdd:COG1579 100 SLKRriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAAKIP 173
mukB PRK04863
chromosome partition protein MukB;
316-525 1.02e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   316 HKEARQRRKELRKKQLaeqeELERQMKELQAANESKQQELEAVRK-----------KLEEAASRAAEEEKKRLQTQVELQ 384
Cdd:PRK04863  444 LEEFQAKEQEATEELL----SLEQKLSVAQAAHSQFEQAYQLVRKiagevsrseawDVARELLRRLREQRHLAEQLQQLR 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   385 ARFStELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALED----ERQARQDEETVRklqaRLLEEESSK 460
Cdd:PRK04863  520 MRLS-ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESlsesVSEARERRMALR----QQLEQLQAR 594
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   461 RAELEK----WHLEQQQAIQTTEAEKQELEN-QRVlkEQALQEAMEQLEQLELERkqalEQYEEVKKKLE 525
Cdd:PRK04863  595 IQRLAArapaWLAAQDALARLREQSGEEFEDsQDV--TEYMQQLLERERELTVER----DELAARKQALD 658
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
317-520 1.08e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    317 KEARQRRKELRKKQLAEQEELERQMKELQAAneskqqeLEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKL 396
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEA-------LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    397 IRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEE----SSKRAELEKWHLEQQ 472
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdlKKERDELEAQLRELE 902
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 93102364    473 QAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEV 520
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
318-528 1.14e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    318 EARQRRKELRKKQL-AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAaeeekKRLQTQV-ELQARFStELEREk 395
Cdd:TIGR02169  818 EQKLNRLTLEKEYLeKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-----EELEAALrDLESRLG-DLKKE- 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    396 liRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEderqARQDEETVRKLQARLLEEESSKRAELEKWhleqQQAI 475
Cdd:TIGR02169  891 --RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEIEDPKGEDEEIPEEELSLEDV----QAEL 960
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 93102364    476 QTTEAEKQELE--NQRVLKE-----QALQEAMEQLEQLELERKQAL---EQYEEVKKKLEMAT 528
Cdd:TIGR02169  961 QRVEEEIRALEpvNMLAIQEyeevlKRLDELKEKRAKLEEERKAILeriEEYEKKKREVFMEA 1023
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
316-524 1.26e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    316 HKEARQRRKELRKKQLAEQEELE---RQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQ--------VELQ 384
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIEnvkSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskleeevSRIE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    385 ARFStELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEE----SSK 460
Cdd:TIGR02169  812 ARLR-EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdlKKE 890
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    461 RAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQ---------------------------- 512
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsledvqaelqrveeeiral 970
                          250
                   ....*....|....*...
gi 93102364    513 ------ALEQYEEVKKKL 524
Cdd:TIGR02169  971 epvnmlAIQEYEEVLKRL 988
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
397-531 1.33e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 397 IRQQMEEQVAQKSSEL--------EQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKwh 468
Cdd:COG4717  43 IRAMLLERLEKEADELfkpqgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-- 120
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364 469 LEQQQAIQTTEAEKQELENQRVLKE---QALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKT 531
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQL 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
318-525 1.37e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    318 EARQRRKELRKKQLAEQEElerQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQarfSTELEREKLI 397
Cdd:TIGR02169  269 EIEQLLEELNKKIKDLGEE---EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID---KLLAEIEELE 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    398 RQQMEEQVaQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKlqarLLEEESSKRAELEKWHLEQQQAIQT 477
Cdd:TIGR02169  343 REIEEERK-RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQR 417
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 93102364    478 TEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
318-528 1.47e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  318 EARQRRKELrkkqlaeqEELERQMKELQ---AANESKQQEL-EAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELER 393
Cdd:PRK02224 245 EHEERREEL--------ETLEAEIEDLRetiAETEREREELaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  394 EKL------IRQQMEEQ---VAQKSSELEQYLQRVRELEDMYLKLQE-ALEDERQARQDEETVRKLQARL--LEEE---- 457
Cdd:PRK02224 317 EELedrdeeLRDRLEECrvaAQAHNEEAESLREDADDLEERAEELREeAAELESELEEAREAVEDRREEIeeLEEEieel 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  458 --------------SSKRAELEKWHLEQQQAIQTTEAEKQELENqRVLKEQALQEA----------------------ME 501
Cdd:PRK02224 397 rerfgdapvdlgnaEDFLEELREERDELREREAELEATLRTARE-RVEEAEALLEAgkcpecgqpvegsphvetieedRE 475
                        250       260
                 ....*....|....*....|....*..
gi 93102364  502 QLEQLELERKQALEQYEEVKKKLEMAT 528
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE 502
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
210-301 1.63e-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: 41.10  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKK-GHRRKNWTERWFVLKPNIISYYVSEdlKDKK--GDILLdENCCVESLPDKD--GKKCLFLVKCFD-KT 283
Cdd:cd13248   6 PVVMSGWLHKQgGSGLKNWRKRWFVLKDNCLYYYKDP--EEEKalGSILL-PSYTISPAPPSDeiSRKFAFKAEHANmRT 82
                        90
                ....*....|....*...
gi 93102364 284 FEISASDKKKKQEWIQAI 301
Cdd:cd13248  83 YYFAADTAEEMEQWMNAM 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
416-525 1.74e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    416 LQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRA---ELEKWHLEQQQAIQTTEAEKQELENQRVLK 492
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleELSRQISALRKDLARLEAEVEQLEERIAQL 752
                           90       100       110
                   ....*....|....*....|....*....|...
gi 93102364    493 EQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
376-525 1.75e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  376 RLQTQVELQARfsTELEREKLIRQQmEEQVAQKSSElEQylQRVRELEdmylklQEALEDERQARQDEETVRK--LQARL 453
Cdd:PRK09510  66 RQQQQQKSAKR--AEEQRKKKEQQQ-AEELQQKQAA-EQ--ERLKQLE------KERLAAQEQKKQAEEAAKQaaLKQKQ 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93102364  454 LEEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAmEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKA-AAEAKKKAEAEAAAKAAAEAKKKAE 204
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
316-505 1.82e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.56  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  316 HKEARQRRKELRKKQ-LAEQEE-LERQMKELQAaNESKQQELEAVRKKLEEAAsraaeeeKKRLQTQVELQARFST-ELE 392
Cdd:COG3096  494 WQTARELLRRYRSQQaLAQRLQqLRAQLAELEQ-RLRQQQNAERLLEEFCQRI-------GQQLDAAEELEELLAElEAQ 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  393 REKLIRQQME--EQVAQKSSELEQYLQRVRELED---MYLKLQEALEdeRQARQDEETVRKLQarlleeesskraelekw 467
Cdd:COG3096  566 LEELEEQAAEavEQRSELRQQLEQLRARIKELAArapAWLAAQDALE--RLREQSGEALADSQ----------------- 626
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 93102364  468 hlEQQQAIQTT---EAEKQELENQRVLKEQALQEAMEQLEQ 505
Cdd:COG3096  627 --EVTAAMQQLlerEREATVERDELAARKQALESQIERLSQ 665
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
315-507 1.97e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    315 PHKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELere 394
Cdd:TIGR00618  694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV--- 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    395 klirqQMEEQVAQKSSELEQYLQ-RVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEEsskRAELEKWHLEQQQ 473
Cdd:TIGR00618  771 -----TAALQTGAELSHLAAEIQfFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE---EEQFLSRLEEKSA 842
                          170       180       190
                   ....*....|....*....|....*....|....
gi 93102364    474 AIQTTEAEKQELENQRVLKEQALQEAMEQLEQLE 507
Cdd:TIGR00618  843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
211-301 1.97e-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: 40.65  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDeNCCVESLPDKD---GKKCLFLVKCFDKTFEIS 287
Cdd:cd01233   6 VSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLS-TARVEYSPDQEallGRPNVFAVYTPTNSYLLQ 84
                        90
                ....*....|....
gi 93102364 288 ASDKKKKQEWIQAI 301
Cdd:cd01233  85 ARSEKEMQDWLYAI 98
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
317-525 2.14e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKL 396
Cdd:pfam13868  98 QEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   397 IRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEAlEDERQARQDEETVRKLQARLLEEESSKRAElekwHLEQQQAIQ 476
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE-EQERKERQKEREEAEKKARQRQELQQAREE----QIELKERRL 252
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 93102364   477 TTEAEKQELENQRVLKEQALQEAMEQLEQlELERKQALEQYEEVKKKLE 525
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEA-EKRRMKRLEHRRELEKQIE 300
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
377-533 2.58e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.73  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   377 LQTQVELQARFSTELERE-KLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLE 455
Cdd:pfam07888  32 LQNRLEECLQERAELLQAqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93102364   456 EESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKS 533
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
COG5022 COG5022
Myosin heavy chain [General function prediction only];
340-541 3.59e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  340 QMKELQAANESKQQELEA---VRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKssELEQYL 416
Cdd:COG5022  811 EYRSYLACIIKLQKTIKRekkLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER--QLQELK 888
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  417 QRVRELEDMYLKLqeaLEDERQARqdeETVRKLQARLLEEESSKRAELEKWhleqQQAIQTTEAEKQELENQRVLKE-QA 495
Cdd:COG5022  889 IDVKSISSLKLVN---LELESEII---ELKKSLSSDLIENLEFKTELIARL----KKLLNNIDLEEGPSIEYVKLPElNK 958
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 93102364  496 LQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHH 541
Cdd:COG5022  959 LHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAEL 1004
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
210-305 3.66e-04

Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. 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: 270109  Cd Length: 126  Bit Score: 40.50  E-value: 3.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMK---KGHRRKNWT--ERWFVLKPNIISYYVS-EDLKDKKGDILLDENCCV----ESLPDKDG--------- 270
Cdd:cd13297  12 DVIERGWLYKeggKGGARGNLTkkKRWFVLTGNSLDYYKSsEKNSLKLGTLVLNSLCSVvppdEKMAKETGywtftvhgr 91
                        90       100       110
                ....*....|....*....|....*....|....*
gi 93102364 271 KKCLFLvkcFDKTFEISasdkkkkQEWIQAIHSTI 305
Cdd:cd13297  92 KHSFRL---YTKLQEEA-------MRWVNAIQDVI 116
PH_Phafin2-like cd01218
Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; ...
212-301 3.94e-04

Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; Phafin2 is differentially expressed in the liver cancer cell and regulates the structure and function of the endosomes through Rab5-dependent processes. Phafin2 modulates the cell's response to extracellular stimulation by modulating the receptor density on the cell surface. Phafin2 contains a PH domain and a FYVE 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: 269927 [Multi-domain]  Cd Length: 123  Bit Score: 40.32  E-value: 3.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 212 LKQGYMMK---KGHRRknwteRWFVLKPNIISY--YVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKTFEI 286
Cdd:cd01218  31 VGEGVLTKvcrKKPKP-----RQFFLFNDILVYgsIVINKKKYNKQRIIPLEDVKIEDLEDTGELKNGWQIISPKKSFVV 105
                        90
                ....*....|....*
gi 93102364 287 SASDKKKKQEWIQAI 301
Cdd:cd01218 106 YAATATEKSEWMDHI 120
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
318-520 3.95e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  318 EARQRRKELRKKQLAEQE---ELERQMKELQAANESKQQELEAVRKKLEeaasraaeeekkRLQTQVELQ---ARFSTEL 391
Cdd:COG3096  289 ELRRELFGARRQLAEEQYrlvEMARELEELSARESDLEQDYQAASDHLN------------LVQTALRQQekiERYQEDL 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  392 ER--EKLIRQQM-----EEQVAQKSSELEQYLQRVRELEDMYLKLQEALeDERQAR--QDEETVRKL-QARLLEEESSKR 461
Cdd:COG3096  357 EEltERLEEQEEvveeaAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQTRaiQYQQAVQALeKARALCGLPDLT 435
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93102364  462 AE-LEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQE---AMEQLEQL--ELERKQALEQYEEV 520
Cdd:COG3096  436 PEnAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQfekAYELVCKIagEVERSQAWQTAREL 500
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
319-501 4.39e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 42.75  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   319 ARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQAR------FSTELE 392
Cdd:pfam19220 207 TRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRdeairaAERRLK 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   393 REKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQE-------ALED-ERQARQDEETVRKLQARLleeesskrAEL 464
Cdd:pfam19220 287 EASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEEraemltkALAAkDAALERAEERIASLSDRI--------AEL 358
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 93102364   465 EKWHLEQQQAIQTTEAE-KQELEN---QRVLKEQALQEAME 501
Cdd:pfam19220 359 TKRFEVERAALEQANRRlKEELQReraERALAQGALEIARE 399
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
309-509 4.50e-04

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 43.11  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   309 KLGSPPPHK------EARQR-RKELRKKQLAEQEELERQMKELQaanESKQQELEavrkkleeaasraaeeekkrlqtqv 381
Cdd:pfam10168 524 KLSSPSPQEclqllsRATQVfREEYLKKHDLAREEIQKRVKLLK---LQKEQQLQ------------------------- 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   382 ELQarfSTELEREKLirQQMEEQVAQKSSEL----EQYLQRVrelEDMYLKLQEAL----EDERQARQD----EETVRKL 449
Cdd:pfam10168 576 ELQ---SLEEERKSL--SERAEKLAEKYEEIkdkqEKLMRRC---KKVLQRLNSQLpvlsDAEREMKKEletiNEQLKHL 647
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   450 QARLleEESSKRAELEKWHLEQQQAIQTTEA----EKQELENQRVLKEQA--LQEAMEQLEQLELE 509
Cdd:pfam10168 648 ANAI--KQAKKKMNYQRYQIAKSQSIRKKSSlslsEKQRKTIKEILKQLGseIDELIKQVKDINKH 711
PTZ00121 PTZ00121
MAEBL; Provisional
282-522 4.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   282 KTFEISASDKKKKQEWIQAIHSTIHLLKLGSPPPHKEARQRRKELRKKQLAEQ-----EELERQMKELQAANESKQQELE 356
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkaEEDKKKADELKKAAAAKKKADE 1422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   357 AVRK----------KLEEAASRAAEEEKKRLQtqvelqarfstELEREKLIRQQMEEqvAQKSSELEQYLQRVRELEDMY 426
Cdd:PTZ00121 1423 AKKKaeekkkadeaKKKAEEAKKADEAKKKAE-----------EAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAK 1489
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   427 LKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHlEQQQAIQTTEAEK----QELENQRVLKEQALQEAMEQ 502
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-EAKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEE 1568
                         250       260
                  ....*....|....*....|
gi 93102364   503 LEQLELERKQALEQYEEVKK 522
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKK 1588
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
317-525 5.10e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  317 KEARQRRKELRKKQlAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKL 396
Cdd:PRK02224 370 SELEEAREAVEDRR-EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  397 IR--------------------QQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETvRKLQARLLEE 456
Cdd:PRK02224 449 LEagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAE 527
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364  457 essKRAELEkwhlEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:PRK02224 528 ---RRETIE----EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
317-529 5.16e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQEELERQMKELQAA-NESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVE--------LQARF 387
Cdd:pfam07888 167 KEEEAERKQLQAKLQQTEEELRSLSKEFQELrNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEalleelrsLQERL 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   388 STELEREKLIRQQMEEQVAQKS---SELEQ----YLQRVRELEDMYLKLQEALEDERQARQ--------DEETVRKLQAR 452
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDrtqAELHQarlqAAQLTLQLADASLALREGRARWAQEREtlqqsaeaDKDRIEKLSAE 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   453 LLE-EESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQ--ALQEAMEQLEQLELERKQALEQYEEVKKKLEMATN 529
Cdd:pfam07888 327 LQRlEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELkaSLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
325-525 5.18e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 5.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    325 ELRKKQLAEQEELERQM---KELQAANESKQQELEAVRKKLEEA------ASRAAEEEKKRLQTQV-ELQARFStELERE 394
Cdd:pfam01576  349 EMRQKHTQALEELTEQLeqaKRNKANLEKAKQALESENAELQAElrtlqqAKQDSEHKRKKLEGQLqELQARLS-ESERQ 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    395 kliRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQE---ALEDERQARQD---EETVRKL----QARLLEEEsskRAEL 464
Cdd:pfam01576  428 ---RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdvsSLESQLQDTQEllqEETRQKLnlstRLRQLEDE---RNSL 501
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93102364    465 EKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:pfam01576  502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
217-301 6.40e-04

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). 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: 270078  Cd Length: 123  Bit Score: 40.00  E-value: 6.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 217 MMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKK---GDILLdENCCVESLPDKDGKKCLFLVkcF----DKTFEISAS 289
Cdd:cd13258  26 QMGGPKKSEVFKERWFKLKGNLLFYFRTNEFGDCSepiGAIVL-ENCRVQMEEITEKPFAFSIV--FndepEKKYIFSCR 102
                        90
                ....*....|..
gi 93102364 290 DKKKKQEWIQAI 301
Cdd:cd13258 103 SEEQCEQWIEAL 114
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
317-514 6.40e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    317 KEARQRRKELrkKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKkrLQTQVELQ---ARFSTELER 393
Cdd:TIGR00618  226 KELKHLREAL--QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRArkaAPLAAHIKA 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    394 EKLIRQQMEEQVAQ---KSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKL--QARLLEEESSKRAELEKwH 468
Cdd:TIGR00618  302 VTQIEQQAQRIHTElqsKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAheVATSIREISCQQHTLTQ-H 380
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 93102364    469 LEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQAL 514
Cdd:TIGR00618  381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
317-465 6.92e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.63  E-value: 6.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLeeaasraaeeekkrLQTQVELQARFSTELEREKL 396
Cdd:pfam15709 387 EEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL--------------QELQRKKQQEEAERAEAEKQ 452
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364   397 IRQQMEEQVAQKSSELEQYLQRVReLEDMYLKlQEALEDERQARQDEETVRKLQARLLEEESSKRAELE 465
Cdd:pfam15709 453 RQKELEMQLAEEQKRLMEMAEEER-LEYQRQK-QEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
PH_FAPP1_FAPP2 cd01247
Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also ...
227-304 6.99e-04

Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also called PLEKHA3/Pleckstrin homology domain-containing, family A member 3) regulates secretory transport from the trans-Golgi network to the plasma membrane. It is recruited through binding of PH domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). These two binding sites have little overlap the FAPP1 PH domain to associate with both ligands simultaneously and independently. FAPP1 has a N-terminal PH domain followed by a short proline-rich region. FAPP1 is a member of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), and Goodpasture antigen binding protein (GPBP). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. FAPP2 (also called PLEKHA8/Pleckstrin homology domain-containing, family A member 8), a member of the Glycolipid lipid transfer protein(GLTP) family has an N-terminal PH domain that targets the TGN and C-terminal GLTP domain. FAPP2 functions to traffic glucosylceramide (GlcCer) which is made in the Golgi. It's interaction with vesicle-associated membrane protein-associated protein (VAP) could be a means of regulation. Some FAPP2s share the FFAT-like motifs found in GLTP. 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: 269951  Cd Length: 100  Bit Score: 39.31  E-value: 6.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 227 WTERWFVLKPNIISYYVSEDLKDK--KGDILLdeNCCVESLPDKDGKKcLFLVKCFDKTFEISASDKKKKQEWIQAIHST 304
Cdd:cd01247  15 WQPRWFVLDDGVLSYYKSQEEVNQgcKGSVKM--SVCEIIVHPTDPTR-MDLIIPGEQHFYLKASSAAERQRWLVALGSA 91
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
394-532 7.55e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.14  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   394 EKLIRQQMEEQVAQKSSELEQYLQRVRELEdmylklQEALEDERQARQDEETVRKLQARLLEEESSKRAElekwhleqQQ 473
Cdd:TIGR02794  45 PGAVAQQANRIQQQKKPAAKKEQERQKKLE------QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE--------QA 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93102364   474 AIQTTEAEKQELEnqrvLKEQALQEAMEQLEQlELERKQALE---QYEEVKKKLEMATNKTK 532
Cdd:TIGR02794 111 AKQAEEKQKQAEE----AKAKQAAEAKAKAEA-EAERKAKEEaakQAEEEAKAKAAAEAKKK 167
PTZ00121 PTZ00121
MAEBL; Provisional
318-537 7.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEA-----VRKKLEEAASRAAEEEKKRLQTQVELQARFSTELE 392
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAkkadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   393 REKLIRQQME---------EQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKL-QARLLEEESSKRA 462
Cdd:PTZ00121 1355 AADEAEAAEEkaeaaekkkEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdEAKKKAEEKKKAD 1434
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   463 ELEKWHLEQQQAiqtTEAEKQELENQRVlkEQALQEAMEQLEQLELERK-QALEQYEEVKKKLEMATNKTKSWKDK 537
Cdd:PTZ00121 1435 EAKKKAEEAKKA---DEAKKKAEEAKKA--EEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKA 1505
mukB PRK04863
chromosome partition protein MukB;
318-513 8.08e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQEELERQMKELQAANESK---QQELEAVRKKLEEAASRAAEEEK------------KRLQTQ-- 380
Cdd:PRK04863  290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAEsdlEQDYQAASDHLNLVQTALRQQEKieryqadleeleERLEEQne 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   381 -VELQARFSTELEREKlirQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQ----DEETVRKLQARLLE 455
Cdd:PRK04863  370 vVEEADEQQEENEARA---EAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglPDLTADNAEDWLEE 446
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   456 -EESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLK-------EQALQEAMEQLEQLELERKQA 513
Cdd:PRK04863  447 fQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLA 512
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
317-520 8.46e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 8.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  317 KEARQRRKELRKKQLAEQ-EELERQMKELQAANESKQQELEAVRKKleeaasrAAEEEKKR------------LQTQVEL 383
Cdd:PRK02224 528 RRETIEEKRERAEELRERaAELEAEAEEKREAAAEAEEEAEEAREE-------VAELNSKLaelkerieslerIRTLLAA 600
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  384 QARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEdmylklqEALEDER--QARQDEETVRKLQARLLEEESSKR 461
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRERLAEKRERKRELE-------AEFDEARieEAREDKERAEEYLEQVEEKLDELR 673
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  462 AELEkwhlEQQQAIQTTEAEKQELENQRvlkeqalqeamEQLEQLElERKQALEQ-YEEV 520
Cdd:PRK02224 674 EERD----DLQAEIGAVENELEELEELR-----------ERREALE-NRVEALEAlYDEA 717
PH_evt cd13265
Evectin Pleckstrin homology (PH) domain; There are 2 members of the evectin family (also ...
211-281 8.80e-04

Evectin Pleckstrin homology (PH) domain; There are 2 members of the evectin family (also called pleckstrin homology domain containing, family B): evt-1 (also called PLEKHB1) and evt-2 (also called PLEKHB2). evt-1 is specific to the nervous system, where it is expressed in photoreceptors and myelinating glia. evt-2 is widely expressed in both neural and nonneural tissues. Evectins possess a single N-terminal PH domain and a C-terminal hydrophobic region. evt-1 is thought to function as a mediator of post-Golgi trafficking in cells that produce large membrane-rich organelles. It is a candidate gene for the inherited human retinopathy autosomal dominant familial exudative vitreoretinopathy and a susceptibility gene for multiple sclerosis. evt-2 is essential for retrograde endosomal membrane transport from the plasma membrane (PM) to the Golgi. Two membrane trafficking pathways pass through recycling endosomes: a recycling pathway and a retrograde pathway that links the PM to the Golgi/ER. Its PH domain that is unique in that it specifically recognizes phosphatidylserine (PS), but not polyphosphoinositides. PS is an anionic phospholipid class in eukaryotic biomembranes, is highly enriched in the PM, and plays key roles in various physiological processes such as the coagulation cascade, recruitment and activation of signaling molecules, and clearance of apoptotic cells. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270085  Cd Length: 108  Bit Score: 39.21  E-value: 8.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMKKGHRRKNWTERWFVLKPN-IISYYVSEDLKDKKGDILLDENC--------CVE-SLPDKDGKKCLFLVKCF 280
Cdd:cd13265   3 LVKSGWLLRQSTILKRWKKNWFVLYGDgNLVYYEDETRREVEGRINMPRECrnirvgleCRDvQPPEGRSRDCLLQIVLR 82

                .
gi 93102364 281 D 281
Cdd:cd13265  83 D 83
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
328-451 9.41e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 9.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 328 KKQLAEQEELERQMKELQAANESKQQELEAVRKKLeeaasraaEEEKKRLQTQVELQARFSTELEREkliRQQMEEQVAQ 407
Cdd:COG3883 132 ADLLEELKADKAELEAKKAELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAE---EAAAEAQLAE 200
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 93102364 408 KSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQA 451
Cdd:COG3883 201 LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
317-422 9.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  317 KEARQRRKELRKkqlaEQEELERQMKELQAANESKQQELEAVRKKLEEAASRaaeeekKRLQTQVELQARFSTEL--ERE 394
Cdd:COG4913  695 EELEAELEELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL------ARLELRALLEERFAAALgdAVE 764
                         90       100
                 ....*....|....*....|....*...
gi 93102364  395 KLIRQQMEEQVAQKSSELEQYLQRVREL 422
Cdd:COG4913  765 RELRENLEERIDALRARLNRAEEELERA 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-550 1.15e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  412 LEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEeesskraelekwHLEQQQAIQTTEAEKQELENQRvl 491
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE------------YSWDEIDVASAEREIAELEAEL-- 677
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364  492 keQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGLIRLIEP 550
Cdd:COG4913  678 --ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
426-532 1.15e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  426 YLKLQEALEDERQARQDEETVRKLQARLLEE----ESSKRAELEKWHL-EQQQAIQTTEAEKQELENQRVLKEQALQEAM 500
Cdd:PRK09510  64 YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQkqaaEQERLKQLEKERLaAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA 143
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 93102364  501 EQLEQLELERKQALE---QYEEVKKKLEMATNKTK 532
Cdd:PRK09510 144 AAKAKAEAEAKRAAAaakKAAAEAKKKAEAEAAKK 178
PH_PLEKHD1 cd13281
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH ...
209-303 1.18e-03

Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain; Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, , dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. 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: 270099  Cd Length: 139  Bit Score: 39.61  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 209 LDVLKQGYMMKK--GHRRKNWTERWFVLKPNIISYYVSEDLKD----------KKGDILLDeNCCVESLPDKDgKKCLFL 276
Cdd:cd13281  10 TKVQLHGILWKKpfGHQSAKWSKRFFIIKEGFLLYYSESEKKDfektrhfnihPKGVIPLG-GCSIEAVEDPG-KPYAIS 87
                        90       100
                ....*....|....*....|....*....
gi 93102364 277 VKCFDKTFEI--SASDKKKKQEWIQAIHS 303
Cdd:cd13281  88 ISHSDFKGNIilAADSEFEQEKWLDMLRE 116
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
331-523 1.19e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  331 LAEQ----EELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQA--RFSTELEREKLIRQQMEEQ 404
Cdd:COG3096  363 LEEQeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAleKARALCGLPDLTPENAEDY 442
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  405 VAQKSSELEQYLQRVRELE-------------DMYLKLQEALEDE-------RQARQDEETVRKLQARLLEEESSKR--A 462
Cdd:COG3096  443 LAAFRAKEQQATEEVLELEqklsvadaarrqfEKAYELVCKIAGEversqawQTARELLRRYRSQQALAQRLQQLRAqlA 522
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93102364  463 ELEKWHLEQQQAIQ-----------------TTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKK 523
Cdd:COG3096  523 ELEQRLRQQQNAERlleefcqrigqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
PRK12704 PRK12704
phosphodiesterase; Provisional
395-532 1.31e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  395 KLIRQQMEEQVAQKSSELEQYLQ-RVRELEDMYLKLQEALEDERQARQDEetVRKLQARLLEEESSkraelekwhLEQQQ 473
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKeALLEAKEEIHKLRNEFEKELRERRNE--LQKLEKRLLQKEEN---------LDRKL 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364  474 aiQTTEAEKQELENQRvlkeqalQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTK 532
Cdd:PRK12704 103 --ELLEKREEELEKKE-------KELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
PH_ORP_plant cd13294
Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain; Plant ORPs ...
215-313 1.42e-03

Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain; Plant ORPs contain a N-terminal PH domain and a C-terminal OSBP-related domain. Not much is known about its specific function in plants to date. Members here include: Arabidopsis, spruce, and petunia. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF 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: 241448  Cd Length: 100  Bit Score: 38.24  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 215 GYMMKKGHRRKNWTERWFVLKPNIISYYV---SEDLKdKKGDILLDENCCVESlpDKDGKKclFLVKCFDKTFEISASDK 291
Cdd:cd13294   3 GILYKWVNYGKGWRSRWFVLQDGVLSYYKvhgPDKVK-PSGEVHLKVSSIRES--RSDDKK--FYIFTGTKTLHLRAESR 77
                        90       100
                ....*....|....*....|..
gi 93102364 292 KKKQEWIQAIHSTIHLLKLGSP 313
Cdd:cd13294  78 EDRAAWLEALQAAKDMFPRMSL 99
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
317-519 1.46e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   317 KEARQRRKELRKKQLAEQEELERQMKELQA----ANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELE 392
Cdd:pfam13868  58 EEEEEKEEERKEERKRYRQELEEQIEEREQkrqeEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   393 REKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEetvrklQARLLEEESSKRAELEKWHLEQQ 472
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIAR------LRAQQEKAQDEKAERDELRAKLY 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 93102364   473 QAIQTTEAEKQELE--NQRVLKEQALQEAMEQLEQLELERKQALEQYEE 519
Cdd:pfam13868 212 QEEQERKERQKEREeaEKKARQRQELQQAREEQIELKERRLAEEAEREE 260
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
320-505 1.47e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   320 RQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKR-LQTQVELQ-ARFSTELEREKLI 397
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQrLQLQAAQErARQQQEEFRRKLQ 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   398 -RQQMEEQVAQKSSELEQylQRVRELEdmylkLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEkwhleqqqaiq 476
Cdd:pfam15709 434 eLQRKKQQEEAERAEAEK--QRQKELE-----MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE----------- 495
                         170       180
                  ....*....|....*....|....*....
gi 93102364   477 ttEAEKQELENQRVLKEQALQEAMEQLEQ 505
Cdd:pfam15709 496 --ERRQKEEEAARLALEEAMKQAQEQARQ 522
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
321-532 1.52e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    321 QRRKELRKKQLAE-QEELERQMKELQAANESKQQ------ELEAVrKKLEEAASRAAEEEKKRLQTQVELQARFSTELER 393
Cdd:pfam15921  429 QRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKvssltaQLEST-KEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    394 EKLIRQQMEEQVAQKSSELEQYLQRVREL------------EDMYLKLQEALEDE--RQARQDEETVRKL---------- 449
Cdd:pfam15921  508 KERAIEATNAEITKLRSRVDLKLQELQHLknegdhlrnvqtECEALKLQMAEKDKviEILRQQIENMTQLvgqhgrtaga 587
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    450 ----QARLLEEESSKRAELEKWHL---EQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQAL-------- 514
Cdd:pfam15921  588 mqveKAQLEKEINDRRLELQEFKIlkdKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevktsrn 667
                          250       260       270
                   ....*....|....*....|....*....|.
gi 93102364    515 ------EQYEEVKK-------KLEMATNKTK 532
Cdd:pfam15921  668 elnslsEDYEVLKRnfrnkseEMETTTNKLK 698
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
209-301 1.68e-03

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. 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: 269947  Cd Length: 107  Bit Score: 38.38  E-value: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 209 LDVLKQGYMMKKGHRRKNWTERWFVLKPN--IISYyvsedlKDKKGDILLDE--------NCCVesLPDKDGKKCLFLVK 278
Cdd:cd01241   1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDgsFIGY------KEKPKPNQDPPplnnfsvaECQL--MKTEKPKPNTFIIR 72
                        90       100
                ....*....|....*....|....*..
gi 93102364 279 CFDKTFEI----SASDKKKKQEWIQAI 301
Cdd:cd01241  73 CLQWTTVIertfHVESEEEREEWMKAI 99
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
374-528 2.03e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  374 KKRLQTQVELQARFSTELErEKLIRQQMEEQVAQKSSEleqYLQRVRELedmyLKLQEALEdERQARQDEETVRklqarl 453
Cdd:COG3096  298 RRQLAEEQYRLVEMARELE-ELSARESDLEQDYQAASD---HLNLVQTA----LRQQEKIE-RYQEDLEELTER------ 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  454 LEEESSKRAELEKWHLEQQQAIQTTEAEKQELEN-----QRVLKEQ------------ALQEAMEQLEQLELERKQALEQ 516
Cdd:COG3096  363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqladyQQALDVQqtraiqyqqavqALEKARALCGLPDLTPENAEDY 442
                        170
                 ....*....|..
gi 93102364  517 YEEVKKKLEMAT 528
Cdd:COG3096  443 LAAFRAKEQQAT 454
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
320-521 2.09e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 320 RQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQ 399
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 400 -QMEEQVAQKSSELEqylqrvreledmylkLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKwhlEQQQAIQTT 478
Cdd:COG2268 279 vQRQLEIAEREREIE---------------LQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEA---IRAKGLAEA 340
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 93102364 479 EAEKQELENQRVLKEQALQEAM-EQLEQLELERKQALEQYEEVK 521
Cdd:COG2268 341 EGKRALAEAWNKLGDAAILLMLiEKLPEIAEAAAKPLEKIDKIT 384
PTZ00121 PTZ00121
MAEBL; Provisional
318-537 2.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQEELERQMKELQAANE-SKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKL 396
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   397 IRQQMEE-QVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDE----ETVRKLQARLLEEESSKRAELEKWHLEQ 471
Cdd:PTZ00121 1235 AKKDAEEaKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAEEA 1314
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   472 QQAIQTTEAEKQELENQRVLKEQAlQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDK 537
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-524 2.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  317 KEARQRRKELR--KKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFST----- 389
Cdd:PRK03918 532 EKLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdae 611
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  390 -ELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVrklqaRLLEEESSKRAELEKWH 468
Cdd:PRK03918 612 kELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL-----ELSRELAGLRAELEELE 686
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364  469 LEQQQAIQTTEAEKQELENqrvlkeqaLQEAMEQLEQLElerkQALEQYEEVKKKL 524
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEE--------REKAKKELEKLE----KALERVEELREKV 730
PH_PHLDB1_2 cd14673
Pleckstrin homology-like domain-containing family B member 2 pleckstrin homology (PH) domain; ...
214-254 2.16e-03

Pleckstrin homology-like domain-containing family B member 2 pleckstrin homology (PH) domain; PHLDB2 (also called LL5beta) and PHLDB1 (also called LL5alpha) are cytoskeleton- and membrane-associated proteins. PHLDB2 has been identified as a key component of the synaptic podosomes that play an important role in in postsynaptic maturation. Both are large proteins containing an N-terminal pleckstrin (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: 270192  Cd Length: 105  Bit Score: 37.94  E-value: 2.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 93102364 214 QGYMMKKGHRRKNWTERWFVLKPN--IISYYVSEDLKDKKGDI 254
Cdd:cd14673   6 RGFLTKMGGKIKTWKKRWFVFDRNkrTLSYYVDKHEKKLKGVI 48
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
332-522 2.16e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  332 AEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSE 411
Cdd:COG3096  934 EQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQ 1013
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  412 LEQYLQRvreledmylklQEALEDERQARQDeeTVRKLQARLLE------EESSKRAELEKWHLEQQqaIQTTEAEKQEL 485
Cdd:COG3096 1014 YSQYNQV-----------LASLKSSRDAKQQ--TLQELEQELEElgvqadAEAEERARIRRDELHEE--LSQNRSRRSQL 1078
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 93102364  486 ENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKK 522
Cdd:COG3096 1079 EKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
318-523 2.28e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 318 EARQRRKELRKkqlaEQEELERQMKELQAANESKQQELEAVRKKLeeaasraaeeekKRLQTQVElqarfsTELEREKLI 397
Cdd:COG1579  21 RLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEI------------KRLELEIE------EVEARIKKY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 398 RQQMEEqvAQKSSELEQYLqrvRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQT 477
Cdd:COG1579  79 EEQLGN--VRNNKEYEALQ---KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 93102364 478 TEAEKQELENQRvlkeqalQEAMEQLEqlelerKQALEQYEEVKKK 523
Cdd:COG1579 154 LEAELEELEAER-------EELAAKIP------PELLALYERIRKR 186
DUF5930 pfam19353
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ...
384-527 2.29e-03

Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.


Pssm-ID: 466052 [Multi-domain]  Cd Length: 320  Bit Score: 40.55  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   384 QARFSTELEreklirqqmeeQVAQKSSELEQYLQRVRELEDMYLKLQEALED---ERQARQDEetVRKLQARLLEEESSK 460
Cdd:pfam19353 104 QERFNAALE-----------QVSVMQSELLASEERRRELETGIEVIQSTLRRtmkERDAARAE--LAALQAELEGGGAAA 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   461 RAELEkwhleqqQAIQTTEAEKQELEN---QRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMA 527
Cdd:pfam19353 171 AARAA-------DADATLDFLTAALAEtaaERDQIAADAQDALAEADELALEIRLMEERNDQIFRQLEEA 233
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
332-535 2.30e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   332 AEQEELERQMkeLQAANESKQQELEAVRKKLEEAASRAAeeekkrLQTQVELQARFSTELE-REKLIRQQMEEQVAQKSS 410
Cdd:pfam05557   2 AELIESKARL--SQLQNEKKQMELEHKRARIELEKKASA------LKRQLDRESDRNQELQkRIRLLEKREAEAEEALRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   411 ELEQYLQRVRELEDMYLKLQEALEDERQARQdeetvrkLQARLLEEESSKRAELEKwhleQQQAIQTTEAEKQELENQRV 490
Cdd:pfam05557  74 QAELNRLKKKYLEALNKKLNEKESQLADARE-------VISCLKNELSELRRQIQR----AELELQSTNSELEELQERLD 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 93102364   491 LKEQALQEAMEQLEQLELERKQALEQYEEVkKKLEMATNKTKSWK 535
Cdd:pfam05557 143 LLKAKASEAEQLRQNLEKQQSSLAEAEQRI-KELEFEIQSQEQDS 186
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
375-517 2.46e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  375 KRLQTQV-ELQARFSTELEREKLIRQQMEEQVAQKS--SELEQY---LQRVRELEDMYLKLQEALEderQARQDEETVRK 448
Cdd:COG4913  613 AALEAELaELEEELAEAEERLEALEAELDALQERREalQRLAEYswdEIDVASAEREIAELEAELE---RLDASSDDLAA 689
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364  449 LQARLleeesskrAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQY 517
Cdd:COG4913  690 LEEQL--------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
337-576 2.53e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   337 LERQMKELQAANESKQQELEAVRKKLEEAASraaeeekkrlqtqvELQARFSTELEREKLIRQqmeEQVAQKSSELEQYL 416
Cdd:pfam10174   1 LQAQLRDLQRENELLRRELDIKESKLGSSMN--------------SIKTFWSPELKKERALRK---EEAARISVLKEQYR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   417 QRVRELEDMYLKLQeALEDERQARQDeetvrkLQARLLEEESSKRAELEKwhLEQQQAIQTTEAEKQELENQRVLKE-QA 495
Cdd:pfam10174  64 VTQEENQHLQLTIQ-ALQDELRAQRD------LNQLLQQDFTTSPVDGED--KFSTPELTEENFRRLQSEHERQAKElFL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   496 LQEAMEQLEQLELERKQALE-QYEEVKKKLEMATNKTKSWKDKVAHHEGLIRLIEPGSKNPHLitnwgpaaftEAELEER 574
Cdd:pfam10174 135 LRKTLEEMELRIETQKQTLGaRDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHL----------EVLLDQK 204

                  ..
gi 93102364   575 EK 576
Cdd:pfam10174 205 EK 206
PH_Gab1_Gab2 cd01266
Grb2-associated binding proteins 1 and 2 pleckstrin homology (PH) domain; The Gab subfamily ...
210-301 2.59e-03

Grb2-associated binding proteins 1 and 2 pleckstrin homology (PH) domain; The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. The members in this cd include the Gab1 and Gab2 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: 241297  Cd Length: 123  Bit Score: 38.00  E-value: 2.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMK----KGHRRKNWTERWFVLK-------PNIISYYVSEdlKDKKGDILLDENCCVE-----SLPDKDGKKC 273
Cdd:cd01266   3 EVVCSGWLRKsppeKKLRRYAWKKRWFVLRsgrlsgdPDVLEYYKND--HAKKPIRVIDLNLCEQvdaglTFNKKELENS 80
                        90       100
                ....*....|....*....|....*....
gi 93102364 274 -LFLVKCFDKTFEISASDKKKKQEWIQAI 301
Cdd:cd01266  81 yIFDIKTIDRIFYLVAETEEDMNKWVRNI 109
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
328-543 2.75e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    328 KKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQ-ARFSTELEREKLIRQQMEEQVA 406
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyLLYLDYLKLNEERIDLLQELLR 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    407 QKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQttEAEKQELE 486
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK--ESEKEKKK 325
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 93102364    487 NQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEG 543
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
PRK12705 PRK12705
hypothetical protein; Provisional
384-528 2.83e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  384 QARFSTELEReklIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQArlLEEESSKRAE 463
Cdd:PRK12705  28 RQRLAKEAER---ILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQ--LDARAEKLDN 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93102364  464 LEKWHLEQQQAIQTTEAEKQELENQ--RVLKEQALQEAMEQLEQL--ELERKQALEQYEEVKKKLEMAT 528
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQldNELYRVAGLTPEQARKLLlkLLDAELEEEKAQRVKKIEEEAD 171
PH_11 pfam15413
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
213-302 2.89e-03

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


Pssm-ID: 405988  Cd Length: 105  Bit Score: 37.57  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   213 KQGYMMKKGHrrKNWTERWF-VLKPNIISYYVSEDLKDKKG--------------DILLDENCCVESLPDKDGKKCLFLV 277
Cdd:pfam15413   1 IEGYLKKKGP--KTWKHRWFaVLRNGVLFYYKSEKMKVVKHvivlsnyivgklgtDIISGALFKIDNIRSETSDDLLLEI 78
                          90       100
                  ....*....|....*....|....*
gi 93102364   278 KCFDKTFEISASDKKKKQEWIQAIH 302
Cdd:pfam15413  79 STETKIFFLYGDNNEETYEWVEALQ 103
mukB PRK04863
chromosome partition protein MukB;
335-522 2.90e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   335 EELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSELEQ 414
Cdd:PRK04863  938 EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ 1017
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   415 YLQRVRELEDMYLKLQEALeDERQARQDEETVRkLQARLLEEESSKRAELekwhleqQQAIQTTEAEKQELENQRVLKEQ 494
Cdd:PRK04863 1018 YNQVLASLKSSYDAKRQML-QELKQELQDLGVP-ADSGAEERARARRDEL-------HARLSANRSRRNQLEKQLTFCEA 1088
                         170       180
                  ....*....|....*....|....*...
gi 93102364   495 ALQEAMEQLEQLELERKQALEQYEEVKK 522
Cdd:PRK04863 1089 EMDNLTKKLRKLERDYHEMREQVVNAKA 1116
PH_Bem3 cd13277
Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces ...
210-305 3.24e-03

Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces cerevisiae involves cell cycle-regulated reorganizations of cortical cytoskeletal elements and requires the action of the Rho-type GTPase Cdc42. Bem3 contains a RhoGAP domain and a PH domain. Though Bem3 and Bem2 both contain a RhoGAP, but only Bem3 is able to stimulate the hydrolysis of GTP on Cdc42. Bem3 is thought to be the GAP for Cdc42. 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: 270096  Cd Length: 111  Bit Score: 37.65  E-value: 3.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 210 DVLKQGYMMKKGHR----RKNWTERWFVLKPNIISYYvsedlkDKKGDILLDE----NCCVESLP----DKDGKKCLFLV 277
Cdd:cd13277   2 DSVKEGYLLKRRKKtlgsTGGWKLRYGVLDGNILELY------ESRGGQLLESiklrNAQIERQPnlpdDKYGTRHGFLI 75
                        90       100       110
                ....*....|....*....|....*....|....*
gi 93102364 278 KCFDKTFEIS-------ASDKKKKQEWIQAIHSTI 305
Cdd:cd13277  76 NEHKKSGLSSttkyylcAETDKERDEWVSALSEYI 110
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
403-525 3.28e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  403 EQVAQKSSELEQYLQRVRELEdmyLKLQEALedeRQARQDEETVRKL--QARLLEEES------SKRAELEKWHlEQQQA 474
Cdd:COG3096  839 AALRQRRSELERELAQHRAQE---QQLRQQL---DQLKEQLQLLNKLlpQANLLADETladrleELREELDAAQ-EAQAF 911
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 93102364  475 IQTTEAEKQELENQrvlkEQALQEAMEQLEQLELERKQALEQYEEVKKKLE 525
Cdd:COG3096  912 IQQHGKALAQLEPL----VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF 958
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
319-522 3.52e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 40.05  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   319 ARQRRKELRKKQLAEQEELERQMKELQAAneskQQELEAVRKKLEEAASRaaeeeKKRLQTQVELQARFSTELEReklir 398
Cdd:pfam19220 130 ETEQNRALEEENKALREEAQAAEKALQRA----EGELATARERLALLEQE-----NRRLQALSEEQAAELAELTR----- 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   399 qqmeeQVAQKSSELEQYLQRVRELEDMYLKLQEalEDERQARQDEETVRKLQARL------LEEESSKRAELEKWHLEQQ 472
Cdd:pfam19220 196 -----RLAELETQLDATRARLRALEGQLAAEQA--ERERAEAQLEEAVEAHRAERaslrmkLEALTARAAATEQLLAEAR 268
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 93102364   473 QAIQTTEAEKQELEnqRVLKEQALQE--AMEQLEQLELERKQALEQYEEVKK 522
Cdd:pfam19220 269 NQLRDRDEAIRAAE--RRLKEASIERdtLERRLAGLEADLERRTQQFQEMQR 318
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
314-423 3.66e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 314 PPHKEARQRRKELRkKQLaeQEELERQMKELQAANESKQQELEAVRKKLeeaasraaEEEKKRLQTQVELQARFsTELER 393
Cdd:COG3206 291 PDVIALRAQIAALR-AQL--QQEAQRILASLEAELEALQAREASLQAQL--------AQLEARLAELPELEAEL-RRLER 358
                        90       100       110
                ....*....|....*....|....*....|
gi 93102364 394 EKlirqqmeeQVAQKSseLEQYLQRVRELE 423
Cdd:COG3206 359 EV--------EVAREL--YESLLQRLEEAR 378
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
317-534 3.72e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  317 KEARQRRKELrKKQLAEQEELERQMKE--------LQAAN-----------ESKQQELEAVRKKLEEAASRAAEEEKK-- 375
Cdd:COG3096  839 AALRQRRSEL-ERELAQHRAQEQQLRQqldqlkeqLQLLNkllpqanlladETLADRLEELREELDAAQEAQAFIQQHgk 917
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  376 ---RLQTQV-----------ELQARFSTELEREKLIRQQME--EQVAQKSSEL--EQYLQRVRELEDMYLKLQEALED-E 436
Cdd:COG3096  918 alaQLEPLVavlqsdpeqfeQLQADYLQAKEQQRRLKQQIFalSEVVQRRPHFsyEDAVGLLGENSDLNEKLRARLEQaE 997
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  437 RQARQDEETVRKLQAR-------LLEEESSKRA------ELEKwHLEQ------QQAIQTTEAEKQELENQRVLKEQALQ 497
Cdd:COG3096  998 EARREAREQLRQAQAQysqynqvLASLKSSRDAkqqtlqELEQ-ELEElgvqadAEAEERARIRRDELHEELSQNRSRRS 1076
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 93102364  498 EAMEQLEQLELERKQALEQYEEVKKKL----EMATNKTKSW 534
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKRLRKAERDYkqerEQVVQAKAGW 1117
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
412-535 3.76e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 39.79  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   412 LEQYLQRVRELEDMYLKLQ---EALEDERQARQDEETVRKLQARLLEEESSKRAELEK-WHLEQQQAIQTTEAEKQELEN 487
Cdd:TIGR00570  92 LREYNDYLEEVEDIVYNLTnniDLENTKKKIETYQKENKDVIQKNKEKSTREQEELEEaLEFEKEEEEQRRLLLQKEEEE 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 93102364   488 QRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWK 535
Cdd:TIGR00570 172 QQMNKRKNKQALLDELETSTLPAAELIAQHKKNSVKLEMQVEKPKPEK 219
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
318-545 3.77e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    318 EARQRRKELRKKQLAEQEE----LERQMKELQAANESKQQELEAVRKKLEEAasraaeeekKRLQTQVELQARFSTELEr 393
Cdd:TIGR00606  733 PGRQSIIDLKEKEIPELRNklqkVNRDIQRLKNDIEEQETLLGTIMPEEESA---------KVCLTDVTIMERFQMELK- 802
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    394 eklirqQMEEQVAQKSSELEQylqrvrelEDMYLKLQEaLEDERQARQDEetvrklqarlLEEESSKRAELEKWHLEQQQ 473
Cdd:TIGR00606  803 ------DVERKIAQQAAKLQG--------SDLDRTVQQ-VNQEKQEKQHE----------LDTVVSKIELNRKLIQDQQE 857
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93102364    474 AIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGLI 545
Cdd:TIGR00606  858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI 929
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
408-520 4.00e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 408 KSSELEQYLQRVRELEdmylKLQEALEDErQARQDEETVRKLQARLLEEESSKRAELEKWHlEQQQAIQTTEAEKQELEn 487
Cdd:COG0542 409 KPEELDELERRLEQLE----IEKEALKKE-QDEASFERLAELRDELAELEEELEALKARWE-AEKELIEEIQELKEELE- 481
                        90       100       110
                ....*....|....*....|....*....|...
gi 93102364 488 QRVLKEQALQEAMEQLEQlELERKQALEQyEEV 520
Cdd:COG0542 482 QRYGKIPELEKELAELEE-ELAELAPLLR-EEV 512
Rabaptin pfam03528
Rabaptin;
318-524 4.25e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 40.09  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   318 EARQRRKELRKKQLAEQEELERQMKELQAANE----------------------------SKQQELEAVRKKLEEAASRA 369
Cdd:pfam03528  30 EFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVeldalqnqlalaraemenikavatvsenTKQEAIDEVKSQWQEEVASL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   370 AEEEKkrlQTQVELQARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQAR--------- 440
Cdd:pfam03528 110 QAIMK---ETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSEGQEEENLEDEMKKAQEDAEKLRsvvmpmeke 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   441 ---------QDEETVRKLQA-------RLLEEESSKRAELEKW--HLEQQQAIQTTEAEKQELENQRVLKEqaLQEAMEQ 502
Cdd:pfam03528 187 iaalkakltEAEDKIKELEAskmkelnHYLEAEKSCRTDLEMYvaVLNTQKSVLQEDAEKLRKELHEVCHL--LEQERQQ 264
                         250       260
                  ....*....|....*....|..
gi 93102364   503 LEQLELERKQALEQYEEVKKKL 524
Cdd:pfam03528 265 HNQLKHTWQKANDQFLESQRLL 286
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
411-535 4.45e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364    411 ELEQYLQRVRELEDMYLKLQEALEDER--QARQDEETVR---KLQARLLEEESSKRAeLEKWHLEQQQAIQTTEAEKQEL 485
Cdd:pfam12128  591 DVPEWAASEEELRERLDKAEEALQSARekQAAAEEQLVQangELEKASREETFARTA-LKNARLDLRRLFDEKQSEKDKK 669
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 93102364    486 ENQRV----LKEQALQEAMEQLEQLELERKQALEQYEEvkKKLEMATNKTKSWK 535
Cdd:pfam12128  670 NKALAerkdSANERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQ 721
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
391-522 4.71e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.09  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   391 LEREKLIRQQMEEQVAQKSSELEQYLQR----VRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEK 466
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   467 WHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKK 522
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
345-527 4.75e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.44  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   345 QAANESKQQELEAVRKkleeaasrAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELED 424
Cdd:TIGR02794  50 QQANRIQQQKKPAAKK--------EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   425 MYLKLQEalEDERQARQDEETVRKLQarlleEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRvlKEQALQEAMEQLE 504
Cdd:TIGR02794 122 EEAKAKQ--AAEAKAKAEAEAERKAK-----EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA--KAKAEAEAKAKAE 192
                         170       180
                  ....*....|....*....|....
gi 93102364   505 QLELERKQALEQYE-EVKKKLEMA 527
Cdd:TIGR02794 193 EAKAKAEAAKAKAAaEAAAKAEAE 216
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
316-498 4.98e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  316 HKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEK---------KRLQTQVELQAR 386
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefyeEYLDELREIEKR 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  387 FSTELEREKLIRQQMEEqVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARL----LEEESSKRA 462
Cdd:PRK03918 316 LSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEKELE 394
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 93102364  463 ELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQE 498
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
227-302 5.20e-03

Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF 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: 270102  Cd Length: 125  Bit Score: 37.37  E-value: 5.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 227 WTERWFVLKPNIISYYVSEDLKD----KKGDILLDENCCveSLPDKDgkKCLFLVKCFDKT---FEISASD--KKKKQEW 297
Cdd:cd13285  23 WRSYWVVLEDGVLSWYHKQADAAagikRQGCKSLTQAKC--TVKSTD--SCFFTIRCFDDTvhrFKVPPKNnpVVTRKKW 98

                ....*
gi 93102364 298 IQAIH 302
Cdd:cd13285  99 LEALE 103
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
313-440 5.47e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 5.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 313 PPPHKEARQRRKELRKKQLAEQ-EELERQMKELQAANESKQQELEAVRKKLeeaasraaeeekKRLQTQVELQARFSTEL 391
Cdd:COG2433 400 EKEHEERELTEEEEEIRRLEEQvERLEAEVEELEAELEEKDERIERLEREL------------SEARSEERREIRKDREI 467
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 93102364 392 EReklirqqMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQAR 440
Cdd:COG2433 468 SR-------LDREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
PRK01156 PRK01156
chromosome segregation protein; Provisional
323-538 5.58e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  323 RKELRKKQLaEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEK--KRLQTQVELQARFSTELeREKLIRQQ 400
Cdd:PRK01156 189 EEKLKSSNL-ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalNELSSLEDMKNRYESEI-KTAESDLS 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  401 MEEQVAQKSSELEQYLQRV--------RELEDMYLKLQEALEDERQARQD--------EETVRKL------------QAR 452
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIindpvyknRNYINDYFKYKNDIENKKQILSNidaeinkyHAIIKKLsvlqkdyndyikKKS 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  453 LLEEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTK 532
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426

                 ....*.
gi 93102364  533 SWKDKV 538
Cdd:PRK01156 427 SLNQRI 432
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
317-466 5.77e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 5.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 317 KEARQRRKELRK---KQLAEQEELERQMKELQAANESKQQELEAVRKKLeeaasraaeeekKRLQTQVELQArFSTELER 393
Cdd:COG1579  34 AELEDELAALEArleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL------------GNVRNNKEYEA-LQKEIES 100
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 93102364 394 EKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEetVRKLQARlLEEESSKRAELEK 466
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE--LAELEAE-LEELEAEREELAA 170
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
388-515 5.91e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.97  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   388 STELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLK-----------LQEALEDERQARQDEET-VRKLQarllE 455
Cdd:pfam09787  46 TLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEeaessreqlqeLEEQLATERSARREAEAeLERLQ----E 121
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102364   456 EESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLK------EQALQEAMEQLEQLELERKQALE 515
Cdd:pfam09787 122 ELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsqssssQSELENRLHQLTETLIQKQTMLE 187
PH_Gab-like cd13324
Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are ...
211-301 8.45e-03

Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. There are 3 families: Gab1, Gab2, and Gab3. 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: 270133  Cd Length: 112  Bit Score: 36.24  E-value: 8.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 211 VLKQGYMMK----KGHRRKNWTERWFVLK-------PNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKC----LF 275
Cdd:cd13324   1 VVYEGWLTKsppeKKIWRAAWRRRWFVLRsgrlsggQDVLEYYTDDHCKKLKGIIDLDQCEQVDAGLTFEKKKFknqfIF 80
                        90       100
                ....*....|....*....|....*.
gi 93102364 276 LVKCFDKTFEISASDKKKKQEWIQAI 301
Cdd:cd13324  81 DIRTPKRTYYLVAETEEEMNKWVRCI 106
PH2_FGD4_insect-like cd13238
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 4 pleckstrin homology (PH) ...
215-301 8.49e-03

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 4 pleckstrin homology (PH) domain, C-terminus, in insect and related arthropods; In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. This cd contains insects, crustaceans, and chelicerates. 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: 270058  Cd Length: 97  Bit Score: 36.09  E-value: 8.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 215 GYMMKKGHRRKNWTERWFVLKPNIISY-YVSEDLKDK---------------KGDILLDENccvesLPDKDGKKCLFLVK 278
Cdd:cd13238   3 GYLKLKTNGRKTWSRRWFALQPDFVLYsYKSQEDKLPltatpvpgflvtlleKGSAVDPLN-----DPKRPRTFKMFHVK 77
                        90       100
                ....*....|....*....|...
gi 93102364 279 cfdKTFEISASDKKKKQEWIQAI 301
Cdd:cd13238  78 ---KSYYFQANDGDEQKKWVLTL 97
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
337-554 8.51e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   337 LERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQ-----QMEEQVAQKSSE 411
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEkkqfeKIAEELKGKEQE 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   412 LEQYLQ-RVRELEDMYLKLQEALEDERQARQDEETVRKLqarlLEEESSKRAEL----EKWHLEQQQAIQTTEAEKQELE 486
Cdd:pfam05483 441 LIFLLQaREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE----LEKEKLKNIELtahcDKLLLENKELTQEASDMTLELK 516
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364   487 NQ------------RVLKE-QALQEAMEQL-EQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGLIRLIEPGS 552
Cdd:pfam05483 517 KHqediinckkqeeRMLKQiENLEEKEMNLrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596

                  ..
gi 93102364   553 KN 554
Cdd:pfam05483 597 NN 598
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
318-525 8.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  318 EARQRRKELR--KKQLA--EQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEK-----KRLQTQVELQARFS 388
Cdd:PRK03918 366 EAKAKKEELErlKKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPVCGREL 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  389 TELEREKLIRQ------QMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRA 462
Cdd:PRK03918 446 TEEHRKELLEEytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364  463 ELEKWH-----LEQQQAIQTTEAEK-QELENQRVLKEQALQEAMEQLEQLELE-RKQALEQYEEVKKKLE 525
Cdd:PRK03918 526 EYEKLKeklikLKGEIKSLKKELEKlEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLK 595
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
295-527 8.92e-03

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 39.12  E-value: 8.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 295 QEWIQAIHSTIHLLKLGSPPphkEARQRRKELRKKQLAEQ-EELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEE 373
Cdd:COG5278 117 DQWLAELEQVIALRRAGGLE---AALALVRSGEGKALMDEiRARLLLLALALAALLLAAAALLLLLLALAALLALAELLL 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 374 KKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARL 453
Cdd:COG5278 194 LALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAAL 273
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102364 454 LEEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMA 527
Cdd:COG5278 274 LLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALL 347
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
390-494 9.67e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 9.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102364 390 ELEReKLIRQQMEEQVAQKSSELEQYlQRVRELEDMYLKLQEALEDERQARQDE-ETVRKLQA--RLLEEESSKRAELEK 466
Cdd:COG0542 415 ELER-RLEQLEIEKEALKKEQDEASF-ERLAELRDELAELEEELEALKARWEAEkELIEEIQElkEELEQRYGKIPELEK 492
                        90       100
                ....*....|....*....|....*...
gi 93102364 467 whleqqqaiQTTEAEKQELENQRVLKEQ 494
Cdd:COG0542 493 ---------ELAELEEELAELAPLLREE 511
 
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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