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Conserved domains on  [gi|2462519995|ref|XP_054222236|]
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RUN and FYVE domain-containing protein 2 isoform X12 [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 ...
45-166 1.35e-82

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: 250.67  E-value: 1.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  45 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 124
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462519995 125 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17695    81 ASVRDLPGlktplgrarawlrlalmqkkladylrcliirrdlLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
185-415 9.08e-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: 51.48  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 185 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 261
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 262 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 341
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 342 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 415
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; ...
45-166 1.35e-82

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: 250.67  E-value: 1.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  45 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 124
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462519995 125 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17695    81 ASVRDLPGlktplgrarawlrlalmqkkladylrcliirrdlLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
80-169 2.25e-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: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  80 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLP------------------GLNE 135
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEqihtpyspdgrgrawirlALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 136 -------------------FYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 169
Cdd:pfam02759  81 klldqwlklllsnkellseYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
185-415 9.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 185 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 261
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 262 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 341
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 342 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 415
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
RUN smart00593
domain involved in Ras-like GTPase signaling;
127-168 6.79e-06

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 43.37  E-value: 6.79e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462519995  127 VRDLPGLNEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 168
Cdd:smart00593  22 LSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
227-405 5.89e-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: 45.50  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 227 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNE 301
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 302 ARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 379
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562
                         170       180
                  ....*....|....*....|....*...
gi 2462519995 380 NEiIARLE--EKTNKItaaMRQLEQSDN 405
Cdd:pfam17380 563 EE-RSRLEamEREREM---MRQIVESEK 586
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
187-407 2.07e-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: 43.89  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  187 NEEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS----- 261
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErlesl 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  262 ENKLILMKTQ-QHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkHEIELAMKLLEKD 340
Cdd:TIGR02168  830 ERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------ALLRSELEELSEE 902
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519995  341 IHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARL--------EEKTNKITAAMRQLEQSDNDL 407
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRL 977
PRK11281 PRK11281
mechanosensitive channel MscK;
313-410 7.47e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  313 RQDVENELAVQVSMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 392
Cdd:PRK11281    38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
                           90       100
                   ....*....|....*....|....
gi 2462519995  393 ITAA------MRQLEQSDNDLLTQ 410
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; ...
45-166 1.35e-82

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: 250.67  E-value: 1.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  45 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 124
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462519995 125 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17695    81 ASVRDLPGlktplgrarawlrlalmqkkladylrcliirrdlLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
45-166 9.23e-63

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: 199.75  E-value: 9.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  45 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 124
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462519995 125 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17694    81 TSARNLPElktavgrgrawlhlalmqkkladylkvlidrkdlLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
45-165 1.27e-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: 199.33  E-value: 1.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  45 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 124
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519995 125 ASVRDLPG----------------------------------LNEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 165
Cdd:cd17681    81 ASVRDLPGiktplgrarawlrlalmqkkladyfralienkdlLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
45-166 7.56e-59

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: 189.82  E-value: 7.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  45 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 124
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462519995 125 ASVRDLPGL----------------------------------NEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17696    81 ASVKDLPGLktpvgrgrawlrlalmqkklseymkalinrkdllSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
80-169 2.25e-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: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  80 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLP------------------GLNE 135
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEqihtpyspdgrgrawirlALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 136 -------------------FYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 169
Cdd:pfam02759  81 klldqwlklllsnkellseYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
48-165 9.38e-11

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: 59.72  E-value: 9.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  48 NLLNMAKLSIKGLIESAlSFgRTLDSDYPPLQQFFVVMEHCLKHGLK---------VRKSFLSYNKT------------- 105
Cdd:cd17684     1 NLVTVCRLSVKSLIDKA-CL-ETIDDSSEELINFAAILEQILSHRLKpvkpwygseEPRTFWDYIRVackkvpqnciasi 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 106 --------------IWGPLELVEKLYpeAEEIGASVRDLPGLNEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 165
Cdd:cd17684    79 eqmenikspkakgrAWIRVALMEKRL--SEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
48-166 1.06e-09

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: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  48 NLLNMAKLSIKGLIESalSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYN--KTIWGPLELVEKLYPE------ 119
Cdd:cd17700     1 NLITVCRFSVKTLIDR--SCFETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHncicsi 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462519995 120 --------------------------AEEIGASVRDLPGLNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17700    79 enmenvsssrakgrawirvalmekrlSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
56-165 1.13e-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: 53.97  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  56 SIKGLIESAL-------SFGRTLDSDYPPLQQFFVVMEHCLKHGLKvRKSFLSYNKTIWGPLELVEKLYPeAEEIGASVR 128
Cdd:cd17671     2 AVKELLESFAdngeaddSAALTLTDDDPVVGRLCAALEAILSHGLK-PKRFGGGKVSFWDFLEALEKLLP-APSLKQAIR 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519995 129 DLP------------------GLNE-------------------FYEYHALMM-EEEGAVIVGLLVGLNVIDANL 165
Cdd:cd17671    80 DINslsnvktddgrgrawirlALNEkslesylaallsdqsllrkYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
48-166 2.67e-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: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  48 NLLNMAKLSIKGLIESALSfgRTLDSDYPPLQQFFVVMEHCLKHGLKV---------RKSFLSY---------NKTI--- 106
Cdd:cd17699     1 NLITVCRFSVKTLLEKYTA--EPIDDSSEEFVNFAAILEQILSHRFKGpvswfssdgQRGFWDYirlacskvpNNCIssi 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519995 107 ---------------WGPLELVEKLYpeAEEIGASVRDLPGLNEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 166
Cdd:cd17699    79 enmenistsrakgraWIRVALMEKRL--SEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
185-415 9.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 185 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 261
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 262 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 341
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 342 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 415
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
194-396 4.38e-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: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 194 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQH 273
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 274 LEVTKV----------DVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHE 343
Cdd:COG4942   117 GRQPPLalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462519995 344 KQDTLIGLRQQLEEVKAinieMYQKLQGSEDGLKEKNEIIARLEEKTNKITAA 396
Cdd:COG4942   197 RQKLLARLEKELAELAA----ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
185-415 5.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 185 LKNEEDIgnKERNVQIAAILDQKNYVEELNRQLN---STVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 261
Cdd:COG1196   218 LKEELKE--LEAELLLLKLRELEAELEELEAELEeleAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 262 EnKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 341
Cdd:COG1196   296 E-LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519995 342 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQTRTIA 415
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
RUN smart00593
domain involved in Ras-like GTPase signaling;
127-168 6.79e-06

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 43.37  E-value: 6.79e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462519995  127 VRDLPGLNEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 168
Cdd:smart00593  22 LSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
199-402 1.84e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 199 QIAAILDQ--KNYVEElnrqlnstvsSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEV 276
Cdd:COG3206   149 LAAAVANAlaEAYLEQ----------NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 277 TK-VDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKL--LEKDIHEKQDTLIGLRQ 353
Cdd:COG3206   219 QQlSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDVIALRA 298
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462519995 354 QLEEVKA--------INIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQ 402
Cdd:COG3206   299 QIAALRAqlqqeaqrILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
194-407 3.58e-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: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 194 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKlilmKTQQH 273
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 274 LEVTKVDVETELQT-YKHSRQGLDEMYnearrqlrdesqLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLR 352
Cdd:COG4942    99 LEAQKEELAELLRAlYRLGRQPPLALL------------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462519995 353 QQLEEVKAINIEMYQKLQGSEDGL----KEKNEIIARLEEKTNKITAAMRQLEQSDNDL 407
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALealkAERQKLLARLEKELAELAAELAELQQEAEEL 225
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
227-405 5.89e-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: 45.50  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 227 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNE 301
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 302 ARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 379
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562
                         170       180
                  ....*....|....*....|....*...
gi 2462519995 380 NEiIARLE--EKTNKItaaMRQLEQSDN 405
Cdd:pfam17380 563 EE-RSRLEamEREREM---MRQIVESEK 586
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
187-407 2.07e-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: 43.89  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  187 NEEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS----- 261
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErlesl 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  262 ENKLILMKTQ-QHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkHEIELAMKLLEKD 340
Cdd:TIGR02168  830 ERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------ALLRSELEELSEE 902
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519995  341 IHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARL--------EEKTNKITAAMRQLEQSDNDL 407
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRL 977
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
223-407 3.02e-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: 43.51  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  223 SLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEN------KLILMKTQQHLEVTKVDVETELQTYKHSRQGLD 296
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  297 EMYNEARRQLRDESQLRQDVENELAvqvSMKHEIELAMKLLEkdihekqdtliGLRQQLEEVKAINIEMYQKLQGSEDGL 376
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELE-----------SLEAELEELEAELEELESRLEELEEQL 381
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462519995  377 KEKNEIIARLEEKTNKITAAMRQLEQSDNDL 407
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERL 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-415 3.07e-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: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  194 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS---ENKLILMKT 270
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  271 QQHLEVTKVDVE-------TELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVE---NELAVQVSMKHEIE--------- 331
Cdd:TIGR02168  343 EEKLEELKEELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnNEIERLEARLERLEdrrerlqqe 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  332 ---LAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLL 408
Cdd:TIGR02168  423 ieeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502

                   ....*..
gi 2462519995  409 TQTRTIA 415
Cdd:TIGR02168  503 GFSEGVK 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-408 3.72e-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: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 199 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEVTK 278
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 279 VDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkhEIELAMKLLEKDIHEKQDTLIGLRQQLEEV 358
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE--------RLEEELEELEEALAELEEEEEEEEEALEEA 447
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462519995 359 KAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLL 408
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
199-410 9.74e-04

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: 41.59  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  199 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnkliLMKTQQHLEVTK 278
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARLSHSR 792
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  279 VD-VETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEE 357
Cdd:TIGR02169  793 IPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462519995  358 VKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQ 410
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
189-407 9.99e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 189 EDIGNKERnvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENklilm 268
Cdd:TIGR04523 314 SELKNQEK--KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI----- 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 269 ktqQHLEVTKVDVETELQTYKHSRQGLDEmynEARRQLRDESQLRQDVENELAVQVSMKHEIelamKLLEKDIHEKQDTL 348
Cdd:TIGR04523 387 ---KNLESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEI----KDLTNQDSVKELII 456
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 349 IGLRQQLEEVKaINIEMYQKLQGSED-GLKEKNEIIARLEEKTNKITAAMRQLEQSDNDL 407
Cdd:TIGR04523 457 KNLDNTRESLE-TQLKVLSRSINKIKqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-378 2.65e-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: 40.43  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  170 EDLDSQVGVIDFSMylkNEEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNI 249
Cdd:TIGR02168  298 SRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  250 IKLQEENHQLRSENKLI------LMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEArrQLRDESQLRQDVENELAVQ 323
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLelqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEEL 452
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462519995  324 VSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAiNIEMYQKLQGSEDGLKE 378
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLERLQENLEGFSE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
188-401 6.69e-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: 38.90  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  188 EEDIGNKERNVQIAAILDQKNYVEElnrqlnsTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRsENKLIL 267
Cdd:TIGR02169  781 LNDLEARLSHSRIPEIQAELSKLEE-------EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-EQIKSI 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  268 MKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQlrdesqlRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDT 347
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------RDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462519995  348 LIGLRQQLEEvkainiemYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLE 401
Cdd:TIGR02169  926 LEALEEELSE--------IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
224-410 7.33e-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: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 224 LHSRVDSLEK-SNT-----KLIEELAIAKNNIIKLQEENHQLRsenklilmktQQHLEVTKVDVETELQTYKHSRQGLDE 297
Cdd:COG1196   198 LERQLEPLERqAEKaeryrELKEELKELEAELLLLKLRELEAE----------LEELEAELEELEAELEELEAELAELEA 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995 298 MYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLK 377
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462519995 378 EKNEIIARLEEKTNKITAAMRQLEQSDNDLLTQ 410
Cdd:COG1196   348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
PRK11281 PRK11281
mechanosensitive channel MscK;
313-410 7.47e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519995  313 RQDVENELAVQVSMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 392
Cdd:PRK11281    38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
                           90       100
                   ....*....|....*....|....
gi 2462519995  393 ITAA------MRQLEQSDNDLLTQ 410
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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