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Conserved domains on  [gi|1317840667|ref|NP_001346138|]
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protein RUFY3 isoform 5 [Mus musculus]

Protein Classification

RUN and FYVE_RUFY3 domain-containing protein (domain architecture ID 13681779)

protein containing domains RUN, GBP_C, and FYVE_RUFY3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
103-224 1.11e-42

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: 397055  Cd Length: 129  Bit Score: 149.72  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 103 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 176
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1317840667 177 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 224
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
561-607 1.30e-18

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


:

Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 79.38  E-value: 1.30e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1317840667 561 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 607
Cdd:cd15744     2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
272-502 5.30e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 59.34  E-value: 5.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  272 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 349
Cdd:COG1196    235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  350 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 428
Cdd:COG1196    315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  429 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 495
Cdd:COG1196    392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                   ....*..
gi 1317840667  496 EKERKSQ 502
Cdd:COG1196    472 LQEELQR 478
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
103-224 1.11e-42

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: 397055  Cd Length: 129  Bit Score: 149.72  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 103 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 176
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1317840667 177 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 224
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
561-607 1.30e-18

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 79.38  E-value: 1.30e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1317840667 561 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 607
Cdd:cd15744     2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
163-225 3.30e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 75.73  E-value: 3.30e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317840667  163 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 225
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
555-610 1.49e-09

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: 54.36  E-value: 1.49e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  555 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 610
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
272-502 5.30e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 59.34  E-value: 5.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  272 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 349
Cdd:COG1196    235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  350 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 428
Cdd:COG1196    315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  429 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 495
Cdd:COG1196    392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                   ....*..
gi 1317840667  496 EKERKSQ 502
Cdd:COG1196    472 LQEELQR 478
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
560-610 1.03e-08

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: 396091 [Multi-domain]  Cd Length: 68  Bit Score: 52.00  E-value: 1.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1317840667 560 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 610
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-504 1.02e-07

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: 55.06  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  243 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 319
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  320 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 399
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  400 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 479
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 1317840667  480 EALTRQRTQLELELKQEKERKSQNR 504
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
268-498 8.61e-05

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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 8.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  268 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 343
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  344 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 409
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  410 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 488
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEdTLDSTAAQ 318
                          250
                   ....*....|
gi 1317840667  489 LELELKQEKE 498
Cdd:pfam01576  319 QELRSKREQE 328
PRK11281 PRK11281
mechanosensitive channel MscK;
267-489 1.27e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.29  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  267 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 335
Cdd:PRK11281   123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  336 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 388
Cdd:PRK11281   192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  389 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRleektNQMAATIKQLEQRLRQAERG--------RQSAELD 460
Cdd:PRK11281   267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTL-----TQQNLRVKNWLDRLTQSERNikeqisvlKGSLLLS 339
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1317840667  461 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 489
Cdd:PRK11281   340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
263-559 1.40e-04

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 44.90  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 263 QKNYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRiitLQEEMERVKEESSYLLESNRKGPKQDRTAEgqal 342
Cdd:NF033930  103 QKAYVKYR-KAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAE---FNKVRAKVVPEAEELAETKKKAEEAKAEEP---- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 343 sEARKHLKEETQLRLDVEKELElqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG--VK 420
Cdd:NF033930  175 -VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSEdyIK 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 421 Q--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 497
Cdd:NF033930  243 EglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVA 322
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317840667 498 ERKSQnrgtpgkGAQKPelRMDGKHRIQEENVKLKKPLEEshrlLTHPAEEQGQPSLSEKPQ 559
Cdd:NF033930  323 DYYKE-------ALEKD--LATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
M_group_A_cterm NF033777
M protein C-terminal domain; M protein (emm) is an important virulence protein and ...
318-456 9.88e-03

M protein C-terminal domain; M protein (emm) is an important virulence protein and serology-defining surface antigen of Streptococcus pyogenes (group A Streptococcus). M protein has an amino-terminal YSIRK-type signal sequence (associated with cross-wall targeting in dividing cells), and a C-terminal LPXTG domain for processing by sortase and covalent attachment to the Gram-positive cell wall. Past the signal peptide, M protein has a hypervariable region, but this HMM describes only the well-conserved region C-terminal to the hypervariable region. It discriminates M protein from two related proteins, Enn and Mrp.


Pssm-ID: 411361 [Multi-domain]  Cd Length: 218  Bit Score: 37.89  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 318 EESSYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ 397
Cdd:NF033777    8 EEQNKISEASRKGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSK 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1317840667 398 LDDLRALKHELAfklQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQS 456
Cdd:NF033777   88 LAALEKLNKELE---ESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAGKAS 143
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
103-224 1.11e-42

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: 397055  Cd Length: 129  Bit Score: 149.72  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 103 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 176
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1317840667 177 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 224
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
561-607 1.30e-18

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 79.38  E-value: 1.30e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1317840667 561 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 607
Cdd:cd15744     2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
163-225 3.30e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 75.73  E-value: 3.30e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317840667  163 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 225
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
561-607 4.74e-17

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: 75.11  E-value: 4.74e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCH 607
Cdd:cd15721    10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
561-617 1.23e-14

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: 68.90  E-value: 1.23e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYSSS 617
Cdd:cd15759    13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
561-615 7.82e-14

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: 66.63  E-value: 7.82e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYS 615
Cdd:cd15758    15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
555-610 1.49e-09

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: 54.36  E-value: 1.49e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  555 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 610
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
561-607 1.57e-09

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: 53.69  E-value: 1.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 607
Cdd:cd00065     2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
560-607 3.50e-09

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: 52.92  E-value: 3.50e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1317840667 560 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPCH 607
Cdd:cd15735     8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
272-502 5.30e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 59.34  E-value: 5.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  272 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 349
Cdd:COG1196    235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  350 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 428
Cdd:COG1196    315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  429 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 495
Cdd:COG1196    392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                   ....*..
gi 1317840667  496 EKERKSQ 502
Cdd:COG1196    472 LQEELQR 478
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
561-606 5.93e-09

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: 52.40  E-value: 5.93e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 606
Cdd:cd15730    12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDAC 59
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
560-610 1.03e-08

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: 396091 [Multi-domain]  Cd Length: 68  Bit Score: 52.00  E-value: 1.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1317840667 560 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 610
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTL 66
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
258-496 1.15e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.19  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  258 TAILDQKNYVEELNRHLNA---TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNR 328
Cdd:COG1196    688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  329 KGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 408
Cdd:COG1196    768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  409 AFKLQSSDlgvKQKSELNSRLEEKTNQMA----------ATIKQLEQRLRQAERGRQSAELDNrlfkQDFGDKINSLQLE 478
Cdd:COG1196    848 EEELEELE---KELEELKEELEELEAEKEeledelkeleEEKEELEEELRELESELAELKEEI----EKLRERLEELEAK 920
                          250
                   ....*....|....*...
gi 1317840667  479 VEALTRQRTQLELELKQE 496
Cdd:COG1196    921 LERLEVELPELEEELEEE 938
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
560-610 1.95e-08

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: 50.85  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667 560 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS-SI-KPERVCNPCHEQL 610
Cdd:cd15720     7 ECHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIeKEVRVCDPCYEKL 61
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
561-606 3.90e-08

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: 50.02  E-value: 3.90e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1317840667 561 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 606
Cdd:cd15734    11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-504 1.02e-07

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: 55.06  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  243 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 319
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  320 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 399
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  400 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 479
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 1317840667  480 EALTRQRTQLELELKQEKERKSQNR 504
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
251-511 1.13e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.11  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  251 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESnrkg 330
Cdd:COG1196    719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE---- 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  331 pkqdRTAEGQALSEARKHLKEetqlrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 410
Cdd:COG1196    795 ----LEELEEELEEAERRLDA-------LERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  411 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQD---FGDKINSLQLEVEALTRQRT 487
Cdd:COG1196    864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKlerLEVELPELEEELEEEYEDTL 943
                          250       260
                   ....*....|....*....|....*
gi 1317840667  488 QLELELKQEK-ERKSQNRGTPGKGA 511
Cdd:COG1196    944 ETELEREIERlEEEIEALGPVNLRA 968
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
268-551 1.17e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.11  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  268 EELNRHLNATVNNL---QTKVDLLEKSNTKLTEELAVANnRIITLQEEMERvKEESSYLLESNRKGPKQDRTAEgqALSE 344
Cdd:COG1196    175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  345 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-- 422
Cdd:COG1196    251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELke 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  423 --SELNSRLEEKTNQM---AATIKQLEQRLRQAE--RGRQSAELDNRlfKQDFGDKINSLQLEVEALTRQRTQLELE--- 492
Cdd:COG1196    331 kiEALKEELEERETLLeelEQLLAELEEAKEELEekLSALLEELEEL--FEALREELAELEAELAEIRNELEELKREies 408
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1317840667  493 LKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLTHPAEEQGQ 551
Cdd:COG1196    409 LEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELER 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
264-505 2.46e-07

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: 53.91  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  264 KNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGpKQDRTAEGQALS 343
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  344 EARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-----------LKHELAFKL 412
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierlearlerLEDRRERLQ 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  413 Q-----SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFkQDFGDKINSLQLEVEALTRQRT 487
Cdd:TIGR02168  421 QeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQE 499
                          250       260
                   ....*....|....*....|....
gi 1317840667  488 QLE------LELKQEKERKSQNRG 505
Cdd:TIGR02168  500 NLEgfsegvKALLKNQSGLSGILG 523
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
569-606 2.63e-07

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: 47.59  E-value: 2.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1317840667 569 SLTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 606
Cdd:cd15732    21 ASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
561-610 2.99e-07

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: 47.77  E-value: 2.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCHEQL 610
Cdd:cd15719    12 CTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
556-606 8.77e-07

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: 46.22  E-value: 8.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667 556 EKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPC 606
Cdd:cd15727     8 KECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
572-606 1.09e-06

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: 46.18  E-value: 1.09e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1317840667 572 KNTCRNCRGTFCNACTTNELPLPSSI--KPERVCNPC 606
Cdd:cd15731    27 RHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
251-501 1.53e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  251 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyllesnRKG 330
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  331 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 410
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  411 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEALTRQRTQL- 489
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELg 985
                          250
                   ....*....|....*...
gi 1317840667  490 ------ELELKQEKERKS 501
Cdd:TIGR02168  986 pvnlaaIEEYEELKERYD 1003
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
559-607 2.82e-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: 44.66  E-value: 2.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1317840667 559 QVCQLCQEddslTKNT-------CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 607
Cdd:cd15717     9 PVCMHCKK----TKFTainrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
274-517 3.23e-06

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 50.02  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 274 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA---------LSE 344
Cdd:COG4372    79 IRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAqdlqtrlktLAE 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 345 ARKHLKEETQLRLDVEKELELQISM----RQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 417
Cdd:COG4372   159 QRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQTAQAIQQRDA 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 418 GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRT-------QLE 490
Cdd:COG4372   239 QISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAAATQRGQVLAGAAQRVaqaqaqaQAQ 318
                         250       260       270
                  ....*....|....*....|....*....|
gi 1317840667 491 LELKQEKERKS--QNRGTPGKG-AQKPELR 517
Cdd:COG4372   319 AQLLSSANRPAalRLRRSPRRGrRQRPVTR 348
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
560-607 5.99e-06

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: 43.82  E-value: 5.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1317840667 560 VCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCH 607
Cdd:cd15760     7 RCDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
572-607 6.49e-06

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: 43.96  E-value: 6.49e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1317840667 572 KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCH 607
Cdd:cd15733    23 KHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
309-529 8.03e-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: 48.91  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  309 LQEEMERVKEESsYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQ 388
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  389 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 449
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  450 AERGRQSAELDNRLFK---QDFGDKINSLQLEVEALTRQRTQLELELKQEKERKsqnrgtpgKGAQKPELRMDGKHRIQE 526
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELE 902

                   ...
gi 1317840667  527 ENV 529
Cdd:TIGR02169  903 RKI 905
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
263-452 1.79e-05

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 47.71  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 263 QKNYV--EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQ 340
Cdd:COG4372   129 RQNLAkaQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATR 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 341 AlsEARKHLKEETQLRLDVEKELELQISMR----QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS- 415
Cdd:COG4372   209 A--NAAQARTEELARRAAAAQQTAQAIQQRdaqiSQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYv 286
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1317840667 416 DLGVKQKSELNSRLE----EKTNQMAATIKQLEQRLRQAER 452
Cdd:COG4372   287 RLRQQAAATQRGQVLagaaQRVAQAQAQAQAQAQLLSSANR 327
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-521 2.70e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  251 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEElavannRIITLQEEMERVKEESSYLLESNRKG 330
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  331 PKQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 397
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  398 LDDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQD 467
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSK 466
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667  468 FGDKINSLQLEVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGK 521
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEEVLKASIQ 521
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
561-607 2.77e-05

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: 41.72  E-value: 2.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1317840667 561 CQLCQEDDSLTKNT--CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 607
Cdd:cd15749     2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
572-612 3.53e-05

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: 41.94  E-value: 3.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1317840667 572 KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIK 612
Cdd:cd15739    26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
274-498 5.89e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.25  E-value: 5.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  274 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEET 353
Cdd:COG1196    300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLE-ELEQLLAELEEAKEELEEKLSALLEELEELF 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  354 QLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKT 433
Cdd:COG1196    379 EALREELAELEAELAEIRN---ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQL 455
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667  434 NQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGDKINSLQLEVEALTRQRTQLELELKQEKE 498
Cdd:COG1196    456 EELRDRLKELERELAELQEELQRLEKE----LSSLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
268-543 6.72e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 45.91  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 268 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARK 347
Cdd:COG0419   170 EKLSELLKEVIKEAKAKIEELEG---QLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 348 HLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQdalvslrQQLDDLRALKHELAFKLQSSDLGVKQKSELNS 427
Cdd:COG0419   247 EKERLEELKARLLEIESLELEALKIREEELRELERLLEELE-------EKIERLEELEREIEELEEELEGLRALLEELEE 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 428 RLEEktnqmaatIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTP 507
Cdd:COG0419   320 LLEK--------LKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAI 391
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1317840667 508 GKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLT 543
Cdd:COG0419   392 QELKEELAELSAALEEIQEELEELEKELEELERELE 427
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
268-498 8.61e-05

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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 8.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  268 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 343
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  344 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 409
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  410 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 488
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEdTLDSTAAQ 318
                          250
                   ....*....|
gi 1317840667  489 LELELKQEKE 498
Cdd:pfam01576  319 QELRSKREQE 328
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
560-610 9.14e-05

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: 40.79  E-value: 9.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667 560 VCQLCQEDDSLTKNT---CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 610
Cdd:cd15755    10 VCMRCQKAKFTPVNRrhhCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
PRK11281 PRK11281
mechanosensitive channel MscK;
267-489 1.27e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.29  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  267 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 335
Cdd:PRK11281   123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  336 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 388
Cdd:PRK11281   192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  389 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRleektNQMAATIKQLEQRLRQAERG--------RQSAELD 460
Cdd:PRK11281   267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTL-----TQQNLRVKNWLDRLTQSERNikeqisvlKGSLLLS 339
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1317840667  461 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 489
Cdd:PRK11281   340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
284-451 1.37e-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: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 284 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 344
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 345 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 422
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1317840667 423 SELNSRLE--EKTNQMAATIKQLEQRLRQAE 451
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEYE 592
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
263-559 1.40e-04

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 44.90  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 263 QKNYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRiitLQEEMERVKEESSYLLESNRKGPKQDRTAEgqal 342
Cdd:NF033930  103 QKAYVKYR-KAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAE---FNKVRAKVVPEAEELAETKKKAEEAKAEEP---- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 343 sEARKHLKEETQLRLDVEKELElqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG--VK 420
Cdd:NF033930  175 -VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSEdyIK 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 421 Q--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 497
Cdd:NF033930  243 EglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVA 322
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317840667 498 ERKSQnrgtpgkGAQKPelRMDGKHRIQEENVKLKKPLEEshrlLTHPAEEQGQPSLSEKPQ 559
Cdd:NF033930  323 DYYKE-------ALEKD--LATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
268-504 2.26e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 44.37  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 268 EELNRHLNATVNNLQTKVDLLEKSNTKLtEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARK 347
Cdd:COG0419   318 EELLEKLKSLEERLEKLEEKLEKLESEL-EELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKE 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 348 HLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL------------KHELAFKLQSS 415
Cdd:COG0419   397 ELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELagagekcpvcgqELPEEHEKELL 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 416 DLGVKQKSELNSRL--EEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELEL 493
Cdd:COG0419   477 ELYELELEELEEELsrEKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQ 556
                         250
                  ....*....|.
gi 1317840667 494 KQEKERKSQNR 504
Cdd:COG0419   557 LKEELRQLEDR 567
mukB PRK04863
chromosome partition protein MukB;
342-504 4.18e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  342 LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 419
Cdd:PRK04863   444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  420 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEALTRQRTQLELELK 494
Cdd:PRK04863   519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                          170
                   ....*....|
gi 1317840667  495 QEKERKSQNR 504
Cdd:PRK04863   590 QLQARIQRLA 599
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
281-450 5.50e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.12  E-value: 5.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  281 LQTKVDLLEKSNTKLTE-----ELAVANNRIITLQEEMERVKEESSYLLESNRKGPkqdrTAEGQALSEARKhlKEETQL 355
Cdd:PRK10929   112 LQVSSQLLEKSRQAQQEqdrarEISDSLSQLPQQQTEARRQLNEIERRLQTLGTPN----TPLAQAQLTALQ--AESAAL 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  356 RLDVEkELEL-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL------QSSDL--GVKQKS 423
Cdd:PRK10929   186 KALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEStellaeQSGDLpkSIVAQF 264
                          170       180
                   ....*....|....*....|....*..
gi 1317840667  424 ELNSRLEEKTNQMAATIKQLEQRLRQA 450
Cdd:PRK10929   265 KINRELSQALNQQAQRMDLIASQQRQA 291
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
258-431 5.70e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.16  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  258 TAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRkgpkqDRTA 337
Cdd:COG1196    351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKE 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  338 EGQALSEARKHLKEETQLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 417
Cdd:COG1196    426 ELKELEAELEELQTELEELNEELEELEEQLEELRD---RLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                          170
                   ....*....|....
gi 1317840667  418 GVKQKSELNSRLEE 431
Cdd:COG1196    503 VRAVLEALESGLPG 516
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-537 6.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 277 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 356
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 357 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 435
Cdd:PRK03918  461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 436 MAATIKQLEQRLRQAErgrqsaELDNRLFKQDfgDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKgaQKPE 515
Cdd:PRK03918  537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN--EYLE 606
                         250       260
                  ....*....|....*....|..
gi 1317840667 516 LRmDGKHRIQEENVKLKKPLEE 537
Cdd:PRK03918  607 LK-DAEKELEREEKELKKLEEE 627
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
256-562 7.01e-04

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: 42.65  E-value: 7.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  256 QITAILDQknyvEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMErvkeessyLLESNRKGPKQDR 335
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE--------LCAAAITCTAQCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  336 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 412
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  413 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQR 486
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317840667  487 TQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEEnvkLKKPLEESHRLLTHPAEEQGQPSLSEKPQVCQ 562
Cdd:TIGR00618  614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT---LTQERVREHALSIRVLPKELLASRQLALQKMQ 686
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
256-408 7.29e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 7.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  256 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNT-------KLTEELAVANNRIITLQEEMERvkeessylLESNR 328
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRR 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  329 KGPKQDRTAEGQALSEARkhlKEETQLRLD-VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE 407
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                   .
gi 1317840667  408 L 408
Cdd:TIGR02168  494 L 494
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
561-606 8.32e-04

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  Cd Length: 58  Bit Score: 37.92  E-value: 8.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1317840667 561 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 606
Cdd:cd15726    10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
269-446 1.06e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 41.98  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 269 ELNRhLNATVNNLQTKVDLL--------------EKSNTKLTEELAVANNRIITLQEEMERVKEesSYLLESNRKGPKQD 334
Cdd:COG4477   275 ELDE-AEEELGLIQEKIESLydllereveaknvvEENLPILPDYLEKAKENNEHLKEEIERVKE--SYRLAETELGSVRK 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 335 RTAEGQALSEARKHLKEETQLRLDVEKELElqiSMRQEMELAMKMLEKDVCEKQDALVSLR-------QQLDDLRALKHE 407
Cdd:COG4477   352 FEKELKELESVLDEILENIEAQEVAYSELQ---DNLEEIEKALTDIEDEQEKVQEHLTSLRkdelearENLERLKSKLHE 428
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1317840667 408 LAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 446
Cdd:COG4477   429 IKRYMEKSNLpGLPE--TFLSLFFTAGHEIQDLMKELSEV 466
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
332-537 1.06e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.01  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  332 KQDRTAEGQALSEARKHLKEetqLRLDVEKELELQISMRQEMELAMKMLEKdvcekqdalvsLRQQLDDLRALKHELAFK 411
Cdd:COG1196    659 KRSSLAQKRELKELEEELAE---LEAQLEKLEEELKSLKNELRSLEDLLEE-----------LRRQLEELERQLEELKRE 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  412 LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEALTRQRTQLEL 491
Cdd:COG1196    725 LAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLE-----------EALAKLKEEIEELEEKRQALQE 793
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1317840667  492 ELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEE 537
Cdd:COG1196    794 ELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEE 839
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
259-502 1.31e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 41.67  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 259 AILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES-NRKGPKQDRTA 337
Cdd:COG0419   484 EELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKlQLQQLKEELRQ 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 338 EGQALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEK----DVCEKQDALVSLRQQLDDLRALKHELA 409
Cdd:COG0419   564 LEDRLQELKELLEELRLLRTRKEELEELRERLKElkkkLKELEERLSQLeellQSLELSEAENELEEAEEELESELEKLN 643
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 410 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTR 484
Cdd:COG0419   644 LQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQlreelEELLKKLGEIEQLIEELES 723
                         250
                  ....*....|....*...
gi 1317840667 485 QRTQLElELKQEKERKSQ 502
Cdd:COG0419   724 RKAELE-ELKKELEKLEK 740
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
555-610 1.53e-03

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: 37.33  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1317840667 555 SEKPQvCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 610
Cdd:cd15729    11 SEAPN-CMQCEVKFTFTKrrHHCRACGKVLCSACCSLKARLEYlDNKEARVCVPCYQTL 68
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
260-547 1.70e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 41.41  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  260 ILDQKNYV-EELNRHLNATVNNLQTKVDLlEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAE 338
Cdd:COG3096    263 ISEATNYVaADYMRHANERRVHLDQALEF-RRELYTSRQQLAAEQYRHVDMSRELAELNGAEG-DLEADYQAASDHLNLV 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  339 GQALSEARKHLK-----EETQLRLDVEKELELQISMRQ-EMELAMKMLEKDVCEKQDALVSLRQQLD--DLRALKHELAF 410
Cdd:COG3096    341 QTALRQQEKIERyqadlEELTIRLEEQNEVVEEANERQeENEARAEAAELEVDELKSQLADYQQALDvqQTRAIQYQQAI 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  411 K--------LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGdkinslqlEVEAL 482
Cdd:COG3096    421 AalerakelCHLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAG--------ELARS 492
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667  483 TRQRTQLELeLKQEKERKSQNRGTPGKGAQKPELrmDGKHRIQEENVKLKKPLEESHRLLTHPAE 547
Cdd:COG3096    493 EAWDVAREL-LREGPDQRHLAEQVQPLRMRLSEL--EQRLRQQQSAERLLADFCKRQGKNLDAEE 554
YloA COG1293
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ...
370-533 1.71e-03

Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 224212 [Multi-domain]  Cd Length: 564  Bit Score: 41.22  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 370 RQEMELAMKMLEKDVC---EKQDALVSLRQqLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQR 446
Cdd:COG1293   230 REALEELLNPLKPNYYykdEKYLDVVPLKA-YADLEKLFNEALDEKFERDKIKQLASELEKKLEKELKKLENKLEKQEDE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 447 LRQAERgrqsaeLDNRLFKQdfGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKGAQ---KPELRMDGKHR 523
Cdd:COG1293   309 LEELEK------AAEELRQK--GELLYANLQLIEEGLKSVRLADFYGNEEIKIELDKSKTPSENAQryfKKYKKLKGAKV 380
                         170
                  ....*....|
gi 1317840667 524 IQEENVKLKK 533
Cdd:COG1293   381 NLDRQLSELK 390
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
561-606 1.79e-03

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: 36.71  E-value: 1.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1317840667 561 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKP--ERVCNPC 606
Cdd:cd15745     2 CAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
572-607 1.83e-03

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  Cd Length: 61  Bit Score: 36.92  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1317840667 572 KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 607
Cdd:cd15738    24 KHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
247-492 2.04e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  247 SSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES 326
Cdd:TIGR02169  708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  327 NRKGPKQDRTAEGQALSEARKHLKEETQlrlDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 406
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  407 ELAFKLQSSDLGVKQ-------------------------KSELNSRLEEKT---NQMAATIKQLEQRLRQAErgrqsae 458
Cdd:TIGR02169  865 ELEEELEELEAALRDlesrlgdlkkerdeleaqlrelerkIEELEAQIEKKRkrlSELKAKLEALEEELSEIE------- 937
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1317840667  459 ldnRLFKQDFGDKINSLQLEVEALTRQRTQLELE 492
Cdd:TIGR02169  938 ---DPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
274-531 2.05e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 274 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEsSYLLESNRKGPK---QDRTAEGQALSEARKHLK 350
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE-IKNLESQINDLEskiQNQEKLNQQKDEQIKKLQ 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 351 EETQLrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDL----RALKHELAFKLQSSDLGV 419
Cdd:TIGR04523 419 QEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLsrsiNKIKQNLEQKQKELKSKE 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 420 KQKSELN---SRLEEKTNQMAATIKQLEQRLRQ-----AERGRQSAELDNRLFKQDFG--------------DKINSLQL 477
Cdd:TIGR04523 496 KELKKLNeekKELEEKVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDFElkkenlekeideknKEIEELKQ 575
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1317840667 478 EVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGKHrIQEENVKL 531
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQkEKEKKDLIKEIEEKEKKISSLEKELEK-AKKENEKL 629
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
310-557 2.81e-03

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: 40.88  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 310 QEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEEtqlRLDVEKELELQiSMRQE-----------MELAMK 378
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE---RMAMERERELE-RIRQEerkrelerirqEEIAME 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 379 M-----LEKDVCEKQDALVSLRQQLDDLRALK---HELAFKLQssdlgvKQKSELNSRLEEKTNQMAATIKQLEQ-RLRQ 449
Cdd:pfam17380 374 IsrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEEeRARE 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 450 AERGRQsaeldnrlfkqdfgdkinslqlevEALTRQRtQLELELKQEKERKSQnrgtpgKGAQKPELRmdGKHRIQEENV 529
Cdd:pfam17380 448 MERVRL------------------------EEQERQQ-QVERLRQQEEERKRK------KLELEKEKR--DRKRAEEQRR 494
                         250       260
                  ....*....|....*....|....*....
gi 1317840667 530 K-LKKPLEESHRLLThpaEEQGQPSLSEK 557
Cdd:pfam17380 495 KiLEKELEERKQAMI---EEERKRKLLEK 520
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
260-502 3.93e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 260 ILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIitlqEEMERVKEESSYLLESNRKGPKQDRTAEg 339
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLE- 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 340 QALSEARKHLkEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGV 419
Cdd:PRK03918  259 EKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 420 KQKSELNSRLEEKTNQMAAtikqLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKER 499
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413

                  ...
gi 1317840667 500 KSQ 502
Cdd:PRK03918  414 IGE 416
YhaN COG4717
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
293-512 4.32e-03

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


Pssm-ID: 227061 [Multi-domain]  Cd Length: 984  Bit Score: 40.21  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 293 TKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELelqismRQE 372
Cdd:COG4717   277 EKREAHLQKTEAEIDALLVRLAELKDLAS-QLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGIEADL------RDK 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 373 MELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAfklqssdlgvkqksELNSRLEEKTNQMAATIKQLEQRLRQAE- 451
Cdd:COG4717   350 EEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEA--------------AYCKRLDEKRLFEDEAEEEARQRLADDEe 415
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317840667 452 --RGRQSAELDNRLFKQDFGDKINSLQLEVEALT---RQRTQLELELKQEKERKSQNRGTPGKGAQ 512
Cdd:COG4717   416 evRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTawqKQRFLREKQTAFERQKTEHTKIIALRLAG 481
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
265-459 4.88e-03

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 39.80  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 265 NYVEELNRHLNATVNNLQTKVDLlEKSNTKLTEELAvANNRIITLQEEMERVKE-ESSYLLESNRKGPKQDRTAEGQALS 343
Cdd:COG4487     2 KEIKVPIQTKPFTIPKCEDSIKG-EQARYKQIEQED-QSRILNTLEEFEKEANEkRAQYRSAKKKELSQLEEQLINQKKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 344 EARKHLKEETQLRLDVEKE---LELQISMRQEMELAMKMLEKDVCEKQDALVSL-----------RQQLDDLRALKHELA 409
Cdd:COG4487    80 QKNLFNEQIKQFELALQDEiakLEALELLNLEKDKELELLEKELDELSKELQKQlqntaeiiekkRENNKNEERLKFENE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1317840667 410 FKLQSSDLGVKQKSElnSRLEEKTNQM--AATIKQLEQRLRQAERGRQSAEL 459
Cdd:COG4487   160 KKLEESLELEREKFE--EQLHEANLDLefKENEEQRESKWAILKKLKRRAEL 209
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
268-505 5.39e-03

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


Pssm-ID: 318193 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  268 EELNRHLNATVNNLQT----KVDLLEKSNTKLtEELavannRIITLQEEmERVKEESSYLLE----SNRKGPKQDRTAE- 338
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQI-EQL-----RKMMLSHE-GVLQEIRSILVDfeeaSGKKIYEHDSMSTm 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  339 -----GQALSEARKHLKEETQLR----LDVEKELE-LQISMRQEMELAMKM----LEKDVCEKQDALVSLRQQLDDLRAL 404
Cdd:pfam15921  214 hfrslGSAISKILRELDTEISYLkgriFPVEDQLEaLKSESQNKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSQ 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667  405 KHELAFKLQssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSA--ELDNRL----------------FKQ 466
Cdd:pfam15921  294 ANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieELEKQLvlanseltearterdqFSQ 370
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1317840667  467 DFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRG 505
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG 409
CCDC154 pfam15450
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ...
349-576 6.50e-03

Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.


Pssm-ID: 406016 [Multi-domain]  Cd Length: 526  Bit Score: 39.43  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 349 LKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCE-KQDALVSLRQQLDDLRALKHELAFKLQssdlgvKQKSELNS 427
Cdd:pfam15450  47 LRELAQLRASMQLQDSELQDLRQEVQQPAKEPEKEAGEfNGPQNQNQMQALDKRLVEVREALTQIR------RKQALQDS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 428 RLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINslqLEVEALTRQRTQLELE-LKQEKERKSQNRGT 506
Cdd:pfam15450 121 ERKGASQEAALRLGKLTGMLKQEEQAREAACSSLQKSQEEASQKVD---REVARMQAQGTKLGEEmSLRFLKREAKLCGF 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317840667 507 pgkgAQKPELRMDGKHRIQEEN-VKLKKPLEESHRLLTHPAEEQGQPSLSekpQVCQLCQEDDSLTKNTCR 576
Cdd:pfam15450 198 ----LQKSFLALEKRMKASESArLSLEGELREELERRWQLLQELAEERLR---ALEGQEEQEEEHLLEQCR 261
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
268-502 8.02e-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: 39.23  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 268 EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEG-------- 339
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 340 -------------QALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 398
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 399 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERGRQSAELDNRLFKQDfgdkINSLQLE 478
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSE 441
                         250       260
                  ....*....|....*....|....
gi 1317840667 479 VEALTRQRTQLELELKQEKERKSQ 502
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRES 465
M_group_A_cterm NF033777
M protein C-terminal domain; M protein (emm) is an important virulence protein and ...
318-456 9.88e-03

M protein C-terminal domain; M protein (emm) is an important virulence protein and serology-defining surface antigen of Streptococcus pyogenes (group A Streptococcus). M protein has an amino-terminal YSIRK-type signal sequence (associated with cross-wall targeting in dividing cells), and a C-terminal LPXTG domain for processing by sortase and covalent attachment to the Gram-positive cell wall. Past the signal peptide, M protein has a hypervariable region, but this HMM describes only the well-conserved region C-terminal to the hypervariable region. It discriminates M protein from two related proteins, Enn and Mrp.


Pssm-ID: 411361 [Multi-domain]  Cd Length: 218  Bit Score: 37.89  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317840667 318 EESSYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ 397
Cdd:NF033777    8 EEQNKISEASRKGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSK 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1317840667 398 LDDLRALKHELAfklQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQS 456
Cdd:NF033777   88 LAALEKLNKELE---ESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAGKAS 143
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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