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Conserved domains on  [gi|1622861379|ref|XP_028688803|]
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ras association domain-containing protein 7 isoform X3 [Macaca mulatta]

Protein Classification

ubiquitin family protein( domain architecture ID 1000087)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 8-90 5.72e-51

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd16135:

Pssm-ID: 475130  Cd Length: 83  Bit Score: 163.58  E-value: 5.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPEECPVGAQATCGQFASDVQFVLRRT 87
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 1622861379  88 GPS 90
Cdd:cd16135    81 GPS 83
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-289 2.61e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgppspMASATERLRQDLAVQERQSAEV 255
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAEL 374

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622861379 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK13831 super family cl30572
conjugal transfer protein TrbI; Provisional
 123-199 8.05e-03

conjugal transfer protein TrbI; Provisional


The actual alignment was detected with superfamily member PRK13831:

Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 37.79  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 123 EPRKTLTPGPAPSLSHPGPAASVTPTPGcctdlrglelRVQRNAEELGHEAFWEQELRREQA----REREGQ--ARLQAL 196
Cdd:PRK13831   86 QQQQTFQPTPVETQQEEKAVNPFTPQPG----------QREERRPTLESEEEWRARLKREQEeqylRERQRQrmARLQAN 155


                  ...
gi 1622861379 197 SAA 199
Cdd:PRK13831  156 AAA 158
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 5.72e-51

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 163.58  E-value: 5.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPEECPVGAQATCGQFASDVQFVLRRT 87
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 1622861379  88 GPS 90
Cdd:cd16135    81 GPS 83
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-88 1.53e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 68.09  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379    8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPEECPVGAQATCGQFASDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 1622861379   81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-86 2.16e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 67.74  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   8 MELKVWVD----GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLV--QRLREKERQLLPEECPVGAQATCGQFAS 78
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVevLERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 1622861379  79 DVQFVLRR 86
Cdd:pfam00788  83 DSRFLLRK 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-289 2.61e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgppspMASATERLRQDLAVQERQSAEV 255
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAEL 374

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622861379 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK09039 PRK09039
peptidoglycan -binding protein;
153-287 2.51e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 153 TDLRGLElrvQRNAEELgheafwEQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAEL----QLAAEAp 228
Cdd:PRK09039   66 ADLLSLE---RQGNQDL------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELdsekQVSARA- 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622861379 229 gppspmASATERLRQDLAVQERQSAEVQGslalvsrALEAAERALQAQAQELEELNREL 287
Cdd:PRK09039  136 ------LAQVELLNQQIAALRRQLAALEA-------ALDASEKRDRESQAKIADLGRRL 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-289 3.98e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  159 ELRVQRNAEELGHEAFWEQELRREQaREREGQARLQALSAATAE-------HAARLQALDAQACALEAELQ-LAAEAPG- 229
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKVAQlelqiasLNNEIERLEARLERLEDRRErLQQEIEEl 426

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  230 PPSPMASATERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:TIGR02168  427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
PRK13831 PRK13831
conjugal transfer protein TrbI; Provisional
 123-199 8.05e-03

conjugal transfer protein TrbI; Provisional


Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 37.79  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 123 EPRKTLTPGPAPSLSHPGPAASVTPTPGcctdlrglelRVQRNAEELGHEAFWEQELRREQA----REREGQ--ARLQAL 196
Cdd:PRK13831   86 QQQQTFQPTPVETQQEEKAVNPFTPQPG----------QREERRPTLESEEEWRARLKREQEeqylRERQRQrmARLQAN 155


                  ...
gi 1622861379 197 SAA 199
Cdd:PRK13831  156 AAA 158
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 5.72e-51

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 163.58  E-value: 5.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPEECPVGAQATCGQFASDVQFVLRRT 87
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 1622861379  88 GPS 90
Cdd:cd16135    81 GPS 83
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 9-90 4.85e-41

Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.


Pssm-ID: 340551  Cd Length: 82  Bit Score: 137.95  E-value: 4.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPEECPVGAQATCGQFASDVQFVLRRTG 88
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 1622861379  89 PS 90
Cdd:cd16134    81 PS 82
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 9-86 1.42e-35

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 123.51  E-value: 1.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQ---TGRFVLVQRLREKERQLLPEECPVGAQATCGQFASDVQFVLR 85
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                  .
gi 1622861379  86 R 86
Cdd:cd16123    81 R 81
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-88 1.53e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 68.09  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379    8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPEECPVGAQATCGQFASDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 1622861379   81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-86 2.16e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 67.74  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   8 MELKVWVD----GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLV--QRLREKERQLLPEECPVGAQATCGQFAS 78
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVevLERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 1622861379  79 DVQFVLRR 86
Cdd:pfam00788  83 DSRFLLRK 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 10-86 2.56e-09

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 53.48  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  10 LKVWVDGIQ-----RVVCgVSEQTTCQEVVIALAQAIG---QTGRFVLVQRL--REKERQLLPEECPVGAQATCGQFASD 79
Cdd:cd17043     2 LKVYDDDLApgsayKSIL-VSSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 1622861379  80 VQFVLRR 86
Cdd:cd17043    81 FRFVLKR 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-289 2.61e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgppspMASATERLRQDLAVQERQSAEV 255
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAEL 374

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622861379 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-289 1.45e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 153 TDLRGLELRVQRNAEELGHEafwEQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgpps 232
Cdd:COG1196   260 AELAELEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE----- 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 233 pMASATERL---RQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196   332 -LEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 9-84 4.36e-06

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 44.45  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQA-----------IGQTGRFVLVQRLREKERQLLPEECPVGAQATCGQFA 77
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                  ....*..
gi 1622861379  78 SDVQFVL 84
Cdd:cd16133    81 PNLQFVL 87
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-289 1.08e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  158 LELRVQRNAEELgheAFWEQELRREQAREREGQARLQALSAATAEH-AARLQALDAQACALEAEL-----------QLAA 225
Cdd:COG4913    293 LEAELEELRAEL---ARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeererrrarleALLA 369

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622861379  226 EAPGPPSPMASATERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-289 1.26e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 155 LRGLELRVQRNAEELGHEafwEQELRREQAREREGQARLQALSAATAEHAARLQAldaqacALEAELQLAAEApgppspm 234
Cdd:COG1196   234 LRELEAELEELEAELEEL---EAELEELEAELAELEAELEELRLELEELELELEE------AQAEEYELLAEL------- 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622861379 235 asatERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196   298 ----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-289 1.69e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 158 LELRVQRNAEELGHEAFWEQELR--REQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgppspma 235
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEalRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE-------- 439

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622861379 236 sATERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196   440 -EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
PRK09039 PRK09039
peptidoglycan -binding protein;
153-287 2.51e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 153 TDLRGLElrvQRNAEELgheafwEQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAEL----QLAAEAp 228
Cdd:PRK09039   66 ADLLSLE---RQGNQDL------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELdsekQVSARA- 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622861379 229 gppspmASATERLRQDLAVQERQSAEVQGslalvsrALEAAERALQAQAQELEELNREL 287
Cdd:PRK09039  136 ------LAQVELLNQQIAALRRQLAALEA-------ALDASEKRDRESQAKIADLGRRL 181
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-289 3.46e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  152 CTDLRGLELRVQRNAEELGHEAFWEQELRREQARERegQARLQALSAATAEHAARLQALDAQACALEAELQLA-AEAPGp 230
Cdd:COG4913    261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARLDALREELDELEAQiRGNGG- 337

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622861379  231 pspmaSATERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4913    338 -----DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
173-290 3.68e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  173 AFWEQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgppSPMASATERLRQ------DLA 246
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE----REIAELEAELERldassdDLA 688

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622861379  247 VQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQC 290
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
176-289 4.21e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 176 EQELRREQAREREGQARLQALSAATAEHA---------ARLQALDAQACALEAELQLAAEAPGPPSPMASATERLRQDLa 246
Cdd:COG3206   225 ESQLAEARAELAEAEARLAALRAQLGSGPdalpellqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL- 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622861379 247 vQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG3206   304 -RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 162-277 9.68e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 9.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 162 VQRNAEELGHEAFWEQELRREQARER----------EGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEApgpp 231
Cdd:PRK09510   85 EQQQAEELQQKQAAEQERLKQLEKERlaaqeqkkqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA---- 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622861379 232 sPMASATERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQA 277
Cdd:PRK09510  161 -KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
179-294 2.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  179 LRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEapgppspmasaterlRQDLAVQERQSAEVQGS 258
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD---------------EIDVASAEREIAELEAE 676

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622861379  259 LALVSRA---LEAAERALQAQAQELEELNRELRQCNLQQ 294
Cdd:COG4913    677 LERLDASsddLAALEEQLEELEAELEELEEELDELKGEI 715
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-289 3.98e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  159 ELRVQRNAEELGHEAFWEQELRREQaREREGQARLQALSAATAE-------HAARLQALDAQACALEAELQ-LAAEAPG- 229
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKVAQlelqiasLNNEIERLEARLERLEDRRErLQQEIEEl 426

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  230 PPSPMASATERLRQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:TIGR02168  427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
177-303 5.79e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379  177 QELRREQAREREGQARLQALSAATAEHaaRLQALDAQACALEAELQLAAEapgppspmasATERLRQDLAVQERQSAEVQ 256
Cdd:COG4913    262 ERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEA----------ELERLEARLDALREELDELE 329

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622861379  257 GSLALVS-RALEAAERALQAQAQELEELNRELRQcnLQQFIQQTGAAL 303
Cdd:COG4913    330 AQIRGNGgDRLEQLEREIERLERELEERERRRAR--LEALLAALGLPL 375
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-303 7.15e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 176 EQELRREQAREREGQARLQALsaatAEHAARLQALDAQACALEAELQLAaeapgppspMASATERLRQDLAVQERQSAEV 255
Cdd:COG4717   138 EAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEEL---------LEQLSLATEEELQDLAEELEEL 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622861379 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQCNLQQFIQQTGAAL 303
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
PRK13831 PRK13831
conjugal transfer protein TrbI; Provisional
 123-199 8.05e-03

conjugal transfer protein TrbI; Provisional


Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 37.79  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 123 EPRKTLTPGPAPSLSHPGPAASVTPTPGcctdlrglelRVQRNAEELGHEAFWEQELRREQA----REREGQ--ARLQAL 196
Cdd:PRK13831   86 QQQQTFQPTPVETQQEEKAVNPFTPQPG----------QREERRPTLESEEEWRARLKREQEeqylRERQRQrmARLQAN 155


                  ...
gi 1622861379 197 SAA 199
Cdd:PRK13831  156 AAA 158
PRK12705 PRK12705
hypothetical protein; Provisional
 176-289 8.84e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 37.77  E-value: 8.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861379 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQACALEAELQLAAEapgppspmasatERLRQdlavQERQSAEV 255
Cdd:PRK12705   33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREE------------ERLVQ----KEEQLDAR 96

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622861379 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:PRK12705   97 AEKLDNLENQLEEREKALSARELELEELEKQLDN 130
 
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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