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Conserved domains on  [gi|1052793228|ref|NP_001317032|]
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RUN and FYVE domain-containing protein 2 isoform d [Homo sapiens]

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; ...
10-165 7.99e-115

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: 338.88  E-value: 7.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228  90 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
534-604 1.66e-43

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed 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.


:

Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 149.79  E-value: 1.66e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 534 GLVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHALLIQRCSSN 604
Cdd:cd15759     1 GQVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
266-535 1.52e-14

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: 77.28  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 266 LMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQD 345
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 346 TLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECL 425
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 426 SKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQE 505
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
                         250       260       270
                  ....*....|....*....|....*....|
gi 1052793228 506 QALQELGNKLSESKLKIEDIKEANKALQGL 535
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGF 506
 
Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
10-165 7.99e-115

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: 338.88  E-value: 7.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228  90 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
534-604 1.66e-43

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed 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.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 149.79  E-value: 1.66e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 534 GLVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHALLIQRCSSN 604
Cdd:cd15759     1 GQVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
45-168 1.76e-38

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: 138.18  E-value: 1.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  45 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLPGLKT---PLGRARAWLRLALMQ 115
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 116 KKMADYLRCLIIQRDLLSEFYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 168
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
536-597 2.08e-28

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 107.85  E-value: 2.08e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228 536 VWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP---SSPKPVRVCDSCHALL 597
Cdd:pfam01363   2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTL 66
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
537-597 8.12e-27

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 103.28  E-value: 8.12e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228  537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSCHALL 597
Cdd:smart00064   4 WIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
RUN smart00593
domain involved in Ras-like GTPase signaling;
105-167 8.04e-16

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 71.88  E-value: 8.04e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228  105 ARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 167
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
266-535 1.52e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.28  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 266 LMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQD 345
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 346 TLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECL 425
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 426 SKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQE 505
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
                         250       260       270
                  ....*....|....*....|....*....|
gi 1052793228 506 QALQELGNKLSESKLKIEDIKEANKALQGL 535
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGF 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
328-554 1.37e-09

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: 61.23  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  328 EIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNkitaamrQLEQRLQQAE 407
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-------QLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  408 KAQMEAEDEDEKYLQEclskSDSLQKQISQKEKQLVQLETDLkiekewrQTLQEDLQKEKDALSHLRNETQQiisLKKEF 487
Cdd:TIGR02168  754 KELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQI-------EQLKEELKALREALDELRAELTL---LNEEA 819
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228  488 LNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIE-----------DIKEANKALQGLVWLKDKEATHCKLCEKEFS 554
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleeLIEELESELEALLNERASLEEALALLRSELE 897
PRK11281 PRK11281
mechanosensitive channel MscK;
312-531 9.18e-09

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 58.77  E-value: 9.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  312 RQDVENELAVQVSMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 391
Cdd:PRK11281    38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  392 ITAA------MRQLEQRLQQAEKAQMEAededekylQECLSKSDSL-----------QKQISQKEKQLVQLETDLK---- 450
Cdd:PRK11281   113 ETREtlstlsLRQLESRLAQTLDQLQNA--------QNDLAEYNSQlvslqtqperaQAALYANSQRLQQIRNLLKggkv 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  451 IEKEWRQTLQEDLQKEKDAL----SHLRNETQ---QIISLKKEFLNLQDENQQLKKiyhEQEQALQELGN----KLSESK 519
Cdd:PRK11281   185 GGKALRPSQRVLLQAEQALLnaqnDLQRKSLEgntQLQDLLQKQRDYLTARIQRLE---HQLQLLQEAINskrlTLSEKT 261
                          250
                   ....*....|...
gi 1052793228  520 LK-IEDIKEANKA 531
Cdd:PRK11281   262 VQeAQSQDEAARI 274
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
248-527 2.40e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.99  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  248 IIKLQEENHQLRSenkliLMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDvenelavqvsmkh 327
Cdd:pfam12128  243 FTKLQQEFNTLES-----AELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD------------- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  328 EIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDG----LKEKNEIIARLEEKTNKITAAMRQLEQRL 403
Cdd:pfam12128  305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSwqseLENLEERLKALTGKHQDVTAKYNRRRSKI 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  404 QQAEKAQMEAEDEDEKYLQECLSK-----SDSLQKQISQKEKQLVQLETDLKIEKE-------WRQTLQEDLQKEKDALS 471
Cdd:pfam12128  385 KEQNNRDIAGIKDKLAKIREARDRqlavaEDDLQALESELREQLEAGKLEFNEEEYrlksrlgELKLRLNQATATPELLL 464
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228  472 HLRN---------ETQQiiSLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKE 527
Cdd:pfam12128  465 QLENfderierarEEQE--AANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
530-594 1.52e-03

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 41.61  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  530 KALQGLVWLKDKEAT-HCKLCEKEF-SLSK----RKHHCRNCGEIFCNAC-------SDNELPLPSSPKPVR---VCDSC 593
Cdd:PTZ00303   446 KLLHNPSWQKDDESSdSCPSCGRAFiSLSRplgtRAHHCRSCGIRLCVFCitkrahySFAKLAKPGSSDEAEerlVCDTC 525

                   .
gi 1052793228  594 H 594
Cdd:PTZ00303   526 Y 526
 
Name Accession Description Interval E-value
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
10-165 7.99e-115

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: 338.88  E-value: 7.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228  90 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
10-164 2.91e-92

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: 280.61  E-value: 2.91e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228  90 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 164
Cdd:cd17681    81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
10-165 7.52e-86

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: 264.46  E-value: 7.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228  90 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17694    81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
10-165 2.87e-82

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: 254.92  E-value: 2.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  10 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIG 89
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228  90 ASVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
534-604 1.66e-43

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed 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.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 149.79  E-value: 1.66e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 534 GLVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHALLIQRCSSN 604
Cdd:cd15759     1 GQVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
537-594 2.69e-41

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed 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 homologue 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 termed 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. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 143.29  E-value: 2.69e-41
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCH 594
Cdd:cd15721     1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
532-602 2.82e-40

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed 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 homologue 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.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 140.97  E-value: 2.82e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 532 LQGLVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHALLIQRCS 602
Cdd:cd15758     1 LKGHAWLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
45-168 1.76e-38

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: 138.18  E-value: 1.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  45 QFFVVMEHCLKHGLKV------RKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLPGLKT---PLGRARAWLRLALMQ 115
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 116 KKMADYLRCLIIQRDLLSEFYEYHALMMEEEGA-VIVGLLVGLNVIDANLCVKG 168
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
536-597 2.08e-28

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 107.85  E-value: 2.08e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228 536 VWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP---SSPKPVRVCDSCHALL 597
Cdd:pfam01363   2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTL 66
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
537-597 1.00e-27

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 105.94  E-value: 1.00e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHALL 597
Cdd:cd15730     3 WADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
13-164 2.82e-27

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: 107.48  E-value: 2.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  13 NLLNMAKLSIKGLIESALSfgRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSY--NKTIWGPLELVEKLYPEaeEIGA 90
Cdd:cd17684     1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKVPQ--NCIA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228  91 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 164
Cdd:cd17684    77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
21-164 6.98e-27

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: 106.74  E-value: 6.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  21 SIKGLIESAL-------SFGRTLDSDYPPLQQFFVVMEHCLKHGLKvRKSFLSYNKTIWGPLELVEKLYPEAEEIGA--S 91
Cdd:cd17671     2 AVKELLESFAdngeaddSAALTLTDDDPVVGRLCAALEAILSHGLK-PKRFGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228  92 VRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANL 164
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
537-597 8.12e-27

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 103.28  E-value: 8.12e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228  537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSCHALL 597
Cdd:smart00064   4 WIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
536-594 2.36e-23

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 93.20  E-value: 2.36e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 536 VWLKDKEATHCKLCEK-EFSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSCH 594
Cdd:cd15717     1 VWVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
533-593 2.49e-23

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 93.56  E-value: 2.49e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 533 QGLVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSC 593
Cdd:cd15731     1 DPPLWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYgqMKPVRVCNHC 63
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
537-594 3.13e-23

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 92.88  E-value: 3.13e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP--KPVRVCDSCH 594
Cdd:cd15733     1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQlyDPVRVCNSCY 60
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
541-594 7.29e-22

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 88.89  E-value: 7.29e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228 541 KEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP---SSPKPVRVCDSCH 594
Cdd:cd15760     3 KPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPhlgPLGVPQRVCDRCF 59
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
537-593 1.44e-21

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 88.16  E-value: 1.44e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSC 593
Cdd:cd15734     2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
537-593 3.04e-21

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 87.26  E-value: 3.04e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP--KPVRVCDSC 593
Cdd:cd15732     2 WVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQlfEPSRVCKSC 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
537-597 6.47e-21

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 86.67  E-value: 6.47e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS--SPKPVRVCDSCHALL 597
Cdd:cd15719     3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
545-594 9.31e-21

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 85.66  E-value: 9.31e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052793228 545 HCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS--SPKPVRVCDSCH 594
Cdd:cd00065     1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
536-593 3.69e-20

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 84.35  E-value: 3.69e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 536 VWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP--SSPKPVRVCDSC 593
Cdd:cd15727     3 PWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
13-165 9.12e-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: 9.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  13 NLLNMAKLSIKGLIESalSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYN--KTIWGPLELVEKLYPEAeeIGA 90
Cdd:cd17700     1 NLITVCRFSVKTLIDR--SCFETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHN--CIC 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228  91 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17700    77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
541-597 9.42e-19

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 80.12  E-value: 9.42e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228 541 KEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSCHALL 597
Cdd:cd15720     3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFgiEKEVRVCDPCYEKL 61
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
537-593 1.07e-18

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 79.91  E-value: 1.07e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 593
Cdd:cd15726     1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
546-594 1.71e-18

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed 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. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 79.38  E-value: 1.71e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 546 CKLCEKE-FSLSKRKHHCRNCGEIFCNACSDNELPLPSS-PKPVRVCDSCH 594
Cdd:cd15744     2 CSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSiYEPARVCDVCY 52
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
536-597 2.59e-18

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 79.31  E-value: 2.59e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 536 VWLKDKEATHCKLCEK-EFSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSCHALL 597
Cdd:cd15755     1 VWVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
13-165 4.67e-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: 81.23  E-value: 4.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  13 NLLNMAKLSIKGLIESALSfgRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYN--KTIWGPLELVEKLYPEaeEIGA 90
Cdd:cd17699     1 NLITVCRFSVKTLLEKYTA--EPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSDgqRGFWDYIRLACSKVPN--NCIS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228  91 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 165
Cdd:cd17699    77 SIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
536-593 8.64e-18

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 77.48  E-value: 8.64e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228 536 VWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSC 593
Cdd:cd15743     2 IWIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYlKNKSARVCDEC 60
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
546-594 1.02e-16

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 74.49  E-value: 1.02e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 546 CKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP--SSPKPVRVCDSCH 594
Cdd:cd15735     9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
537-599 2.21e-16

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 73.92  E-value: 2.21e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNElpLPSSP--KPVRVCDSCHALLIQ 599
Cdd:cd15739     4 WQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKT--VPSGPnrRPARVCDVCHTLLVK 66
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
536-597 3.03e-16

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 73.54  E-value: 3.03e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 536 VWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP-SSPKPVRVCDSCHALL 597
Cdd:cd15729     6 VWVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEyLDNKEARVCVPCYQTL 68
RUN smart00593
domain involved in Ras-like GTPase signaling;
105-167 8.04e-16

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 71.88  E-value: 8.04e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228  105 ARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANLCVK 167
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
537-594 5.53e-15

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 69.66  E-value: 5.53e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKP--VRVCDSCH 594
Cdd:cd15725     2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPgdLRVCTYCC 61
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
537-600 1.05e-14

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 68.91  E-value: 1.05e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNeLPLpsspkPVRVCDSCHALLIQR 600
Cdd:cd15716     4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQF-LPL-----HIRCCHHCKDLLERR 61
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
542-597 1.48e-14

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 68.22  E-value: 1.48e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228 542 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSCHALL 597
Cdd:cd15728     6 DGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFdlNKPVRVCDVCFDVL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
266-535 1.52e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.28  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 266 LMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQD 345
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 346 TLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECL 425
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 426 SKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQE 505
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
                         250       260       270
                  ....*....|....*....|....*....|
gi 1052793228 506 QALQELGNKLSESKLKIEDIKEANKALQGL 535
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGF 506
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
537-597 1.94e-14

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 68.28  E-value: 1.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 537 WLKDKEATHCKLCEKEF-SLSKRKHHCRNCGEIFCNACSDNELPLP-SSPKPVRVCDSCHALL 597
Cdd:cd15741     3 WVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKATLEyDGNKLNRVCKHCYVIL 65
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
537-594 3.27e-14

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 67.35  E-value: 3.27e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 537 WLKDKEATHCKlCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS--SPKPVRVCDSCH 594
Cdd:cd15738     3 WKSFRNVTECS-CSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
537-597 1.10e-13

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 66.13  E-value: 1.10e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 537 WLKDKEATHCKLC-EKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSCHALL 597
Cdd:cd15754     2 WIPDKATDICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
537-593 1.78e-13

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276 [Multi-domain]  Cd Length: 83  Bit Score: 65.99  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCN----ACS--------------------DNELPLPSSPKPVRVCDS 592
Cdd:cd15737     2 WEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCStevpldllssalpdlpfvfkEPQSDIPDDTKSVRVCRD 81

                  .
gi 1052793228 593 C 593
Cdd:cd15737    82 C 82
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
537-595 1.97e-13

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 65.23  E-value: 1.97e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 537 WLKDKEATHCKLCEKE-FSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSCHA 595
Cdd:cd15724     1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGyRENPVRVCDQCYE 61
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
546-593 3.40e-13

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 64.51  E-value: 3.40e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 546 CKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP------KPVRVCDSC 593
Cdd:cd15736     2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSAydprngKWYRCCHSC 55
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
545-593 2.93e-12

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; 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. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 61.36  E-value: 2.93e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 545 HCKLCEKEFSLSKRKHHCRNCGEIFCNACS--DNELPLPSSPKPVRVCDSC 593
Cdd:cd15745     1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSseDLVLSVPDTCIYLRVCKTC 51
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
546-600 3.69e-12

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 61.87  E-value: 3.69e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228 546 CKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSCHALLIQR 600
Cdd:cd15742    12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYlKDRPAKVCDGCFAELRKR 67
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
541-594 8.80e-11

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 57.72  E-value: 8.80e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228 541 KEATHCKLCEKEF-----------SLSKRKHHCRNCGEIFCNACSDNELPLPSS--PKPVRVCDSCH 594
Cdd:cd15718     4 AESDNCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMgfEFPVRVCNECY 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
184-476 2.14e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 184 LKNEEDIgnKERNVQIAAILDQKNYVEELNRQLN---STVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 260
Cdd:COG1196   218 LKEELKE--LEAELLLLKLRELEAELEELEAELEeleAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 261 EnKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 340
Cdd:COG1196   296 E-LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 341 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKY 420
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228 421 LQECLSKSDSLQKQisQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNE 476
Cdd:COG1196   455 EEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
328-554 1.37e-09

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: 61.23  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  328 EIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNkitaamrQLEQRLQQAE 407
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-------QLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  408 KAQMEAEDEDEKYLQEclskSDSLQKQISQKEKQLVQLETDLkiekewrQTLQEDLQKEKDALSHLRNETQQiisLKKEF 487
Cdd:TIGR02168  754 KELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQI-------EQLKEELKALREALDELRAELTL---LNEEA 819
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228  488 LNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIE-----------DIKEANKALQGLVWLKDKEATHCKLCEKEFS 554
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleeLIEELESELEALLNERASLEEALALLRSELE 897
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
546-594 1.56e-09

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 53.66  E-value: 1.56e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052793228 546 CKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPS-SPKPVRVCDSCH 594
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
22-164 1.80e-09

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: 56.47  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  22 IKGLIESALS-FGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLE-LVEKLYPEA---EEIGASVRDLP 96
Cdd:cd17682     2 LKGCVLDLKSeFGEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228  97 GLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMMEEEGAVI-VGLLVGLNVIDANL 164
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEIlLSLLYQLNEINFDL 150
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
539-593 5.88e-09

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 52.31  E-value: 5.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228 539 KDKEATHCKLCEKEF-SLSKRKHHCRNCGEIFCNACSDNElplPSSPKPVRVCDSC 593
Cdd:cd15740     1 REKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKCSEFK---DLASRHNRVCRDC 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
327-525 7.10e-09

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: 58.91  E-value: 7.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  327 HEIELAMKLLEKDIhEKQDTLIGLRQQLEEVKAINIemYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQA 406
Cdd:TIGR02168  196 NELERQLKSLERQA-EKAERYKELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  407 EKAQMEAEDEDEKY---LQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQ---- 479
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkee 352
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1052793228  480 IISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDI 525
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
187-527 8.19e-09

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: 58.93  E-value: 8.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  187 EEDIGNKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKnniiKLQEENHQLRSENKLIL 266
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLK----EKREYEGYELLKEKEAL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  267 MKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMK-HEIELAMKLLEKDIHEKQD 345
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  346 TLiglrQQLEEVKAINIEMYQKLQGSEDGLKEkneiiaRLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKyLQECL 425
Cdd:TIGR02169  316 EL----EDAEERLAKLEAEIDKLLAEIEELER------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE-FAETR 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  426 SKSDSLQKQISQKEKQLVQLETDLKiekewrqTLQEDLQKEKDALSHLRNETQQIISLKKEflnLQDENQQLKKIYHEQE 505
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELD-------RLQEELQRLSEELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQE 454
                          330       340
                   ....*....|....*....|..
gi 1052793228  506 QALQELGNKLSESKLKIEDIKE 527
Cdd:TIGR02169  455 WKLEQLAADLSKYEQELYDLKE 476
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
210-454 8.19e-09

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: 58.93  E-value: 8.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  210 EELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnklilmktqqhlevtKVDVETELQTYKH 289
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE---------------IEELEREIEEERK 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  290 SRQGLDEMYNEARRQLRDesqLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQ 369
Cdd:TIGR02169  351 RRDKLTEEYAELKEELED---LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  370 GSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYlqeclsksDSLQKQISQKEKQLVQLETDL 449
Cdd:TIGR02169  428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY--------DRVEKELSKLQRELAEAEAQA 499

                   ....*
gi 1052793228  450 KIEKE 454
Cdd:TIGR02169  500 RASEE 504
PRK11281 PRK11281
mechanosensitive channel MscK;
312-531 9.18e-09

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 58.77  E-value: 9.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  312 RQDVENELAVQVSMKHEiELAMKLLEKDIHEKQDTLiglrQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNK 391
Cdd:PRK11281    38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  392 ITAA------MRQLEQRLQQAEKAQMEAededekylQECLSKSDSL-----------QKQISQKEKQLVQLETDLK---- 450
Cdd:PRK11281   113 ETREtlstlsLRQLESRLAQTLDQLQNA--------QNDLAEYNSQlvslqtqperaQAALYANSQRLQQIRNLLKggkv 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  451 IEKEWRQTLQEDLQKEKDAL----SHLRNETQ---QIISLKKEFLNLQDENQQLKKiyhEQEQALQELGN----KLSESK 519
Cdd:PRK11281   185 GGKALRPSQRVLLQAEQALLnaqnDLQRKSLEgntQLQDLLQKQRDYLTARIQRLE---HQLQLLQEAINskrlTLSEKT 261
                          250
                   ....*....|...
gi 1052793228  520 LK-IEDIKEANKA 531
Cdd:PRK11281   262 VQeAQSQDEAARI 274
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
309-519 9.32e-09

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: 57.47  E-value: 9.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 309 SQLRQDVENELAvqvsmkhEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEK 388
Cdd:COG4942    19 ADAAAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 389 TNKITAAMRQLEQRLQQAEKAQMEAEDEDekYLQECLSKSDSLQ-------------------KQISQKEKQLVQLETDL 449
Cdd:COG4942    92 IAELRAELEAQKEELAELLRALYRLGRQP--PLALLLSPEDFLDavrrlqylkylaparreqaEELRADLAELAALRAEL 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 450 KIEKEWRQTLQEDLQKEKDALSHLRNETQQII-SLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESK 519
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKLLaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
279-534 1.04e-08

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: 58.54  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  279 DVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkheielamKLLEKDiHEKQdtliglRQQLEEVK 358
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI--------------EQLEQE-EEKL------KERLEELE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  359 AINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDED-EKYLQEC----------LSK 427
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIearlreieqkLNR 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  428 SDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQ-QIISLKKEFLNLQDENQQLKKIYHEQEQ 506
Cdd:TIGR02169  824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEAQLRELER 903
                          250       260
                   ....*....|....*....|....*...
gi 1052793228  507 ALQELGNKLSESKLKIEDIKEANKALQG 534
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSELKAKLEALEE 931
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
264-479 1.49e-08

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: 57.08  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 264 LILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEK 343
Cdd:COG4942     9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 344 QDTLIGLRQQLEEVKAINIEMYQKLQ--GSEDGLK------EKNEIIARLE------EKTNKITAAMRQLEQRLQQAEKA 409
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRALYrlGRQPPLAlllspeDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAE 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 410 QMEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQ 479
Cdd:COG4942   169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
21-142 1.54e-08

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: 53.79  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  21 SIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKvrksflSYNKTIWGPLelVEKLYPEAEEigaSVRDLPGLKT 100
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLR------RGNRGYWPFV--KEFTHKETIK---QIENLPNVTT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1052793228 101 PLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALM 142
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
95-160 1.55e-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: 54.16  E-value: 1.55e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228  95 LPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMM-EEEGAVIVGLLVGLNVI 160
Cdd:cd17689    93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
198-464 1.83e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.33  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 198 QIAAILDQ--KNYVEElnrqlnstvsSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEV 275
Cdd:COG3206   149 LAAAVANAlaEAYLEQ----------NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 276 TK-VDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQvsmkheielamkllekdihekqdtliGLRQQL 354
Cdd:COG3206   219 QQlSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--------------------------QLRAQL 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 355 EEVKAiniemyqKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSDSLQKQ 434
Cdd:COG3206   273 AELEA-------ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
                         250       260       270
                  ....*....|....*....|....*....|
gi 1052793228 435 ISQKEKQLVQLETDLKIEKEWRQTLQEDLQ 464
Cdd:COG3206   346 LPELEAELRRLEREVEVARELYESLLQRLE 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
184-533 1.88e-08

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: 57.34  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 184 LKNEEDIGNKERNvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENK 263
Cdd:TIGR04523  56 LKNLDKNLNKDEE-KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKK 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 264 lilmktqqHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQlrdesqlrqdvenelavqvsmKHEIELAMKLLEKDIHEK 343
Cdd:TIGR04523 135 --------ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ---------------------KEELENELNLLEKEKLNI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 344 QDTLIGLRQQLEEVKAI------NIEMYQKLQGSEDGLKEKN----EIIARLEEKTNKITAAMRQLEQRLQQAEKAQmea 413
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLlsnlkkKIQKNKSLESQISELKKQNnqlkDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ--- 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 414 eDEDEKYLQECLSKSDSLQKQISQKEKQLVQLET---DLKIEKE--WRQTLQEDLQKEKDALSHLRNE-----------T 477
Cdd:TIGR04523 263 -NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSeisDLNNQKEqdWNKELKSELKNQEKKLEEIQNQisqnnkiisqlN 341
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 478 QQIISLKKEFLNLQDENQ-----------QLKKIYHEQEQALQE---LGNKLSESKLKIEDIKEANKALQ 533
Cdd:TIGR04523 342 EQISQLKKELTNSESENSekqreleekqnEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQQKD 411
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
537-594 3.56e-08

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 50.84  E-value: 3.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 537 WLkdkEATHCKLCEKEF-----------SLSKRKHHCRNCGEIFCNACSD--NELPLPSSPKPVRVCDSCH 594
Cdd:cd15756     3 WL---ESDSCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSkrSSYPIMGFEFQVRVCDSCF 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
184-464 3.74e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 184 LKNEEDIGNKERNVQIAAILDQKNYVEELNRQLNS---TVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRS 260
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 261 EnklilmktQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDI 340
Cdd:COG1196   331 E--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 341 HEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKY 420
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1052793228 421 LQEclsksdsLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQ 464
Cdd:COG1196   483 LEE-------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
41-164 3.94e-08

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: 52.88  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  41 PPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDLPGLKTPLGRARAWLRLALMQKKMAD 120
Cdd:cd17697    26 PELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAE 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1052793228 121 YLRCLIIQRDLLSE-FYEYHALMMEEEGAVIVGLLVGLNVIDANL 164
Cdd:cd17697   106 SLQLCLLNPELTGEwYYARSPFLSPELRSDILDSLYELNGVNFDL 150
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
545-596 4.10e-08

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 49.67  E-value: 4.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052793228 545 HCKLCEKEFSLSKRKHHCRNCGEIFCNACsdnelpLPSSPKPVRVCDSCHAL 596
Cdd:cd15750     2 PCESCGAKFSVFKRKRTCADCKRYFCSNC------LSKEERGRRRCRRCRAL 47
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
209-535 4.32e-08

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: 56.60  E-value: 4.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  209 VEELNRQLNStvssLHSRVDSLEKSNTKLIE----ELAIAKNNIIKLQEENHQLRSEnklILMKTQQHLEVT--KVDVET 282
Cdd:TIGR02168  195 LNELERQLKS----LERQAEKAERYKELKAElrelELALLVLRLEELREELEELQEE---LKEAEEELEELTaeLQELEE 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  283 ELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEielamkllekdihekqdtligLRQQLEEVKAINI 362
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN---------------------LERQLEELEAQLE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  363 EMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEdekyLQECLSKSDSLQKQISQKEKQL 442
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLELQIASLNNEI 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  443 VQLETDLK-IEKEWRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLN-----LQDENQQLKKI---YHEQEQALQELGN 513
Cdd:TIGR02168  403 ERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeeLERLEEALEELreeLEEAEQALDAAER 482
                          330       340
                   ....*....|....*....|..
gi 1052793228  514 KLSESKLKIEDIKEANKALQGL 535
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLEGF 504
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
537-594 3.60e-07

FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain.


Pssm-ID: 277296 [Multi-domain]  Cd Length: 70  Bit Score: 47.75  E-value: 3.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 537 WLkdkEATHCKLCEKEF-----------SLSKRKHHCRNCGEIFCNACSD--NELPLPSSPKPVRVCDSCH 594
Cdd:cd15757     3 WL---DSDSCQKCDQPFfwnfkqmwdskKIGLRQHHCRKCGKAVCGKCSSkrSTIPLMGFEFEVRVCDSCH 70
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
546-597 8.08e-07

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 46.34  E-value: 8.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 546 CKLCEKEFS-LSKRKHHCRNCGEIFCNACSDNELP--LPSSPKP------VRVCDSCHALL 597
Cdd:cd15723     2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPrsVMGATAPaaqretVFVCSGCNDKL 62
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
279-471 9.99e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 279 DVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAvqvsmkhEIELAMKLLEKDIHEKQDTLiglRQQLEEVK 358
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAEI---EERREELG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 359 AINIEMYQK---------LQGSED--GLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSK 427
Cdd:COG3883    90 ERARALYRSggsvsyldvLLGSESfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1052793228 428 SDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALS 471
Cdd:COG3883   170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
382-533 1.12e-06

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: 51.98  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  382 IARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSD----------SLQKQISQKEKQLVQLETDLKI 451
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisalrkdlaRLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  452 EKEWRQTLQEDLQKEKDALSHLRnetQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKA 531
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                   ..
gi 1052793228  532 LQ 533
Cdd:TIGR02168  836 TE 837
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
99-164 1.60e-06

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: 48.36  E-value: 1.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228  99 KTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHALMM-EEEGAVIVGLLVGLNVIDANL 164
Cdd:cd17679    95 TTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGLESFQFEL 161
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
43-164 1.74e-06

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: 48.15  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  43 LQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGplELVEKLYPEAeeiGAS-----VRDLPGLKTPLGRARAWLRLALMQKK 117
Cdd:cd17698    36 LHKFCAKLEYLLQFDQKEKTTLLGGRKDYWD--YFCECLAKVK---GLNdgirfVKSLKEVRTSLGKGRAFIRYSLVHQR 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1052793228 118 MADYLR-CLIIQRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANL 164
Cdd:cd17698   111 LADTLQqCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
91-161 2.03e-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: 48.55  E-value: 2.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052793228  91 SVRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHA-LMMEEEGAVIVGLLVGLNVID 161
Cdd:cd17677   103 NVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVD 174
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
248-527 2.40e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.99  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  248 IIKLQEENHQLRSenkliLMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDvenelavqvsmkh 327
Cdd:pfam12128  243 FTKLQQEFNTLES-----AELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD------------- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  328 EIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDG----LKEKNEIIARLEEKTNKITAAMRQLEQRL 403
Cdd:pfam12128  305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSwqseLENLEERLKALTGKHQDVTAKYNRRRSKI 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  404 QQAEKAQMEAEDEDEKYLQECLSK-----SDSLQKQISQKEKQLVQLETDLKIEKE-------WRQTLQEDLQKEKDALS 471
Cdd:pfam12128  385 KEQNNRDIAGIKDKLAKIREARDRqlavaEDDLQALESELREQLEAGKLEFNEEEYrlksrlgELKLRLNQATATPELLL 464
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228  472 HLRN---------ETQQiiSLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKE 527
Cdd:pfam12128  465 QLENfderierarEEQE--AANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
92-161 3.29e-06

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: 48.13  E-value: 3.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228  92 VRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHA-LMMEEEGAVIVGLLVGLNVID 161
Cdd:cd17691   127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVD 197
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
188-559 3.33e-06

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: 50.02  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 188 EDIGNKERnvQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENklilm 267
Cdd:TIGR04523 314 SELKNQEK--KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI----- 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 268 ktqQHLEVTKVDVETELQTYKHSRQGLDEmynEARRQLRDESQLRQDVENELAVQVSMKHEIelamKLLEKDIHEKQDTL 347
Cdd:TIGR04523 387 ---KNLESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEI----KDLTNQDSVKELII 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 348 IGLRQQLEEVKaINIEMYQKLQGSED-GLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQmeaededekylQECLS 426
Cdd:TIGR04523 457 KNLDNTRESLE-TQLKVLSRSINKIKqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI-----------SSLKE 524
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 427 KSDSLQKQISQKEKQLVQLETDLKiekewrqTLQEDLQKEKdalshlrnetqqiisLKKEFLNLQDENQQLKKIYHEQEQ 506
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELN-------KDDFELKKEN---------------LEKEIDEKNKEIEELKQTQKSLKK 582
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 507 ALQELGNKLSESKLKIEDIKEANKALQGLVWLKDKEATHCKLCEKEFSLSKRK 559
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-470 3.39e-06

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: 50.44  E-value: 3.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  185 KNEEDIgnKERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKL 264
Cdd:TIGR02168  681 ELEEKI--EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  265 I----------LMKTQQHL---EVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIEL 331
Cdd:TIGR02168  759 LeaeieeleerLEEAEEELaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  332 AMKLLEKDIHEKQDTLIGL--------------RQQLEEVKAI--------------NIEMYQKLQGSEDGLKEKNEIIA 383
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLaaeieeleelieelESELEALLNErasleealallrseLEELSEELRELESKRSELRRELE 918
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  384 RLEEKTNKITAAMRQLEQRLQQ-----AEKAQMEAEDEDEKYlQECLSKSDSLQKQISQKEKQLVQL-------ETDLKI 451
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNlqerlSEEYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEE 997
                          330       340
                   ....*....|....*....|..
gi 1052793228  452 EKEWRQTL---QEDLQKEKDAL 470
Cdd:TIGR02168  998 LKERYDFLtaqKEDLTEAKETL 1019
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
537-593 3.57e-06

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 44.95  E-value: 3.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 537 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPL-------PSSPKPVRVCDSC 593
Cdd:cd15761     4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLnnsaeydPKNGKWCRCCEKC 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-526 3.58e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  338 KDIHEKQDTLIGLRQQLEEVKAINIEmYQKLQGSEDGLK--EKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAED 415
Cdd:COG4913    245 EDAREQIELLEPIRELAERYAAARER-LAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  416 EDEKYLQECLSKS----DSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQiisLKKEFLNLQ 491
Cdd:COG4913    324 ELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1052793228  492 DENQQLkkiYHEQEQALQELGNKLSESKLKIEDIK 526
Cdd:COG4913    401 EALEEA---LAEAEAALRDLRRELRELEAEIASLE 432
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
210-530 3.85e-06

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: 50.02  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 210 EELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLI---LMKTQQHLEVTK---VDVETE 283
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkkqLSEKQKELEQNNkkiKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 284 LQTYKHSRQGLD-----EMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEE-- 356
Cdd:TIGR04523 290 LNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 357 --VKAINIEMYQKLQGSEDGLKEKNEiiarLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSD---SL 431
Cdd:TIGR04523 370 neIEKLKKENQSYKQEIKNLESQIND----LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikDL 445
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 432 QKQISQKEKQLVQLETDLKIEKEWRQTL----------QEDLQKE-KDALSHLRNETQQIISLKKEFLNLQDENQQLKKI 500
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLsrsinkikqnLEQKQKElKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
                         330       340       350
                  ....*....|....*....|....*....|
gi 1052793228 501 YHEQEQALQELGNKLSESKLKIEDIKEANK 530
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELK 555
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
193-440 4.16e-06

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: 50.06  E-value: 4.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  193 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnklilmktQQH 272
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK--------LDE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  273 LEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQ 352
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  353 QLEEVKAINIEMYQKLQGSE-----DGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEdekyLQECLSK 427
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQLQAR 490
                          250
                   ....*....|...
gi 1052793228  428 SDSLQKQISQKEK 440
Cdd:TIGR02168  491 LDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
382-533 4.31e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 382 IARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQE 461
Cdd:COG1196   188 LERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 462 DLQKEKDALSHLRNE------------------TQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIE 523
Cdd:COG1196   268 ELEELRLELEELELEleeaqaeeyellaelarlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         170
                  ....*....|
gi 1052793228 524 DIKEANKALQ 533
Cdd:COG1196   348 EAEEELEEAE 357
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
208-540 1.10e-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: 48.58  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  208 YVEELNrQLNSTVSSLHSRVDSLEKSNTKLIEE----LAIAKNNIIKLQEENHQLRSENKLILMKTQQHL-EVTKVDVET 282
Cdd:pfam15921  315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEElekqLVLANSELTEARTERDQFSQESGNLDDQLQKLLaDLHKREKEL 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  283 ELQTYKHSRQGLDEMYNEA-----RRQLRDESQLRQDVEnelAVQVSMKHEIELAMKLLEKDIHEKQDTL---IGLRQQL 354
Cdd:pfam15921  394 SLEKEQNKRLWDRDTGNSItidhlRRELDDRNMEVQRLE---ALLKAMKSECQGQMERQMAAIQGKNESLekvSSLTAQL 470
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  355 EEVKAINIEMYQKLQGS----EDGLKEKNEIIARLEEK------TN-KITAAMRQLEQRLQQAEKAQMEAEdedekYLQE 423
Cdd:pfam15921  471 ESTKEMLRKVVEELTAKkmtlESSERTVSDLTASLQEKeraieaTNaEITKLRSRVDLKLQELQHLKNEGD-----HLRN 545
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  424 CLSKSDSLQKQISQKEKQlvqletdLKIEKEWRQTLQEDLQKEKDALSHLRNETQQiisLKKEFLNLQDENQQLKKIYHE 503
Cdd:pfam15921  546 VQTECEALKLQMAEKDKV-------IEILRQQIENMTQLVGQHGRTAGAMQVEKAQ---LEKEINDRRLELQEFKILKDK 615
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1052793228  504 QEQALQELGNKLSEskLKIEDIKEANKALQGLVWLKD 540
Cdd:pfam15921  616 KDAKIRELEARVSD--LELEKVKLVNAGSERLRAVKD 650
FYVE_CARP1 cd15769
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ...
546-596 1.23e-05

FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ubiquitin-protein ligase RNF34, or caspases-8 and -10-associated RING finger protein 1, or FYVE-RING finger protein Momo, or RING finger homologous to inhibitor of apoptosis protein (RFI), or RING finger protein 34, or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell, and negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric and colorectal cancers, suggesting a possible association with the development of the digestive tract cancers. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP1 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP1 harbors a C-terminal RING domain.


Pssm-ID: 277308  Cd Length: 47  Bit Score: 42.67  E-value: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1052793228 546 CKLCEKEFSLSKRKHHCRNCGEIFCNACSdnelplpSSPKPVRVCDSCHAL 596
Cdd:cd15769     4 CKACGLAFSVFRKKHVCCDCKKDFCSVCS-------VLQENLRRCSTCHLL 47
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
339-499 1.25e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.84  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 339 DIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDE 418
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 419 kyLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIIS-LKKEFLNLQDENQQL 497
Cdd:COG1579    91 --YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeLEAELEELEAEREEL 168

                  ..
gi 1052793228 498 KK 499
Cdd:COG1579   169 AA 170
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
366-533 1.40e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  366 QKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEkylqeclskSDSLQKQISQKEKQLVQL 445
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELERL 680
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  446 ETDLKIEKEWRQTLQEdLQKEKDALSHLRNE-TQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIED 524
Cdd:COG4913    681 DASSDDLAALEEQLEE-LEAELEELEEELDElKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759

                   ....*....
gi 1052793228  525 IKEANKALQ 533
Cdd:COG4913    760 GDAVERELR 768
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
193-395 1.81e-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: 47.45  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 193 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQH 272
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 273 LEVTKV----------DVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHE 342
Cdd:COG4942   117 GRQPPLalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 343 KQDTLIGLRQQLEEVKAinieMYQKLQGSEDGLKEKNEIIARLEEKTNKITAA 395
Cdd:COG4942   197 RQKLLARLEKELAELAA----ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
51-161 2.00e-05

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: 44.97  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  51 EHCLKHGLKVRKSFLSYNKTIWGPLELVEKLYPEAEEIGASVRDL------PGLKTPLGRARA-------------WLRL 111
Cdd:cd17687    31 DACLLHGLRKRALGLFRSSSTFSLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIRI 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 112 ALMQKKMadylrCLIIQrDLL---SEFYEYHALMME-EEGAVIVGLLVGLNVID 161
Cdd:cd17687   111 ALFEKVL-----DKIVD-YLVenaSKYYEKEALMADpVDGPLLASLLVGPCALD 158
PTZ00121 PTZ00121
MAEBL; Provisional
299-552 3.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  299 NEARR--QLRDESQLRQDVENELAVQVSMKHEIELA--MKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDG 374
Cdd:PTZ00121  1525 DEAKKaeEAKKADEAKKAEEKKKADELKKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  375 LKEKNEIIARLEEKTNKITAAMRQLEQRlqqAEKAQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQlvQLETDLKIEKE 454
Cdd:PTZ00121  1605 KKMKAEEAKKAEEAKIKAEELKKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKKAEE 1679
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  455 WRQTlQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQG 534
Cdd:PTZ00121  1680 AKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
                          250
                   ....*....|....*...
gi 1052793228  535 LVWLKDKEATHCKLCEKE 552
Cdd:PTZ00121  1759 IAHLKKEEEKKAEEIRKE 1776
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
252-467 3.54e-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: 47.04  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 252 QEENHQLRSENKLILMKTQQHLEVTKVD-------VETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVS 324
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMErqqknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 325 -MKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIAR-LEEKTNKITAAMRQ---L 399
Cdd:pfam17380 439 rLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEEERKrklL 518
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052793228 400 EQRLQQAEKAQMEAED----EDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEK 467
Cdd:pfam17380 519 EKEMEERQKAIYEEERrreaEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
PRK12704 PRK12704
phosphodiesterase; Provisional
389-527 4.68e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 389 TNKITAAMRQLEQRLQQAEK--------AQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEkewrqtlQ 460
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKeaeaikkeALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK-------L 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228 461 EDLQKEKDALSHLRNETQQiisLKKEFLNLQDEnqqLKKIYHEQEQALQELgnklseSKLKIEDIKE 527
Cdd:PRK12704  103 ELLEKREEELEKKEKELEQ---KQQELEKKEEE---LEELIEEQLQELERI------SGLTAEEAKE 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
198-481 4.70e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 4.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  198 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnkliLMKTQQHLEVTK 277
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARLSHSR 792
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  278 VD-VETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEE 356
Cdd:TIGR02169  793 IPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  357 VKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRL---------QQAEKAQMEAEDEDEKYLQECLSK 427
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLselkakleaLEEELSEIEDPKGEDEEIPEEELS 952
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1052793228  428 SDSLQKQISQKEKQLVQLE-TDLKIEKEWRQTL--QEDLQKEKDALSHLRNETQQII 481
Cdd:TIGR02169  953 LEDVQAELQRVEEEIRALEpVNMLAIQEYEEVLkrLDELKEKRAKLEEERKAILERI 1009
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
206-527 5.69e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 206 KNYVEELNRQLNSTVSSLHSRVDSLEKSntklIEELAIAKNniiKLQEENHQLRSENKLILMKtQQHLEVTkvDVETELQ 285
Cdd:PRK03918  400 KEEIEEEISKITARIGELKKEIKELKKA----IEELKKAKG---KCPVCGRELTEEHRKELLE-EYTAELK--RIEKELK 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 286 TykhsrqgLDEMYNEARRQLRDESQLRQDvENELAVQVSMKHEIELAMKLLEKDIHEKqdtLIGLRQQLEEVKAINIEMY 365
Cdd:PRK03918  470 E-------IEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLK 538
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 366 QKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQEcLSKSDSLQKQISQKEKQLVQL 445
Cdd:PRK03918  539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKE-LEPFYNEYLELKDAEKELERE 617
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 446 ETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIISL--KKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIE 523
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697

                  ....
gi 1052793228 524 DIKE 527
Cdd:PRK03918  698 KLKE 701
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
280-511 6.28e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 280 VETELQTYKHSRQGLDEMYNEARRQLRD-ESQLRQDVENELAVQVSMKHEIELamkllekdihekqDTLIGLRQQLEEVK 358
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQKNGLVDLSEEAKLLL-------------QQLSELESQLAEAR 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 359 AINIEMYQKLQGSEDGLKEKNEIIARLEEktnkiTAAMRQLEQRLQQAEkaqMEAEDEDEKY------LQECLSKSDSLQ 432
Cdd:COG3206   233 AELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELE---AELAELSARYtpnhpdVIALRAQIAALR 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 433 KQISQKEKQ-LVQLETDLKIEKEWRQTLQEDLQKEKDALSHLrNETQQiislkkEFLNLQDENQQLKKIYHEQEQALQEL 511
Cdd:COG3206   305 AQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAEL-PELEA------ELRRLEREVEVARELYESLLQRLEEA 377
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-478 6.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 295 DEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEevkaiNIEMYQKLQGSEDG 374
Cdd:COG4717    66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 375 LKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKE 454
Cdd:COG4717   141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
                         170       180
                  ....*....|....*....|....
gi 1052793228 455 WRQTLQEDLQKEKDALSHLRNETQ 478
Cdd:COG4717   221 ELEELEEELEQLENELEAAALEER 244
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
376-531 6.91e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 46.20  E-value: 6.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  376 KEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDE---------------------DEKYLQ---------ECL 425
Cdd:TIGR01612 1544 KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakndksnkaaidiqlslenfENKFLKisdikkkinDCL 1623
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  426 SKSDSLQKQISQkeKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYheqE 505
Cdd:TIGR01612 1624 KETESIEKKISS--FSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNY---E 1698
                          170       180
                   ....*....|....*....|....*..
gi 1052793228  506 QALQELGNKLSES-KLKIEDIKEANKA 531
Cdd:TIGR01612 1699 IGIIEKIKEIAIAnKEEIESIKELIEP 1725
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
384-536 6.96e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 384 RLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQEclSKSDSLQKQISQKEKQLVQLETDLkiekewrQTLQEDL 463
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQL-------AEARAEL 235
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 464 QKEKDALSHLRNETQQIISLKKEFLNlQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQGLV 536
Cdd:COG3206   236 AEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL 307
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
371-533 7.44e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 371 SEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEdekyLQECLSKSDSLQKQISQKEKQLVQLETDLK 450
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE----LEALQAEIDKLQAEIAEAEAEIEERREELG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 451 iekEWRQTLQED-----------------------------LQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKiy 501
Cdd:COG3883    90 ---ERARALYRSggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA-- 164
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1052793228 502 hEQEQALQELGNKLSESKLKIEDIKEANKALQ 533
Cdd:COG3883   165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
342-527 1.00e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 342 EKQDTLIGLRQQLEEVKAIniEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAE------D 415
Cdd:PRK02224  184 DQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiE 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 416 EDEKYLQECLSKSDSLQKQISQKEKQLVQLE---TDLKIEKEWRQTLQEDLQKEKDALSHLRNETQ-------------- 478
Cdd:PRK02224  262 DLRETIAETEREREELAEEVRDLRERLEELEeerDDLLAEAGLDDADAEAVEARREELEDRDEELRdrleecrvaaqahn 341
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052793228 479 -QIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKE 527
Cdd:PRK02224  342 eEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
46 PHA02562
endonuclease subunit; Provisional
197-476 1.24e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.01  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 197 VQIAAILDQ--KNYVEELNRQLnSTVSSLHSRVDSLEKSNTKLIEEL-AIAKNNIIKLQEENHQLRSENKLILM-KTQQH 272
Cdd:PHA02562  162 ISVLSEMDKlnKDKIRELNQQI-QTLDMKIDHIQQQIKTYNKNIEEQrKKNGENIARKQNKYDELVEEAKTIKAeIEELT 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 273 LEVTKVDVETELQTykhsrqgldemynEARRQLRDEsqlrqdvenelAVQVSMKheielaMKLLEKDI--HEKQDTLIGL 350
Cdd:PHA02562  241 DELLNLVMDIEDPS-------------AALNKLNTA-----------AAKIKSK------IEQFQKVIkmYEKGGVCPTC 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 351 RQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAmrqleQRLQQAEKAQMEAEDEDekyLQECLSKSDS 430
Cdd:PHA02562  291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQ-----SKKLLELKNKISTNKQS---LITLVDKAKK 362
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1052793228 431 LQKQISqkekqlvQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNE 476
Cdd:PHA02562  363 VKAAIE-------ELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
335-542 2.12e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 335 LLEKDIHEKQDTLIGLRQQLEEvkaINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAE 414
Cdd:COG4717    46 MLLERLEKEADELFKPQGRKPE---LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 415 DEDEKYlqeclsksdSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEdLQKEKDALSHLRNETQQIISLKKEFLNLQDEN 494
Cdd:COG4717   123 KLLQLL---------PLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEE 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052793228 495 --QQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQGLVWLKDKE 542
Cdd:COG4717   193 elQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
383-536 2.17e-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: 44.28  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  383 ARLEEKTNKITAAMRQLE-----QRLQQAEKAQMEAEDEDEKYLQEClsksDSLQKQISQKEKQLVQLETdlkiEKEWRQ 457
Cdd:TIGR02168  209 AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEEL----EELTAELQELEEKLEELRL----EVSELE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  458 TLQEDLQKEKDALSHLRNE-TQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQGLV 536
Cdd:TIGR02168  281 EEIEELQKELYALANEISRlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
46 PHA02562
endonuclease subunit; Provisional
354-527 2.25e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 354 LEEVKAINIEMYQKLQgsEDGLKEKNEIIARLEEKTNKITAAMRQLE------QRLQQAE---KAQMEAEDEDEKYLQE- 423
Cdd:PHA02562  207 QRKKNGENIARKQNKY--DELVEEAKTIKAEIEELTDELLNLVMDIEdpsaalNKLNTAAakiKSKIEQFQKVIKMYEKg 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 424 -----CLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQE------DLQKEKDAL-SHLRNETQQIISLKKEFLNLQ 491
Cdd:PHA02562  285 gvcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdefnEQSKKLLELkNKISTNKQSLITLVDKAKKVK 364
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1052793228 492 DENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKE 527
Cdd:PHA02562  365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
153-524 2.32e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.18  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 153 LLVGLNVIDANLCVKGEDLDSQVGVIDFSMYLKNEEDIGNKERNVQIAAILDQKNYVEELnRQLNSTVSSLHSRVDSLEK 232
Cdd:COG5185    60 LRSVINVLDGLNYQNDVKKSESSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADIL-ISLLYLYKSEIVALKDELI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 233 SNTKLIEELAIAKNNIIKLQEENH--QLRSENKLILMKTQQH---LEVTKVDVETELQTYKHSRQGLDEMYNEARrQLRD 307
Cdd:COG5185   139 KVEKLDEIADIEASYGEVETGIIKdiFGKLTQELNQNLKKLEifgLTLGLLKGISELKKAEPSGTVNSIKESETG-NLGS 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 308 ESQLRQDVENELavqvsmkhEIELAMKLLEKDIHEkqdtlIGLRQQLEEVKAINIEMYQKLqgSEDGLKEKNEIIARLEE 387
Cdd:COG5185   218 ESTLLEKAKEII--------NIEEALKGFQDPESE-----LEDLAQTSDKLEKLVEQNTDL--RLEKLGENAESSKRLNE 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 388 KTNKITAAMRQLEQRLQQAEKAQ-MEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEwrqTLQEDLQKE 466
Cdd:COG5185   283 NANNLIKQFENTKEKIAEYTKSIdIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQE---SLTENLEAI 359
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228 467 KDALSHLRNEtqQIISLKKEflNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIED 524
Cdd:COG5185   360 KEEIENIVGE--VELSKSSE--ELDSFKDTIESTKESLDEIPQNQRGYAQEILATLED 413
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
226-414 2.44e-04

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: 44.34  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 226 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQ-----LRSENKLILMKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNE 300
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 301 ARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLI--GLRQQLEEVKAINIEMYQKLQGSEDGLKEK 378
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQEQMRKAT 562
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1052793228 379 NEiIARLEEKTNKitaamRQLEQRLQQAEKAQMEAE 414
Cdd:pfam17380 563 EE-RSRLEAMERE-----REMMRQIVESEKARAEYE 592
46 PHA02562
endonuclease subunit; Provisional
334-533 2.57e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 334 KLLEKDIHEKQDTLIGLRQQLEEVKAiNIEMYQKLQGSEDglKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEA 413
Cdd:PHA02562  170 KLNKDKIRELNQQIQTLDMKIDHIQQ-QIKTYNKNIEEQR--KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 414 EDEDEKYlqeclskSDSLQKQISQKEKQLVQLETDLKIEKEWRQ-----TLQEDLQKEKDALSHLRNETQQIISLKKEFL 488
Cdd:PHA02562  247 VMDIEDP-------SAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLD 319
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1052793228 489 NLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQ 533
Cdd:PHA02562  320 TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK 364
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
394-527 2.76e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.92  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 394 AAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKsdsLQKQISQKEKQLVQLEtdlkieKEWrqtlqedlQKEKDALshl 473
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEASFERLAE---LRDELAELEEELEALK------ARW--------EAEKELI--- 470
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 474 rnetQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESkLKIEDIKE 527
Cdd:COG0542   471 ----EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE-VTEEDIAE 519
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
366-536 3.47e-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: 43.21  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 366 QKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEdekyLQECLSKSDSLQKQISQKEKQLVQL 445
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----LAALEAELAELEKEIAELRAELEAQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 446 ETDLK--IEKEWRQTLQEDL------QKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSE 517
Cdd:COG4942   103 KEELAelLRALYRLGRQPPLalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
                         170
                  ....*....|....*....
gi 1052793228 518 SKLKIEDIKEANKALQGLV 536
Cdd:COG4942   183 LEEERAALEALKAERQKLL 201
COG5022 COG5022
Myosin heavy chain [General function prediction only];
396-560 3.61e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  396 MRQLEQRLQQAEKAQMEAEDEDEKyLQECLSKSDSLQKQISQKEKQLvqlETDLKIEKEWrqtLQEDLQKEKDALSHLRN 475
Cdd:COG5022    870 YLQSAQRVELAERQLQELKIDVKS-ISSLKLVNLELESEIIELKKSL---SSDLIENLEF---KTELIARLKKLLNNIDL 942
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  476 ETQQIISL--KKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQGLVWLKDKEATHCKLCEKEF 553
Cdd:COG5022    943 EEGPSIEYvkLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELP 1022

                   ....*..
gi 1052793228  554 SLSKRKH 560
Cdd:COG5022   1023 VEVAELQ 1029
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
252-527 3.93e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  252 QEENHQLRSENkliLMKTQQHLEvtkvDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIEL 331
Cdd:pfam01576    3 QEEEMQAKEEE---LQKVKERQQ----KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  332 AMKLLEKDIHEK--------------QDTLIGLRQQLEEVKAINiemyQKLQ----GSEDGLKEKNEIIARLEEKTNKIT 393
Cdd:pfam01576   76 ILHELESRLEEEeersqqlqnekkkmQQHIQDLEEQLDEEEAAR----QKLQlekvTTEAKIKKLEEDILLLEDQNSKLS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  394 AAMRQLEQRLQQAEKAQMEAEDedekylqeclsKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHL 473
Cdd:pfam01576  152 KERKLLEERISEFTSNLAEEEE-----------KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228  474 RNET----QQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKE 527
Cdd:pfam01576  221 QEQIaelqAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
193-480 4.58e-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: 43.09  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 193 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENkLILMKTQQH 272
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI-IKNNSEIKD 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 273 LEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLE---KDIHEKQDTLIG 349
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEekvKDLTKKISSLKE 524
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 350 LRQQLEEVKAiniEMYQKLQGSEDGLKEKNEIIAR--LEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQEclsk 427
Cdd:TIGR04523 525 KIEKLESEKK---EKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE---- 597
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1052793228 428 SDSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRNETQQI 480
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
193-419 4.59e-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: 42.83  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 193 KERNVQIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKlilmKTQQH 272
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 273 LEVTKVDVETELQT-YKHSRQGLDEMYnearrqlrdesqLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLR 351
Cdd:COG4942    99 LEAQKEELAELLRAlYRLGRQPPLALL------------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052793228 352 QQLEEVKAINIEMYQKLQGSEDGL----KEKNEIIARLEEKTNKITAAMRQL---EQRLQQA-EKAQMEAEDEDEK 419
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALealkAERQKLLARLEKELAELAAELAELqqeAEELEALiARLEAEAAAAAER 242
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
219-476 4.66e-04

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: 43.57  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  219 TVSSLHSRvdSLEKSNTKLIEEL----AIAKNNIIKLQEENHQLRSE--NKLILMKTQQHLEVTKVDVETELQTykhsrQ 292
Cdd:pfam15921  209 SMSTMHFR--SLGSAISKILRELdteiSYLKGRIFPVEDQLEALKSEsqNKIELLLQQHQDRIEQLISEHEVEI-----T 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  293 GLDEMYNEARRQLRD-ESQLRqdvenelAVQVSMKHEIELAMKLLEkdihEKQDTLIGLRQQLEEVKainiEMYqklqgs 371
Cdd:pfam15921  282 GLTEKASSARSQANSiQSQLE-------IIQEQARNQNSMYMRQLS----DLESTVSQLRSELREAK----RMY------ 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  372 EDGLKEkneiiarleektnkitaamrqLEQRLQQAEKAQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQlvqlETDLKI 451
Cdd:pfam15921  341 EDKIEE---------------------LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR----EKELSL 395
                          250       260
                   ....*....|....*....|....*
gi 1052793228  452 EKEWRQTLQEDLQKEKDALSHLRNE 476
Cdd:pfam15921  396 EKEQNKRLWDRDTGNSITIDHLRRE 420
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
379-535 5.01e-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: 42.83  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 379 NEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKylqeclsksdsLQKQISQKEKQLVQLETDLK-IEKEWRQ 457
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-----------LERRIAALARRIRALEQELAaLEAELAE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 458 T------LQEDLQKEKDALSHL--------RNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIE 523
Cdd:COG4942    88 LekeiaeLRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
                         170
                  ....*....|..
gi 1052793228 524 DIKEANKALQGL 535
Cdd:COG4942   168 ELEAERAELEAL 179
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
297-535 5.32e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 297 MYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEvkainiemyqklqgsedgLK 376
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE------------------LE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 377 EKNEIIARLEEKTNKITAAMRQLEQRLQQAekaqmeaededEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWR 456
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKLEEKIREL-----------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 457 QTLQE--DLQKEKDALSHLRNETQQIIS-----------LKKEFLNLQDENQQLKKIYHEQEQALQELGNKLS-ESKLKI 522
Cdd:PRK03918  304 EYLDElrEIEKRLSRLEEEINGIEERIKeleekeerleeLKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTG 383
                         250
                  ....*....|...
gi 1052793228 523 EDIKEANKALQGL 535
Cdd:PRK03918  384 LTPEKLEKELEEL 396
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
337-495 6.30e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 337 EKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQgsedgLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEkaqmeaedE 416
Cdd:COG4717    87 EEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEALEAELAELPERLEELE--------E 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 417 DEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWR--------QTLQEDLQKEKDALSHLRNE----TQQIISLK 484
Cdd:COG4717   154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEEleelEEELEQLE 233
                         170
                  ....*....|.
gi 1052793228 485 KEFLNLQDENQ 495
Cdd:COG4717   234 NELEAAALEER 244
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
229-533 9.80e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 9.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  229 SLEKSNTKLIEELAIAKNNIIKLQEENHQLrsENKLILMKTQQHLEVTKVDVETELQTYKHSrqgldeMYNEARRQLRDE 308
Cdd:pfam01576  128 TTEAKIKKLEEDILLLEDQNSKLSKERKLL--EERISEFTSNLAEEEEKAKSLSKLKNKHEA------MISDLEERLKKE 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  309 SQLRQdvenelavqvsmkhEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKE----KNEIIAR 384
Cdd:pfam01576  200 EKGRQ--------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqKNNALKK 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  385 LEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKY------LQECLSKSDSLQKQISQKEKQLVQLETDLKIE-KEWRQ 457
Cdd:pfam01576  266 IRELEAQISELQEDLESERAARNKAEKQRRDLGEELealkteLEDTLDTTAAQQELRSKREQEVTELKKALEEEtRSHEA 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  458 TLQEDLQKEKDALSHLRNETQQI-----------ISLKKEFLNLQDENQQLKKIYHE-------QEQALQELGNKLSESK 519
Cdd:pfam01576  346 QLQEMRQKHTQALEELTEQLEQAkrnkanlekakQALESENAELQAELRTLQQAKQDsehkrkkLEGQLQELQARLSESE 425
                          330
                   ....*....|....
gi 1052793228  520 LKIEDIKEANKALQ 533
Cdd:pfam01576  426 RQRAELAEKLSKLQ 439
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
301-535 9.91e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  301 ARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEK------DIHEKQDTLIGLRQQLEEVKAINiEMYQKLQGSEDG 374
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqRLAEYSWDEIDVASAEREIAELE-AELERLDASSDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  375 LKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEdekyLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKE 454
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  455 WRQTLQEDLQKEKDAL-SHLRNETQQIISLKKEFLN---------------LQDENQQLKKIY----HEQEQALQELGNK 514
Cdd:COG4913    763 VERELRENLEERIDALrARLNRAEEELERAMRAFNRewpaetadldadlesLPEYLALLDRLEedglPEYEERFKELLNE 842
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1052793228  515 LSE-------SKLK--IEDIKEA----NKALQGL 535
Cdd:COG4913    843 NSIefvadllSKLRraIREIKERidplNDSLKRI 876
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
204-506 1.09e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 204 DQKNYVEELNRQLNSTVSSLHSRVDSLE--KSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILmktqQHLEVTKVDVE 281
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELE 550
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 282 TELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELavqvsmkHEIELAMKLLEkDIHEKQDTLIGLRQQLEEVKAIN 361
Cdd:PRK02224  551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-------ESLERIRTLLA-AIADAEDEIERLREKREALAELN 622
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 362 IEmyqklqgSEDGLKEKNEIIARLEEKTNKitAAMRQLEQRLQQAEKAQMEAEDEdekyLQECLSKSDSLQKQISQkekq 441
Cdd:PRK02224  623 DE-------RRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEK----LDELREERDDLQAEIGA---- 685
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228 442 lvqletdlkiekewrqtlqedlqkekdalshLRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQ 506
Cdd:PRK02224  686 -------------------------------VENELEELEELRERREALENRVEALEALYDEAEE 719
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
92-161 1.16e-03

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: 40.76  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052793228  92 VRDLPGLKTPLGRARAWLRLALMQKKMADYLRCLIIQRDLLSEFYEYHA-LMMEEEGAVIVGLLVGLNVID 161
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVD 200
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
328-531 1.29e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 40.43  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 328 EIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLqgsedglkekNEIIARLEEKTNKITAAMRQLEQRL---- 403
Cdd:pfam04012  19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRL----------EQQTEQAKKLEEKAQAALTKGNEELarea 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 404 -QQAEKAQMEAEDEDEKyLQECLSKSDSLQKQISQKEKQLVQLETDLKIEK--EWRQTLQEDLQKEKDALShlrneTQQI 480
Cdd:pfam04012  89 lAEKKSLEKQAEALETQ-LAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKarLKAAKAQEAVQTSLGSLS-----TSSA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 481 ISLKKEFLNLQDENQQLKKIYHEQEQAlQELGNKLSESKLKI---EDIKEANKA 531
Cdd:pfam04012 163 TDSFERIEEKIEEREARADAAAELASA-VDLDAKLEQAGIQMevsEDVLARLKA 215
mukB PRK04863
chromosome partition protein MukB;
192-454 1.40e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  192 NKERNVQIAAILDQknyvEELNRQLNSTVSSLHSRVDSLEK--------SNTKLIEELAIAKNNIIKLQEENHQLRSENK 263
Cdd:PRK04863   843 NRRRVELERALADH----ESQEQQQRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAEEAKRFVQQHGN 918
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  264 LiLMKTQQHLEVTKVDvETELQTYKHSRQGLDEMYNEARRQLRDESQLRQdVENELAVqvsmkheiELAMKLLEKDihek 343
Cdd:PRK04863   919 A-LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ-RRAHFSY--------EDAAEMLAKN---- 983
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  344 QDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQ--------AEKAQMEAED 415
Cdd:PRK04863   984 SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgAEERARARRD 1063
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1052793228  416 EDEKYLQECLSKSDSLQKQISQKE-------KQLVQLETDLKIEKE 454
Cdd:PRK04863  1064 ELHARLSANRSRRNQLEKQLTFCEaemdnltKKLRKLERDYHEMRE 1109
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
530-594 1.52e-03

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 41.61  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  530 KALQGLVWLKDKEAT-HCKLCEKEF-SLSK----RKHHCRNCGEIFCNAC-------SDNELPLPSSPKPVR---VCDSC 593
Cdd:PTZ00303   446 KLLHNPSWQKDDESSdSCPSCGRAFiSLSRplgtRAHHCRSCGIRLCVFCitkrahySFAKLAKPGSSDEAEerlVCDTC 525

                   .
gi 1052793228  594 H 594
Cdd:PTZ00303   526 Y 526
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
281-560 1.69e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  281 ETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAI 360
Cdd:TIGR00618  562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  361 NIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKY----LQECLSKSDSLQKQIS 436
Cdd:TIGR00618  642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtlLRELETHIEEYDREFN 721
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  437 QKEKQLVQLETDLKIEKEWRQTLQEDLQKEKD-ALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKL 515
Cdd:TIGR00618  722 EIENASSSLGSDLAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL 801
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1052793228  516 SESKLKIE---DIKEANKALQGLVWLKDKEATHCKLCEKEFSLSKRKH 560
Cdd:TIGR00618  802 KTLEAEIGqeiPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
191-519 1.73e-03

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: 41.64  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  191 GNKERnvQIAAILDQKNYVEElnrqlnstVSSLHSRVDSLEKSNTKLIEELAIAKNNI-----------IKLQEENHQLR 259
Cdd:pfam15921  444 GQMER--QMAAIQGKNESLEK--------VSSLTAQLESTKEMLRKVVEELTAKKMTLessertvsdltASLQEKERAIE 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  260 SENKLIL-------MKTQ--QHLEVTK---VDVETELQTYKHSRQGLDEMYNEARRQLRDESQL-RQDVENELAVQVSMK 326
Cdd:pfam15921  514 ATNAEITklrsrvdLKLQelQHLKNEGdhlRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvGQHGRTAGAMQVEKA 593
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  327 H-EIELAMKLLE----KDIHEKQDTLIGLRQ------QLEEVKAINI----------------EMYQKLQGSE---DGLK 376
Cdd:pfam15921  594 QlEKEINDRRLElqefKILKDKKDAKIRELEarvsdlELEKVKLVNAgserlravkdikqerdQLLNEVKTSRnelNSLS 673
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  377 EKNEIIAR--------LEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLsksdSLQKQISQKEKQLVQLETD 448
Cdd:pfam15921  674 EDYEVLKRnfrnkseeMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM----GMQKQITAKRGQIDALQSK 749
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052793228  449 LKIEKEWRQTLQED---LQKEKDALSH-LRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESK 519
Cdd:pfam15921  750 IQFLEEAMTNANKEkhfLKEEKNKLSQeLSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQ 824
PRK12704 PRK12704
phosphodiesterase; Provisional
334-461 1.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 334 KLLEKDIHEKQDTLIGLRQQlEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKaQMEA 413
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEE-AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-KLEL 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1052793228 414 EDEDEKYLQEclsksdsLQKQISQKEKQLVQLETDL-KIEKEWRQTLQE 461
Cdd:PRK12704  105 LEKREEELEK-------KEKELEQKQQELEKKEEELeELIEEQLQELER 146
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
342-532 2.04e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 342 EKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYL 421
Cdd:COG1340    47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 422 QECLSKSD--SLQKQISQKEKQLVQLETDLKIEKEWRQTLQEdLQKEKDALSHLRNE-----------TQQIISLKKEFL 488
Cdd:COG1340   127 TEVLSPEEekELVEKIKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKikelaeeaqelHEEMIELYKEAD 205
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1052793228 489 NLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKAL 532
Cdd:COG1340   206 ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
237-463 2.15e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 237 LIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEvtkvDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVE 316
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 317 NELAVqvsmkHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKainiEMYQKLQGSEDGLKEKNEIIARLEEKTNKIT-AA 395
Cdd:COG4717   123 KLLQL-----LPLYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATeEE 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228 396 MRQLEQRLQQAEKAQMEAEDEDEKylqeclsksdsLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDL 463
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEE-----------AQEELEELEEELEQLENELEAAALEERLKEARL 250
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
279-437 2.70e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 279 DVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAvqvsmkhEIELAMKLLEKDIHEKQDTLIGLRQQLEEVK 358
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 359 ------AINIEMYQ---KLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSD 429
Cdd:COG1579    87 nnkeyeALQKEIESlkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166

                  ....*...
gi 1052793228 430 SLQKQISQ 437
Cdd:COG1579   167 ELAAKIPP 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
328-539 2.75e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 328 EIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAE 407
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 408 KAQMEAEDEDEKYLQEclskSDSLQKQISQKEKQLVQLETDLK--------IEKEWRQTLQEDLQKEKDALSHLRNETQQ 479
Cdd:COG4372   122 KERQDLEQQRKQLEAQ----IAELQSEIAEREEELKELEEQLEslqeelaaLEQELQALSEAEAEQALDELLKEANRNAE 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 480 IISLKKEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKEANKALQGLVWLK 539
Cdd:COG4372   198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
376-533 2.95e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 376 KEK-NEIIARLEEKTnkitaamRQLEQRLQQAEKAQMEAEDEDEKYLQeclsksdslqkqisQKEKQlvqletdlkieKE 454
Cdd:PRK00409  515 KEKlNELIASLEELE-------RELEQKAEEAEALLKEAEKLKEELEE--------------KKEKL-----------QE 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 455 WRQTLQEDLQKE-KDALSHLRNETQQIISLKKEFLNLQDENQQLkkiyHEQEQALQELGNKLSESKLKIEDIKEANKALQ 533
Cdd:PRK00409  563 EEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
203-528 3.04e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  203 LDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQlrsenklilmktqqhlevtkvdVET 282
Cdd:TIGR00618  357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT----------------------IDT 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  283 ELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMK-HEIELAMKLLEKDihEKQDTLIGLRQQLEEVKAIN 361
Cdd:TIGR00618  415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKERE--QQLQTKEQIHLQETRKKAVV 492
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  362 IEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKyLQECLSKSDSLQKQIS---QK 438
Cdd:TIGR00618  493 LARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ-LTSERKQRASLKEQMQeiqQS 571
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  439 EKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHLRN---ETQQIISLKKEF-LNLQDENQQLKKIyhEQEQALQELGNK 514
Cdd:TIGR00618  572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDmlaCEQHALLRKLQPeQDLQDVRLHLQQC--SQELALKLTALH 649
                          330
                   ....*....|....
gi 1052793228  515 LSESKLKIEDIKEA 528
Cdd:TIGR00618  650 ALQLTLTQERVREH 663
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
216-511 3.10e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  216 LNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLILMKTQQHLEVTKvdVETELQTYKHSRQGLD 295
Cdd:TIGR00618  210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE--LRAQEAVLEETQERIN 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  296 EMYNEARRQLRDE--SQLRQDVENELAvqvsmkhEIELAMKLLEKDIHEKQDTligLRQQLEEVKAINIEmyQKLQGSED 373
Cdd:TIGR00618  288 RARKAAPLAAHIKavTQIEQQAQRIHT-------ELQSKMRSRAKLLMKRAAH---VKQQSSIEEQRRLL--QTLHSQEI 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  374 GLKEKNEIIARLEEKTNKITAamrqLEQRLQQAEKaQMEAEDEDEKYLQECLSKSDSLQKQI-------SQKEKQLVQLE 446
Cdd:TIGR00618  356 HIRDAHEVATSIREISCQQHT----LTQHIHTLQQ-QKTTLTQKLQSLCKELDILQREQATIdtrtsafRDLQGQLAHAK 430
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228  447 TDLKIEKEW----RQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQEL 511
Cdd:TIGR00618  431 KQQELQQRYaelcAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
187-450 3.77e-03

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: 40.49  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  187 EEDIGNKERNVQIAAILDQKNyveelnrqlNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKlil 266
Cdd:pfam15921  596 EKEINDRRLELQEFKILKDKK---------DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK--- 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  267 mKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRD-ESQLRQDVENELAVQVSMKHEIELAMKlLEKDIHEKQD 345
Cdd:pfam15921  664 -TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAMG-MQKQITAKRG 741
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  346 TLIGLR---QQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQaEKAQME-AEDEDEKYL 421
Cdd:pfam15921  742 QIDALQskiQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE-KVANMEvALDKASLQF 820
                          250       260
                   ....*....|....*....|....*....
gi 1052793228  422 QEClskSDSLQKQISQKEKQLVQLETDLK 450
Cdd:pfam15921  821 AEC---QDIIQRQEQESVRLKLQHTLDVK 846
ADK_lid pfam05191
Adenylate kinase, active site lid; Comparisons of adenylate kinases have revealed a particular ...
562-600 4.18e-03

Adenylate kinase, active site lid; Comparisons of adenylate kinases have revealed a particular divergence in the active site lid. In some organizms, particularly the Gram-positive bacteria, residues in the lid domain have been mutated to cysteines and these cysteine residues are responsible for the binding of a zinc ion. The bound zinc ion in the lid domain, is clearly structurally homologous to Zinc-finger domains. However, it is unclear whether the adenylate kinase lid is a novel zinc-finger DNA/RNA binding domain, or that the lid bound zinc serves a purely structural function.


Pssm-ID: 461578 [Multi-domain]  Cd Length: 36  Bit Score: 35.13  E-value: 4.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1052793228 562 CRNCGEIFcnacsdNELPLPssPKPVRVCDSCHALLIQR 600
Cdd:pfam05191   4 CPKCGRIY------HVYFNP--PKVEGVCDVCGGELVQR 34
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
204-527 4.30e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.09  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 204 DQKNYVEELNRqlnstVSSLHSRVDSLEKSNTKLIEELAIAKNNiiKLQEENHQLRSENKLILMKTQQHLEVTKV--DVE 281
Cdd:pfam05483 332 EKEAQMEELNK-----AKAAHSFVVTEFEATTCSLEELLRTEQQ--RLEKNEDQLKIITMELQKKSSELEEMTKFknNKE 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 282 TELQTYKhSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMK----HEIELAMKLLEKDIHEKQDTLIGLRQQLEEV 357
Cdd:pfam05483 405 VELEELK-KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 358 KAINIEMYQK----LQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQ---MEAEDEDEKYLQECLSKSDS 430
Cdd:pfam05483 484 KLKNIELTAHcdklLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekeMNLRDELESVREEFIQKGDE 563
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 431 LQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQkekdalshlrNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQE 510
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCN----------NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNA 633
                         330
                  ....*....|....*..
gi 1052793228 511 LGNKLSESKLKIEDIKE 527
Cdd:pfam05483 634 YEIKVNKLELELASAKQ 650
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
216-557 4.40e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  216 LNSTVSSLHSRVDSLEKSNTKLIEELAIAKNniiKLQEENHQlrsenKLILMKTQQHLEVTKVDVETELQTYKHSRqgld 295
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQ-----KNNALKKIRELEAQISELQEDLESERAAR---- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  296 emyNEARRQLRDESQ----LRQDVENEL---AVQVSM--KHEIELAM--KLLEKD--IHEKQ---------DTLIGLRQQ 353
Cdd:pfam01576  288 ---NKAEKQRRDLGEeleaLKTELEDTLdttAAQQELrsKREQEVTElkKALEEEtrSHEAQlqemrqkhtQALEELTEQ 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  354 LEEVKAINIEMYQKLQGSEdglKEKNEIIARL----------EEKTNKITAAMRQLEQRLQQAEKAQMEAEDEdekyLQE 423
Cdd:pfam01576  365 LEQAKRNKANLEKAKQALE---SENAELQAELrtlqqakqdsEHKRKKLEGQLQELQARLSESERQRAELAEK----LSK 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  424 CLSKSDSLQKQISQKEKQLVQLETDLkiekewrQTLQEDLQkekDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHE 503
Cdd:pfam01576  438 LQSELESVSSLLNEAEGKNIKLSKDV-------SSLESQLQ---DTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEE 507
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228  504 QEQA-------LQELGNKLSESKLKIED-------IKEANKALQglvwlKDKEATHCKLCEKEFSLSK 557
Cdd:pfam01576  508 EEEAkrnverqLSTLQAQLSDMKKKLEEdagtleaLEEGKKRLQ-----RELEALTQQLEEKAAAYDK 570
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
177-530 4.64e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.42  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  177 VIDFSMYLKNEEDIGNKERNvqIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEK-SNTKLIEELAIAKNNIIKLQEEN 255
Cdd:TIGR01612 1158 VADKAISNDDPEEIEKKIEN--IVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEvKGINLSYGKNLGKLFLEKIDEEK 1235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  256 ----HQLRSENKLI-----LMKTQQHLEV---TKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDvENELAVQV 323
Cdd:TIGR01612 1236 kkseHMIKAMEAYIedldeIKEKSPEIENemgIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-SLKIIEDF 1314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  324 SMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKAIniemYQKLQgsedgLKEKNEIIARLEEKTNKITAAMRQLEQRL 403
Cdd:TIGR01612 1315 SEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANI----YNILK-----LNKIKKIIDEVKEYTKEIEENNKNIKDEL 1385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  404 QQAEKaqMEAEDEDEKYLQECLSKSDSL--QKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEKDALSHL-------R 474
Cdd:TIGR01612 1386 DKSEK--LIKKIKDDINLEECKSKIESTldDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLfkniemaD 1463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  475 NETQQIISLKKE--------FLNLQDEN------------------QQLKKIYHEQEQALQELGNKLSESKLK------- 521
Cdd:TIGR01612 1464 NKSQHILKIKKDnatndhdfNINELKEHidkskgckdeadknakaiEKNKELFEQYKKDVTELLNKYSALAIKnkfaktk 1543
                          410
                   ....*....|....*
gi 1052793228  522 ------IEDIKEANK 530
Cdd:TIGR01612 1544 kdseiiIKEIKDAHK 1558
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
216-454 4.71e-03

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: 39.75  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 216 LNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSEnkliLMKTQQHLEVTKVDVETELQTYKHSRQGLD 295
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 296 EMYNEARRQLRDESQLRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDTLIGLRQQLEEVKainiEMYQKLQGSEDGL 375
Cdd:COG4942    87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR----EQAEELRADLAEL 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052793228 376 KEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKE 454
Cdd:COG4942   163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
427-535 4.77e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 427 KSDSLQKQISQKEKQLVQLEtdlkIEKEwrqtlqeDLQKEKDALSHLRNEtqqiiSLKKEFLNLQDENQQLKKIYHEQEQ 506
Cdd:COG0542   405 EIDSKPEELDELERRLEQLE----IEKE-------ALKKEQDEASFERLA-----ELRDELAELEEELEALKARWEAEKE 468
                          90       100
                  ....*....|....*....|....*....
gi 1052793228 507 ALQELGNKLSESKLKIEDIKEANKALQGL 535
Cdd:COG0542   469 LIEEIQELKEELEQRYGKIPELEKELAEL 497
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
336-533 4.81e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 336 LEKDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKtnkITAAMRQLEQRLQQAEKAQ----- 410
Cdd:COG3883    28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERARALYRSGgsvsy 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 411 ----MEAEDedekyLQECLSKSDSLQKQISQKEKQLVQLETDlkiekewrqtlQEDLQKEKDALshlRNETQQIISLKKE 486
Cdd:COG3883   105 ldvlLGSES-----FSDFLDRLSALSKIADADADLLEELKAD-----------KAELEAKKAEL---EAKLAELEALKAE 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1052793228 487 FLNLQDENQQLKKiyhEQEQALQELGNKLSESKLKIEDIKEANKALQ 533
Cdd:COG3883   166 LEAAKAELEAQQA---EQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
193-527 4.87e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.81  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 193 KERNVQIAAILDQKNYVEELNRQLNSTVSSL------HSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRSENKLIL 266
Cdd:pfam10174  49 KEEAARISVLKEQYRVTQEENQHLQLTIQALqdelraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 267 MKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQLRDESQLRQDVENELAVQVSMKhEIELAMKLLEKDIHEKQDT 346
Cdd:pfam10174 129 AKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIA-EAEMQLGHLEVLLDQKEKE 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 347 LIGLRQqleevkainiEMYQKLQGSEDGLKEK--NEIIARLEEKTNKITAAMRQLEQRLQ-------------QAEKAQM 411
Cdd:pfam10174 208 NIHLRE----------ELHRRNQLQPDPAKTKalQTVIEMKDTKISSLERNIRDLEDEVQmlktngllhtedrEEEIKQM 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 412 EAEDEDEKYLQeclSKSDSLQKQISQKEKQLVQLETDLKI-------EKEWRQTLQED----------LQKEKDALSHLR 474
Cdd:pfam10174 278 EVYKSHSKFMK---NKIDQLKQELSKKESELLALQTKLETltnqnsdCKQHIEVLKESltakeqraaiLQTEVDALRLRL 354
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052793228 475 NETQQIISLK-KEFLNLQDENQQLKKIYHEQEQALQELGNKLSESKLKIEDIKE 527
Cdd:pfam10174 355 EEKESFLNKKtKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQE 408
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
209-541 5.41e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.03  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  209 VEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNiiKLQEENHQLRSENKLILMKTqqhlEVTKVDVETELQTYK 288
Cdd:TIGR01612  919 VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKES--NLIEKSYKDKFDNTLIDKIN----ELDKAFKDASLNDYE 992
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  289 HSRQGLDEMYNEARRQL---RDESQLRQDVENELAVQ-VSMKHE--------IELAMKLLEKDIHEKQDTLIG-----LR 351
Cdd:TIGR01612  993 AKNNELIKYFNDLKANLgknKENMLYHQFDEKEKATNdIEQKIEdanknipnIEIAIHTSIYNIIDEIEKEIGknielLN 1072
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  352 QQLEEVKAINIEMYQKLQ-----------GSEDGLKEKNEIiarleektNKITAAMRQLEQRLQQAEKAQMEAEDEDEKY 420
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKeklkhynfddfGKEENIKYADEI--------NKIKDDIKNLDQKIDHHIKALEEIKKKSENY 1144
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  421 LQEclsksdsLQKQISQKEK---QLVQLETDLKIEKEwRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLqdenQQL 497
Cdd:TIGR01612 1145 IDE-------IKAQINDLEDvadKAISNDDPEEIEKK-IENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSL----EEV 1212
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1052793228  498 KKIYHEQEQALQELG-NKLSESKLKIED-IKEANKALQGLVWLKDK 541
Cdd:TIGR01612 1213 KGINLSYGKNLGKLFlEKIDEEKKKSEHmIKAMEAYIEDLDEIKEK 1258
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
198-419 5.49e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 198 QIAAILDQKNYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEEnhqlrsenkliLMKTQQHLEVTK 277
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-----------IAEAEAEIEERR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 278 VDVETELQTYKhsRQGLDEMYNEArrqLRDESQLRQDVENELAVQVSMKHEIELaMKLLEKDIHEKQDTLIGLRQQLEEV 357
Cdd:COG3883    86 EELGERARALY--RSGGSVSYLDV---LLGSESFSDFLDRLSALSKIADADADL-LEELKADKAELEAKKAELEAKLAEL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052793228 358 KAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDEK 419
Cdd:COG3883   160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
FYVE_CARP2 cd15770
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ...
546-574 5.89e-03

FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ubiquitin-protein ligase rififylin, or caspases-8 and -10-associated RING finger protein 2, or FYVE-RING finger protein Sakura (Fring), or RING finger and FYVE-like domain-containing protein 1, or RING finger protein 189, or RING finger protein 34-like, is a novel caspase regulator containing a FYVE-type zinc finger domain. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP2 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP2 harbors a C-terminal RING domain.


Pssm-ID: 277309  Cd Length: 49  Bit Score: 35.21  E-value: 5.89e-03
                          10        20
                  ....*....|....*....|....*....
gi 1052793228 546 CKLCEKEFSLSKRKHHCRNCGEIFCNACS 574
Cdd:cd15770     4 CKACGIRFASCARKHPCMDCKKNYCTACS 32
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
382-533 6.12e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 38.92  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 382 IARLEEKTNKITAAMRQLEQRLQQA--EKAQMEAEDEDEKYLQECLSKSDSLQKQISQKEKQLVQLETDLKIEKEWRQTL 459
Cdd:pfam15294 135 IERLKEENEKLKERLKTLESQATQAldEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNASTAL 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 460 QEDLQKEkdalshlrnetqqIISLKKEFLNLQDEnqqlkkiyheQEQALQELGNKLSESKL----------KIEDIKEAN 529
Cdd:pfam15294 215 QKSLEED-------------LASTKHELLKVQEQ----------LEMAEKELEKKFQQTAAyrnmkemltkKNEQIKELR 271

                  ....
gi 1052793228 530 KALQ 533
Cdd:pfam15294 272 KRLS 275
COG5022 COG5022
Myosin heavy chain [General function prediction only];
207-564 6.55e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.68  E-value: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  207 NYVEELNRQLNSTVSSLHSRVDSLEKSNTKLIEELaiaknnIIKLQEENHQLRSENKLILMKTQQHLEVTKVDVETELQT 286
Cdd:COG5022    895 SSLKLVNLELESEIIELKKSLSSDLIENLEFKTEL------IARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKE 968
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  287 YKHSRQGLDEMYNEARRQLRDESQLrqdvenelavqvsmkheielamkllekdIHEKQDTLIGLRQQleevkainiemYQ 366
Cdd:COG5022    969 TSEEYEDLLKKSTILVREGNKANSE----------------------------LKNFKKELAELSKQ-----------YG 1009
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  367 KLQGSEDGLKEKNEIIARLEEKTNKI--TAAMRQLEQRLQQAEKAQMEAEDEDEK-YLQECLSKSDSL--QKQISQKEKQ 441
Cdd:COG5022   1010 ALQESTKQLKELPVEVAELQSASKIIssESTELSILKPLQKLKGLLLLENNQLQArYKALKLRRENSLldDKQLYQLEST 1089
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  442 LVQLET----DLKIEKEWRQTLQEDLQKEKDALSHLRNETQQIISLKKEFLNLQDENQQLKKIYHEQEQALQELGNK--- 514
Cdd:COG5022   1090 ENLLKTinvkDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEalp 1169
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052793228  515 -------LSESKLKIEDI-KEANKALQGLVwlKDKEATHCKLCEKEFSLSKRKHHCRN 564
Cdd:COG5022   1170 spppfaaLSEKRLYQSALyDEKSKLSSSEV--NDLKNELIALFSKIFSGWPRGDKLKK 1225
mukB PRK04863
chromosome partition protein MukB;
226-512 6.72e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 6.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  226 RVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLrseNKLIlmktQQHLEVT-KVDVETELQTykhSRQGLDEMYNEARRQ 304
Cdd:PRK04863   787 RIEQLRAEREELAERYATLSFDVQKLQRLHQAF---SRFI----GSHLAVAfEADPEAELRQ---LNRRRVELERALADH 856
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  305 LRDESQLRQDVENeLAVQVSMKHEIELAMKLLEKDIHekQDTLIGLRQQLE--EVKAINIEMYQKLqgsedgLKEKNEII 382
Cdd:PRK04863   857 ESQEQQQRSQLEQ-AKEGLSALNRLLPRLNLLADETL--ADRVEEIREQLDeaEEAKRFVQQHGNA------LAQLEPIV 927
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  383 ARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEDE--------KY--LQECLSKSDSLQKQISQKekqLVQLETDlkie 452
Cdd:PRK04863   928 SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYedAAEMLAKNSDLNEKLRQR---LEQAEQE---- 1000
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  453 kewRQTLQEDLqkeKDALSHLRNETQQIISLKKEFLNLQDENQQLKkiyheqeQALQELG 512
Cdd:PRK04863  1001 ---RTRAREQL---RQAQAQLAQYNQVLASLKSSYDAKRQMLQELK-------QELQDLG 1047
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
253-518 7.58e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  253 EENHQLRSENKLILMKTQQHLEVTKVDVE---TELQTYKhsrQGLDEM------YNEARRQLRDESQLRQdvENELAVQV 323
Cdd:COG3096    364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDslkSQLADYQ---QALDVQqtraiqYQQAVQALEKARALCG--LPDLTPEN 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  324 SMKHEIELAMKLLEKDihekqDTLIGLRQQL---EEVKAINIEMYQKLQG------SEDGLKEKNEIIAR------LEEK 388
Cdd:COG3096    439 AEDYLAAFRAKEQQAT-----EEVLELEQKLsvaDAARRQFEKAYELVCKiageveRSQAWQTARELLRRyrsqqaLAQR 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  389 TNKITAAMRQLEQRLQQAEKAQmeaededekylqeclsksdSLQKQISQKEKQLVQLETDLKIEKEWRQTLQEDLQKEkd 468
Cdd:COG3096    514 LQQLRAQLAELEQRLRQQQNAE-------------------RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQ-- 572
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1052793228  469 alshLRNETQQIISLKKEFLNLQDENQQLKK---IYHEQEQALQELGNKLSES 518
Cdd:COG3096    573 ----AAEAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLREQSGEA 621
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
187-441 7.86e-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: 39.28  E-value: 7.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  187 EEDIGNKERNVQIAAILDQKNYVEElnrqlnsTVSSLHSRVDSLEKSNTKLIEELAIAKNNIIKLQEENHQLRsENKLIL 266
Cdd:TIGR02169  781 LNDLEARLSHSRIPEIQAELSKLEE-------EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-EQIKSI 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  267 MKTQQHLEVTKVDVETELQTYKHSRQGLDEMYNEARRQlrdesqlRQDVENELAVQVSMKHEIELAMKLLEKDIHEKQDT 346
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------RDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228  347 LIGLRQQLEEvkainiemYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLE-------QRLQQAEKAQMEAEDEDEK 419
Cdd:TIGR02169  926 LEALEEELSE--------IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
                          250       260
                   ....*....|....*....|..
gi 1052793228  420 YLQEclskSDSLQKQISQKEKQ 441
Cdd:TIGR02169  998 LEEE----RKAILERIEEYEKK 1015
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
338-535 9.73e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 338 KDIHEKQDTLIGLRQQLEEVKAINIEMYQKLQGSEDGLKEKNEIIARLEEKTNKITAAMRQLEQRLQQAEKAQMEAEDEd 417
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL- 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052793228 418 EKYLQECLSKSDSLQKQISQKEKQLVQLE------TDLKIEKEWRQTLQEDLQKEKDALSHLRNE----TQQIISLKKEF 487
Cdd:PRK03918  251 EGSKRKLEEKIRELEERIEELKKEIEELEekvkelKELKEKAEEYIKLSEFYEEYLDELREIEKRlsrlEEEINGIEERI 330
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1052793228 488 LNLQDENQQLKKIYHEQEQALQELgNKLSESKLKIEDIKEANKALQGL 535
Cdd:PRK03918  331 KELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERL 377
 
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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