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Conserved domains on  [gi|578825192|ref|XP_006719981|]
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cilium assembly protein DZIP1 isoform X4 [Homo sapiens]

Protein Classification

ATP-binding protein; MDR family MFS transporter( domain architecture ID 13845362)

ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as the toxin for a type IV toxin-antitoxin resistance system| MDR (multi-drug resistance) family major facilitator superfamily (MFS) transporter confers resistance to specific drugs/toxins through their active efflux from the cell

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
104-224 4.40e-47

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


:

Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 163.65  E-value: 4.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  104 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQFTIEYLLHSQEF 183
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 578825192  184 LTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECK 224
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
190-486 6.71e-05

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 190 TLEERLRLSHCDGEQSKK---LLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANyyqchfCDKAFMNQAFLQSHIQRR 266
Cdd:PRK03918 256 KLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE------IEKRLSRLEEEINGIEER 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 267 HTEENShfeyqKNAQIEKLRSEIVVLKEELqltrSELEAAHhasavrfsKEYEMQKTKEEDFLKLFDRWKEEEKEKLV-- 344
Cdd:PRK03918 330 IKELEE-----KEERLEELKKKLKELEKRL----EELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEke 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 345 -DEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGT------LKDAHEFKEDRSPYPQDFHNV---MQLLD 414
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIekeLKEIE 472
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578825192 415 SQESKWTARVQAIHQEHKKEkgRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIK 486
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
 
Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
104-224 4.40e-47

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 163.65  E-value: 4.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  104 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQFTIEYLLHSQEF 183
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 578825192  184 LTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECK 224
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
190-486 6.71e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 190 TLEERLRLSHCDGEQSKK---LLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANyyqchfCDKAFMNQAFLQSHIQRR 266
Cdd:PRK03918 256 KLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE------IEKRLSRLEEEINGIEER 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 267 HTEENShfeyqKNAQIEKLRSEIVVLKEELqltrSELEAAHhasavrfsKEYEMQKTKEEDFLKLFDRWKEEEKEKLV-- 344
Cdd:PRK03918 330 IKELEE-----KEERLEELKKKLKELEKRL----EELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEke 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 345 -DEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGT------LKDAHEFKEDRSPYPQDFHNV---MQLLD 414
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIekeLKEIE 472
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578825192 415 SQESKWTARVQAIHQEHKKEkgRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIK 486
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
270-489 6.97e-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: 43.51  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192   270 ENSHFEYQKNaqIEKLRSEIVVLKEELQLTRSELEAAHHAsavrfskeyemQKTKEEDFLKLfdRWKEEEKEKLVDEMEK 349
Cdd:TIGR02168  669 NSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKE-----------LEELEEELEQL--RKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192   350 VKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLKDA-HEFKEDRSPYPQDFHNVMQLLDSQESKWTArVQAIH 428
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALREALDE-LRAEL 812
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578825192   429 QEHKKEKGRLLSHIEKLRTSMIDdlnasnvfYKKRIEELGQRLQEQNELIITQRQQIKDFT 489
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAA--------TERRLEDLEEQIEELSEDIESLAAEIEELE 865
COG5022 COG5022
Myosin heavy chain [General function prediction only];
224-477 3.15e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  224 KRRKKMISTQQLMieaKANYYQCHFCDKAFMNQAFlqsHIQRRHTEENSHFEY-QKNAQIEKLRSEIV---VLKEELQLT 299
Cdd:COG5022   766 QALKRIKKIQVIQ---HGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYrSYLACIIKLQKTIKrekKLRETEEVE 839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  300 RSELEAAHHASAVRFSKEYEMQKTKEEDFLKLFDRWKEEEKEK-LVDEMEKVKEmfmkeFKELTSKNSALEYQLSEI--- 375
Cdd:COG5022   840 FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERqLQELKIDVKS-----ISSLKLVNLELESEIIELkks 914
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  376 QKSNMQIKSnigtlkdahEFKEDRSPYPQDFHNVMQLLDSQEskwtarvqaIHQEHKKEKGRLLSHIEKLRTS------M 449
Cdd:COG5022   915 LSSDLIENL---------EFKTELIARLKKLLNNIDLEEGPS---------IEYVKLPELNKLHEVESKLKETseeyedL 976
                         250       260
                  ....*....|....*....|....*...
gi 578825192  450 IDDLNASNVFYKKRIEELGQRLQEQNEL 477
Cdd:COG5022   977 LKKSTILVREGNKANSELKNFKKELAEL 1004
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
273-402 9.73e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 37.75  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 273 HFEYQ-KNAQIEKLRSEIVVLKEELQLTRSELEAAHHASAVrFSKEYEMQKTKEEDFLklfDRWKEEEKEKLVDEMEKVK 351
Cdd:cd12926   14 HQQYQdKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKI-FEEQGQTQEKCSKEYL---ERFRREGNEKEMQRILLNS 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578825192 352 EMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLK-DAHEFKEDRSPY 402
Cdd:cd12926   90 ERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKpDLMQLRKIRDQY 141
 
Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
104-224 4.40e-47

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 163.65  E-value: 4.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  104 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQFTIEYLLHSQEF 183
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 578825192  184 LTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECK 224
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
190-486 6.71e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 190 TLEERLRLSHCDGEQSKK---LLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANyyqchfCDKAFMNQAFLQSHIQRR 266
Cdd:PRK03918 256 KLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE------IEKRLSRLEEEINGIEER 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 267 HTEENShfeyqKNAQIEKLRSEIVVLKEELqltrSELEAAHhasavrfsKEYEMQKTKEEDFLKLFDRWKEEEKEKLV-- 344
Cdd:PRK03918 330 IKELEE-----KEERLEELKKKLKELEKRL----EELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEke 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 345 -DEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGT------LKDAHEFKEDRSPYPQDFHNV---MQLLD 414
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIekeLKEIE 472
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578825192 415 SQESKWTARVQAIHQEHKKEkgRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIK 486
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
270-489 6.97e-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: 43.51  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192   270 ENSHFEYQKNaqIEKLRSEIVVLKEELQLTRSELEAAHHAsavrfskeyemQKTKEEDFLKLfdRWKEEEKEKLVDEMEK 349
Cdd:TIGR02168  669 NSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKE-----------LEELEEELEQL--RKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192   350 VKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLKDA-HEFKEDRSPYPQDFHNVMQLLDSQESKWTArVQAIH 428
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALREALDE-LRAEL 812
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578825192   429 QEHKKEKGRLLSHIEKLRTSMIDdlnasnvfYKKRIEELGQRLQEQNELIITQRQQIKDFT 489
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAA--------TERRLEDLEEQIEELSEDIESLAAEIEELE 865
COG5022 COG5022
Myosin heavy chain [General function prediction only];
224-477 3.15e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  224 KRRKKMISTQQLMieaKANYYQCHFCDKAFMNQAFlqsHIQRRHTEENSHFEY-QKNAQIEKLRSEIV---VLKEELQLT 299
Cdd:COG5022   766 QALKRIKKIQVIQ---HGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYrSYLACIIKLQKTIKrekKLRETEEVE 839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  300 RSELEAAHHASAVRFSKEYEMQKTKEEDFLKLFDRWKEEEKEK-LVDEMEKVKEmfmkeFKELTSKNSALEYQLSEI--- 375
Cdd:COG5022   840 FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERqLQELKIDVKS-----ISSLKLVNLELESEIIELkks 914
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  376 QKSNMQIKSnigtlkdahEFKEDRSPYPQDFHNVMQLLDSQEskwtarvqaIHQEHKKEKGRLLSHIEKLRTS------M 449
Cdd:COG5022   915 LSSDLIENL---------EFKTELIARLKKLLNNIDLEEGPS---------IEYVKLPELNKLHEVESKLKETseeyedL 976
                         250       260
                  ....*....|....*....|....*...
gi 578825192  450 IDDLNASNVFYKKRIEELGQRLQEQNEL 477
Cdd:COG5022   977 LKKSTILVREGNKANSELKNFKKELAEL 1004
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-623 5.93e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 277 QKNAQIEKLRSEIVVLKEELQLTRSELEaahhasavRFSKEYEMQKTKEEDFLKLfdRWKEEEKEKLVDEMEKVKEMFM- 355
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIE--------ELKKEIEELEEKVKELKEL--KEKAEEYIKLSEFYEEYLDELRe 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 356 --KEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLKDAHEFKEDRSPYPQDFHNVMQLLDSQEskwtarvqaihqEHKK 433
Cdd:PRK03918 312 ieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE------------RLKK 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 434 EKGRLlsHIEKLRtSMIDDLnasnvfyKKRIEELGQRLQEQNELIITQRQQIKDFTCNpLNSISEPKGN-PLAWQAFESQ 512
Cdd:PRK03918 380 RLTGL--TPEKLE-KELEEL-------EKAKEEIEEEISKITARIGELKKEIKELKKA-IEELKKAKGKcPVCGRELTEE 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 513 PAApavpmNAPALHTLETKSSLP-MVHGRENEQKLNNNKMHLRKALKSNSSLTKgLRTMVEQ--NLMEKL---------- 579
Cdd:PRK03918 449 HRK-----ELLEEYTAELKRIEKeLKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQlkELEEKLkkynleelek 522
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 580 ----------ETLGINADIRGISSD-----QLHRVLKSVESERHKQEREIPNFH-QIREF 623
Cdd:PRK03918 523 kaeeyeklkeKLIKLKGEIKSLKKElekleELKKKLAELEKKLDELEEELAELLkELEEL 582
PTZ00121 PTZ00121
MAEBL; Provisional
203-444 6.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  203 EQSKKLLTKQAGEIKTLKEECK-RRKKMISTQQLMIEAKANyyQCHFCDKAFMNQAFLQSHIQRRHTEENSHFEYQKNAQ 281
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAE--EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  282 IEKLRSEIVVLKEELQLTRSELEAAHHASAVRFSKEY------EMQKTKEEDFLKLFDRWKEEEKEKLVDEMEKVKEMFM 355
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192  356 KEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLK--------DAHEFKEDRSPYPQDFHNVMQLLDSQESKWTARVQAI 427
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeaeedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
                         250
                  ....*....|....*..
gi 578825192  428 HQEHKKEKGRLLSHIEK 444
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDK 1798
PRK01156 PRK01156
chromosome segregation protein; Provisional
193-512 7.67e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 193 ERLRLSHCDGEQSKKLLTKQAGEIKTLKEECKRRKKMISTQQ---LMIEAKANYYqchfcdkafmnqaflqSHIQRRHTE 269
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAEsdlSMELEKNNYY----------------KELEERHMK 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 270 ENSHFEYQKNAQIE---KLRSEIVVLKEELQLTRSEL---EAAHHASAV--RFSKEYEMQKTKEEDFLKLFDRWKEEEKE 341
Cdd:PRK01156 285 IINDPVYKNRNYINdyfKYKNDIENKKQILSNIDAEInkyHAIIKKLSVlqKDYNDYIKKKSRYDDLNNQILELEGYEMD 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 342 --KLVDEMEKVK---EMFMKEFKELTSKNS-----------ALEYQLSEIQKSNMQIKSNIGTL---KDAHEFKEDrspy 402
Cdd:PRK01156 365 ynSYLKSIESLKkkiEEYSKNIERMSAFISeilkiqeidpdAIKKELNEINVKLQDISSKVSSLnqrIRALRENLD---- 440
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 403 pqDFHNVMQLLDSQE-------SKWTARVQAIHQEHKKEKGRLLSHIEKLRTSmIDDLNASNVFYKKRIEELG----QRL 471
Cdd:PRK01156 441 --ELSRNMEMLNGQSvcpvcgtTLGEEKSNHIINHYNEKKSRLEEKIREIEIE-VKDIDEKIVDLKKRKEYLEseeiNKS 517
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 578825192 472 QEQNELIITQRQQIKDFtcnpLNSISEPKGNPLAWQAFESQ 512
Cdd:PRK01156 518 INEYNKIESARADLEDI----KIKINELKDKHDKYEEIKNR 554
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
273-402 9.73e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 37.75  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825192 273 HFEYQ-KNAQIEKLRSEIVVLKEELQLTRSELEAAHHASAVrFSKEYEMQKTKEEDFLklfDRWKEEEKEKLVDEMEKVK 351
Cdd:cd12926   14 HQQYQdKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKI-FEEQGQTQEKCSKEYL---ERFRREGNEKEMQRILLNS 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578825192 352 EMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLK-DAHEFKEDRSPY 402
Cdd:cd12926   90 ERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKpDLMQLRKIRDQY 141
 
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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