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Conserved domains on  [gi|2024499897|ref|XP_040526812|]
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protein RUFY3 isoform X2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
108-263 2.06e-100

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: 303.84  E-value: 2.06e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
606-655 5.65e-22

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: 89.40  E-value: 5.65e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 606 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSI-NPERVCNPCH 655
Cdd:cd15744     1 SCSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-540 1.90e-11

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.39  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  283 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 359
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  360 SSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 439
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  440 LRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDR-----------------QLAQQDNRL 502
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleallneraslEEALALLRS 894
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2024499897  503 FKQEFGDKINSLQLEVEELSRQRSHLELELKRERERWS 540
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
flhF super family cl35529
flagellar biosynthesis protein FlhF;
4-128 7.32e-05

flagellar biosynthesis protein FlhF;


The actual alignment was detected with superfamily member PRK06995:

Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 45.73  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897   4 AERAPLLPPPAESSRDGM-AAETPPGMERRAEPGPEEAAVTEEEDEARPASPPFFLLYPGHGGAAAPHGAWRPPAPRGGA 82
Cdd:PRK06995   61 AAQPPPAAAPAAVSRPAApAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024499897  83 ALPVLLLSYPGPDGASAHPNYLMANERMnlmnMAKL-SIKGLIESAL 128
Cdd:PRK06995  141 RPRVPADAAAAVADAVKARIERIVNDTV----MQELrSLRGMLEEQL 183
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
108-263 2.06e-100

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: 303.84  E-value: 2.06e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
143-266 1.54e-44

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: 155.51  E-value: 1.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 143 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 213
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 214 KKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 266
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
606-655 5.65e-22

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: 89.40  E-value: 5.65e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 606 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSI-NPERVCNPCH 655
Cdd:cd15744     1 SCSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
203-265 2.96e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 79.19  E-value: 2.96e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499897  203 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 265
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
604-658 1.56e-11

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: 60.14  E-value: 1.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897  604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN--PERVCNPCHKQL 658
Cdd:smart00064  10 VSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIerPVRVCDDCYENL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-540 1.90e-11

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: 67.39  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  283 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 359
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  360 SSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 439
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  440 LRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDR-----------------QLAQQDNRL 502
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleallneraslEEALALLRS 894
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2024499897  503 FKQEFGDKINSLQLEVEELSRQRSHLELELKRERERWS 540
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
296-538 8.32e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 8.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 296 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRT 375
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 376 ADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD 455
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 456 mgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRE 535
Cdd:COG1196   393 ---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                  ...
gi 2024499897 536 RER 538
Cdd:COG1196   469 LEE 471
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
604-658 1.53e-10

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: 57.39  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI---NPERVCNPCHKQL 658
Cdd:pfam01363   9 ATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
298-537 9.91e-08

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: 55.61  E-value: 9.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  298 TAILDQKNYVEELNRHLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKeessyilesnRKVTKDRTAD 377
Cdd:pfam12128  611 EALQSAREKQAAAEEQLVQ----ANGELEKASREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAER 676
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  378 GQALTEARKQL-KEETQLRLDVEKELEAQigMRQEMELAMKMLEKD---VCEKQDALVALRQQLDDLRAlkhelSFKLQS 453
Cdd:pfam12128  677 KDSANERLNSLeAQLKQLDKKHQAWLEEQ--KEQKREARTEKQAYWqvvEGALDAQLALLKAAIAARRS-----GAKAEL 749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  454 SDMGVKQKSELNSR--LEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELE 531
Cdd:pfam12128  750 KALETWYKRDLASLgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ 829

                   ....*.
gi 2024499897  532 LKRERE 537
Cdd:pfam12128  830 LARLIA 835
mukB PRK04863
chromosome partition protein MukB;
319-544 5.15e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.96  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  319 NNLQAKVDALEKSNTKLTEELAVANNRI------ITLQEEMERVK---EESSYILESNRKVTKDrTADGQALTEARKQLK 389
Cdd:PRK04863   310 VEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQadlEELEERLEEQNEVVEE-ADEQQEENEARAEAA 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  390 EETQLRL-----DVEKELEAQIGMRQEMELAMKMLEK-------------DVCEKQDALVALRQQLDD-LRALKHelsfK 450
Cdd:PRK04863   389 EEEVDELksqlaDYQQALDVQQTRAIQYQQAVQALERakqlcglpdltadNAEDWLEEFQAKEQEATEeLLSLEQ----K 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  451 LQSSDMGVKQKS-----------------------ELNSRLEEKTNQmAATIKQLEQRLRQAEKDRQLAQQDNRL---FK 504
Cdd:PRK04863   465 LSVAQAAHSQFEqayqlvrkiagevsrseawdvarELLRRLREQRHL-AEQLQQLRMRLSELEQRLRQQQRAERLlaeFC 543
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2024499897  505 QEFGDKINS---LQLEVEELSRQRSHLELELKRERERWSHSHQ 544
Cdd:PRK04863   544 KRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQ 586
flhF PRK06995
flagellar biosynthesis protein FlhF;
4-128 7.32e-05

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 45.73  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897   4 AERAPLLPPPAESSRDGM-AAETPPGMERRAEPGPEEAAVTEEEDEARPASPPFFLLYPGHGGAAAPHGAWRPPAPRGGA 82
Cdd:PRK06995   61 AAQPPPAAAPAAVSRPAApAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024499897  83 ALPVLLLSYPGPDGASAHPNYLMANERMnlmnMAKL-SIKGLIESAL 128
Cdd:PRK06995  141 RPRVPADAAAAVADAVKARIERIVNDTV----MQELrSLRGMLEEQL 183
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
383-521 7.23e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  383 EARKQLKEEtqLRLDVEKELEaqiGMRQEMELAMKMLEK------DVCEKQDALVALRQQL------------DDLRALK 444
Cdd:smart00787 136 EWRMKLLEG--LKEGLDENLE---GLKEDYKLLMKELELlnsikpKLRDRKDALEEELRQLkqledeledcdpTELDRAK 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  445 HELS-------FKLQSSDMGVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAEKDRqlaqQDNRLFKQefgDKINSLQLE 517
Cdd:smart00787 211 EKLKkllqeimIKVKKLEELEEELQELESKIEDLTNK----KSELNTEIAEAEKKL----EQCRGFTF---KEIEKLKEQ 279

                   ....
gi 2024499897  518 VEEL 521
Cdd:smart00787 280 LKLL 283
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
108-263 2.06e-100

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: 303.84  E-value: 2.06e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
108-263 2.95e-98

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: 298.05  E-value: 2.95e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
108-262 5.66e-96

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: 292.17  E-value: 5.66e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 262
Cdd:cd17681    81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
108-263 2.82e-93

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: 285.26  E-value: 2.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17694    81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
143-266 1.54e-44

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: 155.51  E-value: 1.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 143 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 213
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 214 KKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 266
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
111-262 3.52e-36

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: 132.91  E-value: 3.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 111 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 188
Cdd:cd17684     1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 189 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 262
Cdd:cd17684    77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
119-262 4.29e-33

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: 124.46  E-value: 4.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 119 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 189
Cdd:cd17671     2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 190 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANF 262
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
111-263 4.57e-26

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: 104.28  E-value: 4.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 111 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 188
Cdd:cd17700     1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 189 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17700    77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
111-263 1.81e-23

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: 97.02  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 111 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 187
Cdd:cd17699     1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17699    76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
606-655 5.65e-22

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: 89.40  E-value: 5.65e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 606 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSI-NPERVCNPCH 655
Cdd:cd15744     1 SCSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
602-655 4.06e-20

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: 84.36  E-value: 4.06e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 602 GNAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCH 655
Cdd:cd15721     5 KEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
RUN smart00593
domain involved in Ras-like GTPase signaling;
203-265 2.96e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 79.19  E-value: 2.96e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499897  203 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 265
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
603-665 8.95e-18

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: 78.14  E-value: 8.95e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 603 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQLIQQYSTS 665
Cdd:cd15759     9 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
604-663 9.98e-18

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: 77.80  E-value: 9.98e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQLIQQYS 663
Cdd:cd15758    12 ATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
120-259 1.41e-17

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: 79.96  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 120 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 194
Cdd:cd17682     2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 195 GLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 259
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
109-255 5.82e-14

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: 70.31  E-value: 5.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 109 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 176
Cdd:cd17679     1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 177 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGL 255
Cdd:cd17679    81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
193-258 2.57e-12

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: 65.33  E-value: 2.57e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 193 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVI 258
Cdd:cd17689    93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
607-655 3.73e-12

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: 61.39  E-value: 3.73e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN--PERVCNPCH 655
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSgkPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
604-658 1.56e-11

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: 60.14  E-value: 1.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897  604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN--PERVCNPCHKQL 658
Cdd:smart00064  10 VSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIerPVRVCDDCYENL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-540 1.90e-11

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: 67.39  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  283 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 359
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  360 SSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 439
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  440 LRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDR-----------------QLAQQDNRL 502
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleallneraslEEALALLRS 894
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2024499897  503 FKQEFGDKINSLQLEVEELSRQRSHLELELKRERERWS 540
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
604-658 5.60e-11

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: 58.18  E-value: 5.60e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQL 658
Cdd:cd15730     9 VQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
149-259 5.65e-11

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: 61.53  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 149 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 208
Cdd:cd17687    31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 209 LALMQKKLSEYMKALINRKdllSEFYEPNALMME-EEGAIIAGLLVGLNVID 259
Cdd:cd17687   110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
312-616 5.75e-11

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: 65.86  E-value: 5.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  312 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvTKDRTADGQALTEARKQLKEE 391
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  392 -TQLRLDVEKELEAQIGMRQEMelamKMLEKDVCEKQDALVALRQQLDDLRAlkHELSFKLQSSDMGVKQKSELNSRLEE 470
Cdd:TIGR02169  739 lEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEA 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  471 KTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKqefgDKINSLQLEVEELSRQRSHLELELKR---------------E 535
Cdd:TIGR02169  813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKKEELEEELEEleaalrdlesrlgdlK 888
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  536 RERWSH-SHQSSQGNKKGPKNWLKPDGKLRIQDENAKLkQAPREENSVLPHKLQSSTQEEQEQPSGPGNAQICQLCQEES 614
Cdd:TIGR02169  889 KERDELeAQLRELERKIEELEAQIEKKRKRLSELKAKL-EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967

                   ..
gi 2024499897  615 SR 616
Cdd:TIGR02169  968 RA 969
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
148-258 5.96e-11

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: 60.97  E-value: 5.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 148 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRK 227
Cdd:cd17697    35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2024499897 228 DLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 258
Cdd:cd17697   115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
119-240 6.70e-11

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: 60.72  E-value: 6.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 119 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 198
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2024499897 199 PVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALM 240
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
296-538 8.32e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 8.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 296 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRT 375
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 376 ADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD 455
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 456 mgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRE 535
Cdd:COG1196   393 ---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                  ...
gi 2024499897 536 RER 538
Cdd:COG1196   469 LEE 471
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
603-655 1.10e-10

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: 57.54  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 603 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLP--SSINPERVCNPCH 655
Cdd:cd15735     5 DSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
604-658 1.53e-10

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: 57.39  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI---NPERVCNPCHKQL 658
Cdd:pfam01363   9 ATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
607-654 2.29e-10

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: 56.58  E-value: 2.29e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI--NPERVCNPC 654
Cdd:cd15731    14 CMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
287-540 3.99e-10

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: 63.15  E-value: 3.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  287 STKGSEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLES 366
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----LKA 800
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  367 NRKvtkdrtadgqALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHE 446
Cdd:TIGR02168  801 LRE----------ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  447 LSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQqdnrlfkqefgDKINSLQLEVEELSRQRS 526
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR-----------EKLAQLELRLEGLEVRID 939
                          250
                   ....*....|....
gi 2024499897  527 HLeleLKRERERWS 540
Cdd:TIGR02168  940 NL---QERLSEEYS 950
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
114-262 5.66e-10

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: 58.55  E-value: 5.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 114 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPL-ELVEKlVPEAAE 185
Cdd:cd17698     2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFcECLAK-VKGLND 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499897 186 ITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 262
Cdd:cd17698    81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
154-263 6.68e-10

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: 58.95  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 154 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 225
Cdd:cd17677    65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2024499897 226 RKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 263
Cdd:cd17677   140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
607-658 8.29e-10

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: 55.09  E-value: 8.29e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPE-RVCNPCHKQL 658
Cdd:cd15720     8 CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKfGIEKEvRVCDPCYEKL 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-544 1.20e-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: 61.61  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  304 KNYVEELNRHLSAtVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTE 383
Cdd:TIGR02168  263 QELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  384 ARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD-------- 455
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerlqq 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  456 --------MGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFkQEFGDKINSLQLEVEELSRQRSH 527
Cdd:TIGR02168  422 eieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQEN 500
                          250
                   ....*....|....*..
gi 2024499897  528 LELELKRERERWSHSHQ 544
Cdd:TIGR02168  501 LEGFSEGVKALLKNQSG 517
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
607-655 1.93e-09

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: 53.97  E-value: 1.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSS--INPERVCNPCH 655
Cdd:cd15733    10 CFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
604-654 3.37e-09

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: 53.36  E-value: 3.37e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSS--INPERVCNPC 654
Cdd:cd15732     8 AASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
604-658 4.36e-09

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: 53.16  E-value: 4.36e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPS--SINPERVCNPCHKQL 658
Cdd:cd15719     9 GDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
607-654 7.78e-09

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: 52.33  E-value: 7.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSS--INPERVCNPC 654
Cdd:cd15734    11 CSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-538 9.56e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 9.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 308 EELNRhLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvtkdRTADGQALTEARKQ 387
Cdd:COG1196   281 LELEE-AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE--------------LEELEEELEELEEE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 388 LKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSsdmgvkQKSELNSR 467
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA------LLERLERL 419
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 468 LEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERER 538
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
128-261 9.95e-09

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 54.58  E-value: 9.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 128 LNLGRTLD--SDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGR 204
Cdd:cd17686     6 LLLSRSSNvwSTYGGLQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGR 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 205 AWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 261
Cdd:cd17686    85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
606-654 1.84e-08

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: 50.96  E-value: 1.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 606 ICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINP--ERVCNPC 654
Cdd:cd15745     1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
607-660 2.16e-08

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: 51.19  E-value: 2.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQLIQ 660
Cdd:cd15739    13 CPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
604-654 2.26e-08

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: 50.84  E-value: 2.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLP--SSINPERVCNPC 654
Cdd:cd15727    10 CPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
190-263 5.00e-08

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: 53.91  E-value: 5.00e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 190 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 263
Cdd:cd17691   127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
308-596 9.32e-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: 55.41  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 308 EELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQ 387
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 388 LKE--------ETQLRLDVEKELEAQIGMRQ------------------EMELAMKMLEKDVCEKQDALVALRQQL---- 437
Cdd:TIGR04523 290 LNQlkseisdlNNQKEQDWNKELKSELKNQEkkleeiqnqisqnnkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 438 DDLRALKHELSFKLQSSDMGVKQKSELNSRL---EEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGD---KI 511
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDltnQD 449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 512 NSLQLEVEELSRQRSHLELELKRERERWSHSHQSSQGNKKGPKNwlKPDGKLRIQDENAKLKqaprEENSVLPHKLQSST 591
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS--KEKELKKLNEEKKELE----EKVKDLTKKISSLK 523

                  ....*
gi 2024499897 592 QEEQE 596
Cdd:TIGR04523 524 EKIEK 528
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
298-537 9.91e-08

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: 55.61  E-value: 9.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  298 TAILDQKNYVEELNRHLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKeessyilesnRKVTKDRTAD 377
Cdd:pfam12128  611 EALQSAREKQAAAEEQLVQ----ANGELEKASREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAER 676
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  378 GQALTEARKQL-KEETQLRLDVEKELEAQigMRQEMELAMKMLEKD---VCEKQDALVALRQQLDDLRAlkhelSFKLQS 453
Cdd:pfam12128  677 KDSANERLNSLeAQLKQLDKKHQAWLEEQ--KEQKREARTEKQAYWqvvEGALDAQLALLKAAIAARRS-----GAKAEL 749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  454 SDMGVKQKSELNSR--LEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELE 531
Cdd:pfam12128  750 KALETWYKRDLASLgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ 829

                   ....*.
gi 2024499897  532 LKRERE 537
Cdd:pfam12128  830 LARLIA 835
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
296-497 1.04e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 296 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRT 375
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 376 ADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD 455
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024499897 456 mgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQ 497
Cdd:COG1196   456 ---EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
607-655 1.53e-07

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: 48.45  E-value: 1.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI---NPERVCNPCH 655
Cdd:cd15760     8 CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
295-538 1.62e-07

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: 54.00  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 295 GQITAILDQKNYVEELNRHLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDR 374
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 375 TADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQE----MELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFK 450
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 451 LQssdmgvkQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQdnrlfkqefgdKINSLQLEVEELSRQRSHLEL 530
Cdd:COG4942   173 RA-------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAA-----------ELAELQQEAEELEALIARLEA 234

                  ....*...
gi 2024499897 531 ELKRERER 538
Cdd:COG4942   235 EAAAAAER 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
319-535 2.62e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.87  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 319 NNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI-LESNRKVTKDRTAD-GQALTEARKQLkEETQLRL 396
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVdLSEEAKLLLQQLSElESQLAEARAEL-AEAEARL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 397 DvekELEAQIGMRQEmELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDmgvKQKSELNSRLEEKTNQMA 476
Cdd:COG3206   243 A---ALRAQLGSGPD-ALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALR---AQIAALRAQLQQEAQRIL 315
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 477 ATIKQLEQRLRQAEKD--RQLAQQDNRLfkqefgDKINSLQLEVEELSRqrshlELELKRE 535
Cdd:COG3206   316 ASLEAELEALQAREASlqAQLAQLEARL------AELPELEAELRRLER-----EVEVARE 365
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
381-610 3.55e-07

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: 53.80  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  381 LTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDV--CEKQDALVALRQQLDDLRALKHelsfklqssdmgv 458
Cdd:COG3096    443 LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQA------------- 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  459 kqkselnsrLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINsLQLEVEELSRQRSHLELELKRERER 538
Cdd:COG3096    510 ---------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQ 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  539 WSHSHQS--------SQGNKKGPKnWLKPDGKL-RIQDENA------------------KLKQAPREENSVLPHKLQSST 591
Cdd:COG3096    580 RSELRQQleqlrariKELAARAPA-WLAAQDALeRLREQSGealadsqevtaamqqlleREREATVERDELAARKQALES 658
                          250       260
                   ....*....|....*....|
gi 2024499897  592 Q-EEQEQPSGPGNAQICQLC 610
Cdd:COG3096    659 QiERLSQPGGAEDPRLLALA 678
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
322-576 3.81e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 3.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  322 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEessyILESNRKVTKDRTA--DGQALTEARKQLKEE-TQLRLDV 398
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE----RREALQRLAEYSWDeiDVASAEREIAELEAElERLDASS 684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  399 E--KELEAQIgmrQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQssDMGVKQKSELNSRLEEK----- 471
Cdd:COG4913    685 DdlAALEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERfaaal 759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  472 -TNQMAATIKQLEQRLRQAEKDRQLAQQD-NRL---FKQEFGDKINSLQLEVEELSRQRSHL----ELELKRERERWSHS 542
Cdd:COG4913    760 gDAVERELRENLEERIDALRARLNRAEEElERAmraFNREWPAETADLDADLESLPEYLALLdrleEDGLPEYEERFKEL 839
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2024499897  543 HQSSQGNKKGP-----KNWLKpDGKLRIQDENAKLKQAP 576
Cdd:COG4913    840 LNENSIEFVADllsklRRAIR-EIKERIDPLNDSLKRIP 877
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
308-538 6.82e-07

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: 52.76  E-value: 6.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  308 EELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQ 387
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  388 LKEetqLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSR 467
Cdd:TIGR02169  366 LED---LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499897  468 LEEKtnqmAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEfgdkINSLQLEVEELSRQRSHLELELKRERER 538
Cdd:TIGR02169  443 KEDK----ALEIKKQEWKLEQLAADLSKYEQELYDLKEE----YDRVEKELSKLQRELAEAEAQARASEER 505
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
302-477 1.16e-06

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: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 302 DQKNYVEELNRhLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE------SSY-----------IL 364
Cdd:COG3883    31 ELEAAQAELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerarALYrsggsvsyldvLL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 365 ESN---------RKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQ 435
Cdd:COG3883   110 GSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024499897 436 QLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAA 477
Cdd:COG3883   190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
607-654 1.58e-06

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: 45.63  E-value: 1.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPC 654
Cdd:cd15726    10 CLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
604-658 1.62e-06

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: 45.80  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 604 AQICQLCQE-ESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCHKQL 658
Cdd:cd15755     8 ATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
350-535 2.03e-06

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: 50.89  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 350 QEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELE--AQIGMRQEME------LAMKM--- 418
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELErirqeeIAMEIsrm 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 419 --LEKDVCEKQDALVALRQQLDDLRALK-----HELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEqRLRQAEK 491
Cdd:pfam17380 378 reLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREME-RVRLEEQ 456
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 492 DRQlaQQDNRLFKQEFGDKINSLQLE--------VEELSRQRSHLELELKRE 535
Cdd:pfam17380 457 ERQ--QQVERLRQQEEERKRKKLELEkekrdrkrAEEQRRKILEKELEERKQ 506
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
604-655 2.15e-06

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: 45.43  E-value: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 604 AQICQLCQE-ESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCH 655
Cdd:cd15717     8 APVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
338-538 2.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 338 ELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLKEETQL--------------RLDVEKELE 403
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqaeeyellaeLARLEQDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 404 AQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLE 483
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 484 QRLRQAEKDR-QLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERER 538
Cdd:COG1196   386 EELLEALRAAaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
607-655 2.66e-06

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: 44.80  E-value: 2.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499897 607 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN-PERVCNPCH 655
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKGNqKQKVCKQCH 51
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
120-254 2.76e-06

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


Pssm-ID: 439065  Cd Length: 177  Bit Score: 48.08  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 120 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 179
Cdd:cd17703     3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 180 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALINRKdllSEFYEPNALMMEE-EGAIIAGLLVG 254
Cdd:cd17703    82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLVENS---SKYYEKEALLMDPvDGPILASLLVG 157
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
380-539 4.47e-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: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 380 ALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKmlekdvcEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVK 459
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELE-------ELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 460 QKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERERW 539
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
307-532 4.79e-06

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: 50.17  E-value: 4.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  307 VEELNRHLSATVNNLQAKVDALEKSNTKLTEELAvANNRIITLQEEMeRVK--------EESSYILESNRKVTKDRTadg 378
Cdd:pfam01576   17 VKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETELCAEAEEM-RARlaarkqelEEILHELESRLEEEEERS--- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  379 QALTEARKQLKEETQlrlDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGV 458
Cdd:pfam01576   92 QQLQNEKKKMQQHIQ---DLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNL 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897  459 KQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGD---KINSLQLEVEELSRQRSHLELEL 532
Cdd:pfam01576  169 AEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDlqeQIAELQAQIAELRAQLAKKEEEL 245
mukB PRK04863
chromosome partition protein MukB;
319-544 5.15e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.96  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  319 NNLQAKVDALEKSNTKLTEELAVANNRI------ITLQEEMERVK---EESSYILESNRKVTKDrTADGQALTEARKQLK 389
Cdd:PRK04863   310 VEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQadlEELEERLEEQNEVVEE-ADEQQEENEARAEAA 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  390 EETQLRL-----DVEKELEAQIGMRQEMELAMKMLEK-------------DVCEKQDALVALRQQLDD-LRALKHelsfK 450
Cdd:PRK04863   389 EEEVDELksqlaDYQQALDVQQTRAIQYQQAVQALERakqlcglpdltadNAEDWLEEFQAKEQEATEeLLSLEQ----K 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  451 LQSSDMGVKQKS-----------------------ELNSRLEEKTNQmAATIKQLEQRLRQAEKDRQLAQQDNRL---FK 504
Cdd:PRK04863   465 LSVAQAAHSQFEqayqlvrkiagevsrseawdvarELLRRLREQRHL-AEQLQQLRMRLSELEQRLRQQQRAERLlaeFC 543
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2024499897  505 QEFGDKINS---LQLEVEELSRQRSHLELELKRERERWSHSHQ 544
Cdd:PRK04863   544 KRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQ 586
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
304-538 5.59e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 304 KNYVEELNRHLSATvNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVK------EESSYILESNRKVTKDRTAD 377
Cdd:PRK03918  175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkelEELKEEIEELEKELESLEGS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 378 GQALTEARKQLK---EETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSS 454
Cdd:PRK03918  254 KRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 455 DMGVKQKSELNSRLEEKTNQMAAtikqLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR 534
Cdd:PRK03918  334 EEKEERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409

                  ....
gi 2024499897 535 ERER 538
Cdd:PRK03918  410 ITAR 413
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
596-654 6.03e-06

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: 43.95  E-value: 6.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 596 EQPSGPGNaqICQLCQEESSRSKKKNICKNCGGIFCEACSANELP-LPSSIN-PERVCNPC 654
Cdd:cd15728     1 EPPWADGD--YCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPiIKFDLNkPVRVCDVC 59
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
291-533 7.63e-06

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: 49.30  E-value: 7.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  291 SEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILES-NRK 369
Cdd:TIGR02169  712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHS 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  370 VTKDRTADGQALTEARKQLKEETQlrlDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRAlkhelsf 449
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG------- 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  450 klqssdmgvkQKSELNSRLEEKTNQmaatIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGD---KINSLQLEVEELSRQRS 526
Cdd:TIGR02169  862 ----------KKEELEEELEELEAA----LRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSELKAKLE 927

                   ....*..
gi 2024499897  527 HLELELK 533
Cdd:TIGR02169  928 ALEEELS 934
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
601-655 8.81e-06

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: 43.47  E-value: 8.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 601 PGNAQICQlCQEESSRSKKKNICKNCGGIFCEACSANELPLPS--SINPERVCNPCH 655
Cdd:cd15738     6 FRNVTECS-CSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
606-658 1.00e-05

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: 43.41  E-value: 1.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 606 ICQLC-QEESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCHKQL 658
Cdd:cd15754    10 ICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
606-654 1.26e-05

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: 43.19  E-value: 1.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499897 606 ICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN-PERVCNPC 654
Cdd:cd15743    11 MCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLKNkSARVCDEC 60
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
353-538 1.28e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 353 MERVKEESSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVcEKQDALVA 432
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 433 LRQQLDDLRALKHELSfklqssdmgvkqksELNSRLEEKTNQMAAtIKQLEQRLRQAEKDRQLAQQD----NRLFKQEFG 508
Cdd:COG4717   127 LLPLYQELEALEAELA--------------ELPERLEELEERLEE-LRELEEELEELEAELAELQEEleelLEQLSLATE 191
                         170       180       190
                  ....*....|....*....|....*....|
gi 2024499897 509 DKINSLQLEVEELSRQRSHLELELKRERER 538
Cdd:COG4717   192 EELQDLAEELEELQQRLAELEEELEEAQEE 221
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
296-541 1.75e-05

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: 48.04  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  296 QITAILDQknyvEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIItLQEEMERVKEESSyilesnRKVTKDRT 375
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAI------TCTAQCEK 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  376 ADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEME---LAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQ 452
Cdd:TIGR00618  456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  453 SSDMGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAEKdrQLAQQDNRLfKQEFGDKINSLQL---EVEELSRQRSHLE 529
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFS--ILTQCDNRS-KEDIPNLQNITVRlqdLTEKLSEAEDMLA 611
                          250
                   ....*....|..
gi 2024499897  530 LELKRERERWSH 541
Cdd:TIGR00618  612 CEQHALLRKLQP 623
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
308-539 1.99e-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: 48.19  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  308 EELNRHLSATVNNLQA----KVDALEKSNTKLTEELAVANNRIITLQEEMERVK--EESS--YILESNRKVTKDRTADGQ 379
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVdfEEASgkKIYEHDSMSTMHFRSLGS 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  380 ALTEARKQLKEETQLR----LDVEKELEAQIGMRQ-EMELAMKM----LEKDVCEKQDALVALRQQLDDLRALKHELSFK 450
Cdd:pfam15921  221 AISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQ 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  451 LQ--------SSDMGVKQKSELNS-------RLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQ 515
Cdd:pfam15921  301 LEiiqeqarnQNSMYMRQLSDLEStvsqlrsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
                          250       260
                   ....*....|....*....|....
gi 2024499897  516 LEVEELSRQRSHLELELKRERERW 539
Cdd:pfam15921  381 KLLADLHKREKELSLEKEQNKRLW 404
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
604-658 2.10e-05

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: 42.73  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 604 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPE-RVCNPCHKQL 658
Cdd:cd15729    13 APNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEYLDNKEaRVCVPCYQTL 68
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
298-535 3.56e-05

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: 46.87  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 298 TAILDQKNYVEELNRHLSAT--VNNLQAKVDALEKSNTKLTEELAVANNriiTLQEEMERVKEESSYILESNRKVTKDRT 375
Cdd:COG5185   302 TKSIDIKKATESLEEQLAAAeaEQELEESKRETETGIQNLTAEIEQGQE---SLTENLEAIKEEIENIVGEVELSKSSEE 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 376 AD--GQALTEARKQLKEETQLRLDVEKELEAQIgmrqemELAMKMLEKDVCEKQDALVALRQQLDD----LRALKHELSF 449
Cdd:COG5185   379 LDsfKDTIESTKESLDEIPQNQRGYAQEILATL------EDTLKAADRQIEELQRQIEQATSSNEEvsklLNELISELNK 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 450 KLQSSDMGVKQK-----SELNSRLEEKTNQMAATIKQLEQRLRqaEKDRQLAQQDNRLFKQ--EFGDKINSLQLEVEELS 522
Cdd:COG5185   453 VMREADEESQSRleeayDEINRSVRSKKEDLNEELTQIESRVS--TLKATLEKLRAKLERQleGVRSKLDQVAESLKDFM 530
                         250
                  ....*....|...
gi 2024499897 523 RQRSHLELELKRE 535
Cdd:COG5185   531 RARGYAHILALEN 543
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
321-507 3.77e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 321 LQAKVDALEKSNtkltEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTA--DGQALTEARKQLKEETQlRLDv 398
Cdd:COG4717    76 LEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPE-RLE- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 399 ekELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDdlRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQmaat 478
Cdd:COG4717   150 --ELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEE---- 221
                         170       180
                  ....*....|....*....|....*....
gi 2024499897 479 IKQLEQRLRQAEKDRQLAQQDNRLFKQEF 507
Cdd:COG4717   222 LEELEEELEQLENELEAAALEERLKEARL 250
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
190-263 4.40e-05

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: 45.00  E-value: 4.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 190 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 263
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
293-597 4.51e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 293 GDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvtk 372
Cdd:COG4372     1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 373 drtadgqaLTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQ 452
Cdd:COG4372    68 --------LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 453 SSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLR-------QAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQR 525
Cdd:COG4372   140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 526 SHLELELKRERERWSHSHQSSQGNKKGPKNWLKPDGKLRIQDENAKLKQAPREENSVLPHKLQSSTQEEQEQ 597
Cdd:COG4372   220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
261-543 4.73e-05

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 46.33  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 261 NFCMKGEDLDSQVGVIDFSMYLKDGNSTKGSEGDGQITAILDQKNYVEELNRhlsaTVNNLQAKVDALEKSNTKLTEELa 340
Cdd:COG5391   232 RRVSTHPLLSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTSTTQELDM----ERKELNESTSKAIHNILSIFSLF- 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 341 vanNRIITLQEEME----RVKEESSYILESNRKVTkdrtadgQALTEARKQLKEETQLRLDVEKELEAQIgmrqemeLAM 416
Cdd:COG5391   307 ---EKILIQLESEEesltRLLESLNNLLLLVLNFS-------GVFAKRLEQNQNSILNEGVVQAETLRSS-------LKE 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 417 KMLEKDVCEKQ-DALVALRQQLDDLRALKHELSFKLQSSD-MGVKQKSELNSRLEEKT-----NQMAATIKQLEQRLRQ- 488
Cdd:COG5391   370 LLTQLQDEIKSrESLILTDSNLEKLTDQNLEDVEELSRSLrKNSSQRAVVSQQPEGLTsfsklSYKLRDFVQEKSRSKSi 449
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 489 ---AEKDRQLAQQDNRLFK--QEFGDKINslqlevEELSRQRSHLELELKRERERWSHSH 543
Cdd:COG5391   450 eslQQDKEKLEEQLAIAEKdaQEINEELK------NELKFFFSVRNSDLEKILKSVADSH 503
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
379-529 4.76e-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: 45.30  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 379 QALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLD------DLRALKHELSFklq 452
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQKEIES--- 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 453 ssdmgvkQKSELnSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLE 529
Cdd:COG1579   101 -------LKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
46 PHA02562
endonuclease subunit; Provisional
303-531 5.09e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.55  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 303 QKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMErvkeessyilesnrkvtkDRTADGQALT 382
Cdd:PHA02562  200 YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE------------------DPSAALNKLN 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 383 EARKQLKEETQLrldVEKEleaqigmrqemelaMKMLEK-DVC---------------EKQDALVALRQQLDDLRALKHE 446
Cdd:PHA02562  262 TAAAKIKSKIEQ---FQKV--------------IKMYEKgGVCptctqqisegpdritKIKDKLKELQHSLEKLDTAIDE 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 447 LSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQleqrLRQAEKDRQLAQQDNRLFKQEfgdkINSLQLEVEELSRQRS 526
Cdd:PHA02562  325 LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEE----LAKLQDELDKIVKTKS 396

                  ....*
gi 2024499897 527 HLELE 531
Cdd:PHA02562  397 ELVKE 401
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-535 5.72e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 317 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKVTKDRTADGQALTEA-RKQLKEETQLR 395
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA----IEELKKAKGKCPVCGRELTEEhRKELLEEYTAE 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 396 L-DVEKELEAQIGMRQEMELAMKMLEKdVCEKQDALVALRQQLDDLRALKHELS-FKLQSsdmgVKQKSELNSRLEEKTN 473
Cdd:PRK03918  461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKkYNLEE----LEKKAEEYEKLKEKLI 535
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024499897 474 QMAATIKQLEQRLRQAEkdrqlaqqdnrlfkqEFGDKINSLQLEVEELSRQRSHLELELKRE 535
Cdd:PRK03918  536 KLKGEIKSLKKELEKLE---------------ELKKKLAELEKKLDELEEELAELLKELEEL 582
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
300-491 6.21e-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: 6.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  300 ILDQK--NYVEELnRHLSATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYI---LESNRKVTKDR 374
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIearLREIEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  375 TADGQALTEARKQLKE---ETQLRL-DVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFK 450
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEqriDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2024499897  451 LQssdmgvKQKSELNsRLEEKTNQMAATIKQLEQRLRQAEK 491
Cdd:TIGR02169  905 IE------ELEAQIE-KKRKRLSELKAKLEALEEELSEIED 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
333-539 7.01e-05

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: 46.20  E-value: 7.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  333 TKLTEELAVANNRIITLQEEMERVKEessyIL-ESNRKVTKDRTadgQA-LTEARKQLKEE-TQLRLDVE-KELEAQIGM 408
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED----ILnELERQLKSLER---QAeKAERYKELKAElRELELALLvLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  409 RQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQ 488
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024499897  489 AEKDRQLAQQDnrlfKQEFGDKINSLQLEVEELSRQRSHLELELKRERERW 539
Cdd:TIGR02168  321 LEAQLEELESK----LDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
flhF PRK06995
flagellar biosynthesis protein FlhF;
4-128 7.32e-05

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 45.73  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897   4 AERAPLLPPPAESSRDGM-AAETPPGMERRAEPGPEEAAVTEEEDEARPASPPFFLLYPGHGGAAAPHGAWRPPAPRGGA 82
Cdd:PRK06995   61 AAQPPPAAAPAAVSRPAApAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024499897  83 ALPVLLLSYPGPDGASAHPNYLMANERMnlmnMAKL-SIKGLIESAL 128
Cdd:PRK06995  141 RPRVPADAAAAVADAVKARIERIVNDTV----MQELrSLRGMLEEQL 183
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
296-485 7.55e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 7.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  296 QITAILDQKNYVEELNRHLSATVNnlQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyILESNRKVtkdRT 375
Cdd:COG4913    263 RYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREE---LDELEAQI---RG 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  376 ADGQALTEARKQLKeetqlrlDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSS- 454
Cdd:COG4913    335 NGGDRLEQLEREIE-------RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAl 407
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024499897  455 DMGVKQKSELNSRLEEKTNQmaatIKQLEQR 485
Cdd:COG4913    408 AEAEAALRDLRRELRELEAE----IASLERR 434
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
603-656 7.86e-05

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: 40.77  E-value: 7.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 603 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPE--RVCNPCHK 656
Cdd:cd15725     7 SCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
PRK11281 PRK11281
mechanosensitive channel MscK;
312-501 8.49e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  312 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE----SSYILESNRKVTKDRTADGQALTEARKQ 387
Cdd:PRK11281   117 TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlyanSQRLQQIRNLLKGGKVGGKALRPSQRVL 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  388 LKEETQLrldvekeLEAQIGMRQEmELAMKMLEKDVCEKQDALVALRQQL--DDLRALKHELSFK-LQSSDMGVKQKSEL 464
Cdd:PRK11281   197 LQAEQAL-------LNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARIQRleHQLQLLQEAINSKrLTLSEKTVQEAQSQ 268
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2024499897  465 NSRLEEKTN----QMAATIKQLEQRL-RQAEKDRQLAQQDNR 501
Cdd:PRK11281   269 DEAARIQANplvaQELEINLQLSQRLlKATEKLNTLTQQNLR 310
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
603-658 1.06e-04

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: 40.69  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 603 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCHKQL 658
Cdd:cd15742     8 HVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYlKDRPAKVCDGCFAEL 64
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
317-549 1.20e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 44.75  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 317 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRkvtkdrtadgQALTEARKQLKEETQLRL 396
Cdd:pfam09787  41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSR----------EQLQELEEQLATERSARR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 397 DVEKELEAQigmRQEMElamKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSdmgvKQKSELNSRLeektnqma 476
Cdd:pfam09787 111 EAEAELERL---QEELR---YLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSS----SSQSELENRL-------- 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 477 atiKQLEQRLRQAekdrqlaqqdnrlfkqefgdkinslQLEVEELSRQRSHLELELKReRERWSHSHQSSQGN 549
Cdd:pfam09787 173 ---HQLTETLIQK-------------------------QTMLEALSTEKNSLVLQLER-MEQQIKELQGEGSN 216
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
352-490 1.40e-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: 45.11  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 352 EMERVKEES---SYILESNRKVTKDRTADGQAL-TEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQ 427
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELeKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 428 DALV--ALRQQLDDLRALKHELSFKLQSSDMgVKQKSELNSRLE--EKTNQMAATIKQLEQRLRQAE 490
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQEQ-MRKATEERSRLEamEREREMMRQIVESEKARAEYE 592
PTZ00121 PTZ00121
MAEBL; Provisional
351-551 2.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  351 EEMERVKEESSYIL---ESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQ 427
Cdd:PTZ00121  1567 EEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  428 DALVALRQQLDDLRALKHELSFKLQSSdmgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNR----LF 503
Cdd:PTZ00121  1647 KKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaeeLK 1722
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024499897  504 KQEFGDKINSLQLEVEELSRQRSHLELElKRERERWSHSHQSSQGNKK 551
Cdd:PTZ00121  1723 KAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKK 1769
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
304-538 3.27e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  304 KNYVEELNRHLSATVNnLQAKVDALEksntklteELAVANNRIITLQEEMERVKEESSYiLESNRKVTKDRTADgQALTE 383
Cdd:COG4913    231 VEHFDDLERAHEALED-AREQIELLE--------PIRELAERYAAARERLAELEYLRAA-LRLWFAQRRLELLE-AELEE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  384 ARKQLKEETQLRLDVEKELEAQIGMRQEMELAM--------KMLEKDVCEKQDALVALRQQLDDLRALKHELSFKL-QSS 454
Cdd:COG4913    300 LRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLpASA 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  455 DMGVKQKSELNSRLEEKTNQMAAtikqLEQRLRQAEKDRQLAQQDnrlfkqefgdkINSLQLEVEELSRQRSHLELELKR 534
Cdd:COG4913    380 EEFAALRAEAAALLEALEEELEA----LEEALAEAEAALRDLRRE-----------LRELEAEIASLERRKSNIPARLLA 444

                   ....
gi 2024499897  535 ERER 538
Cdd:COG4913    445 LRDA 448
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
605-654 4.05e-04

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: 38.83  E-value: 4.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 605 QICQLCQEE-SSRSKKKNICKNCGGIFCEACSANElplPSSINPERVCNPC 654
Cdd:cd15740     6 QTCKGCNESfNSITKRRHHCKQCGAVICGKCSEFK---DLASRHNRVCRDC 53
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
606-654 4.24e-04

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: 38.70  E-value: 4.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 606 ICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI------NPERVCNPC 654
Cdd:cd15736     1 CCHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSAydprngKWYRCCHSC 55
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
324-533 4.32e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 324 KVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyILESNRKVTKDrtadgqaLTEARKQLKEETQLRLDVeKELE 403
Cdd:TIGR04523  97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ---KKENKKNIDKF-------LTEIKKKEKELEKLNNKY-NDLK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 404 AQIgmrQEMELAMKMLEKDVCEKQDALVALRQQlddLRALKHELSfKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLE 483
Cdd:TIGR04523 166 KQK---EELENELNLLEKEKLNIQKNIDKIKNK---LLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 484 QRLRQAEKDRQLAQQDNRLFKQEFGDKINSL---QLEVEELSRQRSHLELELK 533
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLN 291
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
321-494 4.38e-04

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: 42.22  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 321 LQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLKEETQLR--LDV 398
Cdd:COG1579    15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEAL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 399 EKELEAQigmrqemELAMKMLEKDVCEKQDALVALRQQLDDLRAlkhelsfklqssdmgvkQKSELNSRLEEKTNQMAAT 478
Cdd:COG1579    95 QKEIESL-------KRRISDLEDEILELMERIEELEEELAELEA-----------------ELAELEAELEEKKAELDEE 150
                         170
                  ....*....|....*.
gi 2024499897 479 IKQLEQRLRQAEKDRQ 494
Cdd:COG1579   151 LAELEAELEELEAERE 166
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
407-540 4.52e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  407 GMRQEMELA---MKMLEkDVCEKQDALVALRQQLDDLRALKHELS--FKLQSSDMGVKQKSELNSRLEEKTNQMA---AT 478
Cdd:COG4913    239 RAHEALEDAreqIELLE-PIRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELErleAR 317
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024499897  479 IKQLEQRLRQAEkdRQLAQQDNRlfkqefgdkinslqlEVEELSRQRSHLELELKRERERWS 540
Cdd:COG4913    318 LDALREELDELE--AQIRGNGGD---------------RLEQLEREIERLERELEERERRRA 362
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
614-658 6.82e-04

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: 38.25  E-value: 6.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 614 SSRSKKKNICKNCGGIFCEACSANELP--LPSSINPE------RVCNPCHKQL 658
Cdd:cd15723    10 SVLLKKRRSCNNCGNAFCSRCCSKKVPrsVMGATAPAaqretvFVCSGCNDKL 62
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
307-485 7.02e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 307 VEELNRHLSATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYIL-----ESNRKVTKDR 374
Cdd:PRK04778  280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLEKQL 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 375 TADGQALTEARKQLKEETQLRLDVEKELEaqigmrqEMELAMKMLEKDVCEKQDALVAL-------RQQLDDLRALKHEL 447
Cdd:PRK04778  358 ESLEKQYDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNKLHEI 430
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2024499897 448 SFKLQSSDM-GVKQksELNSRLEEKTNQMAATIKQLEQR 485
Cdd:PRK04778  431 KRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-596 9.33e-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: 42.31  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 300 ILDQKNYVEELNRHLS----------ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI------ 363
Cdd:TIGR04523  91 LKKNKDKINKLNSDLSkinseikndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLkkqkee 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 364 LESNRKVTKDRTADGQ-ALTEARKQLKEETQLRLDVE------KELEAQIgmrQEMELAMKMLEKDVCEKQDALVAL--- 433
Cdd:TIGR04523 171 LENELNLLEKEKLNIQkNIDKIKNKLLKLELLLSNLKkkiqknKSLESQI---SELKKQNNQLKDNIEKKQQEINEKtte 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 434 ----RQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQ----------AEKDRQLAQQD 499
Cdd:TIGR04523 248 isntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelkselKNQEKKLEEIQ 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 500 NRLFKQEfgDKINSLQLEVEELSRQRSHLE---LELKRERERWSHSHQSSQGNKKGPKNWLKpDGKLRIQDENAKLKQAp 576
Cdd:TIGR04523 328 NQISQNN--KIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQ- 403
                         330       340
                  ....*....|....*....|
gi 2024499897 577 REENSVLPHKLQSSTQEEQE 596
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKEL 423
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
217-595 9.45e-04

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: 42.40  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 217 SEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQvgvidfsmyLKDGNSTKGSEgDGQ 296
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---------MEELNKAKAAH-SFV 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 297 ITAILDQKNYVEELNR----HLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLqEEMERVKEESSYILESNRKVTK 372
Cdd:pfam05483 351 VTEFEATTCSLEELLRteqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEK 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 373 drtadgqaltearkqLKEETQlrldvekeleaqiGMRQEMELAMKMLEKDVCEKQDALVALRQQ----LDDLRALKHEL- 447
Cdd:pfam05483 430 ---------------IAEELK-------------GKEQELIFLLQAREKEIHDLEIQLTAIKTSeehyLKEVEDLKTELe 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 448 SFKLQSSDMGVKQKSEL--NSRLEEKTNQMAATIKQLEQRLRQAEK--DRQLAQQDNrLFKQEFGDKiNSLQLEVEELSR 523
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLleNKELTQEASDMTLELKKHQEDIINCKKqeERMLKQIEN-LEEKEMNLR-DELESVREEFIQ 559
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 524 QRSHLELELKRERERWSHSHQSSQGNKKGPKNWLKPDGKLRIQDEN-AKLKQAPREENSVLphKLQSSTQEEQ 595
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENkNKNIEELHQENKAL--KKKGSAENKQ 630
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
379-583 1.15e-03

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: 42.13  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  379 QALTEARKQLKEETQLRLDVEKELEAQIGmrqemeLAMKMLEKDVCEKQDALVALRQQLDDLRALKHElsfKLQSSDMGV 458
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAAAEEQLV------QANGELEKASREETFARTALKNARLDLRRLFDE---KQSEKDKKN 670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  459 KQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEF-----GDKINSLQLEVEELSRQRSHLELELK 533
Cdd:pfam12128  671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAARRSGAKAELK 750
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024499897  534 rERERWSHSHQSSqgnkKGPKNWLKPDGKLRIQDENAKLKQAPREENSVL 583
Cdd:pfam12128  751 -ALETWYKRDLAS----LGVDPDVIAKLKREIRTLERKIERIAVRRQEVL 795
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
324-619 1.16e-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: 42.26  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  324 KVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLKE-ETQLRLDVEKEL 402
Cdd:TIGR00618  174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQsHAYLTQKREAQE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  403 EAQigmRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQL 482
Cdd:TIGR00618  254 EQL---KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  483 EQRLRQAEKDRQLAQQDNRLFKQE--FGDKINSLQLEVEELSRQRSHLElELKRERERWSHSHQSSQGNKKgpknwlkpd 560
Cdd:TIGR00618  331 AAHVKQQSSIEEQRRLLQTLHSQEihIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK--------- 400
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024499897  561 GKLRIQDENAKLKQAPREENSVLPHKLQSSTQEEQEQPSgpgnAQICQLCQEESSRSKK 619
Cdd:TIGR00618  401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY----AELCAAAITCTAQCEK 455
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
302-538 1.50e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 302 DQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyILESNrkvtkdrtadgQAL 381
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAE-----------AEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 382 TEARKQLKEetQLRldvekelEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALkhelsFKLQSSDMgvKQK 461
Cdd:COG3883    82 EERREELGE--RAR-------ALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADL-----LEELKADK--AEL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499897 462 SELNSRLEEKTNQMAATIKQLEQRLRQAEKdrQLAQQDNrlfkqefgdKINSLQLEVEELSRQRSHLELELKRERER 538
Cdd:COG3883   146 EAKKAELEAKLAELEALKAELEAAKAELEA--QQAEQEA---------LLAQLSAEEAAAEAQLAELEAELAAAEAA 211
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
285-524 1.58e-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: 42.03  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  285 GNSTKGSEGDGQITAILDQKNYVEELNRH-----------LSATVNNLQAKVD----ALEKSNTKLTEELAVANNRIITL 349
Cdd:pfam15921  282 GLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdLESTVSQLRSELReakrMYEDKIEELEKQLVLANSELTEA 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  350 QEEMERVKEES---------------------SYILESNRKVTKDRTADGQALTEARKQLKE---ETQLRLDVEKELEAQ 405
Cdd:pfam15921  362 RTERDQFSQESgnlddqlqklladlhkrekelSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSE 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  406 IGMRQEMELAMKMLEKDVCEKQDALVA-LRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAAT---IKQ 481
Cdd:pfam15921  442 CQGQMERQMAAIQGKNESLEKVSSLTAqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATnaeITK 521
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2024499897  482 LEQRLrqaekdrQLAQQDNRLFKQEfGDKINSLQLEVEELSRQ 524
Cdd:pfam15921  522 LRSRV-------DLKLQELQHLKNE-GDHLRNVQTECEALKLQ 556
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-99 1.62e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897   2 AEAERAPLLPPPAESSRDGMAAETPPGMERRAEPGPEEAAVTEEEDEARPASPPffllYPGHGGAAAPHGAWRPPA--PR 79
Cdd:PRK12323  395 AAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP----APAPAPAAAPAAAARPAAagPR 470
                          90       100
                  ....*....|....*....|
gi 2024499897  80 GGAALPVLLLSYPGPDGASA 99
Cdd:PRK12323  471 PVAAAAAAAPARAAPAAAPA 490
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
308-537 1.69e-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: 41.70  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  308 EELNRHLSATVNNLQAKVDALEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYILESNRKVTKDRTADGQALTE 383
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLDEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  384 ARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEK--------------DVCEKQDALVALRQQLDDLRALKHELSF 449
Cdd:pfam01576  164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrklegESTDLQEQIAELQAQIAELRAQLAKKEE 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  450 KLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRlfkqEFGDKINSLQLEVEE-LSRQRSHL 528
Cdd:pfam01576  244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALKTELEDtLDTTAAQQ 319

                   ....*....
gi 2024499897  529 ELELKRERE 537
Cdd:pfam01576  320 ELRSKREQE 328
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1-99 2.62e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897   1 MAEAERAPLLPPPAESSRDGMAAETPPGMERRAEPGPEEAAVTEEEDEARPASPP----FFLLYPGHGGAAAPHGAWRPP 76
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPpspaGNAPAGGAPSPPPAAAPSAQP 466
                          90       100
                  ....*....|....*....|...
gi 2024499897  77 APRGGAALPVLLLSYPGPDGASA 99
Cdd:PRK07764  467 APAPAAAPEPTAAPAPAPPAAPA 489
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
328-537 3.03e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 328 LEKSNTKLTEELAVANNRIITLQEEMERVKEESSY-------ILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEK 400
Cdd:pfam05557  32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEaeealreQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 401 ELE--AQIGMRQEMELAMKMLEKDVcekqdalvaLRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEE------KT 472
Cdd:pfam05557 112 ELSelRRQIQRAELELQSTNSELEE---------LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefeiqSQ 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897 473 NQMAATIKQLEQRL-RQAEKDRQLAQQdnrlfkQEFGDKINSLQLEVEELSRQRSHLELELKRERE 537
Cdd:pfam05557 183 EQDSEIVKNSKSELaRIPELEKELERL------REHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
294-540 3.09e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 294 DGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI---LESNRKV 370
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIkqnLEQKQKE 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 371 TKDRTADGQALTEARKQLKEETQ-------LRLDVEKELEAQIGMRQ-------------EMELAMKMLEKDVCEKQDAL 430
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKdltkkisSLKEKIEKLESEKKEKEskisdledelnkdDFELKKENLEKEIDEKNKEI 570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 431 VALRQQLDDLRALKHELSFKLQSSDmgvKQKSELNSRLEEKTnqmaATIKQLEQRLRQAEKDrqlaqqdnrlfKQEFGDK 510
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKE---KEKKDLIKEIEEKE----KKISSLEKELEKAKKE-----------NEKLSSI 632
                         250       260       270
                  ....*....|....*....|....*....|
gi 2024499897 511 INSLQLEVEELSRQRSHLELELKRERERWS 540
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
CENP-H pfam05837
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ...
458-539 3.28e-03

Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H (CENP-H) sequences. Macromolecular centromere-kinetochore complex plays a critical role in sister chromatid separation, but its complete protein composition as well as its precise dynamic function during mitosis has not yet been clearly determined. CENP-H contains a coiled-coil structure and a nuclear localization signal. CENP-H is specifically and constitutively localized in kinetochores throughout the cell cycle. CENP-H may play a role in kinetochore organization and function throughout the cell cycle. This the C-terminus of the region, which is conserved from fungi to humans.


Pssm-ID: 461756 [Multi-domain]  Cd Length: 114  Bit Score: 37.95  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 458 VKQKSELNSRLEEKTNQMAATIKQL----EQRLRQAEKDRQLAQQDNRLFKQefgdkiNSLQLEVEELSRQRSHLELELK 533
Cdd:pfam05837   5 INRRDELSSAILKLSSELRELQEELteveKENLRLKRKNRELAAELLELAKE------KESRREDPKLRAQLEKLEAELK 78

                  ....*.
gi 2024499897 534 RERERW 539
Cdd:pfam05837  79 KSRRRW 84
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
307-618 3.47e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  307 VEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARK 386
Cdd:TIGR00606  693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  387 QLkEETQLRLDVEKELEAQIGMRQEMELAMKMLEKdvceKQDALVALRQQLDDLRALKhELSFKLQSSDM---GVKQKSE 463
Cdd:TIGR00606  773 LL-GTIMPEEESAKVCLTDVTIMERFQMELKDVER----KIAQQAAKLQGSDLDRTVQ-QVNQEKQEKQHeldTVVSKIE 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  464 LNSRLEEKTNQMAATIKQLEQRLrqaeKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRqrshlELELKRER----ERW 539
Cdd:TIGR00606  847 LNRKLIQDQQEQIQHLKSKTNEL----KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR-----EIKDAKEQdsplETF 917
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024499897  540 SHSHQSSQGNKKGPKNWLKPDGKLRIQDENAKLKQAPREENSvLPHKLQSSTQEEQEQPSGPGNAQICQLCQEESSRSK 618
Cdd:TIGR00606  918 LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD-IENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEK 995
PRK09039 PRK09039
peptidoglycan -binding protein;
379-526 3.51e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 379 QALTEARKQLKEETQLrLDVEKE----LEAQIGMRQEmELAMKMLEKDVCEKQDALVALRQQLDDLRA--LKHELSFKLQ 452
Cdd:PRK09039   53 SALDRLNSQIAELADL-LSLERQgnqdLQDSVANLRA-SLSAAEAERSRLQALLAELAGAGAAAEGRAgeLAQELDSEKQ 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 453 SSDMGVKQKSELNSRLEEKTNQMAAtikqLEQRLRQAEKDRQlaQQDNRLfkQEFGDKINS-LQLEVEELSRQRS 526
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAA----LEAALDASEKRDR--ESQAKI--ADLGRRLNVaLAQRVQELNRYRS 197
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
310-498 3.98e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.42  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  310 LNRHLSATVNNLQAKVDALEK--SNTKLTEELAVANNRII----TLQEEMERVKEessyILESNRKVTkdrtadgQALTE 383
Cdd:PRK10929    80 LSAELRQQLNNERDEPRSVPPnmSTDALEQEILQVSSQLLeksrQAQQEQDRARE----ISDSLSQLP-------QQQTE 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  384 ARKQLKEETQlRLDVEK-----ELEAQIGMRQ-----------EMELA---------MKMLEKDVCEKQ----DA-LVAL 433
Cdd:PRK10929   149 ARRQLNEIER-RLQTLGtpntpLAQAQLTALQaesaalkalvdELELAqlsannrqeLARLRSELAKKRsqqlDAyLQAL 227
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024499897  434 RQQLDDLRALKHELSfkLQSSDMGVKQKSELNSRLEE--KTN-QMAATIKQLEQRLRQ-AEKDRQLAQQ 498
Cdd:PRK10929   228 RNQLNSQRQREAERA--LESTELLAEQSGDLPKSIVAqfKINrELSQALNQQAQRMDLiASQQRQAASQ 294
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
604-655 4.27e-03

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: 35.95  E-value: 4.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499897 604 AQICQLCQEES-SRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCH 655
Cdd:cd15724     7 VSVCMVCQVERfSMFNRRHHCRRCGRVVCSSCSTKKMLVEGyRENPVRVCDQCY 60
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
606-658 4.32e-03

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: 36.31  E-value: 4.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897 606 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSIN-PERVCNPCHKQL 658
Cdd:cd15741    11 MCMRCKEPfNALTRRRHHCRACGYVVCWKCSDYKATLEYDGNkLNRVCKHCYVIL 65
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
475-550 4.37e-03

DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.


Pssm-ID: 462906  Cd Length: 615  Bit Score: 40.38  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024499897 475 MAATIKQLEQrlrQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR---ERERWSHSHQSSQGNK 550
Cdd:pfam09798   2 LRDKLELLQQ---EKEKELEKLKNSYEELKSSHEEELEKLKQEVQKLEDEKKFLLNELRSlsaTSPASSQSHETDTDDS 77
PLN02939 PLN02939
transferase, transferring glycosyl groups
288-541 4.82e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 40.27  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 288 TKGSEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESN 367
Cdd:PLN02939  177 MRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 368 RKVTKdrtadgqaltearkqLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVC-EKQDAL--------------VA 432
Cdd:PLN02939  257 ERVFK---------------LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWwEKVENLqdlldratnqvekaAL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 433 LRQQLDDLRALKHELSFKLQSSDMgvkqkSELNSrleEKTNQMAATIKQLEQRLRQAEKDR----QLAQQDnrlfKQEFG 508
Cdd:PLN02939  322 VLDQNQDLRDKVDKLEASLKEANV-----SKFSS---YKVELLQQKLKLLEERLQASDHEIhsyiQLYQES----IKEFQ 389
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2024499897 509 DKINSLQLEVEELSRQRSHLELelkrERERWSH 541
Cdd:PLN02939  390 DTLSKLKEESKKRSLEHPADDM----PSEFWSR 418
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
321-529 6.67e-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: 39.77  E-value: 6.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  321 LQAKVDALEKSNTKLTEELAVANNRiitLQEEM-------ERVKEESSYILESNRKVTKDRTADGQAlTEARKQLKEETQ 393
Cdd:pfam01576  227 LQAQIAELRAQLAKKEEELQAALAR---LEEETaqknnalKKIRELEAQISELQEDLESERAARNKA-EKQRRDLGEELE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  394 -LRLDVEKELE---AQIGMRQEMELAMKMLEKDVCEKQDALvalRQQLDDLRAlKH-----ELSFKLQSSDMGVKQKSEL 464
Cdd:pfam01576  303 aLKTELEDTLDttaAQQELRSKREQEVTELKKALEEETRSH---EAQLQEMRQ-KHtqaleELTEQLEQAKRNKANLEKA 378
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499897  465 NSRLEEKTNQMAATIKQLEQRLRQAEKDR----------QLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLE 529
Cdd:pfam01576  379 KQALESENAELQAELRTLQQAKQDSEHKRkklegqlqelQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
312-534 6.79e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  312 RHLSATVNNLQAKVDALEKSNTK-LTEELAVANNRIITLQE-------EMERVKEESSYILESNRKVTKDRTADGQALTE 383
Cdd:TIGR00606  119 RYKHGEKVSLSSKCAEIDREMIShLGVSKAVLNNVIFCHQEdsnwplsEGKALKQKFDEIFSATRYIKALETLRQVRQTQ 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  384 ARKQLKEETQLRL-----DVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGV 458
Cdd:TIGR00606  199 GQKVQEHQMELKYlkqykEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499897  459 KQKSELNSRLEEKtnqMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR 534
Cdd:TIGR00606  279 KQMEKDNSELELK---MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR 351
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
383-521 7.23e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  383 EARKQLKEEtqLRLDVEKELEaqiGMRQEMELAMKMLEK------DVCEKQDALVALRQQL------------DDLRALK 444
Cdd:smart00787 136 EWRMKLLEG--LKEGLDENLE---GLKEDYKLLMKELELlnsikpKLRDRKDALEEELRQLkqledeledcdpTELDRAK 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  445 HELS-------FKLQSSDMGVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAEKDRqlaqQDNRLFKQefgDKINSLQLE 517
Cdd:smart00787 211 EKLKkllqeimIKVKKLEELEEELQELESKIEDLTNK----KSELNTEIAEAEKKL----EQCRGFTF---KEIEKLKEQ 279

                   ....
gi 2024499897  518 VEEL 521
Cdd:smart00787 280 LKLL 283
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
294-443 7.41e-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: 39.36  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 294 DGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAvanNRIITLQ-----------------EEMERV 356
Cdd:COG4942    61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYrlgrqpplalllspedfLDAVRR 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 357 KEESSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIG----MRQEMELAMKMLEKDVCEKQDALVA 432
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAaleaLKAERQKLLARLEKELAELAAELAE 217
                         170
                  ....*....|.
gi 2024499897 433 LRQQLDDLRAL 443
Cdd:COG4942   218 LQQEAEELEAL 228
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
314-538 7.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 7.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  314 LSATVNNLQAKVDALEKSN---TKLTEELAVANNRIITLQEEMERVKEESSyILESNRKVTKDRTADGQALTEARKQLKE 390
Cdd:COG4913    666 AEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLAR 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897  391 EtQLRLDVEKELEAQIGMRQEmelamkmlekdvcekQDALVALRQQLDDLRALKHELSFKLqssdmgVKQKSELNSRLEE 470
Cdd:COG4913    745 L-ELRALLEERFAAALGDAVE---------------RELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPA 802
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499897  471 KTNQMAATIKQLE---QRLRQAEKDRqLAQqdnrlFKQEFGDKINSLQleveelSRQRSHLELELKRERER 538
Cdd:COG4913    803 ETADLDADLESLPeylALLDRLEEDG-LPE-----YEERFKELLNENS------IEFVADLLSKLRRAIRE 861
PRK11637 PRK11637
AmiB activator; Provisional
416-597 7.71e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 39.29  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 416 MKMLEKDVCEKQDALVALRQQLDDLRA-LKHELSFKLQSSDMGVKQKSELNsRLEEKTNQMAATIKQLEQrlRQAEKDRQ 494
Cdd:PRK11637   49 LKSIQQDIAAKEKSVRQQQQQRASLLAqLKKQEEAISQASRKLRETQNTLN-QLNKQIDELNASIAKLEQ--QQAAQERL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 495 LAQQDNRLFKQefgDKINSLQLEVEELSRQRSHLEL---------------ELKRERERWSHSHQSSQGNKKGPKNWLKP 559
Cdd:PRK11637  126 LAAQLDAAFRQ---GEHTGLQLILSGEESQRGERILayfgylnqarqetiaELKQTREELAAQKAELEEKQSQQKTLLYE 202
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024499897 560 DgklriQDENAKLKQAPREENSVLPhKLQSSTQEEQEQ 597
Cdd:PRK11637  203 Q-----QAQQQKLEQARNERKKTLT-GLESSLQKDQQQ 234
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
308-529 7.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 308 EELNRHLSATVNNLQAKVDALEKSntklTEELAVANNRIITLQEEMERVKEESSYIL-ESNRKVTKDRTADGQALTEARK 386
Cdd:PRK03918  524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLkELEELGFESVEELEERLKELEP 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 387 QLKEETQLRlDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKlqssdmgvkqkselns 466
Cdd:PRK03918  600 FYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---------------- 662
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024499897 467 RLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFgDKINSLQLEVEELSRQRSHLE 529
Cdd:PRK03918  663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKLEKALERVE 724
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-442 7.90e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 295 GQITAILDQKNYVEELNRHLSATVNNLQAKVDALEK--SNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKVTK 372
Cdd:COG4717    88 EEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEER----LEELRELEE 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499897 373 DRTADGQALTEARKQLKEE-TQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRA 442
Cdd:COG4717   164 ELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
314-575 9.85e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 38.96  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 314 LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE---SSYILESNRKVTKDrtadgQALTEARKQlke 390
Cdd:pfam07111 167 LTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGE-----QVPPEVHSQ--- 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 391 etqlrldvEKELEaqigmRQEMELAMKMLEKDVCEKQDALVALR---QQLDDLRALKHE-LSFKLQSSD-----MGVKQK 461
Cdd:pfam07111 239 --------TWELE-----RQELLDTMQHLQEDRADLQATVELLQvrvQSLTHMLALQEEeLTRKIQPSDslepeFPKKCR 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499897 462 SELNS----------RLEEKTNQMAATIKQLEQRLRQAEKDRQLAQQDNRLFKQEFGDKinSLQLEVEELSRQRSHLELE 531
Cdd:pfam07111 306 SLLNRwrekvfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDK--AAEVEVERMSAKGLQMELS 383
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2024499897 532 LKRE-RERWSHSHQSSQGNKKGPKNWLKpDGKLRIQDENAKLKQA 575
Cdd:pfam07111 384 RAQEaRRRQQQQTASAEEQLKFVVNAMS-STQIWLETTMTRVEQA 427
 
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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