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Conserved domains on  [gi|2217370695|ref|XP_047277276|]
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rhophilin-1 isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRO1_Alix_like super family cl14649
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 162-523 0e+00

Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1 and Rim20 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, HD-PTP, and Brox) and Snf7 (in the case of yeast Bro1, and Rim20). The single domain protein human Brox, and the isolated Bro1-like domains of Alix, HD-PTP and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix, HD-PTP, Bro1, and Rim20 also have a V-shaped (V) domain, which in the case of Alix, has been shown to be a dimerization domain and to contain a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in this superfamily. Alix, HD-PTP and Bro1 also have a proline-rich region (PRR); the Alix PRR binds multiple partners. Rhophilin-1, and -2, in addition to this Bro1-like domain, have an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This protein has a C-terminal, catalytically inactive tyrosine phosphatase domain.


The actual alignment was detected with superfamily member cd09248:

Pssm-ID: 472700  Cd Length: 384  Bit Score: 703.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:cd09248     1 MIPLGLKETKELDLPTPLKELISEHFGEDGTSYEAEIRELEDLRQAMRTPSRSEAGLELLMAYYNQLCFLDARFFPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 242 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDM 321
Cdd:cd09248    81 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLLRENFSNAPSPDM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 322 SAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKA 401
Cdd:cd09248   161 STASLSMLEQLMVAQAQECIFEGLLLPLLATPQDFFAQLQLAQEAAQVAAEYRLVHRTMAQPPVRDYVPFSWTALVHVKA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 402 EYFRSLAHYHVAMALCDGSPATEGELPTHEQVFLQPPTsSKPRGPVLPQELEERRQLGKAHLKRAILGQEEALRLHALCR 481
Cdd:cd09248   241 EHFCALAHYHAAMALCDSSPASEGELATQEKAFLQPHT-SQPEGPSLPQEPEERRKLGKAHLKRAILGQEEALRLHALCR 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2217370695 482 VLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQ 523
Cdd:cd09248   320 ILRKVDLLQAVLTQALRRSLAKYSELDREDDFFETGEAPDIQ 361
HR1 super family cl00087
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
 74-158 5.26e-36

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


The actual alignment was detected with superfamily member cd11633:

Pssm-ID: 469609  Cd Length: 85  Bit Score: 129.95  E-value: 5.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  74 GCDSLTQIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSNLQLLKEELEELSGGVDPGRH 153
Cdd:cd11633     1 GCDPLAATQRSKLQSRRARINQQINKEMRMRAGAENLFKATSNKKVRETVALELSFVNSNLQLLKEELAELNSSVEIYQS 80


                  ....*
gi 2217370695 154 GSEAV 158
Cdd:cd11633    81 DSEAI 85
 
Name Accession Description Interval E-value
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 162-523 0e+00

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily contains the Bro1-like domain of the RhoA-binding protein, Rhophilin-1. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. The Drosophila knockout of the Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Rhophilin-1 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_ like superfamily.


Pssm-ID: 185771  Cd Length: 384  Bit Score: 703.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:cd09248     1 MIPLGLKETKELDLPTPLKELISEHFGEDGTSYEAEIRELEDLRQAMRTPSRSEAGLELLMAYYNQLCFLDARFFPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 242 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDM 321
Cdd:cd09248    81 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLLRENFSNAPSPDM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 322 SAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKA 401
Cdd:cd09248   161 STASLSMLEQLMVAQAQECIFEGLLLPLLATPQDFFAQLQLAQEAAQVAAEYRLVHRTMAQPPVRDYVPFSWTALVHVKA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 402 EYFRSLAHYHVAMALCDGSPATEGELPTHEQVFLQPPTsSKPRGPVLPQELEERRQLGKAHLKRAILGQEEALRLHALCR 481
Cdd:cd09248   241 EHFCALAHYHAAMALCDSSPASEGELATQEKAFLQPHT-SQPEGPSLPQEPEERRKLGKAHLKRAILGQEEALRLHALCR 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2217370695 482 VLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQ 523
Cdd:cd09248   320 ILRKVDLLQAVLTQALRRSLAKYSELDREDDFFETGEAPDIQ 361
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 162-523 3.22e-127

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 214990  Cd Length: 381  Bit Score: 379.77  E-value: 3.22e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSEDSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPPPEGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  242 LGLFFHWYDSL-TGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAP--- 317
Cdd:smart01041  81 LKLSFTWYDSLdTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYLKENFLHALste 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  318 -SPDMSAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLrlaqeAAQVAAEYRLVHRTMAQ-PPVHDYVPVSWTA 395
Cdd:smart01041 161 pSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKNKDSLIAKL-----AAQAAEYYEEALKALQTsEPVKGYIPKSWIK 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  396 LVHVKAEYFRSLAHYHVAMALCDGSPAteGElptheqvflqpptsskprGPVLPQELEERRQLGKAHLKrailgqeealr 475
Cdd:smart01041 236 LVQVKAHHFKALAHYYQALDLEEANKY--GE------------------AIARLQEALERLKEAKKHLR----------- 284

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2217370695  476 lhalCRVLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQ 523
Cdd:smart01041 285 ----CKKLGKADKLQEDLSGLKDVVEEKLKEAEKDNDFIYHERVPDIV 328
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 162-527 6.04e-86

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 460803  Cd Length: 366  Bit Score: 272.53  E-value: 6.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGAS-YEAEIRELEALRQ-AMRTPSRNESGLELLTAYYNQLCFLDARFltPA 239
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTYGSQDPSsFEDDLAELNKLRQdAVRGANEDESGLDLLYKYYAQLELLELRF--PI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 240 -RSLGLFFHWYDSL--TGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHA 316
Cdd:pfam03097  79 dIQIGIEFTWYDAFgtSSKKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYLKENFLHA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 317 PSPDMSAASLCALEQLMMAQAQECVFEglsppASMAPQ--DCL-AQLrlaqeAAQVAAEYRLVHRTMAQPPVHDYvpvSW 393
Cdd:pfam03097 159 PSPDLSPETLKALSNLMLAQAQECFWE-----KAINDNkkDSLiAKL-----AAQVSELYEEALEALKLSGLIDK---EW 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 394 TALVHVKAEYFRSLAHYHVAMAlcdgspategelptheqvflqpptsskprgpvlpqeLEERRQLGK--AHLKRAILGQE 471
Cdd:pfam03097 226 ISHVQAKAHHFKALAQYRQALD------------------------------------DEEAKKYGEeiARLQLALSLLK 269

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217370695 472 EALRLHALCRVLREVDLLRAVISqtlqrslAKYAELDREDDFC------EAAEAPDIQRAPV 527
Cdd:pfam03097 270 EALKSDRYKKVLEDLKGLLDVVE-------EKLKRAEKDNDFIyhervpSESSLPPIKPASM 324
HR1_Rhophilin-1 cd11633
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-1; ...
 74-158 5.26e-36

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-1; Rhophilin-1 is a scaffolding protein that functions as an effector of the Rho family of small GTPases. It has been implicated in sperm motility. Rhophilin-1 contains an N-terminal HR1, a central Bro1-like, and a C-terminal PDZ domain; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; Rhophilin-1 binds RhoA was isolated initially as a RhoA-binding protein.


Pssm-ID: 212023  Cd Length: 85  Bit Score: 129.95  E-value: 5.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  74 GCDSLTQIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSNLQLLKEELEELSGGVDPGRH 153
Cdd:cd11633     1 GCDPLAATQRSKLQSRRARINQQINKEMRMRAGAENLFKATSNKKVRETVALELSFVNSNLQLLKEELAELNSSVEIYQS 80


                  ....*
gi 2217370695 154 GSEAV 158
Cdd:cd11633    81 DSEAI 85
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 88-133 1.61e-08

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: 51.04  E-value: 1.61e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217370695   88 SRRAQIHQQIDKELQMRTGAENLYRATSN-NRVRETVALELSYVNSN 133
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNdRKVLSEAQSMLRESNQK 47
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
 89-139 6.86e-07

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 46.74  E-value: 6.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217370695  89 RRAQIHQQIDKELQMRTGAENLYR---ATSNNRVRETVALELSYVNSNLQLLKE 139
Cdd:pfam02185   1 RLQELRKKIEVEKKIKEGAENMLRllqATKDRKVLAEAESELRESNRKIQLLRE 54
 
Name Accession Description Interval E-value
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 162-523 0e+00

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily contains the Bro1-like domain of the RhoA-binding protein, Rhophilin-1. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. The Drosophila knockout of the Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Rhophilin-1 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_ like superfamily.


Pssm-ID: 185771  Cd Length: 384  Bit Score: 703.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:cd09248     1 MIPLGLKETKELDLPTPLKELISEHFGEDGTSYEAEIRELEDLRQAMRTPSRSEAGLELLMAYYNQLCFLDARFFPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 242 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDM 321
Cdd:cd09248    81 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLLRENFSNAPSPDM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 322 SAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKA 401
Cdd:cd09248   161 STASLSMLEQLMVAQAQECIFEGLLLPLLATPQDFFAQLQLAQEAAQVAAEYRLVHRTMAQPPVRDYVPFSWTALVHVKA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 402 EYFRSLAHYHVAMALCDGSPATEGELPTHEQVFLQPPTsSKPRGPVLPQELEERRQLGKAHLKRAILGQEEALRLHALCR 481
Cdd:cd09248   241 EHFCALAHYHAAMALCDSSPASEGELATQEKAFLQPHT-SQPEGPSLPQEPEERRKLGKAHLKRAILGQEEALRLHALCR 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2217370695 482 VLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQ 523
Cdd:cd09248   320 ILRKVDLLQAVLTQALRRSLAKYSELDREDDFFETGEAPDIQ 361
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
 162-523 0e+00

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; This family contains the Bro1-like domain of RhoA-binding proteins, Rhophilin-1 and -2, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 and -2 bind both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 and -2, contain an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Their PDZ domains have limited homology. Rhophilin-1 and -2 have different activities. The Drosophila knockout of Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. Roles of Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix _like superfamily.


Pssm-ID: 185767  Cd Length: 350  Bit Score: 538.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:cd09244     1 MIPLGLKETKEIDFMEPFKDFILEHYSEDPSLYEDEIADFTDLRQAMRTPSRDEAGIELLFEYYNQLYFVERRFFPPDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 242 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDM 321
Cdd:cd09244    81 LGIYFHWYDSLTGVPSVQRSVAFEKASVLFNIGALYTQIGAKQDRTTEEGIEAAVDAFQRAAGAFNYLRENFSNAPSMDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 322 SAASLCALEQLMMAQAQECVFEGLSPPASMaPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKA 401
Cdd:cd09244   161 SPEMLEALIKLMLAQAQECVFEKLVLPGED-SKDIQACLDLAQEAAQVSDCYSEVHKLMNQEPVKDYIPYSWISLVEVKS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 402 EYFRSLAHYHVAMALCdgspategelptheqvflqpptsskprgpvlpqeLEERRQLGKAHLKRAILGQEEALRLHALCR 481
Cdd:cd09244   240 EHYKALAHYYAAMGLL----------------------------------LEERRLLGKAHLKEALLLHEEALRLHRMCR 285

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2217370695 482 VLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQ 523
Cdd:cd09244   286 FLRNVDSLQEVLKEAHDRSLNKYSSLEEEDDFSDALDAPDIQ 327
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
 162-522 1.58e-129

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily contains the Bro1-like domain of RhoA-binding protein, Rhophilin-2. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-1, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-2, binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-2 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Roles for Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. Rhophilin-2 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185772  Cd Length: 385  Bit Score: 385.74  E-value: 1.58e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:cd09249     1 LIPLGLKETKDVDFSVPLKDFILEHYSEDGSEYEDEIADLMDLRQACRTPSRDEAGVELLMSYFSQLGFLENRFFPPTRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 242 LGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDM 321
Cdd:cd09249    81 MGILFTWYDSFTGVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTQAGLESAVDAFQRAAGVLNYLKETFTHTPSYDM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 322 SAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLaqLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKA 401
Cdd:cd09249   161 SPAMLSVLVKMMLAQAQECLFEKISLPGIRNEFFTL--VKMAQEAAKVGEVYMQVHTAMNQAPVKENIPYSWSSLVQVKA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 402 EYFRSLAHYHVAMALCDgSPATEGELPTHEQVFLQPPTSSKPRGpVLPQEL----EERRQLGKAHLKRAILGQEEALRLH 477
Cdd:cd09249   239 HHYNALAHYFVATLLID-HQLNPSDDEDKQEKALSQLYDHMPEG-LTPLTIlknkQQRRLLGKAHLRRAIMHHEEAIREA 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2217370695 478 ALCRVLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDI 522
Cdd:cd09249   317 SLCKKLRNIDVLQEVLSAAHNRSLLKYAQHQKEDDFLDLIDAPDI 361
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 162-523 3.22e-127

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 214990  Cd Length: 381  Bit Score: 379.77  E-value: 3.22e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSEDSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPPPEGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  242 LGLFFHWYDSL-TGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAP--- 317
Cdd:smart01041  81 LKLSFTWYDSLdTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYLKENFLHALste 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  318 -SPDMSAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLrlaqeAAQVAAEYRLVHRTMAQ-PPVHDYVPVSWTA 395
Cdd:smart01041 161 pSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKNKDSLIAKL-----AAQAAEYYEEALKALQTsEPVKGYIPKSWIK 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  396 LVHVKAEYFRSLAHYHVAMALCDGSPAteGElptheqvflqpptsskprGPVLPQELEERRQLGKAHLKrailgqeealr 475
Cdd:smart01041 236 LVQVKAHHFKALAHYYQALDLEEANKY--GE------------------AIARLQEALERLKEAKKHLR----------- 284

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2217370695  476 lhalCRVLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQ 523
Cdd:smart01041 285 ----CKKLGKADKLQEDLSGLKDVVEEKLKEAEKDNDFIYHERVPDIV 328
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 162-527 6.04e-86

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 460803  Cd Length: 366  Bit Score: 272.53  E-value: 6.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGAS-YEAEIRELEALRQ-AMRTPSRNESGLELLTAYYNQLCFLDARFltPA 239
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTYGSQDPSsFEDDLAELNKLRQdAVRGANEDESGLDLLYKYYAQLELLELRF--PI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 240 -RSLGLFFHWYDSL--TGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHA 316
Cdd:pfam03097  79 dIQIGIEFTWYDAFgtSSKKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYLKENFLHA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 317 PSPDMSAASLCALEQLMMAQAQECVFEglsppASMAPQ--DCL-AQLrlaqeAAQVAAEYRLVHRTMAQPPVHDYvpvSW 393
Cdd:pfam03097 159 PSPDLSPETLKALSNLMLAQAQECFWE-----KAINDNkkDSLiAKL-----AAQVSELYEEALEALKLSGLIDK---EW 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 394 TALVHVKAEYFRSLAHYHVAMAlcdgspategelptheqvflqpptsskprgpvlpqeLEERRQLGK--AHLKRAILGQE 471
Cdd:pfam03097 226 ISHVQAKAHHFKALAQYRQALD------------------------------------DEEAKKYGEeiARLQLALSLLK 269

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217370695 472 EALRLHALCRVLREVDLLRAVISqtlqrslAKYAELDREDDFC------EAAEAPDIQRAPV 527
Cdd:pfam03097 270 EALKSDRYKKVLEDLKGLLDVVE-------EKLKRAEKDNDFIyhervpSESSLPPIKPASM 324
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 162-416 6.05e-65

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins; This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Rim20 (also known as PalA), Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1 participates in endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Bro1. Snf7 binds to a conserved hydrophobic patch on the middle of the concave side of the Bro1 domain. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. The Alix V-domain is also a dimerization domain. The C-terminal portion (V-domain and proline rich-region) of Bro1 interacts with Doa4, a protease that deubiquitinates integral membrane proteins sorted into the lumenal vesicles of late-endosomal multivesicular bodies. It interacts with a YPxL motif in the Doa4 catalytic domain to stimulate its deubiquitination activity.


Pssm-ID: 185765  Cd Length: 348  Bit Score: 217.15  E-value: 6.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARS 241
Cdd:cd09242     1 LISLPLKDTEEVDWKKPLSSYLKRSYGSSTFYYEEEIAEFDRLRQDANGVLADETGRDLLYKYYGQLELLELRFPFNNKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 242 LGLFFHWYDSLTG-VPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPD 320
Cdd:cd09242    81 LKVDFTWYDAFYKsKKVKQHSLAFEKASVLFNIGALLSQLAAEKYREDEDDLKEAITNLQQAAGCFQYINENFLHAPSVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 321 MSAASLCALEQLMMAQAQECVFEGL----SPP--ASMAPQDCLAQLRLaqeaaqvaaeYRLVHRTM--AQPPVHDYVPVS 392
Cdd:cd09242   161 LQQENVKFLVKLMLAQAQEIFLLKLingdDAQkkASLISKLASATANL----------YESCVEFLkeIQEKGISYGDPK 230

                         250       260
                  ....*....|....*....|....
gi 2217370695 393 WTALVHVKAEYFRSLAHYHVAMAL 416
Cdd:cd09242   231 WISLVQCKAHYYKSLAAYYHALAL 254
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 162-420 2.07e-47

Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1 and Rim20 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, HD-PTP, and Brox) and Snf7 (in the case of yeast Bro1, and Rim20). The single domain protein human Brox, and the isolated Bro1-like domains of Alix, HD-PTP and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix, HD-PTP, Bro1, and Rim20 also have a V-shaped (V) domain, which in the case of Alix, has been shown to be a dimerization domain and to contain a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in this superfamily. Alix, HD-PTP and Bro1 also have a proline-rich region (PRR); the Alix PRR binds multiple partners. Rhophilin-1, and -2, in addition to this Bro1-like domain, have an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This protein has a C-terminal, catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185761 [Multi-domain]  Cd Length: 345  Bit Score: 169.84  E-value: 2.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGE-DGASYEAEIRELEALRQAMRTPSRN----ESGLELLTAYYNQLCFLDARFL 236
Cdd:cd09034     1 FIGLPLKKTKEVDVKVPLSKFIPKNYGElEATAVEDLIEKLSKLRNNIVTEQNNdttcENLLEALKEYLPYLLGLEKKLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 237 TPARSLGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARR-AMEAFQRAAGAFSLLRENFSH 315
Cdd:cd09034    81 FQKLRDNVEFTWTDSFDTKKESATSLRYELLSILFNLAALASQLANEKLITGSEEDLKqAIKSLQKAAGYFEYLKEHVLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 316 APS----PDMSAASLCALEQLMMAQAQECVFEglsppasMAPQDCLAQL----RLAQEAAQVAAEYRLVHRTMAQPPVHd 387
Cdd:cd09034   161 LPPdelpVDLTEAVLSALSLIMLAQAQECFLL-------KAEEDKKAKLsllaRLACEAAKYYEEALKCLSGVDLETIK- 232

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2217370695 388 YVPVSWTALVHVKAEYFRSLAHYHVAMALCDGS 420
Cdd:cd09034   233 NIPKKWLLFLKWKKCIFKALAYYYHGLKLDEAN 265
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 167-418 2.20e-45

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2.


Pssm-ID: 185763  Cd Length: 346  Bit Score: 164.39  E-value: 2.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 167 LKETKELDWSTPLKELISVHF--GEDGASYEAEIRELEALRQA--MRTPSRNESGLELLTAYYNQLCFLDARFLTPARSL 242
Cdd:cd09240     8 LKKSSEVDLVKPLEKFIKNTYssGEEQADYKEAIKELNKLRNNavCRPLDKHESSLELLLRYYDQLCAIEPKFPFSESQI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 243 GLFFHWYD-----SLTGVPAQQ--RALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRE---- 311
Cdd:cd09240    88 QVTFTWKDafdkgSLFGGSKKLalSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFNHLKEtvls 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 312 NFSHAPSPDMSAASLCALEQLMMAQAQECVFEglsppasMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPV 391
Cdd:cd09240   168 ALQQEPTPDLSPDTLSALSALMLAQAQEVFYL-------KATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDVRSLLPK 240

                         250       260
                  ....*....|....*....|....*..
gi 2217370695 392 SWTALVHVKAEYFRSLAHYHVAMaLCD 418
Cdd:cd09240   241 DWIPVLAGKQAYFHALAEYHQSL-VAK 266
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 162-416 1.57e-44

Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily; This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to this Bro1-like domain, Alix, Bro1, Rim20, HD_PTP, and proteins belonging to this uncharacterized family, also have a V-shaped (V) domain. The Alix V-domain is a dimerization domain, and contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the BRO1_Alix_like superfamily. Many members of this superfamily also have a proline-rich region (PRR), a protein interaction domain.


Pssm-ID: 185769  Cd Length: 353  Bit Score: 162.18  E-value: 1.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 162 MIPLGLKETKELDWSTPLKELISVHFGEDGA-SYEAEIRELEALRQAMRTPSRNESG-LELLTAYYNQLCFLDARF--LT 237
Cdd:cd09246     1 MLSIHRKKTETVDLVSPLRAYISETYSEREAqDAEDDLAELQQLRSEVRTLQEKHAAsRELLLRYYRALCAVESRFpiSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 238 PARSLGLFFHWYDSLTGVP-AQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFS-- 314
Cdd:cd09246    81 ESGHARVSFSWYDAFRPHRkATQANVHFEKAAVLFNLGALSSQLGLQQDRTTAEGIKQACHAFQAAAGAFAHLRDKVSgk 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 315 --HAPSPDMSAASLCALEQLMMAQAQECVFE-----GLSPpasmAPQDCLAQlrlaqeaaQVAAEYRLVHRTMAQPPVHD 387
Cdd:cd09246   161 tgGFRTPDLTAECLGMLESLMLAQAQECFYEkavadGKSP----AVCSKLAK--------QARSYYEEALEALDSPPLKG 228

                         250       260
                  ....*....|....*....|....*....
gi 2217370695 388 YVPVSWTALVHVKAEYFRSLAHYHVAMAL 416
Cdd:cd09246   229 HFDKSWVAHVQLKAAYFRAEALYRAAKDL 257
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 156-411 1.58e-44

Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP) and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. HD-PTP participates in cell migration and endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185762  Cd Length: 361  Bit Score: 162.60  E-value: 1.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 156 EAVT-VPMIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDAR 234
Cdd:cd09239     1 EAVPrLPMLWLQLKSSGEFTFQPALKKYILENYGEDPELYSEELKSLEQLRQEAVNPPRDFEGCSVLKRYYGQLHLLQSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 235 F-LTPARSLGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENF 313
Cdd:cd09239    81 FpMGAGQEAAVPFTWTDIFSGSEVTHEDIKFEEASVLYNIGALHSQLGASDKRDSEEGMKVACTHFQCAAWAFAYLREHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 314 SHAPS-PDMSAASLCALEQLMMAQAQECVFEglsppASMA---PQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYV 389
Cdd:cd09239   161 PQVYGaVDMSSQLLSFNYSLMLAQAQECLLE-----KSLLdnrKSHITAKVSAQVVEYYKEALRALENWESNSKIILGKI 235

                         250       260
                  ....*....|....*....|..
gi 2217370695 390 PVSWTALVHVKAEYFRSLAHYH 411
Cdd:cd09239   236 QKEWRKLVQMKIAYYASIAHLH 257
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 163-414 2.81e-44

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and related proteins; This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 (also known as PalA) and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Bro1, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Rim20 and Rim23 participate in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Rim20. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain is a dimerization domain that also contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. Rim20 localizes to endosomes under alkaline pH conditions. By binding Snf7, it may bring the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and thus aid in the proteolytic activation of the latter. Rim20 and other intermediates in the Rim101 pathway play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis.


Pssm-ID: 185764  Cd Length: 355  Bit Score: 161.67  E-value: 2.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 163 IPLglKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFltPARsl 242
Cdd:cd09241     5 IPF--KRTLPVDLKDALRNYISNHYFQTPSSFEDDLAEIDKLRNDAINPEPSVNGLSLLKEYYAQLVVLSKKF--PDD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 243 GLFFHWYDSL---TGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLREN--FSHAP 317
Cdd:cd09241    79 QLEFTWYPTLgykSSGPVSLSSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYILQHllPTLSP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695 318 SPDMSAASLCALEQLMMAQAQECVFeglsppaSMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPpvhDYVPVSWTALV 397
Cdd:cd09241   159 PPDLDENTLKALESLMLAQAQECFW-------QKAISDGTKDSLIAKLAAQVSDYYQEALKYANKS---DLIRSDWINHL 228

                         250
                  ....*....|....*..
gi 2217370695 398 HVKAEYFRSLAHYHVAM 414
Cdd:cd09241   229 KVKKHHFKAAAHYRMAL 245
HR1_Rhophilin-1 cd11633
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-1; ...
 74-158 5.26e-36

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-1; Rhophilin-1 is a scaffolding protein that functions as an effector of the Rho family of small GTPases. It has been implicated in sperm motility. Rhophilin-1 contains an N-terminal HR1, a central Bro1-like, and a C-terminal PDZ domain; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; Rhophilin-1 binds RhoA was isolated initially as a RhoA-binding protein.


Pssm-ID: 212023  Cd Length: 85  Bit Score: 129.95  E-value: 5.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217370695  74 GCDSLTQIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSNLQLLKEELEELSGGVDPGRH 153
Cdd:cd11633     1 GCDPLAATQRSKLQSRRARINQQINKEMRMRAGAENLFKATSNKKVRETVALELSFVNSNLQLLKEELAELNSSVEIYQS 80


                  ....*
gi 2217370695 154 GSEAV 158
Cdd:cd11633    81 DSEAI 85
HR1_Rhophilin cd11624
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin; ...
 80-133 2.62e-18

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin; Rhophilins are scaffolding proteins that function as effectors of the Rho family of small GTPases. Vertebrates harbor two proteins, Rhophilin-1 and Rhophilin-2, whose exact functions are yet to be determined. Rhophilin-1 has been implicated in sperm motility. Rhophilin-2 regulates the organization of the actin cytoskeleton. Rhophilins contain N-terminal HR1, central Bro1-like, and C-terminal PDZ domains; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; both Rhophilin-1 and Rhophilin-2 bind RhoA, and Rhophilin-2 has also been shown to bind RhoB.


Pssm-ID: 212014  Cd Length: 76  Bit Score: 79.55  E-value: 2.62e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217370695  80 QIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSN 133
Cdd:cd11624     1 QSGRSQLQHKRAALNQKIHKQMKLRAGAENLFKATKNTKVKETVRLELSFVNSQ 54
HR1_Rhophilin-2 cd11634
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-2; ...
 77-133 9.72e-17

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-2; Rhophilin-2 is a scaffolding protein that functions as an effector of the Rho family of small GTPases. It plays a role in regulating the organization of the actin cytoskeleton. Rhophilin-2 contains an N-terminal HR1, a central Bro1-like, and a C-terminal PDZ domain; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; Rhophilin-2 has been shown to bind both RhoA and RhoB.


Pssm-ID: 212024  Cd Length: 82  Bit Score: 75.44  E-value: 9.72e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217370695  77 SLTQIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSN 133
Cdd:cd11634     1 PLAQTGRSKLQNQRAVLNQQILKAMRMRAGAENLLKATTNNKVREQVLLELSFVNSD 57
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 88-133 1.61e-08

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: 51.04  E-value: 1.61e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217370695   88 SRRAQIHQQIDKELQMRTGAENLYRATSN-NRVRETVALELSYVNSN 133
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNdRKVLSEAQSMLRESNQK 47
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
 89-139 6.86e-07

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 46.74  E-value: 6.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217370695  89 RRAQIHQQIDKELQMRTGAENLYR---ATSNNRVRETVALELSYVNSNLQLLKE 139
Cdd:pfam02185   1 RLQELRKKIEVEKKIKEGAENMLRllqATKDRKVLAEAESELRESNRKIQLLRE 54
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
 85-133 3.26e-06

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 45.01  E-value: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217370695  85 QLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRE---TVALELSYVNSN 133
Cdd:cd00089     2 KLQQRLEELRRKLEKELKIREGAENLLKLYSNPKVKKdlaEVQLNLKESKEK 53
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
 84-132 1.64e-04

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212012  Cd Length: 66  Bit Score: 39.94  E-value: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217370695  84 GQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNS 132
Cdd:cd11622     2 QKLEELKEQIRREIRKELKIKEGAENLRKATTDKKSLAHVESILKKSNR 50
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 246-315 2.92e-04

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185766  Cd Length: 353  Bit Score: 43.48  E-value: 2.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217370695 246 FHWYDSL-TGVPAQQRALAFEKGSVLFNIGALHTQ----IGARQDRSCTEgARRAMEAFQRAAGAFSLLRENFSH 315
Cdd:cd09243    87 FKWTDSLlGNEPSVQQDAIFELASMLFNVALWYTKhaskLAGKEDITEDE-AKDVHKSLRTAAGIFQFVKENYIP 160
 
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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