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Conserved domains on  [gi|109240552|ref|NP_001035882|]
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RUN and FYVE domain-containing protein 2 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN super family cl45896
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
10-131 8.80e-83

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


The actual alignment was detected with superfamily member cd17695:

Pssm-ID: 459241  Cd Length: 156  Bit Score: 250.28  E-value: 8.80e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109240552  90 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17695   81 ASVRDLPGlktplgrarawlrlalmqkkladylrcliirrdlLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
150-380 8.81e-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: 51.09  E-value: 8.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 150 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 226
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 227 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 306
Cdd:COG1196  331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109240552 307 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 380
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
 
Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
10-131 8.80e-83

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 250.28  E-value: 8.80e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109240552  90 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17695   81 ASVRDLPGlktplgrarawlrlalmqkkladylrcliirrdlLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
45-134 2.03e-20

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 86.56  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   45 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLP------------------GLNE 100
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEqihtpyspdgrgrawirlALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 109240552  101 -------------------FYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 134
Cdd:pfam02759  81 klldqwlklllsnkellseYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
150-380 8.81e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 8.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 150 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 226
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 227 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 306
Cdd:COG1196  331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109240552 307 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 380
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
RUN smart00593
domain involved in Ras-like GTPase signaling;
92-133 7.35e-06

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 43.37  E-value: 7.35e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 109240552    92 VRDLPGLNEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 133
Cdd:smart00593  22 LSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
192-370 6.26e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  192 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNE 266
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  267 ARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 344
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562
                         170       180
                  ....*....|....*....|....*...
gi 109240552  345 NEiIARLE--EKTNKItaaMRQLEQSDN 370
Cdd:pfam17380 563 EE-RSRLEamEREREM---MRQIVESEK 586
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-372 3.33e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   152 NEEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS----- 226
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErlesl 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   227 ENKLILMKTQ-QHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkHEIELAMKLLEKD 305
Cdd:TIGR02168  830 ERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------ALLRSELEELSEE 902
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109240552   306 IHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARL--------EEKTNKITAAMRQLEQSDNDL 372
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRL 977
PRK11281 PRK11281
mechanosensitive channel MscK;
278-375 6.94e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  278 RQDVENELAVQVSMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 357
Cdd:PRK11281   38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
                          90       100
                  ....*....|....*....|....
gi 109240552  358 ITAA------MRQLEQSDNDLLTQ 375
Cdd:PRK11281  113 ETREtlstlsLRQLESRLAQTLDQ 136
 
Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
10-131 8.80e-83

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 250.28  E-value: 8.80e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109240552  90 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17695   81 ASVRDLPGlktplgrarawlrlalmqkkladylrcliirrdlLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
10-130 1.14e-62

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 198.56  E-value: 1.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17681    1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109240552  90 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 130
Cdd:cd17681   81 ASVRDLPGiktplgrarawlrlalmqkkladyfralienkdlLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
10-131 2.31e-62

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439056  Cd Length: 156  Bit Score: 197.82  E-value: 2.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109240552  90 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17694   81 TSARNLPElktavgrgrawlhlalmqkkladylkvlidrkdlLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
10-131 1.37e-58

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 188.28  E-value: 1.37e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109240552  90 ASVRDLPGL----------------------------------NEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17696   81 ASVKDLPGLktpvgrgrawlrlalmqkklseymkalinrkdllSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
45-134 2.03e-20

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 86.56  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   45 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLP------------------GLNE 100
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEqihtpyspdgrgrawirlALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 109240552  101 -------------------FYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 134
Cdd:pfam02759  81 klldqwlklllsnkellseYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
13-130 1.28e-10

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 59.33  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  13 NLLNMAKLSIKGLIESALSfgRTLDSDYPPLQQFFVVMEHCLKHGLK---------VRKSFLSYNKT------------- 70
Cdd:cd17684    1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKpvkpwygseEPRTFWDYIRVackkvpqnciasi 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109240552  71 --------------IWGPLELVEKLYpeAEEIGASVRDLPGLNEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 130
Cdd:cd17684   79 eqmenikspkakgrAWIRVALMEKRL--SEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
13-131 9.54e-10

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 56.90  E-value: 9.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  13 NLLNMAKLSIKGLIESalSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYN--KTIWGPLELVEKLYPE------ 84
Cdd:cd17700    1 NLITVCRFSVKTLIDR--SCFETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHncicsi 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109240552  85 --------------------------AEEIGASVRDLPGLNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17700   79 enmenvsssrakgrawirvalmekrlSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
21-130 1.36e-08

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 53.58  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  21 SIKGLIESAL-------SFGRTLDSDYPPLQQFFVVMEHCLKHGLKvRKSFLSYNKTIWGPLELVEKLYPeAEEIGASVR 93
Cdd:cd17671    2 AVKELLESFAdngeaddSAALTLTDDDPVVGRLCAALEAILSHGLK-PKRFGGGKVSFWDFLEALEKLLP-APSLKQAIR 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109240552  94 DLP------------------GLNE-------------------FYEYHALMM-EEEGAVIVGLLVGLNVIDANL 130
Cdd:cd17671   80 DINslsnvktddgrgrawirlALNEkslesylaallsdqsllrkYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
13-131 2.41e-07

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.


Pssm-ID: 439061  Cd Length: 151  Bit Score: 50.02  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  13 NLLNMAKLSIKGLIESALSfgRTLDSDYPPLQQFFVVMEHCLKHGLKV---------RKSFLSY---------NKTI--- 71
Cdd:cd17699    1 NLITVCRFSVKTLLEKYTA--EPIDDSSEEFVNFAAILEQILSHRFKGpvswfssdgQRGFWDYirlacskvpNNCIssi 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109240552  72 ---------------WGPLELVEKLYpeAEEIGASVRDLPGLNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 131
Cdd:cd17699   79 enmenistsrakgraWIRVALMEKRL--SEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
150-380 8.81e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 8.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 150 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 226
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 227 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 306
Cdd:COG1196  331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109240552 307 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 380
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
159-361 4.19e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 159 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQH 238
Cdd:COG4942   37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 239 LEVTKV----------DVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHE 308
Cdd:COG4942  117 GRQPPLalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109240552 309 KQDTLIGLRQQLEEVKAinieMYQKLQGSEDGLKEKNEIIARLEEKTNKITAA 361
Cdd:COG4942  197 RQKLLARLEKELAELAA----ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
150-380 5.96e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 150 LKNEEDIgnKERNVQIAAILDQKNYVEELNRQLN---STVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 226
Cdd:COG1196  218 LKEELKE--LEAELLLLKLRELEAELEELEAELEeleAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 227 EnKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 306
Cdd:COG1196  296 E-LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109240552 307 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 380
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
RUN smart00593
domain involved in Ras-like GTPase signaling;
92-133 7.35e-06

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 43.37  E-value: 7.35e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 109240552    92 VRDLPGLNEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 133
Cdd:smart00593  22 LSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-367 2.36e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 164 QIAAILDQ--KNYVEElnrqlnstvsSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEV 241
Cdd:COG3206  149 LAAAVANAlaEAYLEQ----------NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 242 TK-VDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKL--LEKDIHEKQDTLIGLRQ 318
Cdd:COG3206  219 QQlSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDVIALRA 298
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 109240552 319 QLEEVKA--------INIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQ 367
Cdd:COG3206  299 QIAALRAqlqqeaqrILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
159-372 3.51e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 159 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKlilmKTQQH 238
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 239 LEVTKVDVETELQT-YKHSRQGLDEMYnearrqlrdesqLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLR 317
Cdd:COG4942   99 LEAQKEELAELLRAlYRLGRQPPLALL------------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109240552 318 QQLEEVKAINIEMYQKLQGSEDGL----KEKNEIIARLEEKTNKITAAMRQLEQSDNDL 372
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALealkAERQKLLARLEKELAELAAELAELQQEAEEL 225
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
192-370 6.26e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  192 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNE 266
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  267 ARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 344
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562
                         170       180
                  ....*....|....*....|....*...
gi 109240552  345 NEiIARLE--EKTNKItaaMRQLEQSDN 370
Cdd:pfam17380 563 EE-RSRLEamEREREM---MRQIVESEK 586
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-372 3.33e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   152 NEEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS----- 226
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErlesl 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   227 ENKLILMKTQ-QHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkHEIELAMKLLEKD 305
Cdd:TIGR02168  830 ERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------ALLRSELEELSEE 902
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109240552   306 IHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARL--------EEKTNKITAAMRQLEQSDNDL 372
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRL 977
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
164-373 3.54e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 164 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEVTK 243
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552 244 VDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkhEIELAMKLLEKDIHEKQDTLIGLRQQLEEV 323
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE--------RLEEELEELEEALAELEEEEEEEEEALEEA 447
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109240552 324 KAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLL 373
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-372 4.70e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   188 SLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEN------KLILMKTQQHLEVTKVDVETELQTYKHSRQGLD 261
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   262 EMYNEARRQLRDESQLRQDVENELAvqvSMKHEIELAMKLLEkdihekqdtliGLRQQLEEVKAINIEMYQKLQGSEDGL 341
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELE-----------SLEAELEELEAELEELESRLEELEEQL 381
                          170       180       190
                   ....*....|....*....|....*....|.
gi 109240552   342 KEKNEIIARLEEKTNKITAAMRQLEQSDNDL 372
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERL 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
159-380 4.83e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 4.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   159 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS---ENKLILMKT 235
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   236 QQHLEVTKVDVE-------TELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVE---NELAVQVSMKHEIE--------- 296
Cdd:TIGR02168  343 EEKLEELKEELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnNEIERLEARLERLEdrrerlqqe 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   297 ---LAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLL 373
Cdd:TIGR02168  423 ieeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502

                   ....*..
gi 109240552   374 TQTRTIA 380
Cdd:TIGR02168  503 GFSEGVK 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
164-375 1.35e-03

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: 41.21  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   164 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnkliLMKTQQHLEVTK 243
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARLSHSR 792
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   244 VD-VETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEE 322
Cdd:TIGR02169  793 IPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 109240552   323 VKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQ 375
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
135-343 3.97e-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: 39.65  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   135 EDLDSQVGVIDFSMylkNEEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNI 214
Cdd:TIGR02168  298 SRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552   215 IKLQEENHQLRSENKLI------LMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEArrQLRDESQLRQDVENELAVQ 288
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLelqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEEL 452
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 109240552   289 VSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAiNIEMYQKLQGSEDGLKE 343
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLERLQENLEGFSE 506
PRK11281 PRK11281
mechanosensitive channel MscK;
278-375 6.94e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109240552  278 RQDVENELAVQVSMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 357
Cdd:PRK11281   38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
                          90       100
                  ....*....|....*....|....
gi 109240552  358 ITAA------MRQLEQSDNDLLTQ 375
Cdd:PRK11281  113 ETREtlstlsLRQLESRLAQTLDQ 136
 
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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