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Conserved domains on  [gi|79330131|ref|NP_001032031|]
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potyvirus VPg interacting protein (DUF1423) [Arabidopsis thaliana]

Protein Classification

OBERON family protein( domain architecture ID 11165419)

OBERON family protein similar to Arabidopsis thaliana protein OBERON 1, OBERON 2 and OBERON 3, which are involved in the maintenance and/or establishment of the meristems in Arabidopsis

Gene Ontology:  GO:0008270
PubMed:  18403411|16297627|21514168

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 416-551 9.89e-67

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


:

Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 212.92  E-value: 9.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   416 KKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANEAKREADRLQRIVLAKMDKSEEE 495
Cdd:pfam16312   1 KRARLALDACDRELEDKAREASELKFERQRKKQQIEELESIVRLKQAEAEMFQLKADEARREAEGLQRIALAKSEKSEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79330131   496 YASNYLKQRLSEAEAEKQYLFEKIKLQENSRvasqssgGGGDPSQVMMYSKIRDLL 551
Cdd:pfam16312  81 YASRYLKLRLEEAEEERRYKFEELKLLENSH-------RDYDNMKMRMQSKIQDLL 129
PHD_Oberon pfam07227
PHD - plant homeodomain finger protein; PHD_oberon is a plant homeodomain finger domain of ...
 198-323 6.21e-61

PHD - plant homeodomain finger protein; PHD_oberon is a plant homeodomain finger domain of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Oberon proteins are made up of a PHD finger domain and a coiled-coil domain. The PHD-finger domain is found in a wide variety of proteins involved in the regulation of chromatin structure. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (MP) (or Auxin response factor 7).


:

Pssm-ID: 429357  Cd Length: 130  Bit Score: 197.57  E-value: 6.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   198 CRNIACQNQLPADDCYCDICTNRKGFCNLCMCTICNKFDFSVNTCRWIGC-------DLCSHWTHTDCAIRDGQITTGss 270
Cdd:pfam07227   1 CRNIACRSQLPVDDCDCKICSQEDGFCRRCSCCICHKFDDNKDTCSWIGCsavvsegDSCGHWCHLDCALRDYKTGTV-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 79330131   271 aKNNTSGPGEIVFKCRACNRTSELLGWVKDVFQHCAPNWDRESLMKELDFVSR 323
Cdd:pfam07227  79 -KKGGSGGLDGQFYCRACGKTSELLGHVKKVLQTCAEAWRRDVLCKELDLGRR 130
 
Name Accession Description Interval E-value
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 416-551 9.89e-67

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 212.92  E-value: 9.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   416 KKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANEAKREADRLQRIVLAKMDKSEEE 495
Cdd:pfam16312   1 KRARLALDACDRELEDKAREASELKFERQRKKQQIEELESIVRLKQAEAEMFQLKADEARREAEGLQRIALAKSEKSEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79330131   496 YASNYLKQRLSEAEAEKQYLFEKIKLQENSRvasqssgGGGDPSQVMMYSKIRDLL 551
Cdd:pfam16312  81 YASRYLKLRLEEAEEERRYKFEELKLLENSH-------RDYDNMKMRMQSKIQDLL 129
PHD_Oberon pfam07227
PHD - plant homeodomain finger protein; PHD_oberon is a plant homeodomain finger domain of ...
 198-323 6.21e-61

PHD - plant homeodomain finger protein; PHD_oberon is a plant homeodomain finger domain of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Oberon proteins are made up of a PHD finger domain and a coiled-coil domain. The PHD-finger domain is found in a wide variety of proteins involved in the regulation of chromatin structure. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (MP) (or Auxin response factor 7).


Pssm-ID: 429357  Cd Length: 130  Bit Score: 197.57  E-value: 6.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   198 CRNIACQNQLPADDCYCDICTNRKGFCNLCMCTICNKFDFSVNTCRWIGC-------DLCSHWTHTDCAIRDGQITTGss 270
Cdd:pfam07227   1 CRNIACRSQLPVDDCDCKICSQEDGFCRRCSCCICHKFDDNKDTCSWIGCsavvsegDSCGHWCHLDCALRDYKTGTV-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 79330131   271 aKNNTSGPGEIVFKCRACNRTSELLGWVKDVFQHCAPNWDRESLMKELDFVSR 323
Cdd:pfam07227  79 -KKGGSGGLDGQFYCRACGKTSELLGHVKKVLQTCAEAWRRDVLCKELDLGRR 130
PHD_OBE1_like cd15612
PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins ...
 228-288 1.68e-30

PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins mainly found in plants; Included in this family are OBERON 1 (OBE1, or potyvirus VPg-interacting protein 2) and OBERON 2 (OBE2, or potyvirus VPg-interacting protein 1), which have been involved in the maintenance and/or establishment of the meristems in Arabidopsis. They interact with potyvirus VPg-interacting proteins (PVIP1 and 2) and act as central regulators in auxin-mediated control of development. Both OBE1and OBE2 contain a plant homeodomain (PHD) finger. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277084  Cd Length: 60  Bit Score: 113.48  E-value: 1.68e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79330131 228 MCTICNKFDFSVNTCRWIGCDLCSHWTHTDCAIRDGQITTGSSAKnNTSGPGEIVFKCRAC 288
Cdd:cd15612   1 MCPICSKFDFAVNTCSWIGCDVCSHWTHTDCAIRSGEISMGVSLK-GVEGSTEMEFHCRAC 60
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
392-523 4.09e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 4.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 392 RIAEVVQEtlrkmEIVAEEKMRmfKKARMALETCDRELEDKakevsELKAERQKKKLQIDELERIVRLKQAEadmFQLKA 471
Cdd:COG2268 193 KIAEIIRD-----ARIAEAEAE--RETEIAIAQANREAEEA-----ELEQEREIETARIAEAEAELAKKKAE---ERREA 257

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 79330131 472 NEAKREADRLQRIVLAKMDKSeeeyasnyLKQRLSEAEAEKQylfekIKLQE 523
Cdd:COG2268 258 ETARAEAEAAYEIAEANAERE--------VQRQLEIAERERE-----IELQE 296
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 390-530 5.11e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131    390 CNRIAEVVQETLRKMEIVAEEKMRMFKK-----------ARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVR 458
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEkigeleaeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131    459 LKQAEADMFQLKANEAKREADRLQRivlakmDKSEEEYASNYLKQRLSEAEAEKQYLFEKI--------KLQENSRVASQ 530
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRA------ELEEVDKEFAETRDELKDYREKLEKLKREInelkreldRLQEELQRLSE 420
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 228-259 3.32e-04

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 38.73  E-value: 3.32e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 79330131    228 MCTICNKFDfsvNTCRWIGCDLCSHWTHTDCA 259
Cdd:smart00249   1 YCSVCGKPD---DGGELLQCDGCDRWYHQTCL 29
PRK12704 PRK12704
phosphodiesterase; Provisional
 398-529 3.64e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131  398 QETLRKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKL-QIDELERIVRLKQAEAdmfqlkaneakR 476
Cdd:PRK12704  88 EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeQLQELERISGLTAEEA-----------K 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 79330131  477 EadrlqrIVLAKM-DKSEEEyASNYLKQRLSEAEAEKQYLFEKIKLQENSRVAS 529
Cdd:PRK12704 157 E------ILLEKVeEEARHE-AAVLIKEIEEEAKEEADKKAKEILAQAIQRCAA 203
 
Name Accession Description Interval E-value
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 416-551 9.89e-67

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 212.92  E-value: 9.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   416 KKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANEAKREADRLQRIVLAKMDKSEEE 495
Cdd:pfam16312   1 KRARLALDACDRELEDKAREASELKFERQRKKQQIEELESIVRLKQAEAEMFQLKADEARREAEGLQRIALAKSEKSEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79330131   496 YASNYLKQRLSEAEAEKQYLFEKIKLQENSRvasqssgGGGDPSQVMMYSKIRDLL 551
Cdd:pfam16312  81 YASRYLKLRLEEAEEERRYKFEELKLLENSH-------RDYDNMKMRMQSKIQDLL 129
PHD_Oberon pfam07227
PHD - plant homeodomain finger protein; PHD_oberon is a plant homeodomain finger domain of ...
 198-323 6.21e-61

PHD - plant homeodomain finger protein; PHD_oberon is a plant homeodomain finger domain of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Oberon proteins are made up of a PHD finger domain and a coiled-coil domain. The PHD-finger domain is found in a wide variety of proteins involved in the regulation of chromatin structure. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (MP) (or Auxin response factor 7).


Pssm-ID: 429357  Cd Length: 130  Bit Score: 197.57  E-value: 6.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   198 CRNIACQNQLPADDCYCDICTNRKGFCNLCMCTICNKFDFSVNTCRWIGC-------DLCSHWTHTDCAIRDGQITTGss 270
Cdd:pfam07227   1 CRNIACRSQLPVDDCDCKICSQEDGFCRRCSCCICHKFDDNKDTCSWIGCsavvsegDSCGHWCHLDCALRDYKTGTV-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 79330131   271 aKNNTSGPGEIVFKCRACNRTSELLGWVKDVFQHCAPNWDRESLMKELDFVSR 323
Cdd:pfam07227  79 -KKGGSGGLDGQFYCRACGKTSELLGHVKKVLQTCAEAWRRDVLCKELDLGRR 130
PHD_OBE1_like cd15612
PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins ...
 228-288 1.68e-30

PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins mainly found in plants; Included in this family are OBERON 1 (OBE1, or potyvirus VPg-interacting protein 2) and OBERON 2 (OBE2, or potyvirus VPg-interacting protein 1), which have been involved in the maintenance and/or establishment of the meristems in Arabidopsis. They interact with potyvirus VPg-interacting proteins (PVIP1 and 2) and act as central regulators in auxin-mediated control of development. Both OBE1and OBE2 contain a plant homeodomain (PHD) finger. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277084  Cd Length: 60  Bit Score: 113.48  E-value: 1.68e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79330131 228 MCTICNKFDFSVNTCRWIGCDLCSHWTHTDCAIRDGQITTGSSAKnNTSGPGEIVFKCRAC 288
Cdd:cd15612   1 MCPICSKFDFAVNTCSWIGCDVCSHWTHTDCAIRSGEISMGVSLK-GVEGSTEMEFHCRAC 60
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 228-288 5.74e-12

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 60.64  E-value: 5.74e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79330131 228 MCTICNKFDFSvNTCRWIGCDLCSHWTHTDCAIRDGQITTgssaknntsgpGEIVFKCRAC 288
Cdd:cd15517   1 VCGICNLETAA-VDELWVQCDGCDKWFHQFCLGLSNERYA-----------DEDKFKCPNC 49
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
392-523 4.09e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 4.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 392 RIAEVVQEtlrkmEIVAEEKMRmfKKARMALETCDRELEDKakevsELKAERQKKKLQIDELERIVRLKQAEadmFQLKA 471
Cdd:COG2268 193 KIAEIIRD-----ARIAEAEAE--RETEIAIAQANREAEEA-----ELEQEREIETARIAEAEAELAKKKAE---ERREA 257

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 79330131 472 NEAKREADRLQRIVLAKMDKSeeeyasnyLKQRLSEAEAEKQylfekIKLQE 523
Cdd:COG2268 258 ETARAEAEAAYEIAEANAERE--------VQRQLEIAERERE-----IELQE 296
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 390-530 5.11e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131    390 CNRIAEVVQETLRKMEIVAEEKMRMFKK-----------ARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVR 458
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEkigeleaeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131    459 LKQAEADMFQLKANEAKREADRLQRivlakmDKSEEEYASNYLKQRLSEAEAEKQYLFEKI--------KLQENSRVASQ 530
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRA------ELEEVDKEFAETRDELKDYREKLEKLKREInelkreldRLQEELQRLSE 420
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
 229-288 6.63e-05

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins; This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277087  Cd Length: 57  Bit Score: 40.93  E-value: 6.63e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79330131 229 CTICNK--FDFSVNTCRWIGCDLCSHWTHTDCAIRDGQiTTGSSAKNNTsgpgeIVFKCRAC 288
Cdd:cd15615   2 CILCGQvyEENEGDEKEWVQCDSCSEWVHFECDGRTGL-GAFKYAKSDG-----LQYVCPRC 57
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 378-523 7.45e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 7.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131    378 GEGGRLMAPQDACNRIAEVVQETLRKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELE--- 454
Cdd:TIGR02169  301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkef 380

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79330131    455 RIVRLKQAEA----DMFQLKANEAKREADRLQ-RIVLAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQE 523
Cdd:TIGR02169  381 AETRDELKDYreklEKLKREINELKRELDRLQeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 228-259 3.32e-04

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 38.73  E-value: 3.32e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 79330131    228 MCTICNKFDfsvNTCRWIGCDLCSHWTHTDCA 259
Cdd:smart00249   1 YCSVCGKPD---DGGELLQCDGCDRWYHQTCL 29
PRK12704 PRK12704
phosphodiesterase; Provisional
 398-529 3.64e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131  398 QETLRKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKL-QIDELERIVRLKQAEAdmfqlkaneakR 476
Cdd:PRK12704  88 EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeQLQELERISGLTAEEA-----------K 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 79330131  477 EadrlqrIVLAKM-DKSEEEyASNYLKQRLSEAEAEKQYLFEKIKLQENSRVAS 529
Cdd:PRK12704 157 E------ILLEKVeEEARHE-AAVLIKEIEEEAKEEADKKAKEILAQAIQRCAA 203
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
399-529 6.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 399 ETLRKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADM--FQLKANEAKR 476
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELaeLPERLEELEE 153

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 79330131 477 EADRLQRIvlakmdksEEEYASnyLKQRLSEAEAEKQYLFEKIKLQENSRVAS 529
Cdd:COG4717 154 RLEELREL--------EEELEE--LEAELAELQEELEELLEQLSLATEEELQD 196
PTZ00121 PTZ00121
MAEBL; Provisional
 388-531 6.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   388 DACNRIAEVVQETLRKMEIVAEEKMRMFKKARMALETCDRELE--DKAKEVSELKAERQKKKlqIDELERIVRLKQaEAD 465
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKK--ADAAKKKAEEKK-KAD 1394

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79330131   466 MFQLKANEAKREADRLQRIVLAK------MDKSEEEYASNYLKQRLSE---AEAEKQYLFEKIKLQENSRVASQS 531
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKkkadeaKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEA 1469
RNase_Y_N pfam12072
RNase Y N-terminal region;
399-487 1.00e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   399 ETL-RKMEIVaEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKkklqidELERIVRLKQAEADMFQLKA------ 471
Cdd:pfam12072  92 ETLdRKDESL-EKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQ------ELERISGLTSEEAKEILLDEveeelr 164

                          90       100
                  ....*....|....*....|....*..
gi 79330131   472 -----------NEAKREADRLQRIVLA 487
Cdd:pfam12072 165 heaavmikeieEEAKEEADKKAKEIIA 191
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
387-509 1.43e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 387 QDACNRIAEVvQETLRKMEIVAEEKMRMFKKARMA--LETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEA 464
Cdd:COG4717 398 QELKEELEEL-EEQLEELLGELEELLEALDEEELEeeLEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 79330131 465 DmFQLKANEAKREADRLQRIVLAK--MDKSEEEYASNYLKQRLSEAE 509
Cdd:COG4717 477 E-LEELKAELRELAEEWAALKLALelLEEAREEYREERLPPVLERAS 522
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 386-541 1.63e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 386 PQDACNRIAEVVQETLRKMEIVAEekmrmFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELerivrLKQAEAD 465
Cdd:COG3883 114 FSDFLDRLSALSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ-----QAEQEAL 183

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79330131 466 MFQLKANEAKREADRLQrivLAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQENSRVASQSSGGGGDPSQV 541
Cdd:COG3883 184 LAQLSAEEAAAEAQLAE---LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
393-510 1.67e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 393 IAEVVQETLRKMEIVAEEKM-RMFKKARMALETCDRELEDKAK-------EVSELKAERQKKKLQIDELERIVRLKQAEA 464
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAeREKEHEERELTEEEEEIRRLEEqverleaEVEELEAELEEKDERIERLERELSEARSEE 457

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 79330131 465 DMFQLKANEA---KREADRLQRiVLAKMDKSEEEyasnyLKQRLSEAEA 510
Cdd:COG2433 458 RREIRKDREIsrlDREIERLER-ELEEERERIEE-----LKRKLERLKE 500
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 422-524 1.74e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131  422 LETCDRELEDKAKEVSELK--AERQKKKL--QIDEL-ERIVRLKQAEADMFQLKANEAKREADRlqriVLAKMDKSEEEY 496
Cdd:PRK00409 525 LEELERELEQKAEEAEALLkeAEKLKEELeeKKEKLqEEEDKLLEEAEKEAQQAIKEAKKEADE----IIKELRQLQKGG 600

                         90       100
                 ....*....|....*....|....*...
gi 79330131  497 ASNylkQRLSEAEAEKQYLFEKIKLQEN 524
Cdd:PRK00409 601 YAS---VKAHELIEARKRLNKANEKKEK 625
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
393-523 1.92e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 393 IAEVVQETLRKMEIVAEEkmrmFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKAN 472
Cdd:COG4372  29 LSEQLRKALFELDKLQEE----LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 79330131 473 EAKREADRLQrivlAKMDKSEEEYASnyLKQRLSEAEAEKQYLFEKIKLQE 523
Cdd:COG4372 105 SLQEEAEELQ----EELEELQKERQD--LEQQRKQLEAQIAELQSEIAERE 149
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
 228-259 1.96e-03

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 36.50  E-value: 1.96e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 79330131 228 MCTICNKFDFSVNtcrWIGCDLCSHWTHTDCA 259
Cdd:cd15522   1 ICPICKKPDDGSP---MIGCDECDDWYHWECV 29
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 417-519 3.40e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 3.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 417 KARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERivRLKQAEADMFQLKANEAKREaDRLQRIvlakmdKSEEEY 496
Cdd:COG1579  21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK--EIKRLELEIEEVEARIKKYE-EQLGNV------RNNKEY 91

                        90       100
                ....*....|....*....|....*...
gi 79330131 497 AS-----NYLKQRLSEAEAEKQYLFEKI 519
Cdd:COG1579  92 EAlqkeiESLKRRISDLEDEILELMERI 119
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 385-513 4.03e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.83  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   385 APQDACNRIAEVVQETLRKMEIVAEEKMRMFKKARmaletcdRELEDKAKEVSELKA----ERQKKKLQIDELERIVRL- 459
Cdd:TIGR02794  77 AEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAA-------KQAEEKQKQAEEAKAkqaaEAKAKAEAEAERKAKEEAa 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79330131   460 KQAEADMFQLKANEAKREADRLQRivlakmdKSEEEyasnylkqRLSEAEAEKQ 513
Cdd:TIGR02794 150 KQAEEEAKAKAAAEAKKKAEEAKK-------KAEAE--------AKAKAEAEAK 188
PTZ00121 PTZ00121
MAEBL; Provisional
 398-530 4.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   398 QETLRKMEIV--AEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKlqiDELERIVRLKQaEADMFQLKANEAK 475
Cdd:PTZ00121 1421 DEAKKKAEEKkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAK-KADEAKKKAEEAK 1496

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   476 READRLQRIVLAK-----MDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQENSRVASQ 530
Cdd:PTZ00121 1497 KKADEAKKAAEAKkkadeAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
PTZ00121 PTZ00121
MAEBL; Provisional
 392-530 4.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   392 RIAEVVQ--ETLRKMEIV--AEEKMRMFKKARMAletcdRELEDKAKEVSElKAERQKKKLQIDELERIVRLKQAEADMF 467
Cdd:PTZ00121 1284 KKAEEKKkaDEAKKAEEKkkADEAKKKAEEAKKA-----DEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAAD 1357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79330131   468 QLKANEAKREADRLQrivlakmdKSEEEYASNYLKQRLSEA----EAEKQYLFEKIKLQENSRVASQ 530
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKK--------KEEAKKKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAA 1416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-524 4.48e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 398 QETLRKMEIVAEEKMRMFKKARMALETcdRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANEAKRE 477
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 79330131 478 ADRLQRIVLAKMDKSEEEYASnyLKQRLSEAEAEKQYLFEKIKLQEN 524
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEA 411
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 427-522 5.72e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 39.67  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   427 RELEDKAKEVSELKAERQKKKLQIDELERIVrLKQAEADMFQLKANEAKREADRLQ------------RIVLAKMDKSEE 494
Cdd:pfam05622 363 QKLEEHLEKLHEAQSELQKKKEQIEELEPKQ-DSNLAQKIDELQEALRKKDEDMKAmeerykkyvekaKSVIKTLDPKQN 441

                          90       100       110
                  ....*....|....*....|....*....|....
gi 79330131   495 EYASN---YLKQRLSEAEAEKQYL---FEKIKLQ 522
Cdd:pfam05622 442 PASPPeiqALKNQLLEKDKKIEHLerdFEKSKLQ 475
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 410-513 6.30e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131  410 EKMRMFKKARMALETCDRELED--KAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANE-AKREADRLQRIVL 486
Cdd:PRK09510  78 EEQRKKKEQQQAEELQQKQAAEqeRLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAaAKAKAEAEAKRAA 157

                         90       100
                 ....*....|....*....|....*..
gi 79330131  487 AKMDKSEEEyasnylKQRLSEAEAEKQ 513
Cdd:PRK09510 158 AAAKKAAAE------AKKKAEAEAAKK 178
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 394-530 6.31e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 394 AEVVQETLRKMEIVAEEKMRMFKKARMALEtcDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANE 473
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79330131 474 AKREADRLQRIVLAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQENSRVASQ 530
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
418-519 6.40e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131  418 ARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIV------RLKQAEADMFQL--KANEAKREADRLQRIVLA-- 487
Cdd:COG4913  293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdRLEQLEREIERLerELEERERRRARLEALLAAlg 372

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 79330131  488 -KMDKSEEEYASNY--LKQRLSEAEAEKQYLFEKI 519
Cdd:COG4913  373 lPLPASAEEFAALRaeAAALLEALEEELEALEEAL 407
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 392-477 7.34e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.82  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   392 RIAEVVQETLRKMEivaEEKMRMFKKARMALETCDR---ELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQ 468
Cdd:pfam20492  34 ETAEELEEERRQAE---EEAERLEQKRQEAEEEKERleeSAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110


                  ....*....
gi 79330131   469 LKANEAKRE 477
Cdd:pfam20492 111 EELEEAREE 119
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 394-532 7.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 394 AEVVQETLRKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANE 473
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 474 AKREADRL-QRIVLAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQENSRVASQSS 532
Cdd:COG1196 321 LEEELAELeEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
PTZ00121 PTZ00121
MAEBL; Provisional
 329-530 8.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   329 EDQRGRKLFWKCEELIDKIKGGLAEATAAKLILMFFQEI----ESDSAKSFENGEGGRlMAPQDACNRIAEVVQETLRKM 404
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDArkaeEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAE 1167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   405 EIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKL-QIDELERIVRLKQAEADMFQLKANEAKREADRLQR 483
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE 1247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 79330131   484 IVLAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQENSRVASQ 530
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 402-532 8.03e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.83  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131   402 RKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELERIVRLKQAEADMFQLKANEAKREADRL 481
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79330131   482 QRIV----------LAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIK--LQENSRVASQSS 532
Cdd:pfam05262 261 PKPAdtsspkedkqVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKqeSKASEKEAEDKE 323
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
459-512 8.49e-03

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 38.57  E-value: 8.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 79330131  459 LKQAEADM--FQLKANEAKREADRLQRIVLAKMDKSEEEYASNYLK---QRLSEAEAEK 512
Cdd:PRK10559  87 LAEAEADVayYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQtvlHQLAKAQATR 145
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 228-288 9.49e-03

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 34.60  E-value: 9.49e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79330131 228 MCTICNKFDFSVNtcRWIGCDLCSHWTHTDCAIRDGqittgssaknnTSGPGEIVFKCRAC 288
Cdd:cd15489   1 SCIVCGKGGDLGG--ELLQCDGCGKWFHADCLGPPL-----------SSFVPNGKWICPVC 48
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-530 9.75e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330131 395 EVVQETLRKMEIVAEEKMRMFKKARMALETCDRELEDKAKEVSELKAERQKKKLQIDELE-RIVRLKQAEADMFQLKANE 473
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeALLEAEAELAEAEEELEEL 384

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79330131 474 AKREADRLQRIVLAKMDKSEEEYASNYLKQRLSEAEAEKQYLFEKIKLQENSRVASQ 530
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
 
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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