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Conserved domains on  [gi|1958758164|ref|XP_038955029|]
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RUN and FYVE domain-containing protein 2 isoform X6 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 141-296 6.25e-116

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: 340.42  E-value: 6.25e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 141 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 220
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 221 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-548 1.69e-06

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: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 315 LKNEEEIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 391
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 392 EnelilmrtRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDI 471
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758164 472 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSL 548
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
 
Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 141-296 6.25e-116

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: 340.42  E-value: 6.25e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 141 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 220
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 221 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 176-299 4.52e-40

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: 142.03  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 176 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLPGLKT---PLGRARAWLRLALMQ 246
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958758164 247 KKMADYLRCLIIQRELLSEFYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 299
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
236-298 9.24e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 74.57  E-value: 9.24e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758164  236 ARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 298
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-548 1.69e-06

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: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 315 LKNEEEIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 391
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 392 EnelilmrtRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDI 471
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758164 472 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSL 548
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 357-535 1.43e-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: 48.20  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 357 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENELILMRTRQHLEVTKVDVETELQTYKHSRQGLDEMYDD 431
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 432 ARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 509
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562

                         170       180
                  ....*....|....*....|....*...
gi 1958758164 510 NEiIARLE--EKTNKIttaMRQLEQSDN 535
Cdd:pfam17380 563 EE-RSRLEamEREREM---MRQIVESEK 586
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 319-550 2.85e-05

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: 46.94  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 319 EEIGNKERnvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENelilm 398
Cdd:TIGR04523 314 SELKNQEK--KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI----- 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 399 rtrQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQvgmKHEIelamKLLEKDIHEKQ--- 475
Cdd:TIGR04523 387 ---KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN---NSEI----KDLTNQDSVKElii 456

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 476 DTLIGLRQQLEE-VKAINIEMYQKLQGSEDGLKEkneiiarLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSLVK 550
Cdd:TIGR04523 457 KNLDNTRESLETqLKVLSRSINKIKQNLEQKQKE-------LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
46 PHA02562
endonuclease subunit; Provisional
 328-554 2.69e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 328 VQIAAILDQ--KNYVEELNRQLnSTVSSLHSRVDSLEKSNTKLIEEL-AIAKNNIIKLQEENHQLRSENELILMR-TRQH 403
Cdd:PHA02562  162 ISVLSEMDKlnKDKIRELNQQI-QTLDMKIDHIQQQIKTYNKNIEEQrKKNGENIARKQNKYDELVEEAKTIKAEiEELT 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 404 LEVTKVDVETELQTykhsrqgldemydDARRQLRDEsqlrqdvenelsvQVGMKHEIELAMKLLEkdIHEKQDTLIGLRQ 483
Cdd:PHA02562  241 DELLNLVMDIEDPS-------------AALNKLNTA-------------AAKIKSKIEQFQKVIK--MYEKGGVCPTCTQ 292

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758164 484 QLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIaVSLVKSASS 554
Cdd:PHA02562  293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL-ITLVDKAKK 362
 
Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 141-296 6.25e-116

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: 340.42  E-value: 6.25e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 141 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 220
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 221 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 141-295 1.19e-93

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: 283.31  E-value: 1.19e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 141 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 220
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758164 221 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 295
Cdd:cd17681    81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 141-296 1.60e-88

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: 270.24  E-value: 1.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 141 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 220
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 221 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17694    81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 141-296 4.06e-84

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: 258.77  E-value: 4.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 141 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 220
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 221 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 176-299 4.52e-40

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: 142.03  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 176 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLPGLKT---PLGRARAWLRLALMQ 246
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958758164 247 KKMADYLRCLIIQRELLSEFYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 299
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 144-295 3.33e-28

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: 110.18  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 144 NLLNMAKLSIKGLIESAlSFgRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSY--NKTIWGPLELVEKLYPEaeEIGA 221
Cdd:cd17684     1 NLVTVCRLSVKSLIDKA-CL-ETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKVPQ--NCIA 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758164 222 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 295
Cdd:cd17684    77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 152-295 4.46e-28

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: 109.82  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 152 SIKGLIESAL-------SFGRTLDSDYPPLQQFFVVMEHCLKHGLKvRKSFLSYNKTIWGPLELVEKLYPEAEEIGA--S 222
Cdd:cd17671     2 AVKELLESFAdngeaddSAALTLTDDDPVVGRLCAALEAILSHGLK-PKRFGGGKVSFWDFLEALEKLLPAPSLKQAirD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758164 223 VRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANL 295
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 144-296 7.14e-19

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: 83.48  E-value: 7.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 144 NLLNMAKLSIKGLIESalSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYN--KTIWGPLELVEKLYPEAeeIGA 221
Cdd:cd17700     1 NLITVCRFSVKTLIDR--SCFETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHN--CIC 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758164 222 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17700    77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 144-296 2.58e-18

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: 82.00  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 144 NLLNMAKLSIKGLIESALSfgRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYN--KTIWGPLELVEKLYPEaeEIGA 221
Cdd:cd17699     1 NLITVCRFSVKTLLEKYTA--EPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSDgqRGFWDYIRLACSKVPN--NCIS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758164 222 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 296
Cdd:cd17699    77 SIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
RUN smart00593
domain involved in Ras-like GTPase signaling;
236-298 9.24e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 74.57  E-value: 9.24e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758164  236 ARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 298
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 153-295 2.24e-10

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 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: 439044  Cd Length: 150  Bit Score: 59.16  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 153 IKGLIESALS-FGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLE-LVEKLYPEA---EEIGASVRDLP 227
Cdd:cd17682     2 LKGCVLDLKSeFGEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758164 228 GLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMMEEEGAVI-VGLLVGLNVIDANL 295
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEIlLSLLYQLNEINFDL 150
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 172-295 1.69e-09

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 56.73  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 172 PPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLPGLKTPLGRARAWLRLALMQKKMAD 251
Cdd:cd17697    26 PELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAE 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958758164 252 YLRCLIIQRELLSE-FYEYHALMMEEEGAVIVGLLVGLNVIDANL 295
Cdd:cd17697   106 SLQLCLLNPELTGEwYYARSPFLSPELRSDILDSLYELNGVNFDL 150
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 152-288 2.02e-09

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 56.10  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 152 SIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKvrksflSYNKTIWGPLelVEKLYPEAEEigaSVRDLPGLKT 231
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLR------RGNRGYWPFV--KEFTHKETIK---QIENLPNVTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958758164 232 PLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALM-----MEeegaVIVGLLVGL 288
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLrdsqrLE----LLLTLLSGL 138
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 226-291 1.12e-08

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 54.54  E-value: 1.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758164 226 LPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMM-EEEGAVIVGLLVGLNVI 291
Cdd:cd17689    93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
 153-287 8.20e-08

RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. This model contains the RUN domain of SGSM1.


Pssm-ID: 439065  Cd Length: 177  Bit Score: 52.32  E-value: 8.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 153 IKGLIESALSfGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKS-FLSYNKtIWGPLELVEKLYPEAEEIGASVRDL----- 226
Cdd:cd17703     3 VKQIMEEAVT-RKFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNK-IAALFMKVGKSFPPAEELCRKVQELeqlle 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 227 ------PGLK------------TPLGRARAWLRLALMQKKMADYLRCLIiqrELLSEFYEYHALMMEE-EGAVIVGLLVG 287
Cdd:cd17703    81 nkrnqmQGLQenvrkmpklpnlSPQAIKHLWIRTALFEKVLDKIVHYLV---ENSSKYYEKEALLMDPvDGPILASLLVG 157
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 174-295 1.54e-07

RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.


Pssm-ID: 439060  Cd Length: 158  Bit Score: 51.23  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 174 LQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGplELVEKLYPEAeeiGAS-----VRDLPGLKTPLGRARAWLRLALMQKK 248
Cdd:cd17698    36 LHKFCAKLEYLLQFDQKEKTTLLGGRKDYWD--YFCECLAKVK---GLNdgirfVKSLKEVRTSLGKGRAFIRYSLVHQR 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958758164 249 MADYLRCLIIQRELLSE-FYEYHALMMEEEGAVIVGLLVGLNVIDANL 295
Cdd:cd17698   111 LADTLQQCVMNGKVTSDwYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 223-292 6.70e-07

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053 [Multi-domain]  Cd Length: 206  Bit Score: 50.05  E-value: 6.70e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758164 223 VRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHA-LMMEEEGAVIVGLLVGLNVID 292
Cdd:cd17691   127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVD 197
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 230-295 7.91e-07

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 49.13  E-value: 7.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758164 230 KTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANL 295
Cdd:cd17679    95 TTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGLESFQFEL 161
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 222-292 1.08e-06

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 49.32  E-value: 1.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958758164 222 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHA-LMMEEEGAVIVGLLVGLNVID 292
Cdd:cd17677   103 NVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVD 174
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
 182-292 1.32e-06

RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2.


Pssm-ID: 439049  Cd Length: 161  Bit Score: 48.44  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 182 EHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDL------PGLKTPLGRARA-------------WLRL 242
Cdd:cd17687    31 DACLLHGLRKRALGLFRSSSTFSLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIRI 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958758164 243 ALMQKKMadylrCLIIQR--ELLSEFYEYHALMME-EEGAVIVGLLVGLNVID 292
Cdd:cd17687   111 ALFEKVL-----DKIVDYlvENASKYYEKEALMADpVDGPLLASLLVGPCALD 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-548 1.69e-06

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: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 315 LKNEEEIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 391
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 392 EnelilmrtRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDI 471
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758164 472 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSL 548
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-545 1.32e-05

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: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 314 YLKNEEEIGNKERNVQIAAILDQKNYVEELNRQLN---STVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLR 390
Cdd:COG1196   215 YRELKEELKELEAELLLLKLRELEAELEELEAELEeleAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 391 SEnELILMRTRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKD 470
Cdd:COG1196   295 AE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758164 471 IHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIA 545
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 357-535 1.43e-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: 48.20  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 357 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENELILMRTRQHLEVTKVDVETELQTYKHSRQGLDEMYDD 431
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 432 ARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 509
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562

                         170       180
                  ....*....|....*....|....*...
gi 1958758164 510 NEiIARLE--EKTNKIttaMRQLEQSDN 535
Cdd:pfam17380 563 EE-RSRLEamEREREM---MRQIVESEK 586
YabA pfam06156
Initiation control protein YabA; YabA is involved in initiation control of chromosome ...
 357-431 1.53e-05

Initiation control protein YabA; YabA is involved in initiation control of chromosome replication. It interacts with both DnaA and DnaN, acting as a bridge between these two proteins.


Pssm-ID: 428795 [Multi-domain]  Cd Length: 103  Bit Score: 44.10  E-value: 1.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758164 357 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENElilmRTRQHLEVTKVDVETELQTYKHSRQGLDEMYDD 431
Cdd:pfam06156   9 QLSELEEQLGQLLAQLGELKEQLVELLEENAELRIENE----HLRERLTEEEKKEKEKKQDLGEGYDNLARLYEE 79
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 316-526 2.65e-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: 46.68  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 316 KNEEEIGNKERnvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSE--- 392
Cdd:COG4942    31 QLQQEIAELEK--ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElae 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 393 --NELILMRTRQHLEV-----TKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMK 465
Cdd:COG4942   109 llRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758164 466 LLEKDIHEKQDTLIGLRQQLEEVKAinieMYQKLQGSEDGLKEKNEIIARLEEKTNKITTA 526
Cdd:COG4942   189 ALEALKAERQKLLARLEKELAELAA----ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 319-550 2.85e-05

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: 46.94  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 319 EEIGNKERnvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENelilm 398
Cdd:TIGR04523 314 SELKNQEK--KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI----- 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 399 rtrQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQvgmKHEIelamKLLEKDIHEKQ--- 475
Cdd:TIGR04523 387 ---KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN---NSEI----KDLTNQDSVKElii 456

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758164 476 DTLIGLRQQLEE-VKAINIEMYQKLQGSEDGLKEkneiiarLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSLVK 550
Cdd:TIGR04523 457 KNLDNTRESLETqLKVLSRSINKIKQNLEQKQKE-------LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 382-522 5.71e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.26  E-value: 5.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  382 LQEENHQL----RSENELILMRTRQ--HLEVTKVDVETELQTYKHSRqglDEMYDDARRqlrdESQLRQDVENELSVQVg 455
Cdd:pfam15921   80 LEEYSHQVkdlqRRLNESNELHEKQkfYLRQSVIDLQTKLQEMQMER---DAMADIRRR----ESQSQEDLRNQLQNTV- 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758164  456 mkHEIElAMKLLEKDIHEKQDTliglrqqleevkaiNIEMYQKLQGSEDG-LKEKNEIIARLEEKTNK 522
Cdd:pfam15921  152 --HELE-AAKCLKEDMLEDSNT--------------QIEQLRKMMLSHEGvLQEIRSILVDFEEASGK 202
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-537 1.05e-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: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  317 NEEEIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS----- 391
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErlesl 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  392 ENELILMRTR-QHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELsvqvgmkHEIELAMKLLEKD 470
Cdd:TIGR02168  830 ERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------ALLRSELEELSEE 902

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758164  471 IHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARL--------EEKTNKITTAMRQLEQSDNDL 537
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRL 977
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 324-556 1.17e-04

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: 44.75  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 324 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENElilmRTRQH 403
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 404 LEVTKVDVETELQT-YKHSRQGLDEMYddarrqlrdesqLRQDVENELSVQVGMKHEIELAMKLLEKDIHEKQDTLIGLR 482
Cdd:COG4942    99 LEAQKEELAELLRAlYRLGRQPPLALL------------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758164 483 QQLEEVKAINIEMYQKLQGSEDGL----KEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSLVKSASSDP 556
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALealkAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 335-531 1.32e-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: 45.01  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 335 DQKNYVEELNRQLNSTVSSLHSRVDSLeKSNTKLIEELaiaKNNIIKLQEENHQLRSENELILMRTRQhLEVTKVDVETE 414
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKEL-KSKEKELKKL---NEEKKELEEKVKDLTKKISSLKEKIEK-LESEKKEKESK 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 415 LqtykhsrqgldemyddarrqlrdeSQLRQDVEnelsvqvgmKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIE 494
Cdd:TIGR04523 540 I------------------------SDLEDELN---------KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958758164 495 MYQKLQGSEdglKEKNEIIARLEEKTNKITTAMRQLE 531
Cdd:TIGR04523 587 KQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELE 620
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
329-532 1.58e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 329 QIAAILDQ--KNYVEElnrqlnstvsSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENELILMRTRQHLEV 406
Cdd:COG3206   149 LAAAVANAlaEAYLEQ----------NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 407 TK-VDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKL--LEKDIHEKQDTLIGLRQ 483
Cdd:COG3206   219 QQlSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDVIALRA 298

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758164 484 QLEEVKA--------INIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQ 532
Cdd:COG3206   299 QIAALRAqlqqeaqrILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-538 4.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 319 EEIGNKERNV--QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENELI 396
Cdd:COG1196   284 EEAQAEEYELlaELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 397 LMRTRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELsvqvgmkhEIELAMKLLEKDIHEKQD 476
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE--------RLEEELEELEEALAELEE 435

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958758164 477 TLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLL 538
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 223-292 4.48e-04

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052 [Multi-domain]  Cd Length: 209  Bit Score: 41.92  E-value: 4.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758164 223 VRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRELLSEFYEYHA-LMMEEEGAVIVGLLVGLNVID 292
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVD 200
YabA COG4467
Regulator of replication initiation timing YabA [Replication, recombination and repair];
353-431 4.70e-04

Regulator of replication initiation timing YabA [Replication, recombination and repair];


Pssm-ID: 443564 [Multi-domain]  Cd Length: 107  Bit Score: 39.86  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 353 SLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENElilmRTRQHL-EVTKVDVETELQTYKHSRQGLDEMYDD 431
Cdd:COG4467     5 ELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENE----HLRERLeELEKKKEKKAEKDIGEGYDNLARLYEE 80
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 320-534 7.64e-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: 42.74  E-value: 7.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  320 EIGNKERNVQIAAILDQKNyveelnrqlnstvsSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnelilmr 399
Cdd:TIGR02168  217 ELKAELRELELALLVLRLE--------------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE------- 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  400 tRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDIHEKQDTLI 479
Cdd:TIGR02168  276 -VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758164  480 GLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEK----TNKITTAMRQLEQSD 534
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslNNEIERLEARLERLE 413
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 315-540 1.82e-03

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: 41.16  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 315 LKNEEEIGNKERNvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEne 394
Cdd:TIGR04523  56 LKNLDKNLNKDEE-KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ-- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 395 lilmrtRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQlrdesqlrqdvenelsvqvgmKHEIELAMKLLEKDIHEK 474
Cdd:TIGR04523 133 ------KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ---------------------KEELENELNLLEKEKLNI 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758164 475 QDTLIGLRQQL--EEVKAINIEMYQKLQgsedglKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQ 540
Cdd:TIGR04523 186 QKNIDKIKNKLlkLELLLSNLKKKIQKN------KSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 300-517 2.32e-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: 40.81  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  300 EDLDSQVGVIDFSMylkNEEEIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNI 379
Cdd:TIGR02168  298 SRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  380 IKLQEENHQLRSEneliLMRTRQHLEVTKvdveTELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVEnelsvqvgmKHE 459
Cdd:TIGR02168  375 EELEEQLETLRSK----VAQLELQIASLN----NEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKE 437

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758164  460 IELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLE 517
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 300-533 2.60e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  300 EDLDSQVGVID-FSMYLKNeeeigNKERNVQIAAILDQKN---YVEELNRQLNSTVSSLHSRVDSLEKsNTKLIEElaiA 375
Cdd:TIGR00606  785 KVCLTDVTIMErFQMELKD-----VERKIAQQAAKLQGSDldrTVQQVNQEKQEKQHELDTVVSKIEL-NRKLIQD---Q 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  376 KNNIIKLQEENHQLRSENELI--LMRTRQHLEVTKVDVETELQTykhsrqgLDEMYDDARRQLRDESQLRQDVENELSVQ 453
Cdd:TIGR00606  856 QEQIQHLKSKTNELKSEKLQIgtNLQRRQQFEEQLVELSTEVQS-------LIREIKDAKEQDSPLETFLEKDQQEKEEL 928

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  454 VGMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEevkainiemyQKLQ-GSEDGLKEK----NEIIARLEE---KTNKITT 525
Cdd:TIGR00606  929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE----------NKIQdGKDDYLKQKetelNTVNAQLEEcekHQEKINE 998


                   ....*...
gi 1958758164  526 AMRQLEQS 533
Cdd:TIGR00606  999 DMRLMRQD 1006
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 351-550 2.61e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 39.72  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 351 VSSLHSRVDSLEKSNTK-------LIEELAIAKNNIIKLQEENHQLRSENE-LILMRTRQHLEVTkvDVETELQTYKHSR 422
Cdd:pfam17078   5 IESLHDQIDALTKTNLQltvqsqnLLSKLEIAQQKESKFLENLASLKHENDnLSSMLNRKERRLK--DLEDQLSELKNSY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 423 QGLDEMYDDARRQLRDESQLRQDVENELS-VQVGMKHEIELAMKLLEKdiheKQDTLIGLRQQLEEVKAINIEMYQKLQg 501
Cdd:pfam17078  83 EELTESNKQLKKRLENSSASETTLEAELErLQIQYDALVDSQNEYKDH----YQQEINTLQESLEDLKLENEKQLENYQ- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958758164 502 sEDGLKEKNEIIARLEEKTNKITTaMRQLEQSDNDLLTQTRTIAVSLVK 550
Cdd:pfam17078 158 -QRISSNDKDIDTKLDSYNNKFKN-LDNIYVNKNNKLLTKLDSLAQLLD 204
46 PHA02562
endonuclease subunit; Provisional
 328-554 2.69e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 328 VQIAAILDQ--KNYVEELNRQLnSTVSSLHSRVDSLEKSNTKLIEEL-AIAKNNIIKLQEENHQLRSENELILMR-TRQH 403
Cdd:PHA02562  162 ISVLSEMDKlnKDKIRELNQQI-QTLDMKIDHIQQQIKTYNKNIEEQrKKNGENIARKQNKYDELVEEAKTIKAEiEELT 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 404 LEVTKVDVETELQTykhsrqgldemydDARRQLRDEsqlrqdvenelsvQVGMKHEIELAMKLLEkdIHEKQDTLIGLRQ 483
Cdd:PHA02562  241 DELLNLVMDIEDPS-------------AALNKLNTA-------------AAKIKSKIEQFQKVIK--MYEKGGVCPTCTQ 292

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758164 484 QLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIaVSLVKSASS 554
Cdd:PHA02562  293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL-ITLVDKAKK 362
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 329-540 4.25e-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: 40.05  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  329 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENELILMRTRQHlEVTK 408
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS-RIPE 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  409 VDVETELQTYKHSRqgLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEV 488
Cdd:TIGR02169  796 IQAELSKLEEEVSR--IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958758164  489 KAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQ 540
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 340-545 6.80e-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: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  340 VEELNRQLNstvsSLHSRVDSLEKSNTKLIE----ELAIAKNNIIKLQEENHQLRSE-NELILMRTRqhLEVTKVDVETE 414
Cdd:TIGR02168  195 LNELERQLK----SLERQAEKAERYKELKAElrelELALLVLRLEELREELEELQEElKEAEEELEE--LTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  415 LQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENELSVQVGMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIE 494
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958758164  495 MYQKLQGSEDGLKEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIA 545
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 370-530 7.25e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 370 EELAIAKNNIIKLQEENHQLRSENELILMRTRQHLEVTKVDVETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENE 449
Cdd:COG1196   661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 450 LSVQVGMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAIN---IEMYQKLQGSEDGLKEKNEI----IARLEEKTNK 522
Cdd:COG1196   741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNllaIEEYEELEERYDFLSEQREDleeaRETLEEAIEE 820


                  ....*...
gi 1958758164 523 ITTAMRQL 530
Cdd:COG1196   821 IDRETRER 828
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 329-561 8.51e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 329 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEE----NHQLRSENELILMRTR--- 401
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARaly 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 402 -QHLEVTKVDV---ETELQTYKHSRQGLDEMYDDARRQLRDESQLRQDVENElsvqvgmKHEIELAMKLLEkdihEKQDT 477
Cdd:COG3883    97 rSGGSVSYLDVllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAK-------KAELEAKLAELE----ALKAE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 478 LIGLRQQLEEVKAINIEMYQKLQGSEDGL-KEKNEIIARLEEKTNKITTAMRQLEQSDNDLLTQTRTIAVSLVKSASSDP 556
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAeAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245


                  ....*
gi 1958758164 557 QDQYK 561
Cdd:COG3883   246 AAGAG 250
PRK11281 PRK11281
mechanosensitive channel MscK;
443-540 9.16e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164  443 RQDVENELSVQVGMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 522
Cdd:PRK11281    38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112

                           90       100
                   ....*....|....*....|....
gi 1958758164  523 I------TTAMRQLEQSDNDLLTQ 540
Cdd:PRK11281   113 EtretlsTLSLRQLESRLAQTLDQ 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
314-537 9.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 314 YLKNEEEIGN--KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIE---ELAIAKNNIIKLQEENHQ 388
Cdd:PRK03918  184 FIKRTENIEEliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekELESLEGSKRKLEEKIRE 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 389 LRSENElilmRTRQHLEVTKVDVE--TELQTYKHSRQGLDEMYDDARRQLRD-------ESQLRQDVENELSVQVGMKHE 459
Cdd:PRK03918  264 LEERIE----ELKKEIEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREiekrlsrLEEEINGIEERIKELEEKEER 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758164 460 IElAMKLLEKDIHEKQDTLIGLRQQLEEVKAI--NIEMYQKLQGSEDGLKEKNEIIA------RLEEKTNKITTAMRQLE 531
Cdd:PRK03918  340 LE-ELKKKLKELEKRLEELEERHELYEEAKAKkeELERLKKRLTGLTPEKLEKELEElekakeEIEEEISKITARIGELK 418


                  ....*.
gi 1958758164 532 QSDNDL 537
Cdd:PRK03918  419 KEIKEL 424
 
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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