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Conserved domains on  [gi|209977092|ref|NP_033132|]
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rhotekin isoform b [Mus musculus]

Protein Classification

Hr1 and Anillin domain-containing protein( domain architecture ID 10654333)

protein containing domains Hr1, Anillin, PH-like, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 104-257 2.68e-42

Cell division protein anillin; Anillin is a protein involved in septin organization during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


:

Pssm-ID: 462393  Cd Length: 139  Bit Score: 148.19  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  104 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQIGEQIQDTEMV-LVDRT-LTDISFQNNVLFAEAEPDFELRLE 181
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977092  182 LYGACV-EEEGALAGAPKRLATKLssslgrssgkrvrasldSAGASGNSPVlLPTPAVGGPRFHLLAHTTLTLEEVQ 257
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASKL-----------------ASKSLGRSPG-GKLAVRRGSKFKLLGSLTLTLLSVG 139
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 296-406 2.19e-41

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


The actual alignment was detected with superfamily member cd13249:

Pssm-ID: 473070  Cd Length: 111  Bit Score: 144.45  E-value: 2.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092 296 QPTASGALRVQQAGE-LQNGTLVHGVLKGTNLFCYWRSEDADTGQEPLFTIVINKETRVRAGELEQAPEwPFTLSISNKY 374
Cdd:cd13249    1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKGR-ASSLSIINPY 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 209977092 375 GDDEVTNTLQLESREALQNWMEALWQLFFDMS 406
Cdd:cd13249   80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 23-78 1.74e-11

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


:

Pssm-ID: 128981  Cd Length: 57  Bit Score: 59.51  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 209977092    23 LEDTELQRKLDHEIRMRDGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 78
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 421-532 4.80e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  421 PAPRKPPQALAKQGSLYHEMAIEPLDDIAAVTDILAQREGTRlEPSPPWLAMFTDQPALPSSCSPASVAPVPTWMQPLPW 500
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW-DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          90       100       110
                  ....*....|....*....|....*....|..
gi 209977092  501 GRPRTFSLDAAPADHSLGPSRSVAPLPPQRSP 532
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
 
Name Accession Description Interval E-value
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 104-257 2.68e-42

Cell division protein anillin; Anillin is a protein involved in septin organization during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


Pssm-ID: 462393  Cd Length: 139  Bit Score: 148.19  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  104 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQIGEQIQDTEMV-LVDRT-LTDISFQNNVLFAEAEPDFELRLE 181
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977092  182 LYGACV-EEEGALAGAPKRLATKLssslgrssgkrvrasldSAGASGNSPVlLPTPAVGGPRFHLLAHTTLTLEEVQ 257
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASKL-----------------ASKSLGRSPG-GKLAVRRGSKFKLLGSLTLTLLSVG 139
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 296-406 2.19e-41

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


Pssm-ID: 270069  Cd Length: 111  Bit Score: 144.45  E-value: 2.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092 296 QPTASGALRVQQAGE-LQNGTLVHGVLKGTNLFCYWRSEDADTGQEPLFTIVINKETRVRAGELEQAPEwPFTLSISNKY 374
Cdd:cd13249    1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKGR-ASSLSIINPY 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 209977092 375 GDDEVTNTLQLESREALQNWMEALWQLFFDMS 406
Cdd:cd13249   80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 23-78 1.74e-11

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 59.51  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 209977092    23 LEDTELQRKLDHEIRMRDGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 78
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 300-398 9.79e-06

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: 44.46  E-value: 9.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092   300 SGALRVQQAGELQNGTLVHGVLKGtNLFCYWRSEDADTGQEPLFTIVInKETRVRAGELEQAPEWPFTLSISNKygdDEV 379
Cdd:smart00233   4 EGWLYKKSGGGKKSWKKRYFVLFN-STLLYYKSKKDKKSYKPKGSIDL-SGCTVREAPDPDSSKKPHCFEIKTS---DRK 78

                           90
                   ....*....|....*....
gi 209977092   380 TNTLQLESREALQNWMEAL 398
Cdd:smart00233  79 TLLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 320-398 1.72e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 41.01  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  320 VLKGTNLFcYWRSEDADTGQEPLFTIVINKETRVRAGELEQAP-EWPFTLSISNKYGDDEVTntLQLESREALQNWMEAL 398
Cdd:pfam00169  24 VLFDGSLL-YYKDDKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTGKRTYL--LQAESEEERKDWIKAI 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 421-532 4.80e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  421 PAPRKPPQALAKQGSLYHEMAIEPLDDIAAVTDILAQREGTRlEPSPPWLAMFTDQPALPSSCSPASVAPVPTWMQPLPW 500
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW-DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          90       100       110
                  ....*....|....*....|....*....|..
gi 209977092  501 GRPRTFSLDAAPADHSLGPSRSVAPLPPQRSP 532
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
 
Name Accession Description Interval E-value
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 104-257 2.68e-42

Cell division protein anillin; Anillin is a protein involved in septin organization during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


Pssm-ID: 462393  Cd Length: 139  Bit Score: 148.19  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  104 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQIGEQIQDTEMV-LVDRT-LTDISFQNNVLFAEAEPDFELRLE 181
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977092  182 LYGACV-EEEGALAGAPKRLATKLssslgrssgkrvrasldSAGASGNSPVlLPTPAVGGPRFHLLAHTTLTLEEVQ 257
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASKL-----------------ASKSLGRSPG-GKLAVRRGSKFKLLGSLTLTLLSVG 139
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 296-406 2.19e-41

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


Pssm-ID: 270069  Cd Length: 111  Bit Score: 144.45  E-value: 2.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092 296 QPTASGALRVQQAGE-LQNGTLVHGVLKGTNLFCYWRSEDADTGQEPLFTIVINKETRVRAGELEQAPEwPFTLSISNKY 374
Cdd:cd13249    1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKGR-ASSLSIINPY 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 209977092 375 GDDEVTNTLQLESREALQNWMEALWQLFFDMS 406
Cdd:cd13249   80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 23-78 1.74e-11

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 59.51  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 209977092    23 LEDTELQRKLDHEIRMRDGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 78
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 300-398 9.79e-06

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: 44.46  E-value: 9.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092   300 SGALRVQQAGELQNGTLVHGVLKGtNLFCYWRSEDADTGQEPLFTIVInKETRVRAGELEQAPEWPFTLSISNKygdDEV 379
Cdd:smart00233   4 EGWLYKKSGGGKKSWKKRYFVLFN-STLLYYKSKKDKKSYKPKGSIDL-SGCTVREAPDPDSSKKPHCFEIKTS---DRK 78

                           90
                   ....*....|....*....
gi 209977092   380 TNTLQLESREALQNWMEAL 398
Cdd:smart00233  79 TLLLQAESEEEREKWVEAL 97
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 300-398 7.35e-05

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: 41.76  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092 300 SGALRVQQAGELQNGTLVHGVLKGTNLFCYwrSEDADTGQEPLFTIVINKETRVRAGELEqapEWPFTLSISNKygdDEV 379
Cdd:cd00821    2 EGYLLKRGGGGLKSWKKRWFVLFEGVLLYY--KSKKDSSYKPKGSIPLSGILEVEEVSPK---ERPHCFELVTP---DGR 73

                         90
                 ....*....|....*....
gi 209977092 380 TNTLQLESREALQNWMEAL 398
Cdd:cd00821   74 TYYLQADSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 320-398 1.72e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 41.01  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  320 VLKGTNLFcYWRSEDADTGQEPLFTIVINKETRVRAGELEQAP-EWPFTLSISNKYGDDEVTntLQLESREALQNWMEAL 398
Cdd:pfam00169  24 VLFDGSLL-YYKDDKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTGKRTYL--LQAESEEERKDWIKAI 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 421-532 4.80e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  421 PAPRKPPQALAKQGSLYHEMAIEPLDDIAAVTDILAQREGTRlEPSPPWLAMFTDQPALPSSCSPASVAPVPTWMQPLPW 500
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW-DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          90       100       110
                  ....*....|....*....|....*....|..
gi 209977092  501 GRPRTFSLDAAPADHSLGPSRSVAPLPPQRSP 532
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
PHA03247 PHA03247
large tegument protein UL36; Provisional
 420-534 5.32e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977092  420 TPAPRKPPQALAKQGSLYHEMAIEPLD--DIAAVTDILAQREGTRLEPSPPWLAMFTDQPALPSSCSPASVAPVPTWMQP 497
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDpaDPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV 2856

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 209977092  498 LPWG----RPRTFSLDAAPADHSLGPSRSVAPLPPQRSPKS 534
Cdd:PHA03247 2857 APGGdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTES 2897
 
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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